PMID-sentid	Pub_year	Sent_text	compound_name	comp_offset	prot_official_name	organism	prot_offset
2690654-11	1989	The presence of ADH in certain neurons leads us to speculate that intraneuronal ethanol metabolism may lead to focal accumulation of acetaldehyde.	Acetaldehyde	133-145	aldo-keto reductase family 1 member A1	Rattus norvegicus	16-19
2690658-3	1989	Glyceraldehyde-3-phosphate dehydrogenase is extremely heterogeneous with some isozymes active with acetaldehyde, others inactive.	Acetaldehyde	99-111	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	0-40
2690658-4	1989	The cytoplasmic enzyme, which is the classical glyceraldehyde-3-phosphate dehydrogenase, is inactive with acetaldehyde as substrate; the isozymes that are active with short chain aliphatic aldehydes are localized in the mitochondrial fraction.	Acetaldehyde	106-118	glyceraldehyde-3-phosphate dehydrogenase	Homo sapiens	47-87
2511595-10	1989	The presence of an inactive form of ALDH2 is thought to be responsible for an increase in acetaldehyde levels in the body.	Acetaldehyde	90-102	aldehyde dehydrogenase 2 family member	Homo sapiens	36-41
2557013-12	1989	Above pH 6.5, O2.- generated by xanthine oxidase and acetaldehyde prevented H2O2 from inhibiting myeloperoxidase, increasing the initial rate of H2O2 uptake.	Acetaldehyde	53-65	myeloperoxidase	Homo sapiens	97-112
2505072-0	1989	Acetaldehyde activation of poly(ADP-ribose)polymerase in hepatocytes of mice treated in vivo.	Acetaldehyde	0-12	poly (ADP-ribose) polymerase family, member 1	Mus musculus	27-53
2572305-9	1989	Moreover, both tyrosine hydroxylase (TH) immunocytochemistry and Cresyl violet staining showed an extensive and selective cell loss in the pars compacta of the substantia nigra (SNc) of the mice treated with acetaldehyde or ethanol and MPTP, whereas MPTP alone caused only a limited cell degeneration.	Acetaldehyde	208-220	tyrosine hydroxylase	Mus musculus	15-35
2818634-2	1989	When either preparation was incubated at 37 degrees with 1.5 mM acetaldehyde for 4 hr, acetaldehyde levels fell rapidly in the first 30 min and little inhibition of aspartate aminotransferase (GOT) or alanine aminotransferase (GPT) resulted.	Acetaldehyde	64-76	glutamic--pyruvic transaminase	Rattus norvegicus	227-230
2505072-2	1989	Injection with 1.0 and 3.0 mumole of acetaldehyde induced an increase in poly(ADP-ribose) polymerase activity and in the P450 level, but had no effect on DNA polymerases.	Acetaldehyde	37-49	poly (ADP-ribose) polymerase family, member 1	Mus musculus	73-100
2765201-4	1989	AA rats with high voluntary alcohol consumption had lower ALDH activity (with acetaldehyde as substrate) in the neuropil of the olfactory tubercle but higher activity (with benzaldehyde as substrate) in the spinal cord motoneurons, Purkinje cells and capillary endothelium of the cerebellum as compared to the corresponding structures from the alcohol avoiding ANA rats.	Acetaldehyde	78-90	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	58-62
2773067-7	1989	It is concluded that in the liver of animals with a high ADH/AlDH ratio there are favourable conditions for accumulation of a toxic hepatocyte-damaging acetaldehyde.	Acetaldehyde	152-164	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	61-65
2803227-8	1989	Since the Km value for acetaldehyde for liver ALDH3, 83 mM, is very much higher than those of ALDH1 and ALDH2, ALDH3 thus represents an unique class of human ALDH isozymes and it appears not to be involved in ethanol metabolism.	Acetaldehyde	23-35	aldehyde dehydrogenase 3 family member A1	Homo sapiens	46-51
2803227-8	1989	Since the Km value for acetaldehyde for liver ALDH3, 83 mM, is very much higher than those of ALDH1 and ALDH2, ALDH3 thus represents an unique class of human ALDH isozymes and it appears not to be involved in ethanol metabolism.	Acetaldehyde	23-35	aldehyde dehydrogenase 3 family member A1	Homo sapiens	111-116
2499314-4	1989	Nonetheless, in tracer studies in vivo, more than 75% of the acetaldehyde converted to acetate by the ADH ethanol-degrading pathway appeared to be also catalysed by the ADH enzyme.	Acetaldehyde	61-73	Alcohol dehydrogenase	Drosophila melanogaster	102-105
2499314-4	1989	Nonetheless, in tracer studies in vivo, more than 75% of the acetaldehyde converted to acetate by the ADH ethanol-degrading pathway appeared to be also catalysed by the ADH enzyme.	Acetaldehyde	61-73	Alcohol dehydrogenase	Drosophila melanogaster	169-172
2930794-6	1989	AHD-4 showed "high-Km" properties with respect to acetaldehyde, but differed from the "high-Km" liver mitochondrial enzyme (AHD-1), in that it was not a semialdehyde dehydrogenase.	Acetaldehyde	50-62	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	0-5
2714775-3	1989	Approximately 50% of Orientals lack the mitochondrial aldehyde dehydrogenase (ALDH2) activity, and elimination of acetaldehyde might be disturbed.	Acetaldehyde	114-126	aldehyde dehydrogenase 2 family member	Homo sapiens	78-83
2646962-13	1989	They also provide further support for the notion that acetaldehyde may be produced directly in the brain via catalase and that it may be a factor mediating some of ethanol"s central effects.	Acetaldehyde	54-66	catalase	Rattus norvegicus	109-117
2703546-1	1989	A strong and highly significant correlation was observed between serum aspartate transaminase (AST) activity and an index of the cytotoxic activity associated with serum proteins modified by acetaldehyde in a group of 24 heavy drinkers.	Acetaldehyde	191-203	solute carrier family 17 member 5	Homo sapiens	71-93
2703546-1	1989	A strong and highly significant correlation was observed between serum aspartate transaminase (AST) activity and an index of the cytotoxic activity associated with serum proteins modified by acetaldehyde in a group of 24 heavy drinkers.	Acetaldehyde	191-203	solute carrier family 17 member 5	Homo sapiens	95-98
2703546-3	1989	As it is likely that the concentration of circulating modified protein was largely determined by the quantity of free acetaldehyde generated in the liver and that the AST activity was mainly derived from damaged hepatocytes, the data indicate a correlation between hepatic acetaldehyde generation and hepatocyte damage.	Acetaldehyde	273-285	solute carrier family 17 member 5	Homo sapiens	167-170
2538093-2	1989	Chemiluminescence associated with the oxidation of acetaldehyde by xanthine oxidase was inhibited by superoxide dismutase, catalase, or several hydroxyl radical scavenging agents, and was stimulated by the addition of EDTA or ferric-EDTA.	Acetaldehyde	51-63	catalase	Homo sapiens	123-131
2537080-12	1989	A threshold blood acetaldehyde of 110 microM appeared to be required for hypotension to occur, and this was related to ALDH inhibition of approximately 40%.	Acetaldehyde	18-30	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	119-123
2789522-0	1989	Covalent interactions of acetaldehyde with the actin/microfilament system.	Acetaldehyde	25-37	actin	Oryctolagus cuniculus	47-52
2707550-4	1989	ALDH I, which exhibits a low Km with respect to acetaldehyde (Ac-CHO), was located mainly in the mitochondrial and cytosolic fractions.	Acetaldehyde	48-60	aldehyde dehydrogenase 2 family member	Homo sapiens	0-6
2789522-1	1989	The covalent binding of [14C]acetaldehyde to purified rabbit skeletal muscle actin was characterized.	Acetaldehyde	29-41	actin	Oryctolagus cuniculus	77-82
2789522-3	1989	Under non-reductive conditions, individual and competition binding studies versus albumin both showed that the G-form of actin is more reactive toward acetaldehyde than the F-form.	Acetaldehyde	151-163	actin	Oryctolagus cuniculus	121-126
2789522-4	1989	When proteins were compared on an "equi-lysine" basis under non-reducing conditions, G-actin was found to preferentially compete with albumin for binding to acetaldehyde.	Acetaldehyde	157-169	actin	Oryctolagus cuniculus	87-92
2789522-5	1989	Time-course dialysis studies indicated that acetaldehyde-actin adducts become more stable with prolonged incubation at 37 degrees C. These data raise the possibility that actin could be a preferential target for adduct formation in cellular systems and will serve as the basis for ongoing studies aimed at defining the role of acetaldehyde-protein adducts in ethanol-induced cell injury.	Acetaldehyde	44-56	actin	Oryctolagus cuniculus	57-62
2729894-1	1989	Although mitochondrial aldehyde dehydrogenase (ALDH2) has been thought to play a major role in acetaldehyde detoxification, and the high incidence of "alcohol flushing" among Orientals is attributed to the inherited deficiency of ALDH2, the role of cytosolic aldehyde dehydrogenase (ALDH1) cannot be ignored.	Acetaldehyde	95-107	aldehyde dehydrogenase 2 family member	Homo sapiens	47-52
2789522-5	1989	Time-course dialysis studies indicated that acetaldehyde-actin adducts become more stable with prolonged incubation at 37 degrees C. These data raise the possibility that actin could be a preferential target for adduct formation in cellular systems and will serve as the basis for ongoing studies aimed at defining the role of acetaldehyde-protein adducts in ethanol-induced cell injury.	Acetaldehyde	44-56	actin	Oryctolagus cuniculus	171-176
2729894-1	1989	Although mitochondrial aldehyde dehydrogenase (ALDH2) has been thought to play a major role in acetaldehyde detoxification, and the high incidence of "alcohol flushing" among Orientals is attributed to the inherited deficiency of ALDH2, the role of cytosolic aldehyde dehydrogenase (ALDH1) cannot be ignored.	Acetaldehyde	95-107	aldehyde dehydrogenase 2 family member	Homo sapiens	230-235
2789522-5	1989	Time-course dialysis studies indicated that acetaldehyde-actin adducts become more stable with prolonged incubation at 37 degrees C. These data raise the possibility that actin could be a preferential target for adduct formation in cellular systems and will serve as the basis for ongoing studies aimed at defining the role of acetaldehyde-protein adducts in ethanol-induced cell injury.	Acetaldehyde	327-339	actin	Oryctolagus cuniculus	57-62
2789522-5	1989	Time-course dialysis studies indicated that acetaldehyde-actin adducts become more stable with prolonged incubation at 37 degrees C. These data raise the possibility that actin could be a preferential target for adduct formation in cellular systems and will serve as the basis for ongoing studies aimed at defining the role of acetaldehyde-protein adducts in ethanol-induced cell injury.	Acetaldehyde	327-339	actin	Oryctolagus cuniculus	171-176
2562960-2	1989	Many Orientals lack the mitochondrial aldehyde dehydrogenase (ALDH2) activity responsible for the oxidation of acetaldehyde produced during ethanol metabolism.	Acetaldehyde	111-123	aldehyde dehydrogenase 2 family member	Homo sapiens	62-67
2721331-5	1989	These data and the pharmacokinetics of ethanol and its proximate metabolite, acetaldehyde, in the near-term pregnant ewe indicate that ethanol elimination from the maternal-fetal unit is regulated primarily by maternal hepatic ADH-catalyzed biotransformation of ethanol, and low KM ALDH activity in the fetal liver and placenta protects the fetus from exposure to ethanol-derived acetaldehyde, which is produced primarily in the maternal compartment.	Acetaldehyde	380-392	aldo-keto reductase family 1 member A1	Homo sapiens	227-230
2721481-5	1989	These results suggest that the high Km ALDH level of the outer membrane was increased as a result of a transient increase in the level of acetaldehyde around the liver mitochondria after a single large dose of ethanol, and that high Km ALDH plays an important role in acetaldehyde metabolism.	Acetaldehyde	138-150	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	39-43
2721481-5	1989	These results suggest that the high Km ALDH level of the outer membrane was increased as a result of a transient increase in the level of acetaldehyde around the liver mitochondria after a single large dose of ethanol, and that high Km ALDH plays an important role in acetaldehyde metabolism.	Acetaldehyde	138-150	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	236-240
2721481-5	1989	These results suggest that the high Km ALDH level of the outer membrane was increased as a result of a transient increase in the level of acetaldehyde around the liver mitochondria after a single large dose of ethanol, and that high Km ALDH plays an important role in acetaldehyde metabolism.	Acetaldehyde	268-280	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	39-43
2721481-5	1989	These results suggest that the high Km ALDH level of the outer membrane was increased as a result of a transient increase in the level of acetaldehyde around the liver mitochondria after a single large dose of ethanol, and that high Km ALDH plays an important role in acetaldehyde metabolism.	Acetaldehyde	268-280	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	236-240
2721481-6	1989	However, when ethanol was administered for a long time, the mitochondria were exposed to low concentrations of acetaldehyde over a long time, leading to an increase in levels of low and high Km ALDH in the matrix.	Acetaldehyde	111-123	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	194-198
2723981-6	1989	With ACTH therapy, ACE may resolve early postoperatively, but it tends to recur in most patients, continuing for as long as 3 years after the initial operation.	Acetaldehyde	19-22	proopiomelanocortin	Homo sapiens	5-9
3062940-1	1988	The metabolism of ethanol to acetaldehyde in the liver proceeds via alcohol dehydrogenase (ADH) and the microsomal ethanol-oxidizing system (MOS), whereas catalase plays no significant role.	Acetaldehyde	29-41	aldo-keto reductase family 1 member A1	Homo sapiens	68-89
2509834-0	1989	Increased covalent binding of acetaldehyde to calmodulin in the presence of calcium.	Acetaldehyde	30-42	calmodulin 1	Homo sapiens	46-56
2509834-3	1989	We found that calmodulin formed two to three times more stable adducts with acetaldehyde in the calcium-loaded state as compared to the calcium-free state.	Acetaldehyde	76-88	calmodulin 1	Homo sapiens	14-24
2509834-4	1989	Competition-binding studies showed that calmodulin could preferentially compete with albumin for acetaldehyde in the presence, but not in the absence, of calcium.	Acetaldehyde	97-109	calmodulin 1	Homo sapiens	40-50
2509834-5	1989	When calmodulin was in the calcium-loaded state, trifluoperazine, an inhibitor of calmodulin activity, significantly decreased the stable binding of acetaldehyde to the protein, whereas in the calcium-free state, minimal effects on binding were observed.	Acetaldehyde	149-161	calmodulin 1	Homo sapiens	5-15
2509834-5	1989	When calmodulin was in the calcium-loaded state, trifluoperazine, an inhibitor of calmodulin activity, significantly decreased the stable binding of acetaldehyde to the protein, whereas in the calcium-free state, minimal effects on binding were observed.	Acetaldehyde	149-161	calmodulin 1	Homo sapiens	82-92
2509834-6	1989	Since calmodulin is involved in regulation of multiple important processes in the cell, it is possible that acetaldehyde-calmodulin adducts could contribute to liver injury by perturbation of calcium-dependent homeostatic mechanisms within the hepatocyte.	Acetaldehyde	108-120	calmodulin 1	Homo sapiens	6-16
2509834-6	1989	Since calmodulin is involved in regulation of multiple important processes in the cell, it is possible that acetaldehyde-calmodulin adducts could contribute to liver injury by perturbation of calcium-dependent homeostatic mechanisms within the hepatocyte.	Acetaldehyde	108-120	calmodulin 1	Homo sapiens	121-131
3063212-8	1988	Furthermore, addition of ethanol or acetaldehyde to the incubation medium strongly depressed CPT-I activity and rates of fatty acid oxidation in hepatocytes from ethanol-treated rats, whereas these effects were much less pronounced in cells from control animals.	Acetaldehyde	36-48	carnitine palmitoyltransferase 1B	Rattus norvegicus	93-98
3148735-5	1988	ADH-71k and ADH-F were more subject to the inhibitory action of acetaldehyde than ADH-S and ADH-simulans, with ADH-71k being seven times more sensitive than ADH-S.	Acetaldehyde	64-76	Alcohol dehydrogenase	Drosophila melanogaster	0-3
3148735-5	1988	ADH-71k and ADH-F were more subject to the inhibitory action of acetaldehyde than ADH-S and ADH-simulans, with ADH-71k being seven times more sensitive than ADH-S.	Acetaldehyde	64-76	Alcohol dehydrogenase	Drosophila melanogaster	12-15
3148735-5	1988	ADH-71k and ADH-F were more subject to the inhibitory action of acetaldehyde than ADH-S and ADH-simulans, with ADH-71k being seven times more sensitive than ADH-S.	Acetaldehyde	64-76	Alcohol dehydrogenase	Drosophila melanogaster	12-15
3148735-5	1988	ADH-71k and ADH-F were more subject to the inhibitory action of acetaldehyde than ADH-S and ADH-simulans, with ADH-71k being seven times more sensitive than ADH-S.	Acetaldehyde	64-76	Alcohol dehydrogenase	Drosophila melanogaster	12-15
3148735-5	1988	ADH-71k and ADH-F were more subject to the inhibitory action of acetaldehyde than ADH-S and ADH-simulans, with ADH-71k being seven times more sensitive than ADH-S.	Acetaldehyde	64-76	Alcohol dehydrogenase	Drosophila melanogaster	12-15
3148735-5	1988	ADH-71k and ADH-F were more subject to the inhibitory action of acetaldehyde than ADH-S and ADH-simulans, with ADH-71k being seven times more sensitive than ADH-S.	Acetaldehyde	64-76	Alcohol dehydrogenase	Drosophila melanogaster	12-15
3178876-7	1988	We propose that the metabolism of acetaldehyde (probably via the low Km ALDH) and not acetaldehyde itself is responsible for the ethanol-induced lipid peroxidation in vivo and that the contribution of xanthine oxidase, as an initiator of lipid peroxidation through acetaldehyde oxidation is minute during acute intoxication.	Acetaldehyde	34-46	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	72-76
3062940-1	1988	The metabolism of ethanol to acetaldehyde in the liver proceeds via alcohol dehydrogenase (ADH) and the microsomal ethanol-oxidizing system (MOS), whereas catalase plays no significant role.	Acetaldehyde	29-41	aldo-keto reductase family 1 member A1	Homo sapiens	91-94
3062940-8	1988	The product of ethanol oxidation by ADH, MEOS and catalase is acetaldehyde.	Acetaldehyde	62-74	aldo-keto reductase family 1 member A1	Homo sapiens	36-39
2901278-3	1988	Moreover, it has been stated that IEM-611 reduced threefold the activity of liver aldehyde dehydrogenase (AlDH) by the inhibition of AlDH isoenzymes with low and high Km for acetaldehyde.	Acetaldehyde	174-186	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	82-104
3219186-3	1988	formed during acetaldehyde oxidation by xanthine oxidase after chronic alcohol consumption; the second one is enolase activity with both isoenzyme forms: nonneuronal enolase (NNE) and neuron specific enolase (NSE) which has been shown to be modified in many injuries related to the glycolytic pathways.	Acetaldehyde	14-26	enolase 1	Homo sapiens	154-173
3219186-3	1988	formed during acetaldehyde oxidation by xanthine oxidase after chronic alcohol consumption; the second one is enolase activity with both isoenzyme forms: nonneuronal enolase (NNE) and neuron specific enolase (NSE) which has been shown to be modified in many injuries related to the glycolytic pathways.	Acetaldehyde	14-26	enolase 1	Homo sapiens	175-178
3219186-3	1988	formed during acetaldehyde oxidation by xanthine oxidase after chronic alcohol consumption; the second one is enolase activity with both isoenzyme forms: nonneuronal enolase (NNE) and neuron specific enolase (NSE) which has been shown to be modified in many injuries related to the glycolytic pathways.	Acetaldehyde	14-26	enolase 2	Homo sapiens	184-207
3219186-3	1988	formed during acetaldehyde oxidation by xanthine oxidase after chronic alcohol consumption; the second one is enolase activity with both isoenzyme forms: nonneuronal enolase (NNE) and neuron specific enolase (NSE) which has been shown to be modified in many injuries related to the glycolytic pathways.	Acetaldehyde	14-26	enolase 2	Homo sapiens	209-212
3203107-10	1988	It is concluded that MDA dehydrogenase isoform I is identical to mitochondrial aldehyde dehydrogenase having a low Km for acetaldehyde, whereas isoform II may be localized in liver cytosol.	Acetaldehyde	122-134	aldehyde dehydrogenase 2 family member	Rattus norvegicus	65-101
2905277-1	1988	Calcium pantothenate (CaP), calcium 4"-phosphopantothenate (CaPP), pantethine, panthenol, sulfopantetheine and CoA decrease acute toxicity of acetaldehyde in mice.	Acetaldehyde	142-154	HPS3, biogenesis of lysosomal organelles complex 2 subunit 1	Mus musculus	111-114
3166490-5	1988	Incubation of acetaldehyde with rat liver supernatant at 37 degrees C converted xanthine dehydrogenase to xanthine oxidase in a dose-dependent manner, whereas incubation of ethanol with rat liver supernatant did not lead to conversion.	Acetaldehyde	14-26	xanthine dehydrogenase	Rattus norvegicus	80-102
2901278-3	1988	Moreover, it has been stated that IEM-611 reduced threefold the activity of liver aldehyde dehydrogenase (AlDH) by the inhibition of AlDH isoenzymes with low and high Km for acetaldehyde.	Acetaldehyde	174-186	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	106-110
3366642-11	1988	The characteristics of the intra-acinar profiles of high-Km and low-Km ALDH activity are discussed with respect to hepatic acetaldehyde oxidation and alcoholic liver damage.	Acetaldehyde	123-135	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	71-75
3343508-9	1988	AlDH in upper GI tissues and in liver nodules shared three characteristics: a sharp localization; a preference for Bz and NADP compared to the aliphatic substrate acetaldehyde and NAD; and a high co-enzyme-independent activity in the presence of Bz.	Acetaldehyde	163-175	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	0-4
3279858-10	1988	The relative resistance of the C57BL/6J strain may be associated with the increase in liver ALDH activity which is expected to facilitate the elimination of acetaldehyde, the toxic metabolite.	Acetaldehyde	157-169	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	92-96
3355670-3	1988	Evidence for a functional role of ethanol oxidation by brain catalase in the action of this substance was given by the fact that rats pretreated with AT (1 g/kg IP) exhibited a significant shorter narcosis than untreated controls, strongly suggesting the mediation of acetaldehyde in this effect.	Acetaldehyde	268-280	catalase	Rattus norvegicus	61-69
3355672-7	1988	Apparently, ALDH I isozyme from cytosol and mitochondria is primarily responsible for the oxidation of small amounts of acetaldehyde normally found in the blood of nonalcoholics after drinking moderate amounts of alcohol.	Acetaldehyde	120-132	aldehyde dehydrogenase 2 family member	Homo sapiens	12-18
3355672-8	1988	However, in alcoholics who exhibit higher blood acetaldehyde concentrations after drinking alcohol, ALDH II isozyme may be of greater physiological significance.	Acetaldehyde	48-60	aldehyde dehydrogenase 2 family member	Homo sapiens	100-104
3390237-1	1988	Acetaldehyde (A), an ethanol metabolite, was incubated with rabbit serum albumin (RSA) and human serum albumin (HSA) to form the corresponding soluble haptenized proteins, A-RSA and A-HSA respectively.	Acetaldehyde	0-12	albumin	Homo sapiens	67-80
3390237-1	1988	Acetaldehyde (A), an ethanol metabolite, was incubated with rabbit serum albumin (RSA) and human serum albumin (HSA) to form the corresponding soluble haptenized proteins, A-RSA and A-HSA respectively.	Acetaldehyde	0-12	albumin	Homo sapiens	97-110
3416486-2	1988	Incubation of intact red cells or undiluted red cell lysates at 37 degrees C for 4 h with 1-10 mmol/l acetaldehyde decreased only GOT, GPT and aldolase activities among the 26 enzymes tested.	Acetaldehyde	102-114	glutamic--pyruvic transaminase	Homo sapiens	135-138
3377754-9	1988	ADH null mutants differed physiologically from the wild type by their higher sensitivity to anaerobic treatment in plants and significantly reduced resistance to acetaldehyde in suspension cultures.	Acetaldehyde	162-174	alcohol dehydrogenase 1	Arabidopsis thaliana	0-3
3067025-7	1988	Individuals with the deficient ALDH2 phenotype do not have altered ethanol elimination rates but they do exhibit high blood acetaldehyde levels and dysphoric symptoms such as facial flushing, nausea and tachycardia, after drinking alcohol.	Acetaldehyde	124-136	aldehyde dehydrogenase 2 family member	Homo sapiens	31-36
3366301-2	1988	The activity of liver microsomal high Km-ALDH and mitochondrial low Km-ALDH, which may be primarily responsible for the oxidation of acetaldehyde after ethanol administration was found to be predominantly distributed in the centrilobular area.	Acetaldehyde	133-145	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	41-45
3366301-2	1988	The activity of liver microsomal high Km-ALDH and mitochondrial low Km-ALDH, which may be primarily responsible for the oxidation of acetaldehyde after ethanol administration was found to be predominantly distributed in the centrilobular area.	Acetaldehyde	133-145	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	71-75
3067025-9	1988	We would predict that individuals who have low ALDH2 activity because of liver disease or because they have the inactive ALDH2 variant isoenzyme might form more protein-acetaldehyde adducts and elicit a greater immune response.	Acetaldehyde	169-181	aldehyde dehydrogenase 2 family member	Homo sapiens	47-52
3067025-9	1988	We would predict that individuals who have low ALDH2 activity because of liver disease or because they have the inactive ALDH2 variant isoenzyme might form more protein-acetaldehyde adducts and elicit a greater immune response.	Acetaldehyde	169-181	aldehyde dehydrogenase 2 family member	Homo sapiens	121-126
3691517-1	1987	Microquantitative measurements of total and of low-Km aldehyde dehydrogenase (ALDH) activity with millimolar and micromolar concentrations of acetaldehyde and propionaldehyde were carried out on the livers of male and female rats.	Acetaldehyde	142-154	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	54-76
3145522-5	1988	The results also suggest that brain catalase activity may be part of an enzymatic system controlling the production and elimination of acetaldehyde in brain.	Acetaldehyde	135-147	catalase	Rattus norvegicus	36-44
2979011-0	1988	[Inhibition by ethanol and acetaldehyde the plasmin activity and plasminogen activation induced by urokinase and streptokinase].	Acetaldehyde	27-39	plasminogen	Homo sapiens	44-51
2979011-3	1988	Acetaldehyde inhibits the plasmin activity towards casein, fibrin and H-D-Val-Leu-Lys-pNA.	Acetaldehyde	0-12	plasminogen	Homo sapiens	26-33
3693368-7	1987	Acetaldehyde increased the steady-state level of collagen alpha 1(I) and collagen alpha 2(I) mRNAs about 3-fold and had small effects on beta-actin mRNA (+50%) and collagenase mRNA (-50%).	Acetaldehyde	0-12	POTE ankyrin domain family member F	Homo sapiens	137-147
3693368-9	1987	Acetaldehyde increased both collagen alpha 1(I) and collagen alpha 1(III) transcriptional activity by 2.5-fold and had small effects on beta-actin and collagenase gene transcription.	Acetaldehyde	0-12	POTE ankyrin domain family member F	Homo sapiens	136-146
3691517-1	1987	Microquantitative measurements of total and of low-Km aldehyde dehydrogenase (ALDH) activity with millimolar and micromolar concentrations of acetaldehyde and propionaldehyde were carried out on the livers of male and female rats.	Acetaldehyde	142-154	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	78-82
3691517-5	1987	The two substrates acetaldehyde and propionaldehyde yielded similar values of ALDH activity, the intraacinar distribution profiles of which showed characteristic sex differences.	Acetaldehyde	19-31	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	78-82
3324799-2	1987	Cyanamide, an aldehyde dehydrogenase inhibitor (ALDH) elevates blood acetaldehyde levels in the presence of ethanol.	Acetaldehyde	69-81	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	48-52
3324799-12	1987	It is conceivable that ALDH plays this role by regulating the levels of acetaldehyde in brain.	Acetaldehyde	72-84	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	23-27
3324802-3	1987	The Km values with gamma-aminobutyraldehyde with both isozymes are high relative to Km values with acetaldehyde (50 microM for E1 and 1 microM for E2).	Acetaldehyde	99-111	small nucleolar RNA, H/ACA box 73A	Homo sapiens	127-135
3606116-0	1987	Covalent binding of acetaldehyde to tubulin: evidence for preferential binding to the alpha-chain.	Acetaldehyde	20-32	Fc gamma receptor and transporter	Homo sapiens	86-97
3319346-5	1987	Metabolism occurs, principally by alcohol dehydrogenase, in the liver to acetaldehyde.	Acetaldehyde	73-85	aldo-keto reductase family 1 member A1	Homo sapiens	34-55
3122352-11	1987	ADH in Drosophila has a dual function and thus can catalyze oxidation of both ethanol and its toxic metabolite, acetaldehyde.	Acetaldehyde	112-124	Alcohol dehydrogenase	Drosophila melanogaster	0-3
3674384-0	1987	Oxidation product(s) in acetaldehyde reacts with NAD(P)H and interferes with assay of alcohol dehydrogenase.	Acetaldehyde	24-36	aldo-keto reductase family 1 member A1	Homo sapiens	86-107
3606116-7	1987	Denaturation studies showed that the native tubulin conformation was necessary for the alpha-chain to show enhanced reactivity toward acetaldehyde.	Acetaldehyde	134-146	Fc gamma receptor and transporter	Homo sapiens	87-98
3606116-8	1987	Competition binding studies showed that alpha-tubulin could effectively compete with beta-tubulin and bovine serum albumin for a limited amount of acetaldehyde.	Acetaldehyde	147-159	albumin	Homo sapiens	109-122
3606116-11	1987	These data indicate that the alpha-chain of free tubulin is the preferential site of stable acetaldehyde-tubulin adduct formation.	Acetaldehyde	92-104	Fc gamma receptor and transporter	Homo sapiens	29-40
16665461-9	1987	All forms of catalase in tobacco show peroxidatic (measured as ethanol to acetaldehyde conversion) as well as catalatic activities.	Acetaldehyde	74-86	catalase isozyme 1	Nicotiana tabacum	13-21
3429208-2	1987	A simple rate equation for alcohol dehydrogenase was obtained by assuming independent binding sites for ethanol and NAD+ and fully competitive inhibition by the products of the reaction, acetaldehyde and NADH.	Acetaldehyde	187-199	aldo-keto reductase family 1 member A1	Rattus norvegicus	27-48
3429208-6	1987	The parameters for alcohol dehydrogenase partially purified from rat liver were: Km for ethanol = 0.746 mM, Km for NAD+ = 0.0563 mM, Km for acetaldehyde = 7.07 microM, Km for NADH = 4.77 microM and Keq = 2.36 X 10(-4).	Acetaldehyde	140-152	aldo-keto reductase family 1 member A1	Rattus norvegicus	19-40
3580137-4	1987	In vitro, hepatic ALA-D activity was not modified by ethanol; instead it was non-competitively inhibited by acetaldehyde.	Acetaldehyde	108-120	aminolevulinate, delta-, dehydratase	Mus musculus	18-23
3111530-7	1987	The discrepancy between glycerol and sucrose could be largely reconciled by correcting for diffusion-unrelated effects as estimated from rate studies of considerably slower CA II catalyzed acetaldehyde hydration and p-nitrophenyl acetate hydrolysis.	Acetaldehyde	189-201	carbonic anhydrase 2	Homo sapiens	173-178
3580137-6	1987	Therefore, a mechanism for the action of ethanol on ALA-D, based on the inhibitory effect of acetaldehyde, is proposed.	Acetaldehyde	93-105	aminolevulinate, delta-, dehydratase	Mus musculus	52-57
3551665-3	1987	ALDH1 is localized principally in hepatocyte cytosol and exhibits a Km for acetaldehyde of about 0.1 mM at pH 9.5.	Acetaldehyde	75-87	aldehyde dehydrogenase 1 family member A1	Homo sapiens	0-5
3818635-7	1987	Furthermore, microsomal dihydroxyacetone phosphate acyltransferase activity is inhibited at all acetaldehyde concentrations.	Acetaldehyde	96-108	glyceronephosphate O-acyltransferase	Homo sapiens	24-66
3551665-4	1987	ALDH2 is mitochondrial in origin and exhibits low Km for acetaldehyde, about 1 microM.	Acetaldehyde	57-69	aldehyde dehydrogenase 2 family member	Homo sapiens	0-5
3426677-1	1987	This paper presents a series of experiments that define the energetics of liver alcohol dehydrogenase and allow the construction of a free energy profile for the ethanol-acetaldehyde interconversion.	Acetaldehyde	170-182	aldo-keto reductase family 1 member A1	Homo sapiens	80-101
3620014-2	1987	Cyanamide, an ALDH inhibitor elevates blood acetaldehyde levels in the presence of ethanol.	Acetaldehyde	44-56	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	14-18
3620014-12	1987	It is conceivable that ALDH plays this role by regulating the levels of acetaldehyde in brain.	Acetaldehyde	72-84	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	23-27
3828063-3	1987	On the opposite, the presence of 3-amino-1,2,4-triazole (10 to 40 mM), a known catalase inhibitor, induced a concentration dependent reduction of the amount of AcH recovered during incubation even in presence of glucose oxidase.	Acetaldehyde	160-163	catalase	Rattus norvegicus	79-87
3426694-0	1987	Rate determining factors of ethanol oxidation in hepatocytes from starved and fed rats: effect of acetaldehyde concentration on the rate of NADH oxidation catalyzed by alcohol dehydrogenase.	Acetaldehyde	98-110	aldo-keto reductase family 1 member A1	Rattus norvegicus	168-189
3426694-1	1987	Rates of reduction of acetaldehyde and pyruvate catalyzed by alcohol dehydrogenase and lactate dehydrogenase have been estimated in isolated hepatocytes from rats metabolizing ethanol and [2-3H]lactate.	Acetaldehyde	22-34	aldo-keto reductase family 1 member A1	Rattus norvegicus	61-82
3426717-3	1987	Invariably, significantly higher blood acetaldehyde levels were measured in ALDH I-deficient subjects after ethanol loading.	Acetaldehyde	39-51	aldehyde dehydrogenase 2 family member	Homo sapiens	76-82
3106030-4	1987	The ALDH I with a low Km for acetaldehyde is predominantly of mitochondrial origin and ALDH II which has a relatively higher Km is of cytosolic origin.	Acetaldehyde	29-41	aldehyde dehydrogenase 2 family member	Homo sapiens	4-10
3474930-4	1987	The formation of alpha-chain specific stable acetaldehyde-tubulin adducts results in functional impairment of the ability of tubulin to polymerize.	Acetaldehyde	45-57	Fc gamma receptor and transporter	Homo sapiens	17-28
3474930-5	1987	Under relatively physiologic conditions where acetaldehyde-to-protein ratios are low, alpha-chain specific binding is prominent.	Acetaldehyde	46-58	Fc gamma receptor and transporter	Homo sapiens	86-97
3610592-3	1987	ALDH I has a low Km for acetaldehyde and is primarily a mitochondrial enzyme, while ALDH II has a higher Km and is of cytosolic origin.	Acetaldehyde	24-36	aldehyde dehydrogenase 2 family member	Homo sapiens	0-6
2432930-3	1986	They reduce the corresponding dopamine aldehydes (3,4-dihydroxyphenyl)acetaldehyde and (4-hydroxy-3-methoxyphenyl)acetaldehyde (HMPAL) with kcat/Km values varying from 7800 to 190,000 mM-1 min-1, considerably more efficient than the reduction of acetaldehyde with kcat/Km values from 780 to 4900 mM-1 min-1.	Acetaldehyde	70-82	Mix1 homeobox-like 1 (Xenopus laevis)	Mus musculus	184-194
2432930-3	1986	They reduce the corresponding dopamine aldehydes (3,4-dihydroxyphenyl)acetaldehyde and (4-hydroxy-3-methoxyphenyl)acetaldehyde (HMPAL) with kcat/Km values varying from 7800 to 190,000 mM-1 min-1, considerably more efficient than the reduction of acetaldehyde with kcat/Km values from 780 to 4900 mM-1 min-1.	Acetaldehyde	70-82	Mix1 homeobox-like 1 (Xenopus laevis)	Mus musculus	296-306
3768432-4	1986	The kinetics of ethanol oxidation into acetaldehyde by cumene hydroperoxide was studied at 30 degrees C in the phosphate buffer pH 6.6; this reaction was shown to proceed with the participation of catalase and its cat-str conjugate.	Acetaldehyde	39-51	catalase	Homo sapiens	197-205
3003181-2	1986	Objectives of this study were first, to determine if liver cancers in vinyl chloride-treated rats also expressed this AlDH phenotype, and second, to quantitate the NAD- and NADP-dependent AlDH activity for the substrates Bz and acetaldehyde (Ac) in the cancers and surrounding tissue.	Acetaldehyde	228-240	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	188-192
3773650-5	1986	Though ethanol had an inhibitory effect on collagen synthesis by FSCs, acetaldehyde stimulated collagen production by the cells from CCl4-induced hepatic fibrosis, whereas collagen synthesis by the cells from normal rats was not influenced by acetaldehyde.	Acetaldehyde	71-83	C-C motif chemokine ligand 4	Rattus norvegicus	133-137
3743603-6	1986	The data showed that cells derived from aggregates of cultures treated with formaldehyde or acetaldehyde followed by exposure to TPA possessed a considerably higher ability to form colonies in soft agar than untreated control cells.	Acetaldehyde	92-104	plasminogen activator, tissue type	Rattus norvegicus	129-132
3697954-0	1986	Modification potentials of ethyl alcohol and acetaldehyde on development of preneoplastic glutathione S-transferase P-form-positive liver cell foci initiated by diethylnitrosamine in the rat.	Acetaldehyde	45-57	glutathione S-transferase pi 1	Rattus norvegicus	90-117
2937708-3	1986	[14C]Acetaldehyde was incubated with alcohol dehydrogenase, glucose-6-phosphate dehydrogenase, lactate dehydrogenase and RNase A, each at 37 degrees C (pH 7.4).	Acetaldehyde	5-17	aldo-keto reductase family 1 member A1	Homo sapiens	37-58
2937708-3	1986	[14C]Acetaldehyde was incubated with alcohol dehydrogenase, glucose-6-phosphate dehydrogenase, lactate dehydrogenase and RNase A, each at 37 degrees C (pH 7.4).	Acetaldehyde	5-17	glucose-6-phosphate dehydrogenase	Homo sapiens	60-93
2937708-3	1986	[14C]Acetaldehyde was incubated with alcohol dehydrogenase, glucose-6-phosphate dehydrogenase, lactate dehydrogenase and RNase A, each at 37 degrees C (pH 7.4).	Acetaldehyde	5-17	ribonuclease A family member 1, pancreatic	Homo sapiens	121-128
3003181-2	1986	Objectives of this study were first, to determine if liver cancers in vinyl chloride-treated rats also expressed this AlDH phenotype, and second, to quantitate the NAD- and NADP-dependent AlDH activity for the substrates Bz and acetaldehyde (Ac) in the cancers and surrounding tissue.	Acetaldehyde	242-244	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	188-192
2937417-11	1986	Based on recent findings, a convincing mechanism is the higher accumulation of acetaldehyde in flushing subjects because they have an unusual, less-active liver aldehyde dehydrogenase isozyme (ALDHI).	Acetaldehyde	79-91	aldehyde dehydrogenase 2 family member	Homo sapiens	193-198
2937417-12	1986	The possibility that an "atypical" alcohol dehydrogenase, which is present in 85-90% of Oriental subjects, can contribute to increased blood acetaldehyde levels in flushing subjects cannot be ruled out.	Acetaldehyde	141-153	aldo-keto reductase family 1 member A1	Homo sapiens	35-56
2867670-3	1985	Cysteinylglycine, the first metabolite in the glutathione breakdown by gamma-glutamyltranspeptidase, showed a rapid and equimolar reactivity to acetaldehyde and such was comparable to the reaction seen with L-cysteine or D-penicillamine.	Acetaldehyde	144-156	inactive glutathione hydrolase 2	Homo sapiens	71-99
3515990-10	1986	The role of the placenta ALDH in the acetaldehyde placental transfer is discussed.	Acetaldehyde	37-49	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	25-29
2999539-0	1985	Blockade of ethanol induced conditioned taste aversion by 3-amino-1,2,4-triazole: evidence for catalase mediated synthesis of acetaldehyde in rat brain.	Acetaldehyde	126-138	catalase	Rattus norvegicus	95-103
3789876-1	1986	Ethanol metabolism to acetaldehyde by NAD+-dependent alcohol dehydrogenase (ADH) activity reduces, in part, androgen secretion by rat Leydig cells.	Acetaldehyde	22-34	aldo-keto reductase family 1 member A1	Rattus norvegicus	53-74
3789876-1	1986	Ethanol metabolism to acetaldehyde by NAD+-dependent alcohol dehydrogenase (ADH) activity reduces, in part, androgen secretion by rat Leydig cells.	Acetaldehyde	22-34	aldo-keto reductase family 1 member A1	Rattus norvegicus	76-79
3943656-8	1986	The kinetic results support proposals that AHD-2 may be the primary enzyme for oxidizing acetaldehyde during ethanol oxidation in vivo.	Acetaldehyde	89-101	aldehyde dehydrogenase family 1, subfamily A1	Mus musculus	43-48
3749513-1	1986	It is known that aldehyde dehydrogenase (ALDH) responsible for metabolism of acetaldehyde deriving from ethanol has two distinct forms of isozymes: ALDH-I (low Km ALDH) and ALDH-II (high Km ALDH), and that many Orientals lack ALDH-I isozyme genetically.	Acetaldehyde	77-89	aldehyde dehydrogenase 2 family member	Homo sapiens	148-154
3749513-1	1986	It is known that aldehyde dehydrogenase (ALDH) responsible for metabolism of acetaldehyde deriving from ethanol has two distinct forms of isozymes: ALDH-I (low Km ALDH) and ALDH-II (high Km ALDH), and that many Orientals lack ALDH-I isozyme genetically.	Acetaldehyde	77-89	aldehyde dehydrogenase 2 family member	Homo sapiens	173-179
3749513-4	1986	Questionnaire study of Japanese volunteers indicated that ALDH-I deficient individuals showed flushing, palpitation and other uncomfortable somatic signs, due to reduced metabolism of acetaldehyde, much more frequently than ALDH-I positive ones.	Acetaldehyde	184-196	aldehyde dehydrogenase 2 family member	Homo sapiens	58-64
4092214-1	1985	The reaction of human serum albumin (HSA) with aldoses (C3-C6) and acetaldehyde has been studied.	Acetaldehyde	67-79	albumin	Homo sapiens	22-35
2870701-0	1985	Effect of acetaldehyde treatment in vivo on rat liver tryptophan oxygenase and tyrosine aminotransferase activities.	Acetaldehyde	10-22	tryptophan 2,3-dioxygenase	Rattus norvegicus	54-74
2867670-0	1985	Conjugation of acetaldehyde with cysteinylglycine, the first metabolite in glutathione breakdown by gamma-glutamyltranspeptidase.	Acetaldehyde	15-27	inactive glutathione hydrolase 2	Homo sapiens	100-128
2867670-2	1985	When acetaldehyde was incubated with glutathione alone, there was only a slight decrease of acetaldehyde, while an apparently equimolar reaction between acetaldehyde and free sulfhydryl was observed with the addition of gamma-glutamyltranspeptidase.	Acetaldehyde	5-17	inactive glutathione hydrolase 2	Homo sapiens	220-248
2995452-7	1985	In contrast, methemoglobin formation by xanthine oxidase plus acetaldehyde was significantly greater than that caused by stimulated PMNs (P less than 0.001).	Acetaldehyde	62-74	hemoglobin subunit gamma 2	Homo sapiens	13-26
4085411-0	1985	Effect of ethanol and acetaldehyde on the release of arginine-vasopressin and oxytocin from the isolated hypothalamo-hypophyseal system of rats.	Acetaldehyde	22-34	arginine vasopressin	Rattus norvegicus	53-86
4085411-1	1985	Effects of ethanol and acetaldehyde on the release of arginine-vasopressin (AVP) and oxytocin (OXT) were examined using a superfusion system of the isolated hypothalamo-hypophyseal complex of rats.	Acetaldehyde	23-35	arginine vasopressin	Rattus norvegicus	76-79
4085411-1	1985	Effects of ethanol and acetaldehyde on the release of arginine-vasopressin (AVP) and oxytocin (OXT) were examined using a superfusion system of the isolated hypothalamo-hypophyseal complex of rats.	Acetaldehyde	23-35	oxytocin/neurophysin I prepropeptide	Rattus norvegicus	95-98
6497899-4	1984	At millimolar acetaldehyde concentrations, NAD-dependent ALDH was primarily mitochondrial (up to 80%).	Acetaldehyde	14-26	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	57-61
4026957-7	1985	Ascorbic acid (2.5-10 mM) increased by 31-46 percent (p less than 0.001) the irreversible binding of acetaldehyde to human serum albumin and by 8-10 percent (p less than 0.05) the irreversible reaction of acetaldehyde with serum proteins.	Acetaldehyde	101-113	albumin	Homo sapiens	123-136
4026957-8	1985	We conclude that the nonenzymatic binding of acetaldehyde to Hb, human serum albumin and serum proteins is influenced by factors other than acetaldehyde concentration.	Acetaldehyde	45-57	albumin	Homo sapiens	71-84
16664175-7	1985	After 15 hours, the recovery of NADPH cytochrome c reductase is 15% of that in controls, fumarase is 50%, and catalase is 75%.Glyoxysomes and ER are capable of converting ethanol to acetaldehyde which was measured using the fluorogenic reagent, 5,5-dimethyl-1,3-cyclohexanedione.	Acetaldehyde	182-194	catalase isozyme 1-like	Ricinus communis	110-118
4040382-3	1985	We further hypothesized that brain catalase and aldehyde dehydrogenase, the enzymes controlling the production and elimination of acetaldehyde in the brain, may represent a biological marker system underlying the affinity of the animals to consume ethanol.	Acetaldehyde	130-142	catalase	Homo sapiens	35-70
4015825-8	1985	Approximately 15% of the acetaldehyde disappearance at 200 microM was catalyzed by high-Km ALDH, and nearly 30% of the acetaldehyde was lost through binding to cytosolic proteins.	Acetaldehyde	25-37	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	91-95
4015839-7	1985	The very high affinity of AHD-5 for acetaldehyde suggests that this enzyme is predominantly responsible for acetaldehyde oxidation in mouse liver mitochondria.	Acetaldehyde	36-48	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	26-31
4015839-7	1985	The very high affinity of AHD-5 for acetaldehyde suggests that this enzyme is predominantly responsible for acetaldehyde oxidation in mouse liver mitochondria.	Acetaldehyde	108-120	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	26-31
4015841-6	1985	Study of partially purified (enriched) baboon cytosolic ALDH confirmed changes seen in the original cytosols and kinetic characterization of the enriched enzyme revealed a 9-fold higher Km for acetaldehyde in ALDH from an ethanol treated animal.	Acetaldehyde	193-205	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	209-213
3966800-0	1985	Aldehyde dehydrogenase activity as the rate-limiting factor for acetaldehyde metabolism in rat liver.	Acetaldehyde	64-76	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	0-22
3966800-1	1985	The velocity of acetaldehyde metabolism in rat liver may be governed either by the rate of regeneration of NAD from NADH through the electron transport system or by the activity of aldehyde dehydrogenase (ALDH).	Acetaldehyde	16-28	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	181-203
3966800-1	1985	The velocity of acetaldehyde metabolism in rat liver may be governed either by the rate of regeneration of NAD from NADH through the electron transport system or by the activity of aldehyde dehydrogenase (ALDH).	Acetaldehyde	16-28	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	205-209
3966800-3	1985	To confirm that ALDH activity was the rate-limiting factor, low-Km ALDH in slices or intact mitochondria was partially inhibited by treatment with cyanamide and the rate of acetaldehyde metabolism measured.	Acetaldehyde	173-185	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	16-20
3966800-3	1985	To confirm that ALDH activity was the rate-limiting factor, low-Km ALDH in slices or intact mitochondria was partially inhibited by treatment with cyanamide and the rate of acetaldehyde metabolism measured.	Acetaldehyde	173-185	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	67-71
3966800-4	1985	Any inhibition of low-Km ALDH resulted in a decreased rate of acetaldehyde metabolism, indicating that no excess of low-Km ALDH existed.	Acetaldehyde	62-74	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	25-29
3966800-9	1985	By measuring acetaldehyde accumulation during ethanol metabolism, it was also established that low-Km ALDH activity was rate-limiting for acetaldehyde oxidation during concomitant ethanol oxidation.	Acetaldehyde	13-25	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	102-106
6397229-7	1984	Michaelis constants for all class I and II isozymes vary by more than 8000-fold, from less than 1 microM for beta 1 gamma 1 and beta 1 beta 1 with octanal to 8.3 mM for pi-ADH for acetaldehyde.	Acetaldehyde	180-192	aldo-keto reductase family 1 member A1	Homo sapiens	172-175
6442148-0	1984	Acetaldehyde utilization and toxicity in Drosophila adults lacking alcohol dehydrogenase or aldehyde oxidase.	Acetaldehyde	0-12	Alcohol dehydrogenase	Drosophila melanogaster	67-88
6442148-7	1984	Toxicity tests showed that ADH-negative flies were more sensitive to acetaldehyde than wild type, but this is most likely explained by the transformation of the aldehyde into alcohol.	Acetaldehyde	69-81	Alcohol dehydrogenase	Drosophila melanogaster	27-30
3994763-6	1985	In intact mitochondria, with 200 microM acetaldehyde or benzaldehyde the matrix space enzyme accounted for 77 and 62%, respectively, of the total ALDH activity.	Acetaldehyde	40-52	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	146-150
3994763-8	1985	With subcellular fractions, from livers of disulfiram-treated and control rats, a greater degree of inhibition of ALDH was obtained when acetaldehyde was a substrate compared to that with benzaldehyde in cytosol and mitochondria.	Acetaldehyde	137-149	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	114-118
3994763-13	1985	It can be concluded that, in rat, disulfiram inhibiting liver ALDH not only affects oxidation of acetaldehyde, but also that of benzaldehyde.	Acetaldehyde	97-109	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	62-66
4015825-3	1985	Mitochondrial low-Km aldehyde dehydrogenase (ALDH) was partially inactivated and the effect on acetaldehyde oxidation measured.	Acetaldehyde	95-107	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	21-43
4015825-3	1985	Mitochondrial low-Km aldehyde dehydrogenase (ALDH) was partially inactivated and the effect on acetaldehyde oxidation measured.	Acetaldehyde	95-107	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	45-49
4015825-6	1985	The level of remaining ALDH activity after cyanamide treatment was correlated with the ability of either rat liver mitochondria or liver slices to oxidize acetaldehyde.	Acetaldehyde	155-167	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	23-27
4015825-7	1985	Any inhibition of ALDH resulted in a decreased rate of acetaldehyde oxidation, indicating that there is no excess of ALDH in the cell above what is needed to oxidize acetaldehyde.	Acetaldehyde	55-67	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	18-22
4015825-7	1985	Any inhibition of ALDH resulted in a decreased rate of acetaldehyde oxidation, indicating that there is no excess of ALDH in the cell above what is needed to oxidize acetaldehyde.	Acetaldehyde	166-178	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	18-22
3966800-9	1985	By measuring acetaldehyde accumulation during ethanol metabolism, it was also established that low-Km ALDH activity was rate-limiting for acetaldehyde oxidation during concomitant ethanol oxidation.	Acetaldehyde	138-150	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	102-106
3985669-6	1985	Ethanol and acetaldehyde inhibited the release of the lysozyme of monocytes at concentrations of greater than 0.75% and greater than 0.03% respectively, but granulocytes were unaffected; the release of beta-glucuronidase and lactate dehydrogenase remained stable.	Acetaldehyde	12-24	glucuronidase beta	Homo sapiens	202-220
3996732-7	1985	Based upon the kinetic characteristics, it is suggested that AHD-5 may be the primary enzyme for oxidizing mitochondrial acetaldehyde during ethanol oxidation in vivo.	Acetaldehyde	121-133	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	61-66
6093697-7	1984	Ascorbate also caused enhanced acetaldehyde adduct formation with other purified proteins, including cytochrome c and histones, as well as the polyamino acid, poly-L-lysine.	Acetaldehyde	31-43	cytochrome c, somatic	Homo sapiens	101-113
6486817-2	1984	Although a poor substrate for oxidation, crotonaldehyde is an effective inhibitor of the oxidation of acetaldehyde by mitochondrial aldehyde dehydrogenase, by intact mitochondria, and by isolated hepatocytes.	Acetaldehyde	102-114	aldehyde dehydrogenase 2 family member	Rattus norvegicus	118-154
6442934-1	1984	The in vitro influence of ethanol and acetaldehyde on diamine oxidase catalyzed reaction was measured with guinea pig liver and intestine.	Acetaldehyde	38-50	amiloride-sensitive amine oxidase [copper-containing]	Cavia porcellus	54-69
6725272-2	1984	This laboratory has recently reported that, in a reconstituted enzyme system containing alcohol-induced isozyme 3a of liver microsomal cytochrome P-450, the sum of acetaldehyde generated by the monooxygenation of ethanol and of hydrogen peroxide produced by the NADPH oxidase activity is inadequate to account for the O2 and NADPH consumed.	Acetaldehyde	164-176	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	135-151
6514184-0	1984	Changes in Ca2+ ion activity within unrestrained rat"s hippocampus perfused with alcohol or acetaldehyde.	Acetaldehyde	92-104	carbonic anhydrase 2	Rattus norvegicus	11-14
6514184-10	1984	Acetaldehyde evoked an intense and concentration-dependent enhancement of Ca2+ ion efflux from the perfused tissue at all of the sites in the hippocampus examined.	Acetaldehyde	0-12	carbonic anhydrase 2	Rattus norvegicus	74-77
6514184-13	1984	The mechanism of action of acetaldehyde is envisaged to be due to its affinity to membrane sulfhydryl groups which alters protein conformation and thus interferes with both Ca2+ channels and Ca2+ binding properties.	Acetaldehyde	27-39	carbonic anhydrase 2	Rattus norvegicus	173-176
6514184-13	1984	The mechanism of action of acetaldehyde is envisaged to be due to its affinity to membrane sulfhydryl groups which alters protein conformation and thus interferes with both Ca2+ channels and Ca2+ binding properties.	Acetaldehyde	27-39	carbonic anhydrase 2	Rattus norvegicus	191-194
6541256-4	1984	Other compounds elicited significant elevations in ethanol-derived blood acetaldehyde only at 9 h. We suggest that latent inhibitors of AlDH such as 5 or 8 might be useful as alcohol deterrent agents.	Acetaldehyde	73-85	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	136-140
6378202-3	1984	The elevation of blood acetaldehyde elicited by cyanamide after ethanol administration to rats was attenuated more than 90 percent by pretreatment with the catalase inhibitor, 3-amino-1,2,4-triazole.	Acetaldehyde	23-35	catalase	Bos taurus	156-164
6378202-5	1984	Although hepatic catalase was also inhibited by cyanamide, a positive correlation between blood acetaldehyde and hepatic catalase activity was observed.	Acetaldehyde	96-108	catalase	Bos taurus	121-129
6378202-8	1984	Although hepatic catalase was also inhibited by cyanamide, a positive correlation between blood acetaldehyde and hepatic catalase activity was observed.	Acetaldehyde	96-108	catalase	Bos taurus	121-129
6377951-4	1984	Oral pretreatment with the alcohol dehydrogenase inhibitor, 4-methylpyrazole, reduced ethanol elimination by 15-25% and strongly suppressed acetaldehyde accumulation.	Acetaldehyde	140-152	aldo-keto reductase family 1 member A1	Homo sapiens	27-48
6327680-6	1984	In iron-depleted systems containing cytochrome P-450 LM2 or cytochrome P-450 LMeb , an appropriate stoichiometry was attained between the NADPH consumed and the sum of hydrogen peroxide and acetaldehyde produced.	Acetaldehyde	190-202	cytochrome P450 2B4	Oryctolagus cuniculus	36-56
6327680-6	1984	In iron-depleted systems containing cytochrome P-450 LM2 or cytochrome P-450 LMeb , an appropriate stoichiometry was attained between the NADPH consumed and the sum of hydrogen peroxide and acetaldehyde produced.	Acetaldehyde	190-202	cytochrome P-450	Oryctolagus cuniculus	36-52
6701903-1	1984	The effect of treatment of rats with acetaldehyde on the subcellular NAD+-aldehyde dehydrogenase (EC 1.2.1.3, ALDH) activities and acetaldehyde oxidation by isolated intact mitochondria of the liver and the brain was studied.	Acetaldehyde	37-49	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	110-114
6701903-2	1984	Inhalation of acetaldehyde caused a significant decrease in the liver mitochondrial low Km-ALDH activity, while brain mitochondrial ALDH activity remained unchanged.	Acetaldehyde	14-26	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	91-95
6663362-6	1983	When acetaldehyde was injected intravenously to rabbits, thiamin concentration and the transketolase activity in blood decreased gradually and after 12 h the thiamin level reached its lowest value, then increased slowly and normalized in 72 h. Thus, it could be postulated that the decrease in thiamin after an acute ethanol ingestion linked greatly to the acetaldehyde catabolism.	Acetaldehyde	5-17	transketolase	Oryctolagus cuniculus	87-100
6497955-1	1984	The heptic metabolism of acetaldehyde in carbon tetrachloride (CCl4)-intoxicated rats was studied using a non-recirculating haemoglobin-free liver-perfusion system.	Acetaldehyde	25-37	C-C motif chemokine ligand 4	Rattus norvegicus	63-67
6497955-2	1984	Acetaldehyde uptake by the liver from acutely CCl4-treated animals (4.16 mmol/kg,i.p.)	Acetaldehyde	0-12	C-C motif chemokine ligand 4	Rattus norvegicus	46-50
6497955-8	1984	(5) The rate of ethanol production from acetaldehyde by the catalytic action of alcohol dehydrogenase was found to be unaltered when low concentrations of acetaldehyde (0.01-0.2 mM) were used, whereas a significant suppression of the rate of ethanol production was detected in the presence of high concentrations of acetaldehyde (0.6-5 mM).	Acetaldehyde	40-52	aldo-keto reductase family 1 member A1	Rattus norvegicus	80-101
6497955-8	1984	(5) The rate of ethanol production from acetaldehyde by the catalytic action of alcohol dehydrogenase was found to be unaltered when low concentrations of acetaldehyde (0.01-0.2 mM) were used, whereas a significant suppression of the rate of ethanol production was detected in the presence of high concentrations of acetaldehyde (0.6-5 mM).	Acetaldehyde	155-167	aldo-keto reductase family 1 member A1	Rattus norvegicus	80-101
6497955-8	1984	(5) The rate of ethanol production from acetaldehyde by the catalytic action of alcohol dehydrogenase was found to be unaltered when low concentrations of acetaldehyde (0.01-0.2 mM) were used, whereas a significant suppression of the rate of ethanol production was detected in the presence of high concentrations of acetaldehyde (0.6-5 mM).	Acetaldehyde	155-167	aldo-keto reductase family 1 member A1	Rattus norvegicus	80-101
6317450-3	1983	The O-2 production by the xanthine oxidase-acetaldehyde system was not inhibited by TPTCl.	Acetaldehyde	43-55	immunoglobulin kappa variable 1D-39	Homo sapiens	4-7
6353979-4	1983	4-Methylpyrazole, an alcohol dehydrogenase inhibitor, efficiently reduced blood acetaldehyde levels when injected intravenously (7 mg/kg) at the height of the reaction.	Acetaldehyde	80-92	aldo-keto reductase family 1 member A1	Homo sapiens	21-42
6875556-2	1983	A significant increase of ALDH activity was found in whole brain of old rats with both acetaldehyde (39%) and propionylaldehyde (15%) used as substrates.	Acetaldehyde	87-99	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	26-30
6875556-3	1983	In different brain areas of old rats, with acetaldehyde used as substrate, a significant increase of ALDH activity was found in striatum (30-50%) and cerebral cortex (37%).	Acetaldehyde	43-55	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	101-105
6632378-14	1983	The present experiments demonstrated that the rise in blood acetaldehyde levels coincided with the inhibition rates of the low-Km ALDH activity by the cephem antibiotics.	Acetaldehyde	60-72	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	130-134
6347204-6	1983	Mitochondria, because of their relatively high aldehyde dehydrogenase (ALDH) activity, prevented the accumulation of acetaldehyde, or quickly removed acetaldehyde already accumulated.	Acetaldehyde	117-129	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	71-75
6347204-6	1983	Mitochondria, because of their relatively high aldehyde dehydrogenase (ALDH) activity, prevented the accumulation of acetaldehyde, or quickly removed acetaldehyde already accumulated.	Acetaldehyde	150-162	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	71-75
6353979-0	1983	Cardiovascular effects of acetaldehyde accumulation after ethanol ingestion: their modification by beta-adrenergic blockade and alcohol dehydrogenase inhibition.	Acetaldehyde	26-38	aldo-keto reductase family 1 member A1	Homo sapiens	128-149
6353979-7	1983	These changes are reversed by preventing acetaldehyde formation through alcohol dehydrogenase inhibition.	Acetaldehyde	41-53	aldo-keto reductase family 1 member A1	Homo sapiens	72-93
7159468-5	1982	The brain ALDH-activity with a high acetaldehyde concentration was significantly decreased by coprine and cyanamide but not by disulfiram.	Acetaldehyde	36-48	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	10-14
6135422-5	1983	Acetaldehyde produced non-competitive inhibition of (Na+K+) ATPase and Mg2+ ATPase at concentrations of 6 and 56 mM respectively and 5" nucleotidase activity was also inhibited at these concentrations.	Acetaldehyde	0-12	mucin 7, secreted	Homo sapiens	71-74
6135422-6	1983	We conclude that ethanol and acetaldehyde inhibit (Na+K+) ATPase and Mg2+ ATPase activities as part of a generalised effect on the liver plasma membrane.	Acetaldehyde	29-41	mucin 7, secreted	Homo sapiens	69-80
7159468-4	1982	The brain ALDH-activity with a low acetaldehyde concentration was significantly decreased by coprine and cyanamide at both times tested, whereas disulfiram caused no change after 2 hr but an inhibition of 38% after 24 hr.	Acetaldehyde	35-47	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	10-14
6346128-10	1983	The results indicate the presence of NAD-dependent ALDH in various subcellular fractions of the female genital system which may be important in the gonadal metabolic detoxification of ethanol derived acetaldehyde.	Acetaldehyde	200-212	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	51-55
6830235-0	1983	Acetaldehyde adducts with proteins: binding of [14C]acetaldehyde to serum albumin.	Acetaldehyde	0-12	albumin	Homo sapiens	68-81
6830235-2	1983	Bovine serum albumin (BSA) was used as the model protein incubated in the presence of 0.2 mM [14C]acetaldehyde at pH 7.4 and at 37 degrees C. Acetaldehyde formed both stable and unstable adducts with serum albumin.	Acetaldehyde	142-154	albumin	Homo sapiens	7-20
6830235-2	1983	Bovine serum albumin (BSA) was used as the model protein incubated in the presence of 0.2 mM [14C]acetaldehyde at pH 7.4 and at 37 degrees C. Acetaldehyde formed both stable and unstable adducts with serum albumin.	Acetaldehyde	142-154	albumin	Homo sapiens	200-213
6354997-3	1983	In liver extracts and other tissues of Japanese an isozyme of ALDH (ALDH I) with a low Km for acetaldehyde was found to be deficient.	Acetaldehyde	94-106	aldehyde dehydrogenase 2 family member	Homo sapiens	68-74
7097272-1	1982	Rats were treated with either coprine or disulfiram and the inhibition of aldehyde dehydrogenase (ALDH) in liver and brain mitochondria was measured with acetaldehyde, 3,4-dihydroxyphenylacetaldehyde (DOPAL), and succinate semialdehyde at different concentrations.	Acetaldehyde	154-166	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	74-96
7180842-2	1982	A remarkably higher frequency of acute alcohol intoxication among Orientals than among Caucasians could be related to the absence of the ALDH2 isozyme, which has a low apparent Km for acetaldehyde.	Acetaldehyde	184-196	aldehyde dehydrogenase 2 family member	Homo sapiens	137-142
6292103-6	1982	Both A. fumigatus and R. oryzae hyphae were damaged by the myeloperoxidase-hydrogen peroxide-halide system either with reagent hydrogen peroxide or enzymatic systems for generating hydrogen peroxide (glucose oxidase with glucose, or xanthine oxidase with either hypoxanthine or acetaldehyde).	Acetaldehyde	278-290	myeloperoxidase	Homo sapiens	59-74
7157414-1	1982	Rat liver mitochondria contain an aldehyde dehydrogenase (ALDH, EC 1.2.1.3) with a low Km for acetaldehyde (2 microM) which is susceptible to inhibition by a variety of agents including p-chloromercuribenzoate and arsenite.	Acetaldehyde	94-106	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	34-56
7157414-1	1982	Rat liver mitochondria contain an aldehyde dehydrogenase (ALDH, EC 1.2.1.3) with a low Km for acetaldehyde (2 microM) which is susceptible to inhibition by a variety of agents including p-chloromercuribenzoate and arsenite.	Acetaldehyde	94-106	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	58-62
7157414-11	1982	This ALDH isozyme is considered to be the most important enzyme in acetaldehyde metabolism.	Acetaldehyde	67-79	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	5-9
7157414-12	1982	Malondialdehyde inhibition of the low Km ALDH may be important since both ethanol and acetaldehyde are thought to stimulate hepatic lipid peroxidation.	Acetaldehyde	86-98	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	41-45
7097272-1	1982	Rats were treated with either coprine or disulfiram and the inhibition of aldehyde dehydrogenase (ALDH) in liver and brain mitochondria was measured with acetaldehyde, 3,4-dihydroxyphenylacetaldehyde (DOPAL), and succinate semialdehyde at different concentrations.	Acetaldehyde	154-166	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	98-102
7097272-3	1982	The ALDH activity both in the liver and the brain was inhibited at low concentrations of acetaldehyde and DOPAL, but not with succinate semialdehyde.	Acetaldehyde	89-101	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	4-8
7097272-7	1982	Kinetic studies on ALDH preparations from brain and liver mitochondria suggested that acetaldehyde and DOPAL are metabolized by the same low-Km ALDH.	Acetaldehyde	86-98	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	19-23
7097272-7	1982	Kinetic studies on ALDH preparations from brain and liver mitochondria suggested that acetaldehyde and DOPAL are metabolized by the same low-Km ALDH.	Acetaldehyde	86-98	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	144-148
7108552-7	1982	The main part of the aldehyde dehydrogenase activities with acetaldehyde, DOPAL, and succinate semialdehyde, but only little activity of the marker enzyme for the outer membrane (monoamine oxidase, MAO), was released from a purified mitochondrial fraction subjected to sonication.	Acetaldehyde	60-72	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	21-43
6799006-2	1982	Acetaldehyde and to a lesser degree phenobarbital, at concentrations which did not modify the activity of a preparation of hog kidney diamine oxidase, increased delta1 -pyrroline formation in kidney homogenate, which suggests that aldehyde-metabolizing enzymes present in this tissue may interfere with the yield of delta1 -pyrroline formation and that the use of  acetaldehyde may give better information on kidney diamine oxidase activity.	Acetaldehyde	0-12	amine oxidase, copper containing 1	Rattus norvegicus	416-431
7085677-7	1982	This cytochrome displays the highest activity of all of the rabbit isozymes in the oxidation of ethanol to acetaldehyde and the p-hydroxylation of aniline when reconstituted with NADPH-cytochrome P-450 reductase and phospholipid in the presence of NADPH and oxygen.	Acetaldehyde	107-119	NADPH--cytochrome P450 reductase	Oryctolagus cuniculus	179-211
7080214-0	1982	[Interaction of acetaldehyde with bovine serum albumin].	Acetaldehyde	16-28	albumin	Homo sapiens	47-54
7080214-1	1982	At pH 6.8-7.4 acetaldehyde interacts with six primary amino groups of bovine serum albumin to form the Schiff base.	Acetaldehyde	14-26	albumin	Homo sapiens	83-90
7108552-9	1982	These results indicate that the ALDH activities with acetaldehyde, DOPAL and succinate semialdehyde are located in the matrix compartment.	Acetaldehyde	53-65	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	32-36
7080065-4	1982	Blood acetaldehyde concentrations were significantly increased 1, 2, 3 and 4 h after ethanol administration at CCl4 doses of 15 microliter/kg and higher, with DBA and C57 mice exhibiting similar dose-response effects up to the 150 microliter/kg dose.	Acetaldehyde	6-18	chemokine (C-C motif) ligand 4	Mus musculus	111-115
6284006-7	1982	Ceruloplasmin also inhibited reduction of cytochrome c and NBT mediated by the aerobic action of xanthine oxidase on acetaldehyde (another superoxide-generating system) and mimicked the activity of purified human erythrocyte SOD by inhibiting photoreduction of NBT and by accelerating aerobic photooxidation of dianisidine.	Acetaldehyde	117-129	ceruloplasmin	Homo sapiens	0-13
6284006-7	1982	Ceruloplasmin also inhibited reduction of cytochrome c and NBT mediated by the aerobic action of xanthine oxidase on acetaldehyde (another superoxide-generating system) and mimicked the activity of purified human erythrocyte SOD by inhibiting photoreduction of NBT and by accelerating aerobic photooxidation of dianisidine.	Acetaldehyde	117-129	cytochrome c, somatic	Homo sapiens	42-54
7135154-3	1982	About 43% of Japanese, who lacked the low Km enzyme (ALDH I) showed an elevated acetaldehyde concentration due to their inability to metabolize acetaldehyde quickly and effectively.	Acetaldehyde	80-92	aldehyde dehydrogenase 2 family member	Homo sapiens	53-59
7135154-3	1982	About 43% of Japanese, who lacked the low Km enzyme (ALDH I) showed an elevated acetaldehyde concentration due to their inability to metabolize acetaldehyde quickly and effectively.	Acetaldehyde	144-156	aldehyde dehydrogenase 2 family member	Homo sapiens	53-59
7080065-5	1982	A CCL4 dose of 500 microliter/kg produced differences in blood acetaldehyde elevation between the two inbred strains (DBA - 5-fold, C57 - 3-fold).	Acetaldehyde	63-75	chemokine (C-C motif) ligand 4	Mus musculus	2-6
7080065-7	1982	Using male genetically heterogeneous stock (HS) mice it was shown that phenobarbital pretreatment potentiated the CCl4-induced decrease in in vivo acetaldehyde oxidation.	Acetaldehyde	147-159	chemokine (C-C motif) ligand 4	Mus musculus	114-118
7080065-10	1982	These data show that in vivo acetaldehyde oxidation is inhibited by very low doses of CCl4 (15 microliter/kg, i.g.)	Acetaldehyde	29-41	chemokine (C-C motif) ligand 4	Mus musculus	86-90
7030108-1	1981	4-methylpyrazole (4-MP), an inhibitor of alcohol dehydrogenase, rapidly abolished the accumulation of acetaldehyde following alcohol ingestion both in volunteers pretreated with the Antabuse analog calcium carbimide and in an antabuse-treated alcoholic.	Acetaldehyde	102-114	aldo-keto reductase family 1 member A1	Homo sapiens	41-62
7337698-1	1981	Liver aldehyde dehydrogenase (ALDH), the enzyme involved in the oxidation of aldehydes such as acetaldehyde derived from ethanol, exists in multiple forms in most mammals.	Acetaldehyde	95-107	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	6-28
7337698-1	1981	Liver aldehyde dehydrogenase (ALDH), the enzyme involved in the oxidation of aldehydes such as acetaldehyde derived from ethanol, exists in multiple forms in most mammals.	Acetaldehyde	95-107	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	30-34
7323448-1	1981	Paraldehyde (PAL) was shown to be metabolized to acetaldehyde (AcH) by rat liver microsomes in vitro only when the cofactors for the cytochrome P-450 system were present.	Acetaldehyde	49-61	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	133-149
7323448-1	1981	Paraldehyde (PAL) was shown to be metabolized to acetaldehyde (AcH) by rat liver microsomes in vitro only when the cofactors for the cytochrome P-450 system were present.	Acetaldehyde	63-66	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	133-149
7032509-0	1981	The rate-determining step in the liver alcohol dehydrogenase- catalysed reduction of acetaldehyde is an isomerization of the enzyme.	Acetaldehyde	85-97	aldo-keto reductase family 1 member A1	Homo sapiens	39-60
6787051-5	1981	Externally added hydrogen peroxide markedly stimulated cytochrome P-450-dependent ethanol oxidation, but not until the concentration of H2O2 reached 0.3 mM, whereas the hydroxyl radical scavenger mannitol completely inhibited the cytochrome P-450-dependent acetaldehyde production.	Acetaldehyde	257-269	cytochrome P-450	Oryctolagus cuniculus	55-71
7196192-2	1981	The bulk of ethanol is metabolized in the liver, where alcohol dehydrogenase, a complex mixture of isoenzymes, oxidizes ethanol to acetaldehyde.	Acetaldehyde	131-143	aldo-keto reductase family 1 member A1	Homo sapiens	55-76
7018435-6	1981	The study shows that interstitial tissue possesses both ADH and ALDH, which are essential for the respective metabolism of ethanol and acetaldehyde, and that the seminiferous tubules possesses greater affinity for the metabolism of acetaldehyde than that of the interstitial tissue.	Acetaldehyde	135-147	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	64-68
6783302-4	1981	These results suggest that aldehyde-metabolizing enzymes present in homogenate may interfere with the amount of delta 1-pyrroline formation and that the use of acetaldehyde may give better information on tissue diamine oxidase activity.	Acetaldehyde	160-172	amine oxidase, copper containing 1	Rattus norvegicus	211-226
6785257-1	1981	In the presence of acetaldehyde, metabolizing human erythrocytes accumulate an altered hemoglobin product showing chromatographic similarity to hemoglobin AIa or AIb.	Acetaldehyde	19-31	ANIB1	Homo sapiens	162-165
7242849-5	1981	However, the acetaldehyde concentration necessary to produce neuronal degeneration in a 1 h exposure is many times greater than ever reported in CSF in human alcoholism.	Acetaldehyde	13-25	colony stimulating factor 2	Homo sapiens	145-148
7004234-7	1980	Prevention of the inhibition of brain catalase in vivo by prior administration of ethanol constitutes indirect evidence for the oxidation of ethanol to acetaldehyde in rat brain.	Acetaldehyde	152-164	catalase	Rattus norvegicus	38-46
6895072-0	1981	Stimulatory effect of ceruloplasmin on hemolysis caused by the action of xanthine oxidase on acetaldehyde.	Acetaldehyde	93-105	ceruloplasmin	Homo sapiens	22-35
7424741-5	1980	On the other hand acetaldehyde at concentrations ranging from 0.01 - 0.5% w/v (2 - 114 mM) showed marked inhibition of all the abovementioned enzymes except acetylcholinesterase.	Acetaldehyde	18-30	acetylcholinesterase	Rattus norvegicus	157-177
6998946-1	1980	Mutants of Escherichia coli (adh) in which alcohol dehydrogenase is derepressed under aerobic conditions were also found to overproduce acetaldehyde coenzyme a dehydrogenase.	Acetaldehyde	136-148	Alcohol dehydrogenase	Escherichia coli	43-64
7432008-4	1980	It was shown that the inhibition of ornithine decarboxylase was most likely caused by the ethanol itself because the inhibition was still apparent after treatment with 4-methylpyrazole which so retarded acetaldehyde formation that none was detectable in the wall of the stomach and in the blood and very little in the wall of small intestine.	Acetaldehyde	203-215	ornithine decarboxylase 1	Rattus norvegicus	36-59
6999879-4	1980	From the data obtained on liver enzymes--alcohol dehydrogenase (ADH), aldehyde dehydrogenase (ALDH) and superoxide dismutase (SOD)--it is suggested that the increased ALDH activity would be the consequence of an increased formation of the product of ETOH oxidation, the acetaldehyde.	Acetaldehyde	270-282	Superoxide dismutase 1	Drosophila melanogaster	126-129
6999879-4	1980	From the data obtained on liver enzymes--alcohol dehydrogenase (ADH), aldehyde dehydrogenase (ALDH) and superoxide dismutase (SOD)--it is suggested that the increased ALDH activity would be the consequence of an increased formation of the product of ETOH oxidation, the acetaldehyde.	Acetaldehyde	270-282	Aldehyde dehydrogenase	Drosophila melanogaster	167-171
30822877-4	1980	In the mixed culture, increased acid and acetaldehyde production were noted in milk sample steamed for 30 min.	Acetaldehyde	41-53	Weaning weight-maternal milk	Bos taurus	79-83
391080-1	1979	Two isoenzymes of alcohol dehydrogenase have been purified from human stomach and characterized with regard to electrophoretic mobility and kinetic properties with ethanol, hexanol, and acetaldehyde.	Acetaldehyde	186-198	aldo-keto reductase family 1 member A1	Homo sapiens	18-39
6264495-4	1980	Alcohol dehydrogenase was more stimulated by ethanol than aldehyde dehydrogenase; therefore acetaldehyde may be accumulated.	Acetaldehyde	92-104	aldo-keto reductase family 1 member A1	Rattus norvegicus	0-21
525358-4	1979	In disulfiram-treated rats with a low DBH-activity, a fall in blood pressure was observed at acetaldehyde levels being slightly higher than those found in control rats.	Acetaldehyde	93-105	dopamine beta-hydroxylase	Rattus norvegicus	38-41
525358-7	1979	The results suggest that acetaldehyde is the main determinant of the hypotension elicited by ethanol in rats pretreated with ALDH-inhibitors, and that the role of DBH in the disulfiram-ethanol reaction has been over-estimated in previous studies.	Acetaldehyde	25-37	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	125-129
225142-12	1978	The microbicidal activity of acetaldehyde and xanthine oxidase is increased considerably by MPO and chloride.	Acetaldehyde	29-41	myeloperoxidase	Homo sapiens	92-95
152168-6	1978	Acetaldehyde diminishes myocardial protein synthesis and inhibits Ca++-activated myofibrillar ATPase.	Acetaldehyde	0-12	dynein axonemal heavy chain 8	Homo sapiens	94-100
362901-2	1978	Eighteen alcoholics with various degrees of biopsy-proven liver damage showed increased MIF production in response to acetaldehyde; the mean value of the group differed significantly from 15 healthy controls, 15 subjects with nonalcoholic liver disease, and 15 alcoholics without liver involvement (P less than 0.001, P less than 0.001, P less than 0.02, respectively).	Acetaldehyde	118-130	macrophage migration inhibitory factor	Homo sapiens	88-91
707135-8	1978	The inhibition of ALDH in intoxicated and control rats and its relation to acetaldehyde oxidation and the disulfiram-ethanol reaction are discussed.	Acetaldehyde	75-87	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	18-22
639259-3	1978	The peroxide is reacted with ethanol in the presence of catalase to form acetaldehyde and water, and the acetaldehyde is reduced by NADH in the presence of alcohol dehydrogenase to ethanol.	Acetaldehyde	73-85	catalase	Homo sapiens	56-64
350009-2	1978	The ratio acetaldehyde/ethanol in the alveolar air was measured by gas chromatography and was taken as an index of the aldehyde dehydrogenase (ALDH) activity.	Acetaldehyde	10-22	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	119-141
350009-2	1978	The ratio acetaldehyde/ethanol in the alveolar air was measured by gas chromatography and was taken as an index of the aldehyde dehydrogenase (ALDH) activity.	Acetaldehyde	10-22	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	143-147
22327-2	1977	Simultaneous determination of the rate of appearance of 3H in water from [(1R)-1-3H1] ethanol and the rate of acetaldehyde formation in the presence of rat or ox liver catalase under conditions of steady-state generation of H2O2 allowed calculation of the 3H isotope effect.	Acetaldehyde	110-122	catalase	Rattus norvegicus	168-176
624349-2	1978	Alcohol caused no disturbance under normal conditions but an acetaldehyde level above 40 muM inhibited cell multiplication and elevated SCE considerably.	Acetaldehyde	61-73	latexin	Homo sapiens	89-92
197102-1	1977	Xanthine oxidase, acting on acetaldehyde under aerobic conditions, produces a flux of O2- and H2O2 which attacks artificial liposomes and washed human erythrocytes.	Acetaldehyde	28-40	immunoglobulin kappa variable 1D-39	Homo sapiens	86-98
20305-1	1977	The organic hydroperoxide cumene hydroperoxide is capable of oxidizing ethanol to acetaldehyde in the presence of either catalase, purified cytochrome P-450 or rat liver microsomes.	Acetaldehyde	82-94	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	140-156
913241-3	1977	Kinetic characterization of partially purified liver ALDH revealed similar Km values for either acetaldehyde or propionaldehyde in pregnant and non-pregnant animals.	Acetaldehyde	96-108	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	53-57
913241-5	1977	Induction of liver ALDH was found to significantly decrease blood acetaldehyde concentrations in pregnant mice receiving 2.0 or 3.0 g/kg ethanol when compared to the respective control (non-pregnant) animals.	Acetaldehyde	66-78	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	19-23
913244-3	1977	We found that rats will self-administer acetaldehyde delivered into the cerebral ventricles, and that this operant behaviour can be attenuated by injections of a dopamine-beta-hydroxylase inhibitor.	Acetaldehyde	40-52	dopamine beta-hydroxylase	Rattus norvegicus	162-187
870682-1	1977	The role of various cytosolic aldehyde dehydrogenase (ALDH) isozymes in acetaldehyde metabolism was determined.	Acetaldehyde	72-84	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	54-58
191295-6	1977	Acetaldehyde production from ethanol via the microsomal subfraction can be accounted for by the combined activities of catalase-H2O2 and alcohol dehydrogenase.	Acetaldehyde	0-12	catalase	Homo sapiens	119-127
920487-4	1977	The AcH concentration leaving the liver during the ethanol metabolism was regulated by both the ethanol and AcH oxidation rates, which in turn were regulated by the cytosolic redox state and the ALDH activity, respectively.	Acetaldehyde	4-7	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	195-199
844204-2	1977	Ethanol is converted to acetaldehyde by alcohol dehydrogenase, and the NADH formed transfers its hydrogen through the phenazine methosulphate-p-iodonitrotetrazolium violet (PMS-INT) system to produce the red formazan which is stable and absorbs at 505 nm.	Acetaldehyde	24-36	aldo-keto reductase family 1 member A1	Homo sapiens	40-61
849292-1	1977	Data are provided which indicate that pyruvate and/or acetaldehyde can reverse the inhibition of alanine aminotransferase and aspartate aminotransferase by amino-oxyacetate.	Acetaldehyde	54-66	glutamic--pyruvic transaminase	Homo sapiens	97-121
1151772-10	1975	These results suggest that in the presence of NADPH microsomes oxidize ethanol to acetaldehyde by a process which involves, at least in part, the form I of cytochrome P-450 and in which H2O2 generation by NADPH oxidase is not the rate-limiting step.	Acetaldehyde	82-94	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	156-172
179700-3	1976	Alcohol dehydrogenase from Morris hepatoma 7288ctc, a fast-growing, poorly differentiated tumor, had properties similar to those found with the Becker-H-252 tumor, including a high Km for ethanol and acetaldehyde and the absence of substrate inhibition.	Acetaldehyde	200-212	aldo-keto reductase family 1 member A1	Rattus norvegicus	0-21
196537-0	1976	Studies on the effects of pyrogallol and the structurally related dopa decarboxylase inhibitor RO4-4602 on acetaldehyde metabolism.	Acetaldehyde	107-119	dopa decarboxylase	Homo sapiens	66-84
1009935-6	1976	The results indicate that alcohol dehydrogenase and aldehyde dehydrogenase do not share a common pool of NAD, and that NADH formed during acetaldehyde oxidation is utilized for reductions in the cytosol to a smaller extent than the NADH formed in the alcohol dehydrogenase reaction.	Acetaldehyde	138-150	aldo-keto reductase family 1 member A1	Rattus norvegicus	26-47
1009935-6	1976	The results indicate that alcohol dehydrogenase and aldehyde dehydrogenase do not share a common pool of NAD, and that NADH formed during acetaldehyde oxidation is utilized for reductions in the cytosol to a smaller extent than the NADH formed in the alcohol dehydrogenase reaction.	Acetaldehyde	138-150	aldo-keto reductase family 1 member A1	Rattus norvegicus	251-272
999391-3	1976	Disulfiram, which inhibits both aldehyde dehydrogenase and dopamine-beta-hydroxylase had an intermediate effect in terms of raising blood acetaldehyde levels and in suppressing ethanol intake.	Acetaldehyde	138-150	dopamine beta-hydroxylase	Rattus norvegicus	59-84
145633-3	1976	These same concentrations of acetaldehyde inhibited the Ca2+-dependent myofibrillar ATPase.	Acetaldehyde	29-41	dynein axonemal heavy chain 8	Homo sapiens	84-90
1029022-1	1976	Rapid and progressive inactivation in vitro of both alcohol dehydrogenase and aldehyde dehydrogenase by low concentrations of acetaldehyde or formaldehyde is illustrated.	Acetaldehyde	126-138	aldo-keto reductase family 1 member A1	Homo sapiens	52-73
1200030-3	1975	This identity in population frequencies points to a causative relationship between the two phenomena and suggests that alcohol sensitivity might be due to the increased acetaldehyde formation in individuals carrying the atypical ADH gene.	Acetaldehyde	169-181	aldo-keto reductase family 1 member A1	Homo sapiens	229-232
19999728-2	1973	Glycogen phosphorylase b modified by NaBH4 and aliphatic aldehydes of varying chain length: ranging from acetaldehyde to n-heptanaldehyde were purified by heat-treatment.	Acetaldehyde	105-117	glycogen phosphorylase B	Homo sapiens	0-24
164901-4	1975	Ethanol, acetaldehyde, and isobutyramide bind with appropriate affinities to the Co(II) substituted alcohol dehydrogenases decreasing the number of fast exchanging protons at the catalytic Co(II) site by greater than or equal to 54 percent.	Acetaldehyde	9-21	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	81-87
164901-4	1975	Ethanol, acetaldehyde, and isobutyramide bind with appropriate affinities to the Co(II) substituted alcohol dehydrogenases decreasing the number of fast exchanging protons at the catalytic Co(II) site by greater than or equal to 54 percent.	Acetaldehyde	9-21	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	189-195
1101546-7	1975	The elevation of ADH isozymes has also been demonstrated spectrophotometrically for the first 5 minutes of reaction time, using acetaldehyde as substrate.	Acetaldehyde	128-140	aldo-keto reductase family 1 member A1	Rattus norvegicus	17-20
4359937-7	1974	Further studies with erythrocytes demonstrated that the cellular content of PLP is determined not only by the activities of these PLP-synthesizing enzymes but also by the activity of a phosphate-sensitive, membrane-associated, neutral phosphatase, which hydrolyzes phosphorylated B(6) compounds.Acetaldehyde, but not ethanol, impaired the net formation of PLP from pyridoxal, pyridoxine, and pyridoxine phosphate by erythrocytes.	Acetaldehyde	295-307	pyridoxal phosphatase	Homo sapiens	76-79
32480415-8	2021	Interestingly, patients with mutated allele rs1229984 in ADH1B had lower level of signature J while mutated allele rs671 in ALDH2 exhibited higher signature J abundance, suggesting acetaldehyde is one cause of signature J. Intriguingly, somatic mutations of three potential cancer driver genes (TP53, CUL3 and NSD1) were found the critical contributors for increased mutational load of signature J in alcohol consumption patients.	Acetaldehyde	181-193	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	57-62
33714857-9	2021	Although the use of FALDH resulted in the increase in the sensor output from aldehydes, such as acetaldehyde and formaldehyde, considering their concentrations in body fluids, the influence on the sensor output is limited.	Acetaldehyde	96-108	alcohol dehydrogenase 5 (class III), chi polypeptide	Homo sapiens	20-25
34033815-7	2021	We found that blockade or silencing of CD39 prevented acetaldehyde-induced proliferation of HSC-T6 cells and the expression of fibrogenic factors.	Acetaldehyde	54-66	ectonucleoside triphosphate diphosphohydrolase 1	Mus musculus	39-43
32480415-8	2021	Interestingly, patients with mutated allele rs1229984 in ADH1B had lower level of signature J while mutated allele rs671 in ALDH2 exhibited higher signature J abundance, suggesting acetaldehyde is one cause of signature J. Intriguingly, somatic mutations of three potential cancer driver genes (TP53, CUL3 and NSD1) were found the critical contributors for increased mutational load of signature J in alcohol consumption patients.	Acetaldehyde	181-193	aldehyde dehydrogenase 2 family member	Homo sapiens	124-129
32480415-8	2021	Interestingly, patients with mutated allele rs1229984 in ADH1B had lower level of signature J while mutated allele rs671 in ALDH2 exhibited higher signature J abundance, suggesting acetaldehyde is one cause of signature J. Intriguingly, somatic mutations of three potential cancer driver genes (TP53, CUL3 and NSD1) were found the critical contributors for increased mutational load of signature J in alcohol consumption patients.	Acetaldehyde	181-193	tumor protein p53	Homo sapiens	295-299
32480415-8	2021	Interestingly, patients with mutated allele rs1229984 in ADH1B had lower level of signature J while mutated allele rs671 in ALDH2 exhibited higher signature J abundance, suggesting acetaldehyde is one cause of signature J. Intriguingly, somatic mutations of three potential cancer driver genes (TP53, CUL3 and NSD1) were found the critical contributors for increased mutational load of signature J in alcohol consumption patients.	Acetaldehyde	181-193	cullin 3	Homo sapiens	301-305
32480415-8	2021	Interestingly, patients with mutated allele rs1229984 in ADH1B had lower level of signature J while mutated allele rs671 in ALDH2 exhibited higher signature J abundance, suggesting acetaldehyde is one cause of signature J. Intriguingly, somatic mutations of three potential cancer driver genes (TP53, CUL3 and NSD1) were found the critical contributors for increased mutational load of signature J in alcohol consumption patients.	Acetaldehyde	181-193	nuclear receptor binding SET domain protein 1	Homo sapiens	310-314
34010294-2	2021	The acetaldehyde breath test (ABT) may demonstrate ALDH2 gene polymorphisms.	Acetaldehyde	4-16	aldehyde dehydrogenase 2 family member	Homo sapiens	51-56
33740503-2	2021	Acetaldehyde dehydrogenase 2 (ALDH2) is primarily responsible for detoxifying ethanol-derived acetaldehyde and endogenous lipid aldehydes derived from lipid peroxidation.	Acetaldehyde	94-106	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	0-28
33858805-0	2021	Expression of p53 is associated with microbial acetaldehyde production in oralsquamous cell carcinoma.	Acetaldehyde	47-59	tumor protein p53	Homo sapiens	14-17
33858805-1	2021	OBJECTIVES: The objective of this study was to investigate the association between p53 expression and microbial acetaldehyde production in patients with oral squamous cell carcinoma (OSCC).	Acetaldehyde	112-124	tumor protein p53	Homo sapiens	83-86
33858805-6	2021	A significant positive correlation between microbial acetaldehyde production and p53 expression levels in OSCC samples was seen in the intermediate and superficial layers of the epithelium of the infiltrative zone (P = .0005 and P = .0004, respectively) and in the superficial layer of the healthy appearing mucosa next to the tumor (P = .0391).	Acetaldehyde	53-65	tumor protein p53	Homo sapiens	81-84
33858805-8	2021	CONCLUSIONS: Our results show an association between microbial acetaldehyde production and immunostaining of p53 in OSCC samples.	Acetaldehyde	63-75	tumor protein p53	Homo sapiens	109-112
33744437-2	2021	This drug works by blocking the second step of ethanol metabolism by inhibiting aldehyde dehydrogenase-2 (ALDH2), the enzyme responsible for acetaldehyde oxidation into acetic acid.	Acetaldehyde	141-153	aldehyde dehydrogenase 2 family member	Homo sapiens	80-104
33744437-2	2021	This drug works by blocking the second step of ethanol metabolism by inhibiting aldehyde dehydrogenase-2 (ALDH2), the enzyme responsible for acetaldehyde oxidation into acetic acid.	Acetaldehyde	141-153	aldehyde dehydrogenase 2 family member	Homo sapiens	106-111
33690904-7	2021	An oxidative stress and ER stress as measured by GRP78, unspliced XBP1, p-eIF2alpha, and CHOP along with activation of p-JNK1/2, p-ERK1/2, and p-P38MAPK were found in cells treated with EtOH, acetaldehyde or FAEEs were increased concentration dependently.	Acetaldehyde	192-204	mitogen-activated protein kinase 8	Homo sapiens	121-127
33740503-2	2021	Acetaldehyde dehydrogenase 2 (ALDH2) is primarily responsible for detoxifying ethanol-derived acetaldehyde and endogenous lipid aldehydes derived from lipid peroxidation.	Acetaldehyde	94-106	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	30-35
34056354-1	2021	Mitochondrial aldehyde dehydrogenase 2 (ALDH2) is predominantly linked with acetaldehyde detoxification in the second stage of alcohol metabolism.	Acetaldehyde	76-88	aldehyde dehydrogenase 2 family member	Homo sapiens	40-45
34056355-0	2021	New Plausible Mechanism for Gastric and Colorectal Carcinogenesis: Free Radical-Mediated Acetaldehyde Generation in a Heme/Myoglobin-Linoleate-Ethanol Mixture.	Acetaldehyde	89-101	myoglobin	Homo sapiens	123-132
34056355-2	2021	A survey of the mutation spectra of the p53 tumor suppressor gene in these cancers suggested that the types of mutations and the hot spots are similar to those induced by acetaldehyde (AcAld) in an in vitro p53 mutation analysis system.	Acetaldehyde	171-183	tumor protein p53	Homo sapiens	40-43
34056355-2	2021	A survey of the mutation spectra of the p53 tumor suppressor gene in these cancers suggested that the types of mutations and the hot spots are similar to those induced by acetaldehyde (AcAld) in an in vitro p53 mutation analysis system.	Acetaldehyde	171-183	tumor protein p53	Homo sapiens	207-210
33181285-0	2021	Antrodia camphorata extract (ACE)-induced apoptosis is associated with BMP4 expression and p53-dependent ROS generation in human colon cancer cells.	Acetaldehyde	29-32	bone morphogenetic protein 4	Homo sapiens	71-75
31646946-1	2021	Aldehyde dehydrogenase 1A1 (ALDH1A1) is a cytosolic enzyme that mainly catalyzes the oxidation of acetaldehyde into acetic acid and participates in the regulation of differentiation and gene expression in fat cell growth and development.	Acetaldehyde	98-110	aldehyde dehydrogenase 1 family member A1	Bos taurus	0-26
31646946-1	2021	Aldehyde dehydrogenase 1A1 (ALDH1A1) is a cytosolic enzyme that mainly catalyzes the oxidation of acetaldehyde into acetic acid and participates in the regulation of differentiation and gene expression in fat cell growth and development.	Acetaldehyde	98-110	aldehyde dehydrogenase 1 family member A1	Bos taurus	28-35
33592568-2	2021	When individuals with the ALDH2 mutation consume alcohol, accumulating acetaldehyde in the blood can cause reddened face, headache, nausea, and palpitations; symptoms referred to as Alcohol Flushing Reaction.	Acetaldehyde	71-83	aldehyde dehydrogenase 2 family member	Homo sapiens	26-31
33181285-0	2021	Antrodia camphorata extract (ACE)-induced apoptosis is associated with BMP4 expression and p53-dependent ROS generation in human colon cancer cells.	Acetaldehyde	29-32	tumor protein p53	Homo sapiens	91-94
33388347-5	2021	Sulforaphane treatment induced the activity of acetaldehyde-metabolizing mitochondrial aldehyde dehydrogenase (ALDH2) in HepaRG cells and suppressed the acetaldehyde-induced proliferation and profibrogenic activity in LX-2 cells with upregulation of Nrf2-regulated antioxidant genes, including HMOX1, NQO1, and GSTM3.	Acetaldehyde	47-59	aldehyde dehydrogenase 2 family member	Homo sapiens	111-116
33752472-7	2022	In both samples, the changes in organic acids and volatile flavor components were not significant during frozen storage, except acetic, citric and oxalic acids and acetaldehyde in GK sample.	Acetaldehyde	164-176	glycerol kinase	Bos taurus	180-182
33750341-9	2021	CONCLUSION: In Eastern Asians, ALDH2 rs671 polymorphisms are associated with esophageal cancer, which may be linked to acetaldehyde accumulation.	Acetaldehyde	119-131	aldehyde dehydrogenase 2 family member	Homo sapiens	31-36
33892361-1	2021	cis-2-Methyl-4-propyl-1,3-oxathiane (cis-2-MPO), arising from 3-sulfanylhexan-1-ol (3-SH) and acetaldehyde, was recently identified in wine, but the enantiomeric distribution was unknown.	Acetaldehyde	94-106	suppressor of cytokine signaling 2	Homo sapiens	0-5
33892361-1	2021	cis-2-Methyl-4-propyl-1,3-oxathiane (cis-2-MPO), arising from 3-sulfanylhexan-1-ol (3-SH) and acetaldehyde, was recently identified in wine, but the enantiomeric distribution was unknown.	Acetaldehyde	94-106	suppressor of cytokine signaling 2	Homo sapiens	37-42
33892361-1	2021	cis-2-Methyl-4-propyl-1,3-oxathiane (cis-2-MPO), arising from 3-sulfanylhexan-1-ol (3-SH) and acetaldehyde, was recently identified in wine, but the enantiomeric distribution was unknown.	Acetaldehyde	94-106	myeloperoxidase	Homo sapiens	43-46
33892361-6	2021	Additionally, cis-2,4,4,6-tetramethyl-1,3-oxathiane, constituted from acetaldehyde and 4-methyl-4-sulfanylpentan-2-ol (4-MSPOH), was identified in wine for the first time.	Acetaldehyde	70-82	suppressor of cytokine signaling 2	Homo sapiens	14-19
33388347-5	2021	Sulforaphane treatment induced the activity of acetaldehyde-metabolizing mitochondrial aldehyde dehydrogenase (ALDH2) in HepaRG cells and suppressed the acetaldehyde-induced proliferation and profibrogenic activity in LX-2 cells with upregulation of Nrf2-regulated antioxidant genes, including HMOX1, NQO1, and GSTM3.	Acetaldehyde	47-59	NFE2 like bZIP transcription factor 2	Homo sapiens	250-254
33388347-5	2021	Sulforaphane treatment induced the activity of acetaldehyde-metabolizing mitochondrial aldehyde dehydrogenase (ALDH2) in HepaRG cells and suppressed the acetaldehyde-induced proliferation and profibrogenic activity in LX-2 cells with upregulation of Nrf2-regulated antioxidant genes, including HMOX1, NQO1, and GSTM3.	Acetaldehyde	47-59	heme oxygenase 1	Homo sapiens	294-299
33388347-5	2021	Sulforaphane treatment induced the activity of acetaldehyde-metabolizing mitochondrial aldehyde dehydrogenase (ALDH2) in HepaRG cells and suppressed the acetaldehyde-induced proliferation and profibrogenic activity in LX-2 cells with upregulation of Nrf2-regulated antioxidant genes, including HMOX1, NQO1, and GSTM3.	Acetaldehyde	47-59	NAD(P)H quinone dehydrogenase 1	Homo sapiens	301-305
33388347-5	2021	Sulforaphane treatment induced the activity of acetaldehyde-metabolizing mitochondrial aldehyde dehydrogenase (ALDH2) in HepaRG cells and suppressed the acetaldehyde-induced proliferation and profibrogenic activity in LX-2 cells with upregulation of Nrf2-regulated antioxidant genes, including HMOX1, NQO1, and GSTM3.	Acetaldehyde	47-59	glutathione S-transferase mu 3	Homo sapiens	311-316
33544749-0	2021	Dietary iso-alpha-acids prevent acetaldehyde-induced liver injury through Nrf2-mediated gene expression.	Acetaldehyde	32-44	nuclear factor, erythroid derived 2, like 2	Mus musculus	74-78
32991036-4	2021	A decarboxylative Claisen condensation of the malonyl-CoA and acetaldehyde ensues in the presence of acyltransferases to form 3-hydroxybutyryl-CoA that is subsequently reduced by aldehyde reductase to obtain 1,3-butanediol (1,3-BDO).	Acetaldehyde	62-74	aldo-keto reductase family 1 member A1	Homo sapiens	179-197
33544749-7	2021	The acetaldehyde-induced increases in serum aspartate aminotransferase (AST) and alanine aminotransferase (ALT) levels were suppressed by iso-alpha-acids intake.	Acetaldehyde	4-16	solute carrier family 17 (anion/sugar transporter), member 5	Mus musculus	44-70
33544749-7	2021	The acetaldehyde-induced increases in serum aspartate aminotransferase (AST) and alanine aminotransferase (ALT) levels were suppressed by iso-alpha-acids intake.	Acetaldehyde	4-16	solute carrier family 17 (anion/sugar transporter), member 5	Mus musculus	72-75
33544749-7	2021	The acetaldehyde-induced increases in serum aspartate aminotransferase (AST) and alanine aminotransferase (ALT) levels were suppressed by iso-alpha-acids intake.	Acetaldehyde	4-16	glutamic pyruvic transaminase, soluble	Mus musculus	81-105
33544749-7	2021	The acetaldehyde-induced increases in serum aspartate aminotransferase (AST) and alanine aminotransferase (ALT) levels were suppressed by iso-alpha-acids intake.	Acetaldehyde	4-16	glutamic pyruvic transaminase, soluble	Mus musculus	107-110
33544749-10	2021	These results suggest that iso-alpha-acid intake prevents acetaldehyde-induced liver injury by reducing oxidative stress via Nrf2-mediated gene expression.	Acetaldehyde	58-70	nuclear factor, erythroid derived 2, like 2	Mus musculus	125-129
33188956-7	2021	We show that expression of the atrogenes Atrogin1 and MuRF1 significantly increased in myogenic cells following acetaldehyde treatment, an outcome significantly inhibited in vitro by Trolox C, an anti-oxidant.	Acetaldehyde	112-124	F-box protein 32	Mus musculus	41-49
33382614-5	2021	The subsequent application of AcH to label RNase A without and with ligands has assisted to assign lysines involved in ligand-RNase A binding by detecting the time-dependent changes in accessibility profiles.	Acetaldehyde	30-33	ribonuclease A family member 1, pancreatic	Homo sapiens	43-50
33382614-5	2021	The subsequent application of AcH to label RNase A without and with ligands has assisted to assign lysines involved in ligand-RNase A binding by detecting the time-dependent changes in accessibility profiles.	Acetaldehyde	30-33	ribonuclease A family member 1, pancreatic	Homo sapiens	126-133
33604575-6	2021	Pretreating hepatocytes with an alcohol dehydrogenase inhibitor suppressed the effects of ethanol on hormone-induced Ca2+ increases, whereas inhibiting aldehyde dehydrogenase potentiated the inhibitory actions of ethanol, suggesting that acetaldehyde is the underlying mediator.	Acetaldehyde	238-250	aldo-keto reductase family 1 member A1	Rattus norvegicus	32-53
33121948-10	2021	Mechanistically, Wnt/beta-catenin pathway was activated in acetaldehyde-activated HSC-T6 cells and CD73 silencing or overexpression could regulate Wnt/beta-catenin signaling pathway.	Acetaldehyde	59-71	catenin beta 1	Rattus norvegicus	21-33
33492922-1	2021	In this work, SnS-SnS2 heterostructured upright nanosheet frameworks are constructed on FTO substrates, which demonstrate promising photocatalytic performances for the conversion of CO2 and water to C2 (acetaldehyde) and C3 (acetone) hydrocarbons without H2 formation.	Acetaldehyde	203-215	sodium voltage-gated channel alpha subunit 11	Homo sapiens	18-22
33283290-1	2021	BACKGROUND: Aldehyde dehydrogenase-2 (ALDH2) plays an important role in the alcohol detoxification and acetaldehyde metabolism.	Acetaldehyde	103-115	aldehyde dehydrogenase 2 family member	Homo sapiens	12-36
33283290-1	2021	BACKGROUND: Aldehyde dehydrogenase-2 (ALDH2) plays an important role in the alcohol detoxification and acetaldehyde metabolism.	Acetaldehyde	103-115	aldehyde dehydrogenase 2 family member	Homo sapiens	38-43
33137447-7	2021	Surprisingly, silibinin significantly increased the cell viability and reduced the leakage of alanine amino transferase (ALT) and aspartate amino transferase (AST) in acetaldehyde-treated hepatocytes, suggesting that silibinin protected cell injury caused by acetaldehyde treatment.	Acetaldehyde	167-179	glutamic pyruvic transaminase, soluble	Mus musculus	94-119
33137447-7	2021	Surprisingly, silibinin significantly increased the cell viability and reduced the leakage of alanine amino transferase (ALT) and aspartate amino transferase (AST) in acetaldehyde-treated hepatocytes, suggesting that silibinin protected cell injury caused by acetaldehyde treatment.	Acetaldehyde	167-179	glutamic pyruvic transaminase, soluble	Mus musculus	121-124
33137447-7	2021	Surprisingly, silibinin significantly increased the cell viability and reduced the leakage of alanine amino transferase (ALT) and aspartate amino transferase (AST) in acetaldehyde-treated hepatocytes, suggesting that silibinin protected cell injury caused by acetaldehyde treatment.	Acetaldehyde	167-179	solute carrier family 17 (anion/sugar transporter), member 5	Mus musculus	159-162
33137447-8	2021	The apoptosis-inducing effect of acetaldehyde was demonstrated by the increased number of cells in sub-G1 phase as well as caspase-3 activation.	Acetaldehyde	33-45	caspase 3	Mus musculus	123-132
33121948-5	2021	In this study, both ethanol plus CCl4-induced liver fibrosis mice model and acetaldehyde-activated HSC-T6 cell model were employed and the expression of CD73 was consistently elevated in vivo and in vitro.	Acetaldehyde	76-88	5' nucleotidase, ecto	Rattus norvegicus	153-157
33121948-10	2021	Mechanistically, Wnt/beta-catenin pathway was activated in acetaldehyde-activated HSC-T6 cells and CD73 silencing or overexpression could regulate Wnt/beta-catenin signaling pathway.	Acetaldehyde	59-71	catenin beta 1	Rattus norvegicus	151-163
33188956-7	2021	We show that expression of the atrogenes Atrogin1 and MuRF1 significantly increased in myogenic cells following acetaldehyde treatment, an outcome significantly inhibited in vitro by Trolox C, an anti-oxidant.	Acetaldehyde	112-124	tripartite motif-containing 63	Mus musculus	54-59
33352912-5	2020	Western blot analyses revealed that EPQ treatment increased protein levels of ROS-scavenging heme oxygenase-1 and superoxide dismutase, as well as the levels of aldehyde dehydrogenase (ALDH) 1, ALDH2, and ALDH3, under acetaldehyde-induced cellular stress.	Acetaldehyde	218-230	aldehyde dehydrogenase 2 family member	Rattus norvegicus	161-192
33219537-19	2021	cepa extract (ACE) alleviated hyperlipidemia with downregulation of HMGCR and upregulation of LDLR, suggesting that ACE might be a potential option for hyperlipidemia as non-statin lipid-lowering agent.	Acetaldehyde	14-17	3-hydroxy-3-methylglutaryl-CoA reductase	Rattus norvegicus	68-73
33219537-19	2021	cepa extract (ACE) alleviated hyperlipidemia with downregulation of HMGCR and upregulation of LDLR, suggesting that ACE might be a potential option for hyperlipidemia as non-statin lipid-lowering agent.	Acetaldehyde	14-17	low density lipoprotein receptor	Rattus norvegicus	94-98
33208242-2	2021	Alcohol is metabolized into genotoxic acetaldehyde in hepatocytes, which is catalyzed by aldehyde dehydrogenase 2 (ALDH2).	Acetaldehyde	38-50	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	89-113
33208242-2	2021	Alcohol is metabolized into genotoxic acetaldehyde in hepatocytes, which is catalyzed by aldehyde dehydrogenase 2 (ALDH2).	Acetaldehyde	38-50	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	115-120
33208242-6	2021	Besides, we believe that knockout of ALDH2 will help to shorten the time course of transformation, as ALDH2 deficiency will significantly increase the accumulation of acetaldehyde in hepatocytes.	Acetaldehyde	167-179	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	37-42
33208242-6	2021	Besides, we believe that knockout of ALDH2 will help to shorten the time course of transformation, as ALDH2 deficiency will significantly increase the accumulation of acetaldehyde in hepatocytes.	Acetaldehyde	167-179	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	102-107
33352912-0	2020	Ent-Peniciherqueinone Suppresses Acetaldehyde-Induced Cytotoxicity and Oxidative Stress by Inducing ALDH and Suppressing MAPK Signaling.	Acetaldehyde	33-45	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	100-104
33352912-6	2020	Finally, EPQ reduced acetaldehyde-induced phosphorylation of p38 and c-Jun N-terminal kinase, which are associated with ROS-induced oxidative stress.	Acetaldehyde	21-33	mitogen activated protein kinase 14	Rattus norvegicus	61-64
32603918-6	2020	Myosin light chain (MYL1 and MYL3) showed high oxidative susceptibility owing to peptidyl methionine and proline oxidation as well as acetaldehyde adduct formation on lysine or histidine residues.	Acetaldehyde	134-146	myosin light chain 1	Homo sapiens	20-24
32603918-6	2020	Myosin light chain (MYL1 and MYL3) showed high oxidative susceptibility owing to peptidyl methionine and proline oxidation as well as acetaldehyde adduct formation on lysine or histidine residues.	Acetaldehyde	134-146	myosin light chain 3	Homo sapiens	29-33
32896553-3	2020	Aldehyde dehydrogenase (ALDH) is the rate-limiting enzyme in clearing acetaldehyde from the body.	Acetaldehyde	70-82	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	0-22
33206981-0	2021	Abnormally High Blood Acetaldehyde Concentrations Suggest a Potential of Post-Mortem Ethanol Generation.	Acetaldehyde	22-34	solute carrier family 35 member G1	Homo sapiens	73-77
32896553-3	2020	Aldehyde dehydrogenase (ALDH) is the rate-limiting enzyme in clearing acetaldehyde from the body.	Acetaldehyde	70-82	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	24-28
32896553-4	2020	The clinical relevance of ALDH in skeletal function has been established by the discovery of single nucleotide polymorphism, SNP (rs671) in the ALDH2 gene giving rise to an inactive form of the enzyme (ALDH2*2) that causes increased serum acetaldehyde and osteoporosis in the affected individuals.	Acetaldehyde	239-251	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	26-30
32896553-4	2020	The clinical relevance of ALDH in skeletal function has been established by the discovery of single nucleotide polymorphism, SNP (rs671) in the ALDH2 gene giving rise to an inactive form of the enzyme (ALDH2*2) that causes increased serum acetaldehyde and osteoporosis in the affected individuals.	Acetaldehyde	239-251	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	144-149
32896553-14	2020	This review will critically discuss the molecular mechanism of the ethanol and its principal metabolite, acetaldehyde in the context of ALDH2 in bone cells, and skeletal homeostasis.	Acetaldehyde	105-117	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	136-141
32738395-2	2020	Alcohol is metabolized to the toxic metabolite, acetaldehyde by alcohol dehydrogenase or CYP2E1 in the hepatic tissue, and also induces reactive oxygen species (ROS), which together play a pivotal role in cell and tissue damage.	Acetaldehyde	48-60	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	89-95
33036195-10	2020	However, acetic acid and acetaldehyde production decrease when TSA1 is absent.	Acetaldehyde	25-37	thioredoxin peroxidase TSA1	Saccharomyces cerevisiae S288C	63-67
32980528-3	2020	Alcohol dehydrogenase (ADH, EC 1.1.1.1) converts alcohol into a known carcinogenic metabolite, acetaldehyde and while ADH levels in oral mucosa are low, several oral commensal species possess ADH and could produce genotoxic levels of acetaldehyde.	Acetaldehyde	95-107	aldo-keto reductase family 1 member A1	Homo sapiens	0-21
32980528-3	2020	Alcohol dehydrogenase (ADH, EC 1.1.1.1) converts alcohol into a known carcinogenic metabolite, acetaldehyde and while ADH levels in oral mucosa are low, several oral commensal species possess ADH and could produce genotoxic levels of acetaldehyde.	Acetaldehyde	95-107	aldo-keto reductase family 1 member A1	Homo sapiens	23-26
32980528-3	2020	Alcohol dehydrogenase (ADH, EC 1.1.1.1) converts alcohol into a known carcinogenic metabolite, acetaldehyde and while ADH levels in oral mucosa are low, several oral commensal species possess ADH and could produce genotoxic levels of acetaldehyde.	Acetaldehyde	234-246	aldo-keto reductase family 1 member A1	Homo sapiens	0-21
32980528-3	2020	Alcohol dehydrogenase (ADH, EC 1.1.1.1) converts alcohol into a known carcinogenic metabolite, acetaldehyde and while ADH levels in oral mucosa are low, several oral commensal species possess ADH and could produce genotoxic levels of acetaldehyde.	Acetaldehyde	234-246	aldo-keto reductase family 1 member A1	Homo sapiens	23-26
32960060-2	2020	In this work, in situ ATR-SEIRAS technique incorporating a micro-machined Si wafer window, p-polarized infrared radiation and isotope labelling is extended to revisit acetaldehyde oxidation reaction (AOR) on Pt electrode in acidic media.	Acetaldehyde	167-179	ATR serine/threonine kinase	Homo sapiens	22-25
32325250-1	2020	Aldehyde dehydrogenase 2 (ALDH2) is the enzyme that oxidizes the acetaldehyde produced by alcohol metabolism.	Acetaldehyde	65-77	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	0-24
32338108-5	2020	UDPGT).The intestinal microbiome plays a significant role in the ethanol biotransformation and in the initiation and progression of liver diseases stimulated by ethanol and its metabolite - acetaldehyde, or by lipopolysaccharide and ROS.	Acetaldehyde	190-202	UDP glucuronosyltransferase family 1 member A4	Homo sapiens	0-5
32687612-2	2020	During the elimination of alcohol, ALDH2 metabolizes acetaldehyde to acetate; inhibiting this enzyme can lead to aversive reactions due to the accumulation of acetaldehyde.	Acetaldehyde	53-65	aldehyde dehydrogenase 2 family member	Homo sapiens	35-40
32687612-2	2020	During the elimination of alcohol, ALDH2 metabolizes acetaldehyde to acetate; inhibiting this enzyme can lead to aversive reactions due to the accumulation of acetaldehyde.	Acetaldehyde	159-171	aldehyde dehydrogenase 2 family member	Homo sapiens	35-40
32556414-3	2020	Especially, the highest enzyme activity towards acetaldehyde by Bdh2p(Y) was 117.95 U/mg with cofactor nicotinamide adenine dinucleotide reduced (NADH).	Acetaldehyde	48-60	putative dehydrogenase BDH2	Saccharomyces cerevisiae S288C	64-69
32718916-0	2020	Correction to "MicroRNA hsa-miR-1301-3p Regulates Human ADH6, ALDH5A1 and ALDH8A1 in the Ethanol-Acetaldehyde-Acetate Metabolic Pathway".	Acetaldehyde	97-109	alcohol dehydrogenase 6 (class V)	Homo sapiens	56-60
32718916-0	2020	Correction to "MicroRNA hsa-miR-1301-3p Regulates Human ADH6, ALDH5A1 and ALDH8A1 in the Ethanol-Acetaldehyde-Acetate Metabolic Pathway".	Acetaldehyde	97-109	aldehyde dehydrogenase 5 family member A1	Homo sapiens	62-69
32718916-0	2020	Correction to "MicroRNA hsa-miR-1301-3p Regulates Human ADH6, ALDH5A1 and ALDH8A1 in the Ethanol-Acetaldehyde-Acetate Metabolic Pathway".	Acetaldehyde	97-109	aldehyde dehydrogenase 8 family member A1	Homo sapiens	74-81
32821333-6	2020	Here, we review how chronic alcohol use results in oxidative stress through increased metabolism via the cytochrome P450 2E1 system producing reactive oxygen species, acetaldehyde and protein and DNA adducts.	Acetaldehyde	167-179	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	105-124
31204364-3	2020	It is well known that the inactive ALDH2 carriers, specific to East Asian populations, have an increased risk of several cancer types because of increased exposure to acetaldehyde after alcohol consumption.	Acetaldehyde	167-179	aldehyde dehydrogenase 2 family member	Homo sapiens	35-40
32755306-7	2020	Thus, we observed an activation of the IRE1alpha-XBP1 and ATF6alpha, but not pPERK-peIF2alpha-ATF4-CHOP arms of ER-stress in HBV-transfected cells treated with acetaldehyde-generating system (AGS).	Acetaldehyde	160-172	endoplasmic reticulum to nucleus signaling 1	Homo sapiens	39-48
32755306-7	2020	Thus, we observed an activation of the IRE1alpha-XBP1 and ATF6alpha, but not pPERK-peIF2alpha-ATF4-CHOP arms of ER-stress in HBV-transfected cells treated with acetaldehyde-generating system (AGS).	Acetaldehyde	160-172	activating transcription factor 6	Homo sapiens	58-67
32681823-1	2020	Mitochondrial aldehyde dehydrogenase 2 (ALDH2), which is a homotetramer assembled by two equivalent dimers, is an important enzyme that metabolizes ethanol-derived acetaldehyde to acetate in a coenzyme-dependent manner.	Acetaldehyde	164-176	aldehyde dehydrogenase 2 family member	Homo sapiens	40-45
32681823-2	2020	The highly reactive acetaldehyde exhibits a toxic effect, indicating that the proper functioning of ALDH2 is essential to counteract aldehyde-associated diseases.	Acetaldehyde	20-32	aldehyde dehydrogenase 2 family member	Homo sapiens	100-105
32499331-0	2020	MicroRNA hsa-miR-1301-3p Regulates Human ADH6, ALDH5A1 and ALDH8A1 in the Ethanol-Acetaldehyde-Acetate Metabolic Pathway.	Acetaldehyde	82-94	alcohol dehydrogenase 6 (class V)	Homo sapiens	41-45
32499331-0	2020	MicroRNA hsa-miR-1301-3p Regulates Human ADH6, ALDH5A1 and ALDH8A1 in the Ethanol-Acetaldehyde-Acetate Metabolic Pathway.	Acetaldehyde	82-94	aldehyde dehydrogenase 5 family member A1	Homo sapiens	47-54
32499331-0	2020	MicroRNA hsa-miR-1301-3p Regulates Human ADH6, ALDH5A1 and ALDH8A1 in the Ethanol-Acetaldehyde-Acetate Metabolic Pathway.	Acetaldehyde	82-94	aldehyde dehydrogenase 8 family member A1	Homo sapiens	59-66
32850324-3	2020	We compared patient BM, LUAD, and para-LUAD tissues using proteomic analysis and identified aldehyde dehydrogenase 2 (ALDH2), which can detoxify acetaldehyde to acetic acid, as one of the key regulators in lung tumor metastasis.	Acetaldehyde	145-157	aldehyde dehydrogenase 2 family member	Homo sapiens	92-116
32850324-3	2020	We compared patient BM, LUAD, and para-LUAD tissues using proteomic analysis and identified aldehyde dehydrogenase 2 (ALDH2), which can detoxify acetaldehyde to acetic acid, as one of the key regulators in lung tumor metastasis.	Acetaldehyde	145-157	aldehyde dehydrogenase 2 family member	Homo sapiens	118-123
31018006-11	2020	The increases in ADH1 contribute to explaining the remarkable effect of fenofibrate in raising blood levels of acetaldehyde in ethanol-consuming animals, in which a marked reduction of alcohol intake is recorded.	Acetaldehyde	111-123	alcohol dehydrogenase 1C (class I), gamma polypeptide	Rattus norvegicus	17-21
32325250-1	2020	Aldehyde dehydrogenase 2 (ALDH2) is the enzyme that oxidizes the acetaldehyde produced by alcohol metabolism.	Acetaldehyde	65-77	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	26-31
32576773-5	2020	A dose of 500 mM EtOH induced a greater decrease in Aldh2-KO mice (P < 0.05) than in WT mice, indicating the action of AcH.	Acetaldehyde	119-122	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	52-57
32059264-2	2020	Our previous study showed that ETBE-induced toxicity in aldehyde dehydrogenase 2 (Aldh2) gene knockout (KO) mice was caused by its primary metabolite acetaldehyde, which was toxic.	Acetaldehyde	150-162	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	56-80
32059264-2	2020	Our previous study showed that ETBE-induced toxicity in aldehyde dehydrogenase 2 (Aldh2) gene knockout (KO) mice was caused by its primary metabolite acetaldehyde, which was toxic.	Acetaldehyde	150-162	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	82-87
32132394-8	2020	The Scn11a mice showed increased sensitivity to mechanical, heat and cold stimuli, and hypersensitivity to acetaldehyde and formalin, which could account for the alcohol intake-induced pain phenotype in patients.	Acetaldehyde	107-119	sodium channel, voltage-gated, type XI, alpha	Mus musculus	4-10
32132394-9	2020	Moreover, acetaldehyde increased the mutant mNav1.9 channel current and excitability of Scn11a mouse DRG neurons.	Acetaldehyde	10-22	sodium channel, voltage-gated, type XI, alpha	Mus musculus	44-51
32132394-9	2020	Moreover, acetaldehyde increased the mutant mNav1.9 channel current and excitability of Scn11a mouse DRG neurons.	Acetaldehyde	10-22	sodium channel, voltage-gated, type XI, alpha	Mus musculus	88-94
32576773-6	2020	Similarly, perfusion of 200 and 500 microM AcH decreased glutamate in the frontal cortex of Aldh2-KO mice (P < 0.05), but this decrease was not seen in WT mice at any AcH dose, due to the subsequent oxidation of AcH by mitochondrial aldehyde dehydrogenase 2.	Acetaldehyde	43-46	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	92-97
32369366-4	2020	The results show that two primary ozonides (syn- and anti-POZ) can be formed in the ozonolysis of VA and that FA coupled with the simplest Criegee intermediate (CH2OO) can be produced as the main nascent products.	Acetaldehyde	98-100	synemin	Homo sapiens	44-47
32151565-10	2020	These results suggested that 6-MSITC is possible to protect acetaldehyde toxicity in hepatocytes by induction of mitochondrial ALDH2 expression through Nrf2/ARE pathway.	Acetaldehyde	60-72	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	127-132
32775346-5	2020	Summary: The strongest evidence for the local carcinogenicity of ACH in man provides a point mutation in the aldehyde dehydrogenase 2 (ALDH2) gene, which has randomized millions of alcohol consumers to markedly increased ACH exposure via saliva.	Acetaldehyde	221-224	aldehyde dehydrogenase 2 family member	Homo sapiens	109-133
32775346-5	2020	Summary: The strongest evidence for the local carcinogenicity of ACH in man provides a point mutation in the aldehyde dehydrogenase 2 (ALDH2) gene, which has randomized millions of alcohol consumers to markedly increased ACH exposure via saliva.	Acetaldehyde	221-224	aldehyde dehydrogenase 2 family member	Homo sapiens	135-140
32775346-13	2020	In ALDH2-deficient subjects excess ACH during the long-term ACH exposure phase is most probably derived from salivary glands.	Acetaldehyde	35-38	aldehyde dehydrogenase 2 family member	Homo sapiens	3-8
32775346-13	2020	In ALDH2-deficient subjects excess ACH during the long-term ACH exposure phase is most probably derived from salivary glands.	Acetaldehyde	60-63	aldehyde dehydrogenase 2 family member	Homo sapiens	3-8
32775346-14	2020	Key Message: ALDH2 gene mutation proves the causal relationship between local ACH exposure via saliva and oropharyngeal cancer and provides new means for the quantitative assessment of local ACH exposure in relation to oropharyngeal cancer risk.	Acetaldehyde	78-81	aldehyde dehydrogenase 2 family member	Homo sapiens	13-18
32775346-14	2020	Key Message: ALDH2 gene mutation proves the causal relationship between local ACH exposure via saliva and oropharyngeal cancer and provides new means for the quantitative assessment of local ACH exposure in relation to oropharyngeal cancer risk.	Acetaldehyde	191-194	aldehyde dehydrogenase 2 family member	Homo sapiens	13-18
32775346-5	2020	Summary: The strongest evidence for the local carcinogenicity of ACH in man provides a point mutation in the aldehyde dehydrogenase 2 (ALDH2) gene, which has randomized millions of alcohol consumers to markedly increased ACH exposure via saliva.	Acetaldehyde	65-68	aldehyde dehydrogenase 2 family member	Homo sapiens	109-133
32775346-5	2020	Summary: The strongest evidence for the local carcinogenicity of ACH in man provides a point mutation in the aldehyde dehydrogenase 2 (ALDH2) gene, which has randomized millions of alcohol consumers to markedly increased ACH exposure via saliva.	Acetaldehyde	65-68	aldehyde dehydrogenase 2 family member	Homo sapiens	135-140
32403082-1	2020	BACKGROUND: Aldehyde dehydrogenase 2 (ALDH2) catalyzes the detoxification of aliphatic aldehydes, including acetaldehyde.	Acetaldehyde	108-120	aldehyde dehydrogenase 2 family member	Homo sapiens	12-36
32255634-8	2020	Those identified from the unimolecular decay of syn-MACR-oxide and subsequent reaction of O2 are acetaldehyde (37 +- 7%), vinyl alcohol (9 +- 1%), methylketene (2 +- 1%), and acrolein (52 +- 5%).	Acetaldehyde	97-109	synemin	Homo sapiens	48-51
32255634-8	2020	Those identified from the unimolecular decay of syn-MACR-oxide and subsequent reaction of O2 are acetaldehyde (37 +- 7%), vinyl alcohol (9 +- 1%), methylketene (2 +- 1%), and acrolein (52 +- 5%).	Acetaldehyde	122-135	synemin	Homo sapiens	48-51
32403082-1	2020	BACKGROUND: Aldehyde dehydrogenase 2 (ALDH2) catalyzes the detoxification of aliphatic aldehydes, including acetaldehyde.	Acetaldehyde	108-120	aldehyde dehydrogenase 2 family member	Homo sapiens	38-43
32403082-9	2020	INTERPRETATION: Since ~80% of the world population consumes ethanol and since acetaldehyde accumulation contributes to a variety of diseases, the identification of additional inactivating variants of ALDH2 in different ethnic groups may help develop new "precision medicine" for carriers of these inactive ALDH2.	Acetaldehyde	78-90	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	200-205
31074772-2	2020	Aldehyde dehydrogenase2 (ALDH2) is an enzyme that detoxify acetaldehyde, and its activity is reduced by ALDH2 gene polymorphism.	Acetaldehyde	59-71	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	0-23
32124282-2	2020	Chronic alcohol consumption increases intracellular acetaldehyde levels which enhances the generation of reactive oxygen and nitrogen species (ROS and RNS).	Acetaldehyde	52-64	FAM20C golgi associated secretory pathway kinase	Homo sapiens	151-154
32124282-4	2020	Treatment of human erythrocytes with different concentrations of acetaldehyde (0.05-2 mM) for 24 h at 37  C increased intracellular generation of ROS and RNS.	Acetaldehyde	65-77	FAM20C golgi associated secretory pathway kinase	Homo sapiens	154-157
32124282-9	2020	Our results show that acetaldehyde enhances the generation of ROS and RNS that results in oxidative modification of cellular components.	Acetaldehyde	22-34	FAM20C golgi associated secretory pathway kinase	Homo sapiens	70-73
31074772-2	2020	Aldehyde dehydrogenase2 (ALDH2) is an enzyme that detoxify acetaldehyde, and its activity is reduced by ALDH2 gene polymorphism.	Acetaldehyde	59-71	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	25-30
31074772-2	2020	Aldehyde dehydrogenase2 (ALDH2) is an enzyme that detoxify acetaldehyde, and its activity is reduced by ALDH2 gene polymorphism.	Acetaldehyde	59-71	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	104-109
31074772-3	2020	Reduction of ALDH2 activity increases blood, salivary, and breath acetaldehyde levels after alcohol intake, and it is deeply associated with a development of ESCC.	Acetaldehyde	66-78	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	13-18
31074772-11	2020	These results indicate the protective effects of ALDH2 activation by Alda-1 on esophageal DNA damage levels in individuals with ALDH2 gene polymorphism, providing a new insight into acetaldehyde-mediated esophageal carcinogenesis and prevention.	Acetaldehyde	182-194	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	49-54
31074772-11	2020	These results indicate the protective effects of ALDH2 activation by Alda-1 on esophageal DNA damage levels in individuals with ALDH2 gene polymorphism, providing a new insight into acetaldehyde-mediated esophageal carcinogenesis and prevention.	Acetaldehyde	182-194	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	128-133
32254049-1	2020	Human O-phosphoethanolamine phospho-lyase (hEtnppl; EC 4.2.3.2) is a pyridoxal 5"-phosphate-dependent enzyme that catalyzes the degradation of O-phosphoethanolamine (PEA) into acetaldehyde, phosphate and ammonia.	Acetaldehyde	176-188	ethanolamine-phosphate phospho-lyase	Homo sapiens	43-50
32062779-1	2020	We aimed to investigate whether ethanol (EtOH) and acetaldehyde (AcH) can affect glutamate and its receptors GluN1 and GluA1 in the hippocampus of Aldh2-knockout (Aldh2-KO) and C57BL/6N (wild-type (WT)) mice.	Acetaldehyde	65-68	glutamate receptor, ionotropic, AMPA1 (alpha 1)	Mus musculus	119-124
32006326-5	2020	The rate constants for acetaldehyde production from ethanol and acetaldehyde loss averaged 3.0 +- 3.4 x 10-3 min-1 and 2.3 +- 4.5 x 10-2 min-1 respectively.	Acetaldehyde	23-35	CD59 molecule (CD59 blood group)	Homo sapiens	109-142
32006326-5	2020	The rate constants for acetaldehyde production from ethanol and acetaldehyde loss averaged 3.0 +- 3.4 x 10-3 min-1 and 2.3 +- 4.5 x 10-2 min-1 respectively.	Acetaldehyde	64-76	CD59 molecule (CD59 blood group)	Homo sapiens	109-142
32006326-6	2020	The branching ratio for acetaldehyde production from ethanol was 0.46 +- 0.26 and estimated acetaldehyde biological production rates ranged from 0.022 to 0.800 nM min-1.	Acetaldehyde	92-104	CD59 molecule (CD59 blood group)	Homo sapiens	163-168
32143280-2	2020	Two additional pathways of acetaldehyde generation are by microsomal ethanol oxidizing system (cytochrome P450 2E1) and catalase.	Acetaldehyde	27-39	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	95-114
32143280-2	2020	Two additional pathways of acetaldehyde generation are by microsomal ethanol oxidizing system (cytochrome P450 2E1) and catalase.	Acetaldehyde	27-39	catalase	Homo sapiens	120-128
32005715-2	2020	Somewhat conversely, the ALDH2 Lys allele also confers a protective effect against alcohol-induced carcinogenesis, by decreasing alcohol consumption due to acetaldehyde-related adverse effects.	Acetaldehyde	156-168	aldehyde dehydrogenase 2 family member	Homo sapiens	25-30
32062779-0	2020	High Ethanol and Acetaldehyde Inhibit Glutamatergic Transmission in the Hippocampus of Aldh2-Knockout and C57BL/6N Mice: an In Vivo and Ex Vivo Analysis.	Acetaldehyde	17-29	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	87-92
32062779-1	2020	We aimed to investigate whether ethanol (EtOH) and acetaldehyde (AcH) can affect glutamate and its receptors GluN1 and GluA1 in the hippocampus of Aldh2-knockout (Aldh2-KO) and C57BL/6N (wild-type (WT)) mice.	Acetaldehyde	51-63	glutamate receptor, ionotropic, NMDA1 (zeta 1)	Mus musculus	109-114
32062779-1	2020	We aimed to investigate whether ethanol (EtOH) and acetaldehyde (AcH) can affect glutamate and its receptors GluN1 and GluA1 in the hippocampus of Aldh2-knockout (Aldh2-KO) and C57BL/6N (wild-type (WT)) mice.	Acetaldehyde	65-68	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	147-152
32062779-1	2020	We aimed to investigate whether ethanol (EtOH) and acetaldehyde (AcH) can affect glutamate and its receptors GluN1 and GluA1 in the hippocampus of Aldh2-knockout (Aldh2-KO) and C57BL/6N (wild-type (WT)) mice.	Acetaldehyde	51-63	glutamate receptor, ionotropic, AMPA1 (alpha 1)	Mus musculus	119-124
32062779-1	2020	We aimed to investigate whether ethanol (EtOH) and acetaldehyde (AcH) can affect glutamate and its receptors GluN1 and GluA1 in the hippocampus of Aldh2-knockout (Aldh2-KO) and C57BL/6N (wild-type (WT)) mice.	Acetaldehyde	51-63	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	147-152
32062779-1	2020	We aimed to investigate whether ethanol (EtOH) and acetaldehyde (AcH) can affect glutamate and its receptors GluN1 and GluA1 in the hippocampus of Aldh2-knockout (Aldh2-KO) and C57BL/6N (wild-type (WT)) mice.	Acetaldehyde	51-63	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	163-168
32062779-1	2020	We aimed to investigate whether ethanol (EtOH) and acetaldehyde (AcH) can affect glutamate and its receptors GluN1 and GluA1 in the hippocampus of Aldh2-knockout (Aldh2-KO) and C57BL/6N (wild-type (WT)) mice.	Acetaldehyde	65-68	glutamate receptor, ionotropic, NMDA1 (zeta 1)	Mus musculus	109-114
32062779-1	2020	We aimed to investigate whether ethanol (EtOH) and acetaldehyde (AcH) can affect glutamate and its receptors GluN1 and GluA1 in the hippocampus of Aldh2-knockout (Aldh2-KO) and C57BL/6N (wild-type (WT)) mice.	Acetaldehyde	65-68	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	163-168
32062779-4	2020	A dose of 500 mM EtOH induced a greater decrease in Aldh2-KO mice (p < 0.05) than in WT mice, indicating the action of AcH.	Acetaldehyde	119-122	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	52-57
32062779-5	2020	Similarly, perfusion of 200 muM and 500 muM AcH decreased glutamate in Aldh2-KO mice (p < 0.05), but this decrease was not seen in WT mice at any AcH dose.	Acetaldehyde	44-47	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	71-76
32062779-6	2020	Second, we tested whether the EtOH- and AcH-induced decrease in glutamate was associated with decreases in GluN1 and GluA1 expression, as measured by real-time PCR and Western blot.	Acetaldehyde	40-43	glutamate receptor, ionotropic, NMDA1 (zeta 1)	Mus musculus	107-112
32062779-6	2020	Second, we tested whether the EtOH- and AcH-induced decrease in glutamate was associated with decreases in GluN1 and GluA1 expression, as measured by real-time PCR and Western blot.	Acetaldehyde	40-43	glutamate receptor, ionotropic, AMPA1 (alpha 1)	Mus musculus	117-122
32062779-7	2020	We found a significant decrease in GluN1 (p < 0.05) and GluA1 (p < 0.05) subunits after a high dose of EtOH (4.0 g/kg) and AcH (200 mg/kg) in WT mice.	Acetaldehyde	123-126	glutamate receptor, ionotropic, NMDA1 (zeta 1)	Mus musculus	35-40
32062779-7	2020	We found a significant decrease in GluN1 (p < 0.05) and GluA1 (p < 0.05) subunits after a high dose of EtOH (4.0 g/kg) and AcH (200 mg/kg) in WT mice.	Acetaldehyde	123-126	glutamate receptor, ionotropic, AMPA1 (alpha 1)	Mus musculus	56-61
32062779-10	2020	Together, these in vivo and ex vivo data suggest that EtOH and AcH decrease extracellular glutamate in the hippocampus of mice with a concomitant decrease in GluN1 and GluA1 subunits, but these effects require relatively high concentrations and may, therefore, explain the consequences of EtOH intoxication.	Acetaldehyde	63-66	glutamate receptor, ionotropic, NMDA1 (zeta 1)	Mus musculus	158-163
32062779-10	2020	Together, these in vivo and ex vivo data suggest that EtOH and AcH decrease extracellular glutamate in the hippocampus of mice with a concomitant decrease in GluN1 and GluA1 subunits, but these effects require relatively high concentrations and may, therefore, explain the consequences of EtOH intoxication.	Acetaldehyde	63-66	glutamate receptor, ionotropic, AMPA1 (alpha 1)	Mus musculus	168-173
31801381-3	2020	The ALDH2*2 allele common genetic variant has a glutamic acid-to-lysine substitution at position 487 (E487K), which reduces the oxidizing ability of the enzyme resulting in systemic accumulation of acetaldehyde with ethanol ingestion.	Acetaldehyde	198-210	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	4-9
31870920-3	2020	Acute and chronic carbon tetrachloride (CCl4), and acute LPS-induced liver injury repressed hepatic ALDH2 activity and expression and consequently, blood and liver acetaldehyde concentrations were increased in these models.	Acetaldehyde	164-176	chemokine (C-C motif) ligand 4	Mus musculus	40-44
31801381-6	2020	We hypothesized that a one-time administration of an adeno-associated virus (AAV) serotype rh.10 gene transfer vector expressing the human ALDH2 cDNA (AAVrh.10hALDH2) would persistently correct ALDH2 deficiency, prevent systemic accumulation of acetaldehyde, and reduce esophageal DNA damage and adducts accumulation from chronic ethanol ingestion.	Acetaldehyde	245-257	aldehyde dehydrogenase 2 family member	Homo sapiens	139-144
31801381-6	2020	We hypothesized that a one-time administration of an adeno-associated virus (AAV) serotype rh.10 gene transfer vector expressing the human ALDH2 cDNA (AAVrh.10hALDH2) would persistently correct ALDH2 deficiency, prevent systemic accumulation of acetaldehyde, and reduce esophageal DNA damage and adducts accumulation from chronic ethanol ingestion.	Acetaldehyde	245-257	aldehyde dehydrogenase 2 family member	Homo sapiens	151-165
31801381-6	2020	We hypothesized that a one-time administration of an adeno-associated virus (AAV) serotype rh.10 gene transfer vector expressing the human ALDH2 cDNA (AAVrh.10hALDH2) would persistently correct ALDH2 deficiency, prevent systemic accumulation of acetaldehyde, and reduce esophageal DNA damage and adducts accumulation from chronic ethanol ingestion.	Acetaldehyde	245-257	aldehyde dehydrogenase 2 family member	Homo sapiens	160-165
31801381-11	2020	Compared to non-ethanol drinking littermates, untreated ALDH2-/- and ALDH2E487K+/+ mice had decreased body weight and hemoglobin levels, poor performance in locomotor activity tests, elevated serum acetaldehyde levels, increased esophageal gammaH2AX positive cells, and increased esophageal N2-et-dG adducts (all p&lt;0.05).	Acetaldehyde	198-210	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	69-74
31756635-0	2020	Acetaldehyde induces phosphorylation of dynamin-related protein 1 and mitochondrial dysfunction via elevating intracellular ROS and Ca2+ levels.	Acetaldehyde	0-12	dynamin 1 like	Homo sapiens	40-65
31669900-2	2020	The ratios of the slopes of the correlations between -DlnA350 values and individual DBPs concentrations (SNH2Cl/SHOCl) were observed to be linearly correlated with the ratios of the Gibbs free energies (DeltaGNH2Cl/DeltaGHOCl) of the corresponding reactions of chloramine and chlorine with acetaldehyde which was used as a model DBP precursor in QC simulations.	Acetaldehyde	290-302	D-box binding PAR bZIP transcription factor	Homo sapiens	84-87
32140062-1	2020	Acetaldehyde dehydrogenase 2 (ALDH2) is the key enzyme responsible for metabolism of the alcohol metabolite acetaldehyde in the liver.	Acetaldehyde	108-120	aldehyde dehydrogenase 2 family member	Homo sapiens	0-28
32140062-1	2020	Acetaldehyde dehydrogenase 2 (ALDH2) is the key enzyme responsible for metabolism of the alcohol metabolite acetaldehyde in the liver.	Acetaldehyde	108-120	aldehyde dehydrogenase 2 family member	Homo sapiens	30-35
32140062-6	2020	This review summarizes new progress in understanding tissue-specific acetaldehyde metabolism by ALDH2 as well as the association of ALDH2 gene polymorphisms with liver disease and cancer.	Acetaldehyde	69-81	aldehyde dehydrogenase 2 family member	Homo sapiens	96-101
31670032-2	2020	Herein, we identified that gasdermin D (GSDMD) membrane pore is critical in mediating IL-1beta hypersecretion from chronic ethanol or acetaldehyde-stimulated macrophages.	Acetaldehyde	134-146	gasdermin D	Mus musculus	27-38
31670032-2	2020	Herein, we identified that gasdermin D (GSDMD) membrane pore is critical in mediating IL-1beta hypersecretion from chronic ethanol or acetaldehyde-stimulated macrophages.	Acetaldehyde	134-146	gasdermin D	Mus musculus	40-45
31670032-2	2020	Herein, we identified that gasdermin D (GSDMD) membrane pore is critical in mediating IL-1beta hypersecretion from chronic ethanol or acetaldehyde-stimulated macrophages.	Acetaldehyde	134-146	interleukin 1 beta	Mus musculus	86-94
31756635-10	2020	Both ROS and Ca2+-mediated signaling pathways played important roles in acetaldehyde-induced Drp1 phosphorylation.	Acetaldehyde	72-84	dynamin 1 like	Homo sapiens	93-97
31690451-1	2020	The p53 protein plays a number of roles in protecting organisms from different genotoxic stresses and this includes DNA damage induced by acetaldehyde, a metabolite of alcohol.	Acetaldehyde	138-150	tumor protein p53	Homo sapiens	4-7
32161021-1	2020	Labile HbA1c migrates in the #C fraction with modified hemoglobin (Hb) (such as carbamylated Hb, acetaldehyde Hb, and acetylated Hb) when HbA1c is measured by Arkray"s high-performance liquid chromatography (HPLC).	Acetaldehyde	97-109	hemoglobin subunit alpha 1	Homo sapiens	7-11
31756635-5	2020	Further analyses showed that acetaldehyde induced the phosphorylation of mitochondrial fission related protein dynamin-related protein 1 (Drp1) at Ser616 and promoted its translocation to mitochondria.	Acetaldehyde	29-41	dynamin 1 like	Homo sapiens	111-136
31756635-5	2020	Further analyses showed that acetaldehyde induced the phosphorylation of mitochondrial fission related protein dynamin-related protein 1 (Drp1) at Ser616 and promoted its translocation to mitochondria.	Acetaldehyde	29-41	dynamin 1 like	Homo sapiens	138-142
31756635-6	2020	The elevation of Drp1 phosphorylation was partly dependent on the reactive oxygen species (ROS)-mediated activation of c-Jun-N-terminal kinase (JNK) and p38 mitogen-activated protein kinase (MAPK), as N-acetyl-l-cysteine (NAC) pretreatment inhibited the activation of JNK and p38 MAPK while attenuating Drp1 phosphorylation in acetaldehyde-treated cells.	Acetaldehyde	327-339	dynamin 1 like	Homo sapiens	17-21
31756635-6	2020	The elevation of Drp1 phosphorylation was partly dependent on the reactive oxygen species (ROS)-mediated activation of c-Jun-N-terminal kinase (JNK) and p38 mitogen-activated protein kinase (MAPK), as N-acetyl-l-cysteine (NAC) pretreatment inhibited the activation of JNK and p38 MAPK while attenuating Drp1 phosphorylation in acetaldehyde-treated cells.	Acetaldehyde	327-339	mitogen-activated protein kinase 8	Homo sapiens	119-142
31756635-7	2020	In addition, acetaldehyde treatment elevated intracellular Ca2+ level and activated Ca2+/calmodulin-dependent protein kinase II (CaMKII).	Acetaldehyde	13-25	calcium/calmodulin dependent protein kinase II gamma	Homo sapiens	84-127
31756635-7	2020	In addition, acetaldehyde treatment elevated intracellular Ca2+ level and activated Ca2+/calmodulin-dependent protein kinase II (CaMKII).	Acetaldehyde	13-25	calcium/calmodulin dependent protein kinase II gamma	Homo sapiens	129-135
31756635-8	2020	Pretreatment of CaMKII inhibitor prevented Drp1 phosphorylation in acetaldehyde-treated cells and ameliorated acetaldehyde-induced cytotoxicity, suggesting that CaMKII was a key effector mediating acetaldehyde-induced Drp1 phosphorylation and mitochondrial dysfunction.	Acetaldehyde	67-79	calcium/calmodulin dependent protein kinase II gamma	Homo sapiens	16-22
31756635-8	2020	Pretreatment of CaMKII inhibitor prevented Drp1 phosphorylation in acetaldehyde-treated cells and ameliorated acetaldehyde-induced cytotoxicity, suggesting that CaMKII was a key effector mediating acetaldehyde-induced Drp1 phosphorylation and mitochondrial dysfunction.	Acetaldehyde	67-79	dynamin 1 like	Homo sapiens	43-47
31756635-8	2020	Pretreatment of CaMKII inhibitor prevented Drp1 phosphorylation in acetaldehyde-treated cells and ameliorated acetaldehyde-induced cytotoxicity, suggesting that CaMKII was a key effector mediating acetaldehyde-induced Drp1 phosphorylation and mitochondrial dysfunction.	Acetaldehyde	67-79	calcium/calmodulin dependent protein kinase II gamma	Homo sapiens	161-167
31756635-8	2020	Pretreatment of CaMKII inhibitor prevented Drp1 phosphorylation in acetaldehyde-treated cells and ameliorated acetaldehyde-induced cytotoxicity, suggesting that CaMKII was a key effector mediating acetaldehyde-induced Drp1 phosphorylation and mitochondrial dysfunction.	Acetaldehyde	67-79	dynamin 1 like	Homo sapiens	218-222
31756635-8	2020	Pretreatment of CaMKII inhibitor prevented Drp1 phosphorylation in acetaldehyde-treated cells and ameliorated acetaldehyde-induced cytotoxicity, suggesting that CaMKII was a key effector mediating acetaldehyde-induced Drp1 phosphorylation and mitochondrial dysfunction.	Acetaldehyde	110-122	calcium/calmodulin dependent protein kinase II gamma	Homo sapiens	16-22
31756635-8	2020	Pretreatment of CaMKII inhibitor prevented Drp1 phosphorylation in acetaldehyde-treated cells and ameliorated acetaldehyde-induced cytotoxicity, suggesting that CaMKII was a key effector mediating acetaldehyde-induced Drp1 phosphorylation and mitochondrial dysfunction.	Acetaldehyde	110-122	calcium/calmodulin dependent protein kinase II gamma	Homo sapiens	161-167
31756635-8	2020	Pretreatment of CaMKII inhibitor prevented Drp1 phosphorylation in acetaldehyde-treated cells and ameliorated acetaldehyde-induced cytotoxicity, suggesting that CaMKII was a key effector mediating acetaldehyde-induced Drp1 phosphorylation and mitochondrial dysfunction.	Acetaldehyde	110-122	calcium/calmodulin dependent protein kinase II gamma	Homo sapiens	16-22
31756635-8	2020	Pretreatment of CaMKII inhibitor prevented Drp1 phosphorylation in acetaldehyde-treated cells and ameliorated acetaldehyde-induced cytotoxicity, suggesting that CaMKII was a key effector mediating acetaldehyde-induced Drp1 phosphorylation and mitochondrial dysfunction.	Acetaldehyde	110-122	calcium/calmodulin dependent protein kinase II gamma	Homo sapiens	161-167
31756635-9	2020	Taken together, acetaldehyde induced cytotoxicity by promoting excessive Drp1 phosphorylation and mitochondrial fragmentation.	Acetaldehyde	16-28	dynamin 1 like	Homo sapiens	73-77
31772208-7	2019	The alcohol metabolite, acetaldehyde, significantly decreased TER and reduced junctional ZO-1 localization, while increasing FD4 permeability in RWV cells compared with static, motion and flask control cells.	Acetaldehyde	24-36	tight junction protein 1	Homo sapiens	89-93
31829281-9	2019	These data indicate that impairment in the metabolism of aldehydes, and specifically ethanol-derived acetaldehyde, is a contributor to AD associated pathology and highlights the likely risk of alcohol consumption in the general population and especially in East Asians that carry ALDH2*2 mutation.	Acetaldehyde	101-113	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	280-285
31596176-4	2019	The lowest LOD was found for acetaldehyde (0.03 microg L-1), while the lowest LOQ value (1.0 microg L-1) was found for acetaldehyde and EC, formaldehyde and furfural.	Acetaldehyde	119-131	L1 cell adhesion molecule	Homo sapiens	100-103
31792171-1	2019	Aldehyde dehydrogenase 2 (ALDH2), a key enzyme for detoxification the ethanol metabolite acetaldehyde, is recognized as a promising therapeutic target to treat alcohol use disorders (AUDs).	Acetaldehyde	89-101	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	0-24
31792171-1	2019	Aldehyde dehydrogenase 2 (ALDH2), a key enzyme for detoxification the ethanol metabolite acetaldehyde, is recognized as a promising therapeutic target to treat alcohol use disorders (AUDs).	Acetaldehyde	89-101	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	26-31
31792171-3	2019	This study aims to elucidate the relative contribution of different organs in acetaldehyde clearance through ALDH2 by using global- (Aldh2 -/-) and tissue-specific Aldh2-deficient mice, and to examine whether liver-specific ALDH2 inhibition can prevent alcohol-seeking behavior.	Acetaldehyde	78-90	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	109-114
31792171-4	2019	Aldh2 -/- mice showed markedly higher acetaldehyde concentrations than wild-type (WT) mice after acute ethanol gavage.	Acetaldehyde	38-50	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	0-5
31792171-5	2019	Acetaldehyde levels in hepatocyte-specific Aldh2 knockout (Aldh2 Hep-/-) mice were significantly higher than those in WT mice post gavage, but did not reach the levels observed in Aldh2 -/- mice.	Acetaldehyde	0-12	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	43-48
31792171-5	2019	Acetaldehyde levels in hepatocyte-specific Aldh2 knockout (Aldh2 Hep-/-) mice were significantly higher than those in WT mice post gavage, but did not reach the levels observed in Aldh2 -/- mice.	Acetaldehyde	0-12	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	59-64
31792171-10	2019	In conclusion, although the liver is the major organ responsible for acetaldehyde metabolism, a cumulative effect of ALDH2 from other organs likely also contributes to systemic acetaldehyde clearance.	Acetaldehyde	177-189	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	117-122
31325696-0	2019	New insights into the synergistic effect of active radicals and adsorptive ability on the photodegradation of gaseous acetaldehyde over reduced graphene Oxide/P25 composite.	Acetaldehyde	118-130	tubulin polymerization promoting protein	Homo sapiens	159-162
31487269-5	2019	Acetaldehyde generated by ADH in both liver and Schwann cells surrounding nociceptors was required for TRPA1-induced mechanical allodynia.	Acetaldehyde	0-12	aldo-keto reductase family 1, member A1 (aldehyde reductase)	Mus musculus	26-29
31487269-5	2019	Acetaldehyde generated by ADH in both liver and Schwann cells surrounding nociceptors was required for TRPA1-induced mechanical allodynia.	Acetaldehyde	0-12	transient receptor potential cation channel, subfamily A, member 1	Mus musculus	103-108
31487269-6	2019	Plp1-Cre Trpa1fl/fl mice with a tamoxifen-inducible specific deletion of TRPA1 in Schwann cells revealed that channel activation by acetaldehyde in these cells initiates a NADPH oxidase-1-dependent (NOX1-dependent) production of hydrogen peroxide (H2O2) and 4-hydroxynonenal (4-HNE), which sustains allodynia by paracrine targeting of nociceptor TRPA1.	Acetaldehyde	132-144	proteolipid protein (myelin) 1	Mus musculus	0-4
31487269-6	2019	Plp1-Cre Trpa1fl/fl mice with a tamoxifen-inducible specific deletion of TRPA1 in Schwann cells revealed that channel activation by acetaldehyde in these cells initiates a NADPH oxidase-1-dependent (NOX1-dependent) production of hydrogen peroxide (H2O2) and 4-hydroxynonenal (4-HNE), which sustains allodynia by paracrine targeting of nociceptor TRPA1.	Acetaldehyde	132-144	transient receptor potential cation channel, subfamily A, member 1	Mus musculus	73-78
31487269-6	2019	Plp1-Cre Trpa1fl/fl mice with a tamoxifen-inducible specific deletion of TRPA1 in Schwann cells revealed that channel activation by acetaldehyde in these cells initiates a NADPH oxidase-1-dependent (NOX1-dependent) production of hydrogen peroxide (H2O2) and 4-hydroxynonenal (4-HNE), which sustains allodynia by paracrine targeting of nociceptor TRPA1.	Acetaldehyde	132-144	NADPH oxidase 1	Mus musculus	172-187
31487269-6	2019	Plp1-Cre Trpa1fl/fl mice with a tamoxifen-inducible specific deletion of TRPA1 in Schwann cells revealed that channel activation by acetaldehyde in these cells initiates a NADPH oxidase-1-dependent (NOX1-dependent) production of hydrogen peroxide (H2O2) and 4-hydroxynonenal (4-HNE), which sustains allodynia by paracrine targeting of nociceptor TRPA1.	Acetaldehyde	132-144	NADPH oxidase 1	Mus musculus	199-203
31487269-6	2019	Plp1-Cre Trpa1fl/fl mice with a tamoxifen-inducible specific deletion of TRPA1 in Schwann cells revealed that channel activation by acetaldehyde in these cells initiates a NADPH oxidase-1-dependent (NOX1-dependent) production of hydrogen peroxide (H2O2) and 4-hydroxynonenal (4-HNE), which sustains allodynia by paracrine targeting of nociceptor TRPA1.	Acetaldehyde	132-144	transient receptor potential cation channel, subfamily A, member 1	Mus musculus	346-351
31542594-1	2019	The Yatsushiro Sea in Japan is contaminated with mercury in wastewater discharge from the Chisso Company, which produced acetaldehyde from 1932 onwards.	Acetaldehyde	121-133	S13 erythroblastosis (avian) oncogene homolog	Homo sapiens	15-18
31542594-6	2019	The amount of acetaldehyde produced in Chisso over time was correlated with the T-Hg concentrations in the sediments from the Yatsushiro Sea.	Acetaldehyde	14-26	S13 erythroblastosis (avian) oncogene homolog	Homo sapiens	137-140
31002879-6	2019	RESULTS: We identified variations in the ADH1A, SRPRB, and PGM1 genes, which are directly associated with blood alcohol or acetaldehyde concentrations.	Acetaldehyde	123-135	alcohol dehydrogenase 1A (class I), alpha polypeptide	Homo sapiens	41-46
31326413-14	2019	Predicted levels of butyrate and substrates involved in butyrate synthesis (ethanol or acetaldehyde) were significantly associated with clinical remission following anti-TNF therapy, verified by fecal metabolomic analyses.	Acetaldehyde	87-99	tumor necrosis factor	Homo sapiens	170-173
31833292-0	2019	Relationship between Blood Acetaldehyde Concentration and Psychomotor Function of Individuals with Different ALDH2 Genotypes after Alcohol Consumption.	Acetaldehyde	27-39	aldehyde dehydrogenase 2 family member	Homo sapiens	109-114
31833292-10	2019	Conclusion There are significant differences between the psychomotor function of ALDH2 wild type and mutant type individuals after alcohol consumption estimated to be related to the difference in blood acetaldehyde concentration after alcohol consumption.	Acetaldehyde	202-214	aldehyde dehydrogenase 2 family member	Homo sapiens	81-86
31283017-8	2019	Treatment of WT ESCs with AcH or 4-hydroxynonenal (4-HNE), another substrate of ALDH2, increased differentiation-associated transcripts compared to levels in untreated cells.	Acetaldehyde	26-29	aldehyde dehydrogenase 2 family member	Homo sapiens	80-85
31283017-9	2019	mRNAs of genes involved in retinoic acid (RA) synthesis (Stra6 and Rdh10) were also increased by EtOH, AcH, and 4-HNE treatment.	Acetaldehyde	103-106	signaling receptor and transporter of retinol STRA6	Homo sapiens	57-62
31283017-9	2019	mRNAs of genes involved in retinoic acid (RA) synthesis (Stra6 and Rdh10) were also increased by EtOH, AcH, and 4-HNE treatment.	Acetaldehyde	103-106	retinol dehydrogenase 10	Homo sapiens	67-72
31283017-10	2019	Retinoic acid receptor-gamma (RARgamma) is required for both EtOH- and AcH-mediated increases in Hoxa1 and Stra6, demonstrating the critical role of RA:RARgamma signaling in AcH-induced ESC differentiation.	Acetaldehyde	71-74	retinoic acid receptor gamma	Homo sapiens	0-28
31283017-10	2019	Retinoic acid receptor-gamma (RARgamma) is required for both EtOH- and AcH-mediated increases in Hoxa1 and Stra6, demonstrating the critical role of RA:RARgamma signaling in AcH-induced ESC differentiation.	Acetaldehyde	71-74	retinoic acid receptor gamma	Homo sapiens	30-38
31279903-2	2019	Approximately 30-40% of the Asian population are deficient for aldehyde dehydrogenase 2 (ALDH2), a key enzyme that detoxifies the ethanol metabolite acetaldehyde.	Acetaldehyde	149-161	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	63-87
31279903-2	2019	Approximately 30-40% of the Asian population are deficient for aldehyde dehydrogenase 2 (ALDH2), a key enzyme that detoxifies the ethanol metabolite acetaldehyde.	Acetaldehyde	149-161	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	89-94
31279903-9	2019	Furthermore, our results from in vivo and in vitro mechanistic studies revealed that after CCl4 plus ethanol exposure, Aldh2-deficient hepatocytes produced a large amount of harmful oxidized mitochondrial DNA via extracellular vesicles, which were then transferred into neighboring HCC cells and together with acetaldehyde activated multiple oncogenic pathways (JNK, STAT3, BCL-2, and TAZ), thereby promoting HCC.	Acetaldehyde	310-322	chemokine (C-C motif) ligand 4	Mus musculus	91-95
31319242-5	2019	The highest average C1/C2 (formaldehyde/acetaldehyde) ratio was observed in summer (2.10) compared to those (1.33-2.03) in other seasons, implying the photochemical activities had a positive effect on increasing the ratio of C1/C2.	Acetaldehyde	40-52	heterogeneous nuclear ribonucleoprotein C	Homo sapiens	20-25
31283017-5	2019	RESULTS: By using kinetic assays, we confirmed that AcH is primarily oxidized by ALDH2 rather than ALDH1A2.	Acetaldehyde	52-55	aldehyde dehydrogenase 2 family member	Homo sapiens	81-86
31283017-5	2019	RESULTS: By using kinetic assays, we confirmed that AcH is primarily oxidized by ALDH2 rather than ALDH1A2.	Acetaldehyde	52-55	aldehyde dehydrogenase 1 family member A2	Homo sapiens	99-106
31283017-10	2019	Retinoic acid receptor-gamma (RARgamma) is required for both EtOH- and AcH-mediated increases in Hoxa1 and Stra6, demonstrating the critical role of RA:RARgamma signaling in AcH-induced ESC differentiation.	Acetaldehyde	71-74	homeobox A1	Homo sapiens	97-102
31283017-10	2019	Retinoic acid receptor-gamma (RARgamma) is required for both EtOH- and AcH-mediated increases in Hoxa1 and Stra6, demonstrating the critical role of RA:RARgamma signaling in AcH-induced ESC differentiation.	Acetaldehyde	71-74	signaling receptor and transporter of retinol STRA6	Homo sapiens	107-112
31283017-10	2019	Retinoic acid receptor-gamma (RARgamma) is required for both EtOH- and AcH-mediated increases in Hoxa1 and Stra6, demonstrating the critical role of RA:RARgamma signaling in AcH-induced ESC differentiation.	Acetaldehyde	71-74	retinoic acid receptor gamma	Homo sapiens	152-160
31283017-10	2019	Retinoic acid receptor-gamma (RARgamma) is required for both EtOH- and AcH-mediated increases in Hoxa1 and Stra6, demonstrating the critical role of RA:RARgamma signaling in AcH-induced ESC differentiation.	Acetaldehyde	174-177	retinoic acid receptor gamma	Homo sapiens	0-28
31283017-10	2019	Retinoic acid receptor-gamma (RARgamma) is required for both EtOH- and AcH-mediated increases in Hoxa1 and Stra6, demonstrating the critical role of RA:RARgamma signaling in AcH-induced ESC differentiation.	Acetaldehyde	174-177	retinoic acid receptor gamma	Homo sapiens	30-38
31283017-10	2019	Retinoic acid receptor-gamma (RARgamma) is required for both EtOH- and AcH-mediated increases in Hoxa1 and Stra6, demonstrating the critical role of RA:RARgamma signaling in AcH-induced ESC differentiation.	Acetaldehyde	174-177	homeobox A1	Homo sapiens	97-102
31283017-10	2019	Retinoic acid receptor-gamma (RARgamma) is required for both EtOH- and AcH-mediated increases in Hoxa1 and Stra6, demonstrating the critical role of RA:RARgamma signaling in AcH-induced ESC differentiation.	Acetaldehyde	174-177	signaling receptor and transporter of retinol STRA6	Homo sapiens	107-112
31283017-10	2019	Retinoic acid receptor-gamma (RARgamma) is required for both EtOH- and AcH-mediated increases in Hoxa1 and Stra6, demonstrating the critical role of RA:RARgamma signaling in AcH-induced ESC differentiation.	Acetaldehyde	174-177	retinoic acid receptor gamma	Homo sapiens	152-160
31283017-12	2019	We demonstrate that AcH increases differentiation-associated mRNAs in ESCs via RARgamma.	Acetaldehyde	20-23	retinoic acid receptor gamma	Homo sapiens	79-87
31002879-6	2019	RESULTS: We identified variations in the ADH1A, SRPRB, and PGM1 genes, which are directly associated with blood alcohol or acetaldehyde concentrations.	Acetaldehyde	123-135	SRP receptor subunit beta	Homo sapiens	48-53
29509552-1	2019	BACKGROUND: It is estimated that 1 billion people in the world have a point mutation in the gene encoding the aldehyde dehydrogenase 2 (ALDH2) enzyme, the primary enzyme responsible for the metabolism of acetaldehyde.	Acetaldehyde	204-216	aldehyde dehydrogenase 2 family member	Homo sapiens	110-134
29509552-1	2019	BACKGROUND: It is estimated that 1 billion people in the world have a point mutation in the gene encoding the aldehyde dehydrogenase 2 (ALDH2) enzyme, the primary enzyme responsible for the metabolism of acetaldehyde.	Acetaldehyde	204-216	aldehyde dehydrogenase 2 family member	Homo sapiens	136-141
29509552-3	2019	Because of limited ability to metabolize acetaldehyde, individuals with ALDH2 deficiency experience elevated levels of blood acetaldehyde after exposure to various common sources such as recreational alcohol.	Acetaldehyde	41-53	aldehyde dehydrogenase 2 family member	Homo sapiens	72-77
31002879-6	2019	RESULTS: We identified variations in the ADH1A, SRPRB, and PGM1 genes, which are directly associated with blood alcohol or acetaldehyde concentrations.	Acetaldehyde	123-135	phosphoglucomutase 1	Homo sapiens	59-63
29509552-3	2019	Because of limited ability to metabolize acetaldehyde, individuals with ALDH2 deficiency experience elevated levels of blood acetaldehyde after exposure to various common sources such as recreational alcohol.	Acetaldehyde	125-137	aldehyde dehydrogenase 2 family member	Homo sapiens	72-77
29509552-4	2019	Because of higher levels of acetaldehyde, individuals with ALDH2 deficiency are at higher risk for numerous diseases, including liver cirrhosis, esophageal and gastric cancer, osteoporosis, and Alzheimer disease.	Acetaldehyde	28-40	aldehyde dehydrogenase 2 family member	Homo sapiens	59-64
29509552-6	2019	MEASURES AND OUTCOMES: The primary outcome was change in acetaldehyde levels in the blood after exposure to alcohol in individuals with ALDH2 deficiency before and after the use of study nutritional supplement.	Acetaldehyde	57-69	aldehyde dehydrogenase 2 family member	Homo sapiens	136-141
29509552-9	2019	RESULTS AND CONCLUSIONS: ALDH2 deficient subjects showed a significant decrease in average blood acetaldehyde level 20 minutes after alcohol consumption (from 0.91 mg/dL to 0.71 mg/dL, P value = 0.02) after receiving 28 days of the nutritional supplement.	Acetaldehyde	97-109	aldehyde dehydrogenase 2 family member	Homo sapiens	25-30
31002879-7	2019	Namely, the T allele of SRPRB rs17376019 and the C allele of PGM1 rs4643 were associated with lower blood alcohol levels, while the ADH1 rs1229976 C allele group exhibited markedly higher blood acetaldehyde levels than those of the ADH1 rs1229976 T allele group.	Acetaldehyde	194-206	SRP receptor subunit beta	Homo sapiens	24-29
31002879-7	2019	Namely, the T allele of SRPRB rs17376019 and the C allele of PGM1 rs4643 were associated with lower blood alcohol levels, while the ADH1 rs1229976 C allele group exhibited markedly higher blood acetaldehyde levels than those of the ADH1 rs1229976 T allele group.	Acetaldehyde	194-206	phosphoglucomutase 1	Homo sapiens	61-65
31002879-7	2019	Namely, the T allele of SRPRB rs17376019 and the C allele of PGM1 rs4643 were associated with lower blood alcohol levels, while the ADH1 rs1229976 C allele group exhibited markedly higher blood acetaldehyde levels than those of the ADH1 rs1229976 T allele group.	Acetaldehyde	194-206	alcohol dehydrogenase 1A (class I), alpha polypeptide	Homo sapiens	132-136
31002879-8	2019	CONCLUSION: This study demonstrates that genetic variations in ADH1A, SRPRB, and PGM1 are associated with variations in blood alcohol and acetaldehyde concentration after alcohol intake.	Acetaldehyde	138-150	alcohol dehydrogenase 1A (class I), alpha polypeptide	Homo sapiens	63-68
31002879-8	2019	CONCLUSION: This study demonstrates that genetic variations in ADH1A, SRPRB, and PGM1 are associated with variations in blood alcohol and acetaldehyde concentration after alcohol intake.	Acetaldehyde	138-150	SRP receptor subunit beta	Homo sapiens	70-75
31002879-8	2019	CONCLUSION: This study demonstrates that genetic variations in ADH1A, SRPRB, and PGM1 are associated with variations in blood alcohol and acetaldehyde concentration after alcohol intake.	Acetaldehyde	138-150	phosphoglucomutase 1	Homo sapiens	81-85
31219017-4	2019	Our new technique, named ExoNANO, adopts a double-antibody sandwich strategy using anti-CD63 antibody-conjugated superparamagnetic iron oxide particles (SIOPs) and acridinium ester (ACE)-labeled anti-CD9 antibodies.	Acetaldehyde	182-185	CD9 molecule	Homo sapiens	200-203
31649957-3	2019	ALDH2 is the key enzyme in ethanol metabolism; with ethanol challenge, the common ALDH2*2 (E487K) mutation results in accumulation of toxic acetaldehyde.	Acetaldehyde	140-152	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	0-5
31649957-3	2019	ALDH2 is the key enzyme in ethanol metabolism; with ethanol challenge, the common ALDH2*2 (E487K) mutation results in accumulation of toxic acetaldehyde.	Acetaldehyde	140-152	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	82-87
31649957-7	2019	Following acute ethanol ingestion, untreated ALDH2-deficient mice had elevated acetaldehyde levels and performed poorly in behavioral tests.	Acetaldehyde	79-91	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	45-50
31649957-8	2019	In contrast, treated Aldh2 -/- and Aldh2 E487K+/+ mice had lower serum acetaldehyde levels and improved behavior.	Acetaldehyde	71-83	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	21-26
31649957-8	2019	In contrast, treated Aldh2 -/- and Aldh2 E487K+/+ mice had lower serum acetaldehyde levels and improved behavior.	Acetaldehyde	71-83	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	35-40
31141391-11	2019	Collectively, all these downstream events reduced the display of HBV peptide-MHC class I complexes on the hepatocyte surface, which may suppress CTL activation and the recognition of CTL epitopes on HBV-expressing hepatocytes by immune cells, thereby leading to persistence of liver inflammation.NEW &amp; NOTEWORTHY Our study shows that in HBV-expressing HepG2.2.15 cells, acetaldehyde alters HBV peptide processing by suppressing chymotrypsin- and trypsin-like proteasome activities and decreases IFNgamma-stimulated immunoproteasome function and expression of PA28 activator and immunoproteasome subunits.	Acetaldehyde	374-386	interferon gamma	Homo sapiens	499-507
30121625-1	2019	OBJECTIVE: Aldehyde dehydrogenase 2 (ALDH2), a key enzyme to detoxify acetaldehyde in the liver, exists in both active and inactive forms in humans.	Acetaldehyde	70-82	aldehyde dehydrogenase 2 family member	Homo sapiens	11-35
31115629-2	2019	Herein, we report that a novel aldehyde reductase Ykl107wp deduced from YKL107W from S. cerevisiae belongs to the classical SDR group and can catalyze the reduction reactions of acetaldehyde (AA), glycolaldehyde (GA), furfural (FF), formaldehyde (FA), and propionaldehyde (PA) but cannot reduce the six representative ketones.	Acetaldehyde	178-190	short-chain dehydrogenase/reductase	Saccharomyces cerevisiae S288C	124-127
30121625-10	2019	Acetaldehyde also attenuated interferon-gamma production in phytohaemagglutinin-stimulated human peripheral lymphocytes.	Acetaldehyde	0-12	interferon gamma	Homo sapiens	29-45
30121625-1	2019	OBJECTIVE: Aldehyde dehydrogenase 2 (ALDH2), a key enzyme to detoxify acetaldehyde in the liver, exists in both active and inactive forms in humans.	Acetaldehyde	70-82	aldehyde dehydrogenase 2 family member	Homo sapiens	37-42
30121625-2	2019	Individuals with inactive ALDH2 accumulate acetaldehyde after alcohol consumption.	Acetaldehyde	43-55	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	26-31
31066241-2	2019	Although the aldehyde dehydrogenase 2 (ALDH2) polymorphism (rs671: Glu>Lys) has a strong effect on acetaldehyde metabolism, the association of rs671 with BC risk and its interaction with alcohol intake have not been fully elucidated.	Acetaldehyde	99-111	aldehyde dehydrogenase 2 family member	Homo sapiens	13-37
31066241-2	2019	Although the aldehyde dehydrogenase 2 (ALDH2) polymorphism (rs671: Glu>Lys) has a strong effect on acetaldehyde metabolism, the association of rs671 with BC risk and its interaction with alcohol intake have not been fully elucidated.	Acetaldehyde	99-111	aldehyde dehydrogenase 2 family member	Homo sapiens	39-44
30768969-1	2019	Plant cytosolic aldehyde dehydrogenases from family 2 (ALDH2s, EC 1.2.1.3) are non-specific enzymes and participate for example in the metabolism of acetaldehyde or biosynthesis of phenylpropanoids.	Acetaldehyde	149-161	aldehyde dehydrogenase 2	Zea mays	55-60
30942073-4	2019	HO2 and CH3C(O)O2 were formed by Cl-atom reactions with CH3OH and CH3CHO, respectively.	Acetaldehyde	66-72	heme oxygenase 2	Homo sapiens	0-3
30771931-6	2019	The ADH-immobilized mesh containing a solution of the oxidized form of NAD (NAD+) or reduced form (NADH) was used as an EtOH-imaging mesh and an AcH-imaging mesh, respectively.	Acetaldehyde	145-148	aldo-keto reductase family 1 member A1	Homo sapiens	4-7
30771931-7	2019	The distributions of the EtOH and AcH concentrations were visualized through the fluorescence of NADH (the excitation wavelength was 340 nm; the emission wavelength was 490 nm) occurring by the ADH-mediated redox reaction.	Acetaldehyde	34-37	aldo-keto reductase family 1 member A1	Homo sapiens	98-101
30771931-9	2019	The ADH-mediated reactions of EtOH and AcH showed maximum activities at pH 9.0 and pH 6.5, respectively.	Acetaldehyde	39-42	aldo-keto reductase family 1 member A1	Homo sapiens	4-7
31059574-0	2019	Genome-Wide CRISPR Screening Identifies the Tumor Suppressor Candidate OVCA2 As a Determinant of Tolerance to Acetaldehyde.	Acetaldehyde	110-122	TSC complex subunit 1	Homo sapiens	44-60
31059574-0	2019	Genome-Wide CRISPR Screening Identifies the Tumor Suppressor Candidate OVCA2 As a Determinant of Tolerance to Acetaldehyde.	Acetaldehyde	110-122	OVCA2 serine hydrolase domain containing	Homo sapiens	71-76
31059574-5	2019	Unexpectedly, the tumor suppressor gene OVCA2, whose function is unknown, was identified in our screen as a determinant of acetaldehyde tolerance.	Acetaldehyde	123-135	TSC complex subunit 1	Homo sapiens	18-34
31059574-5	2019	Unexpectedly, the tumor suppressor gene OVCA2, whose function is unknown, was identified in our screen as a determinant of acetaldehyde tolerance.	Acetaldehyde	123-135	OVCA2 serine hydrolase domain containing	Homo sapiens	40-45
31059574-6	2019	Disruption of the OVCA2 gene resulted in increased acetaldehyde sensitivity and higher accumulation of the acetaldehyde-derived DNA adduct N2-ethylidene-dG.	Acetaldehyde	51-63	OVCA2 serine hydrolase domain containing	Homo sapiens	18-23
31059574-6	2019	Disruption of the OVCA2 gene resulted in increased acetaldehyde sensitivity and higher accumulation of the acetaldehyde-derived DNA adduct N2-ethylidene-dG.	Acetaldehyde	107-119	OVCA2 serine hydrolase domain containing	Homo sapiens	18-23
30721697-4	2019	Reduced ALDH2 greatly affects acetaldehyde metabolism, leading to its accumulation in the body after the consumption of alcohol and the consequent development of a wide range of phenotypes.	Acetaldehyde	30-42	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	8-13
31114208-10	2019	Conclusion: Our meta-analysis indicates that the ALDH2 rs671 G&gt;A polymorphism may play an important role in the occurrence of IS by reducing the activity of ALDH2 and interfering with the metabolic processes involving acetaldehyde.	Acetaldehyde	221-233	aldehyde dehydrogenase 2 family member	Homo sapiens	49-54
31114208-10	2019	Conclusion: Our meta-analysis indicates that the ALDH2 rs671 G&gt;A polymorphism may play an important role in the occurrence of IS by reducing the activity of ALDH2 and interfering with the metabolic processes involving acetaldehyde.	Acetaldehyde	221-233	aldehyde dehydrogenase 2 family member	Homo sapiens	160-165
30521820-2	2019	Recently, it was described that N-(1,3-benzodioxol-5-ylmethyl)-2,6-dichlorobenzamide (ALDA-1) activates aldehyde dehydrogenase-2 (ALDH2), enzyme that catalyzes the oxidation of ethanol-derived acetaldehyde to acetate.	Acetaldehyde	193-205	aldehyde dehydrogenase 1 family, member A1	Rattus norvegicus	104-128
30931596-5	2019	Genetic variants in two enzymes involved in the metabolism of ethanol, alcohol-dehydrogenase ADH1B *2 and aldehyde-dehydrogenase ALDH2 *2 through increasing the blood level of acetaldehyde, may play a "protective" role against alcoholism.	Acetaldehyde	176-188	aldo-keto reductase family 1 member A1	Homo sapiens	71-92
30931596-5	2019	Genetic variants in two enzymes involved in the metabolism of ethanol, alcohol-dehydrogenase ADH1B *2 and aldehyde-dehydrogenase ALDH2 *2 through increasing the blood level of acetaldehyde, may play a "protective" role against alcoholism.	Acetaldehyde	176-188	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	93-98
30556202-0	2019	PDC1, a pyruvate/alpha-ketoacid decarboxylase, is involved in acetaldehyde, propanal and pentanal biosynthesis in melon (Cucumis melo L.) fruit.	Acetaldehyde	62-74	pyruvate decarboxylase 1	Cucumis melo	0-4
30556202-5	2019	RNAi-mediated transient and stable silencing of PDC1 expression in melon showed that this gene is involved in acetaldehyde, propanal and pentanal production, while it does not contribute to branched-chain amino acid (BCAA)-derived aldehyde biosynthesis in melon fruit.	Acetaldehyde	110-122	pyruvate decarboxylase 1	Cucumis melo	48-52
30893362-13	2019	These data suggest that ethanol and acetaldehyde selectively sensitize intrinsic constrictor responses upon activation of vascular alpha1-adrenergic and/or vasopressin receptors at clinically relevant concentrations.	Acetaldehyde	36-48	arginine vasopressin	Rattus norvegicus	156-167
30641047-6	2019	Both 1 and 100 nM luteolin increased expression and activity of ALDH2, which metabolized toxic acetaldehyde into nontoxic acetic acid.	Acetaldehyde	95-107	aldehyde dehydrogenase 2 family member	Homo sapiens	64-69
30677184-2	2019	This pathway contains four enzymes termed DmdA, DmdB, DmdC and DmdD/AcuH, which together catabolize DMSP to acetylaldehyde and methanethiol as carbon and sulfur sources respectively.	Acetaldehyde	108-122	sarcoglycan gamma	Homo sapiens	42-46
30931596-5	2019	Genetic variants in two enzymes involved in the metabolism of ethanol, alcohol-dehydrogenase ADH1B *2 and aldehyde-dehydrogenase ALDH2 *2 through increasing the blood level of acetaldehyde, may play a "protective" role against alcoholism.	Acetaldehyde	176-188	aldehyde dehydrogenase 2 family member	Homo sapiens	129-134
30931596-6	2019	The P450 CYP2E1 *5 c2, an inducible microsomal oxidase, upregulated by ethanol and by formation of acetaldehyde and reactive oxygen species, increases liver toxicity.	Acetaldehyde	99-111	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	9-15
30521820-2	2019	Recently, it was described that N-(1,3-benzodioxol-5-ylmethyl)-2,6-dichlorobenzamide (ALDA-1) activates aldehyde dehydrogenase-2 (ALDH2), enzyme that catalyzes the oxidation of ethanol-derived acetaldehyde to acetate.	Acetaldehyde	193-205	aldehyde dehydrogenase 1 family, member A1	Rattus norvegicus	130-135
30728884-9	2019	ADE upregulated ERS-related CHOP expression dose-dependently in primary cultured cortical neuronal cells.	Acetaldehyde	0-3	DNA-damage inducible transcript 3	Mus musculus	28-32
30854037-10	2019	Furthermore, human PIWI-like protein 4 was consistently upregulated in ethanol and acetaldehyde-treated normal oral keratinocytes.	Acetaldehyde	83-95	piwi like RNA-mediated gene silencing 4	Homo sapiens	19-38
30375985-1	2019	Acetaldehyde dehydrogenase 2 (ALDH2) is a mitochondrial enzyme detoxifying acetaldehyde and endogenous lipid aldehydes; previous studies suggest a protective role of ALDH2 against cardiovascular disease (CVD).	Acetaldehyde	75-87	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	0-28
30375985-1	2019	Acetaldehyde dehydrogenase 2 (ALDH2) is a mitochondrial enzyme detoxifying acetaldehyde and endogenous lipid aldehydes; previous studies suggest a protective role of ALDH2 against cardiovascular disease (CVD).	Acetaldehyde	75-87	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	30-35
30375985-1	2019	Acetaldehyde dehydrogenase 2 (ALDH2) is a mitochondrial enzyme detoxifying acetaldehyde and endogenous lipid aldehydes; previous studies suggest a protective role of ALDH2 against cardiovascular disease (CVD).	Acetaldehyde	75-87	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	166-171
30542011-6	2019	The catalyst calcined at 450 C (Mg-Al-450) exhibited the highest basicity as measured by the CO2-TPD with ethanol conversion of 45.8% and acetaldehyde yield of 29.7% at 350 C.	Acetaldehyde	138-150	complement C2	Homo sapiens	93-96
31368095-8	2019	Noteworthy, studies in SHRs and in estrogen deprived or replete normotensive rats implicate acetaldehyde in triggering oxidative stress in autonomic nuclei and the heart via (i) the Akt/extracellular signal-regulated kinases (ERK)/nitric oxide synthase (NOS) cascade and (ii) estrogen receptor-alpha (ERalpha) mediation of the higher catalase activity, which generates higher ethanol-derived acetaldehyde in female heart.	Acetaldehyde	92-104	estrogen receptor 1	Rattus norvegicus	301-308
31368097-5	2019	Considering that an estimated 560 million East Asians carry a common ALDH2 deficient variant which causes the well-known alcohol flushing syndrome due to acetaldehyde accumulation, the importance of understanding the role of ALDH2 in these diseases should be highlighted.	Acetaldehyde	154-166	aldehyde dehydrogenase 2 family member	Homo sapiens	69-74
31368105-3	2019	Mitochondrial aldehyde dehydrogenase (ALDH2) is a vital enzyme metabolizing various acetaldehyde and toxic aldehydes.	Acetaldehyde	84-96	aldehyde dehydrogenase 2 family member	Homo sapiens	38-43
31368106-1	2019	Aldehyde dehydrogenase 2 (ALDH2) is an important member of the functional aldehyde dehydrogenases (ALDHs) family in human beings, playing a fundamental role in the detoxification of acetaldehyde and other aldehydes.	Acetaldehyde	182-194	aldehyde dehydrogenase 2 family member	Homo sapiens	0-24
31368106-1	2019	Aldehyde dehydrogenase 2 (ALDH2) is an important member of the functional aldehyde dehydrogenases (ALDHs) family in human beings, playing a fundamental role in the detoxification of acetaldehyde and other aldehydes.	Acetaldehyde	182-194	aldehyde dehydrogenase 2 family member	Homo sapiens	26-31
31368108-1	2019	Aldehyde dehydrogenase 2 (ALDH2) is a key enzyme in the detoxification of toxic aldehydes, especially acetaldehyde, which is commonly considered as a carcinogen.	Acetaldehyde	102-114	aldehyde dehydrogenase 2 family member	Homo sapiens	0-24
31368108-1	2019	Aldehyde dehydrogenase 2 (ALDH2) is a key enzyme in the detoxification of toxic aldehydes, especially acetaldehyde, which is commonly considered as a carcinogen.	Acetaldehyde	102-114	aldehyde dehydrogenase 2 family member	Homo sapiens	26-31
31368108-2	2019	ALDH2 mutation and impaired enzymatic activity will cause acetaldehyde accumulation and thus participate in the development of cancers.	Acetaldehyde	58-70	aldehyde dehydrogenase 2 family member	Homo sapiens	0-5
30641601-4	2019	CYP2E1 is induced by ethanol, oxidizes ethanol to acetaldehyde, and generates ROS during this process.	Acetaldehyde	50-62	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	0-6
30538742-5	2018	The present study aimed to analyze the mechanism of action of alpha mangostin on acetaldehyde induced liver fibrosis model on TGF-beta and ERK 1/2 pathways.	Acetaldehyde	81-93	transforming growth factor beta 1	Homo sapiens	126-134
30284013-3	2018	However, the practical application of DERA as a biocatalyst is limited by its poor tolerance towards industrially relevant concentrations of aldehydes, in particular acetaldehyde.	Acetaldehyde	166-178	deoxyribose-phosphate aldolase	Homo sapiens	38-42
30538742-5	2018	The present study aimed to analyze the mechanism of action of alpha mangostin on acetaldehyde induced liver fibrosis model on TGF-beta and ERK 1/2 pathways.	Acetaldehyde	81-93	mitogen-activated protein kinase 3	Homo sapiens	139-146
30424581-2	2018	Pathogenetic events are linked to the metabolism of ethanol and acetaldehyde as its first oxidation product generated via hepatic alcohol dehydrogenase (ADH) and the microsomal ethanol-oxidizing system (MEOS), which depends on cytochrome P450 2E1 (CYP 2E1), and is inducible by chronic alcohol use.	Acetaldehyde	64-76	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	227-246
30424581-2	2018	Pathogenetic events are linked to the metabolism of ethanol and acetaldehyde as its first oxidation product generated via hepatic alcohol dehydrogenase (ADH) and the microsomal ethanol-oxidizing system (MEOS), which depends on cytochrome P450 2E1 (CYP 2E1), and is inducible by chronic alcohol use.	Acetaldehyde	64-76	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	248-255
29616362-9	2018	CONCLUSION: The observed ALDH2-alcohol drinking interaction and the direct effect of ALDH2 Lys alleles may suggest the involvement of acetaldehyde in the development of gastric cancer.	Acetaldehyde	134-146	aldehyde dehydrogenase 2 family member	Homo sapiens	25-30
30058099-6	2018	In addition, the regulatory protein AcoR promoted the expression of this operon using acetaldehyde, a cleavage product of acetoin, as its direct effector.	Acetaldehyde	86-98	transcriptional regulator AcoR	Pseudomonas aeruginosa PAO1	36-40
29616362-9	2018	CONCLUSION: The observed ALDH2-alcohol drinking interaction and the direct effect of ALDH2 Lys alleles may suggest the involvement of acetaldehyde in the development of gastric cancer.	Acetaldehyde	134-146	aldehyde dehydrogenase 2 family member	Homo sapiens	85-90
30036570-5	2018	Treatment with 100 and 200 mg/kg AcH increased levels of salsolinol in both WT and Aldh2-KO mice, with 200 mg/kg AcH inducing a higher level of salsolinol in Aldh2-KO mice than in WT mice.	Acetaldehyde	33-36	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	83-88
30036570-5	2018	Treatment with 100 and 200 mg/kg AcH increased levels of salsolinol in both WT and Aldh2-KO mice, with 200 mg/kg AcH inducing a higher level of salsolinol in Aldh2-KO mice than in WT mice.	Acetaldehyde	113-116	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	158-163
30036570-0	2018	Acetaldehyde administration induces salsolinol formation in vivo in the dorsal striatum of Aldh2-knockout and C57BL/6N mice.	Acetaldehyde	0-12	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	91-96
30036570-6	2018	Treatment with 50 mg/kg AcH produced a small increase in salsolinol levels in Aldh2-KO mice, whereas no elevation of salsolinol was detected in WT mice.	Acetaldehyde	24-27	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	78-83
30036570-2	2018	This study aimed to investigate the effect of administration of AcH on dopamine (DA), DA-derived salsolinol and serotonin (5-HT) levels in the dorsal striatum of Aldh2-knockout (Aldh2-KO) and C57BL/6 N (WT) mice.	Acetaldehyde	64-67	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	162-167
29637262-13	2018	In multivariable analysis, the use of RF needle and BNP level was related to the incidence of ACE (OR = 0.499, 95% CI 0.270-0.922, P = 0.03 and OR = 1.005, 95% CI 1.000-1.010, P = 0.03).	Acetaldehyde	94-97	natriuretic peptide B	Homo sapiens	52-55
30188114-6	2018	In particular very high emission rates were estimated of two relevant indoor air pollutants, formaldehyde and acetaldehyde as 355 mug h-1 and 257 mug h-1 for 1 m2, respectively.	Acetaldehyde	110-122	H1.5 linker histone, cluster member	Homo sapiens	134-162
30186426-7	2018	Acetaldehyde presented a mesenchymal cell characteristic in hepatocytes, accompanied by an increased expression of mesenchymal markers, including vimentin and fibronectin, and decreased E-cadherin.	Acetaldehyde	0-12	vimentin	Homo sapiens	146-154
30186426-7	2018	Acetaldehyde presented a mesenchymal cell characteristic in hepatocytes, accompanied by an increased expression of mesenchymal markers, including vimentin and fibronectin, and decreased E-cadherin.	Acetaldehyde	0-12	fibronectin 1	Homo sapiens	159-170
30186426-7	2018	Acetaldehyde presented a mesenchymal cell characteristic in hepatocytes, accompanied by an increased expression of mesenchymal markers, including vimentin and fibronectin, and decreased E-cadherin.	Acetaldehyde	0-12	cadherin 1	Homo sapiens	186-196
30186426-8	2018	Baicalin and puerarin abrogated the increased expression of vimentin and fibronectin, and rescued E-cadherin expression in acetaldehyde-treated hepatocytes.	Acetaldehyde	123-135	cadherin 1	Homo sapiens	98-108
30186426-10	2018	A decreased expression of tight function markers, including ZO-1, occludin and claudin, were also found in the acetaldehyde-treated hepatocytes.	Acetaldehyde	111-123	tight junction protein 1	Homo sapiens	60-64
30186426-10	2018	A decreased expression of tight function markers, including ZO-1, occludin and claudin, were also found in the acetaldehyde-treated hepatocytes.	Acetaldehyde	111-123	occludin	Homo sapiens	66-74
29847918-9	2018	The model simulations suggest that slightly higher or similar ethanol elimination rates for ADH1B*2/*2 and ADH1B*3/*3 individuals compared with those for ADH1B*1/*1 individuals may result from higher hepatocellular acetaldehyde.	Acetaldehyde	215-227	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	92-97
29542129-8	2018	The diethylacetal and acetaldehyde average contents in 24 beer products were 11.83 and 4.36 mg L-1 respectively.	Acetaldehyde	22-34	immunoglobulin kappa variable 1-16	Homo sapiens	95-98
29859945-3	2018	Aldehyde dehydrogenase 1b1 (Aldh1b1) is the aldehyde dehydrogenase isoform with the second highest affinity for acetaldehyde after Aldh2, and is highly expressed in the intestine and liver.	Acetaldehyde	112-124	aldehyde dehydrogenase 1 family, member B1	Mus musculus	0-26
29859945-3	2018	Aldehyde dehydrogenase 1b1 (Aldh1b1) is the aldehyde dehydrogenase isoform with the second highest affinity for acetaldehyde after Aldh2, and is highly expressed in the intestine and liver.	Acetaldehyde	112-124	aldehyde dehydrogenase 1 family, member B1	Mus musculus	28-35
29859945-3	2018	Aldehyde dehydrogenase 1b1 (Aldh1b1) is the aldehyde dehydrogenase isoform with the second highest affinity for acetaldehyde after Aldh2, and is highly expressed in the intestine and liver.	Acetaldehyde	112-124	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	131-136
30636825-8	2018	In addition, ACE-treated mice showed a substantial reduction in acetylcholinesterase, D-amino acid oxidase enzyme activity, and nitrite levels which were elevated by the administration of MK-801.	Acetaldehyde	13-16	acetylcholinesterase	Mus musculus	64-84
29542129-6	2018	For both diethylacetal and acetaldehyde analyses, the limit of detection was 0.005 mg L-1 with relative standard deviation &lt; 5.5%.	Acetaldehyde	27-39	immunoglobulin kappa variable 1-16	Homo sapiens	86-89
29847918-9	2018	The model simulations suggest that slightly higher or similar ethanol elimination rates for ADH1B*2/*2 and ADH1B*3/*3 individuals compared with those for ADH1B*1/*1 individuals may result from higher hepatocellular acetaldehyde.	Acetaldehyde	215-227	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	107-112
29847918-9	2018	The model simulations suggest that slightly higher or similar ethanol elimination rates for ADH1B*2/*2 and ADH1B*3/*3 individuals compared with those for ADH1B*1/*1 individuals may result from higher hepatocellular acetaldehyde.	Acetaldehyde	215-227	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	107-112
29912589-4	2018	Epidermal growth factor receptor (EGFR) signaling mediates the L. plantarum-mediated protection of tight junctions (TJs) and barrier function from acetaldehyde, the EtOH metabolite, in Caco-2 cell monolayers.	Acetaldehyde	147-159	epidermal growth factor receptor	Mus musculus	34-38
29638019-2	2018	Upon alcohol consumption, alcohol is sequentially oxidized to acetaldehyde and acetate by the endogenous alcohol dehydrogenase and aldehyde dehydrogenase, respectively.	Acetaldehyde	62-74	aldo-keto reductase family 1, member A1 (aldehyde reductase)	Mus musculus	105-126
29579152-0	2018	Cardioprotection induced by a brief exposure to acetaldehyde: role of aldehyde dehydrogenase 2.	Acetaldehyde	48-60	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	70-94
29579152-4	2018	The ALDH2*2 mice have impaired acetaldehyde clearance, recapitulating the human phenotype.	Acetaldehyde	31-43	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	4-9
29579152-7	2018	However, acetaldehyde pre-treatment of hearts of ALDH2*2 mice resulted in a three-fold increase in cardiac acetaldehyde levels and exacerbated I/R injury.	Acetaldehyde	9-21	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	49-54
29579152-7	2018	However, acetaldehyde pre-treatment of hearts of ALDH2*2 mice resulted in a three-fold increase in cardiac acetaldehyde levels and exacerbated I/R injury.	Acetaldehyde	107-119	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	49-54
29579152-8	2018	Therefore, exogenous acetaldehyde appears to have a bimodal effect in I/R, depending on the ALDH2 genotype.	Acetaldehyde	21-33	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	92-97
29579152-11	2018	Conclusion: Taken together, our findings suggest that low levels of acetaldehyde are cardioprotective whereas high levels are damaging in an ex vivo model of I/R injury and that ALDH2 is a major, but not the only, regulator of cardiac acetaldehyde levels and protection from I/R.	Acetaldehyde	68-80	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	178-183
29579152-11	2018	Conclusion: Taken together, our findings suggest that low levels of acetaldehyde are cardioprotective whereas high levels are damaging in an ex vivo model of I/R injury and that ALDH2 is a major, but not the only, regulator of cardiac acetaldehyde levels and protection from I/R.	Acetaldehyde	235-247	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	178-183
29651717-1	2018	Liver mitochondrial aldehyde dehydrogenase 2 (ALDH2) enzyme is responsible for the rapid conversion of acetaldehyde to acetic acid.	Acetaldehyde	103-115	aldehyde dehydrogenase 2 family member	Homo sapiens	46-51
29638019-2	2018	Upon alcohol consumption, alcohol is sequentially oxidized to acetaldehyde and acetate by the endogenous alcohol dehydrogenase and aldehyde dehydrogenase, respectively.	Acetaldehyde	62-74	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	131-153
29156373-2	2018	Breakdown of acetaldehyde by aldehyde dehydrogenase 2 (ALDH2) in the mitochondria consumes NAD+ and generates reactive oxygen/nitrogen species, which represents a fundamental mechanism in the pathogenesis of alcoholic liver disease (ALD).	Acetaldehyde	13-25	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	29-53
29482068-1	2018	Aldehyde dehydrogenase 2 (ALDH2) is the enzyme that degrades and detoxifies the acetaldehyde produced by alcohol metabolism.	Acetaldehyde	80-92	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	0-24
29482068-1	2018	Aldehyde dehydrogenase 2 (ALDH2) is the enzyme that degrades and detoxifies the acetaldehyde produced by alcohol metabolism.	Acetaldehyde	80-92	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	26-31
29506696-0	2018	Alcohol puts the heart under pressure: Acetaldehyde activates a localized renin angiotensin aldosterone system within the myocardium in alcoholic cardiomyopathy.	Acetaldehyde	39-51	renin	Homo sapiens	74-79
29483359-0	2018	FHR5 Binds to Laminins, Uses Separate C3b and Surface-Binding Sites, and Activates Complement on Malondialdehyde-Acetaldehyde Surfaces.	Acetaldehyde	113-125	complement factor H related 5	Homo sapiens	0-4
29483359-3	2018	Furthermore, we identify malondialdehyde-acetaldehyde (MAA) epitopes, which are exposed on the surface of human necrotic cells (Homo sapiens), as new FHR5 ligands.	Acetaldehyde	41-53	complement factor H related 5	Homo sapiens	150-154
29156373-9	2018	In addition, alcohol-increased circulating acetaldehyde levels were accompanied by reduced intestinal ALDH activity and impaired intestinal barrier.	Acetaldehyde	43-55	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	102-106
29156373-13	2018	This study demonstrated that speeding up acetaldehyde clearance by preserving ALDH2 activity critically mediates the beneficial effect of MitoQ on alcohol-induced pathogenesis at the gut-liver axis.	Acetaldehyde	41-53	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	78-83
29248712-6	2018	Furthermore, the ADH5 variant showed a significant interaction with drinking and the genetic variant near ALDH2 encoding the enzyme oxidizing acetaldehyde, a carcinogenic product resulted from alcohol oxidation catalyzed by ADHs.	Acetaldehyde	142-154	alcohol dehydrogenase 5 (class III), chi polypeptide	Homo sapiens	17-21
29248712-6	2018	Furthermore, the ADH5 variant showed a significant interaction with drinking and the genetic variant near ALDH2 encoding the enzyme oxidizing acetaldehyde, a carcinogenic product resulted from alcohol oxidation catalyzed by ADHs.	Acetaldehyde	142-154	aldehyde dehydrogenase 2 family member	Homo sapiens	106-111
29623947-1	2018	BACKGROUND Human mitochondrial aldehyde dehydrogenase 2 (ALDH2) plays a critical role in the detoxification of the ethanol metabolite acetaldehyde.	Acetaldehyde	134-146	aldehyde dehydrogenase 2 family member	Homo sapiens	57-62
29156373-2	2018	Breakdown of acetaldehyde by aldehyde dehydrogenase 2 (ALDH2) in the mitochondria consumes NAD+ and generates reactive oxygen/nitrogen species, which represents a fundamental mechanism in the pathogenesis of alcoholic liver disease (ALD).	Acetaldehyde	13-25	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	55-60
29156373-7	2018	It also reversed alcohol-reduced hepatic ALDH activity and accelerated acetaldehyde clearance through modulating ALDH2 cysteine S-nitrosylation, tyrosine nitration and 4-hydroxynonenol adducts formation.	Acetaldehyde	71-83	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	113-118
29582627-1	2018	Alcohol detoxification is governed by ADH1B,ALDH2, GSTM1 and GSTT1 genes that encode functional enzymes which are coordinated with each other to removehighly toxic metabolites i.e. acetaldehyde as well as reactive oxygen species generated through detoxification processes.Some communities in the population appears to be at greater risk for development of the liver cancer due to geneticpredispositions.	Acetaldehyde	181-193	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	38-43
29582627-1	2018	Alcohol detoxification is governed by ADH1B,ALDH2, GSTM1 and GSTT1 genes that encode functional enzymes which are coordinated with each other to removehighly toxic metabolites i.e. acetaldehyde as well as reactive oxygen species generated through detoxification processes.Some communities in the population appears to be at greater risk for development of the liver cancer due to geneticpredispositions.	Acetaldehyde	181-193	aldehyde dehydrogenase 2 family member	Homo sapiens	44-49
29582627-1	2018	Alcohol detoxification is governed by ADH1B,ALDH2, GSTM1 and GSTT1 genes that encode functional enzymes which are coordinated with each other to removehighly toxic metabolites i.e. acetaldehyde as well as reactive oxygen species generated through detoxification processes.Some communities in the population appears to be at greater risk for development of the liver cancer due to geneticpredispositions.	Acetaldehyde	181-193	glutathione S-transferase mu 1	Homo sapiens	51-56
29582627-1	2018	Alcohol detoxification is governed by ADH1B,ALDH2, GSTM1 and GSTT1 genes that encode functional enzymes which are coordinated with each other to removehighly toxic metabolites i.e. acetaldehyde as well as reactive oxygen species generated through detoxification processes.Some communities in the population appears to be at greater risk for development of the liver cancer due to geneticpredispositions.	Acetaldehyde	181-193	glutathione S-transferase theta 1	Homo sapiens	61-66
28731573-1	2018	This study aims to evaluate the effect of ADH1B and ADH7 genotypes on blood acetaldehyde and ethanol levels after alcohol ingestion, and to measure the genotoxic effect of smoking and ethanol on the buccal cells, also controlling for ADH variants.	Acetaldehyde	76-88	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	42-47
29570189-4	2018	Under the influence of alcohol-dehydrogenase, ethanol will metabolise to acetaldehyde, which is a known carcinogen.	Acetaldehyde	73-85	aldo-keto reductase family 1 member A1	Homo sapiens	23-44
29390059-2	2018	ADH enzymes oxidize ethanol to acetaldehyde, both of which are human carcinogens.	Acetaldehyde	31-43	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	0-3
28731573-1	2018	This study aims to evaluate the effect of ADH1B and ADH7 genotypes on blood acetaldehyde and ethanol levels after alcohol ingestion, and to measure the genotoxic effect of smoking and ethanol on the buccal cells, also controlling for ADH variants.	Acetaldehyde	76-88	alcohol dehydrogenase 1A (class I), alpha polypeptide	Homo sapiens	42-45
28731573-8	2018	Corresponding acetaldehyde levels were 1.5muM (IQR 0.7-2.6) for ADH1B GG genotype and 1.6muM (IQR 1.5-1.7) for ADH1B CG/GG genotype.	Acetaldehyde	14-26	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	64-69
28731573-8	2018	Corresponding acetaldehyde levels were 1.5muM (IQR 0.7-2.6) for ADH1B GG genotype and 1.6muM (IQR 1.5-1.7) for ADH1B CG/GG genotype.	Acetaldehyde	14-26	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	111-116
28731573-10	2018	Corresponding acetaldehyde levels were 1.5 muM (IQR 0.7-2.6) for ADH7 CC genotype and 1.5 muM (IQR 1.4-1.6) for ADH7 CG/GG genotypes.	Acetaldehyde	14-26	latexin	Homo sapiens	43-46
28731573-10	2018	Corresponding acetaldehyde levels were 1.5 muM (IQR 0.7-2.6) for ADH7 CC genotype and 1.5 muM (IQR 1.4-1.6) for ADH7 CG/GG genotypes.	Acetaldehyde	14-26	alcohol dehydrogenase 7 (class IV), mu or sigma polypeptide	Homo sapiens	65-69
28731573-10	2018	Corresponding acetaldehyde levels were 1.5 muM (IQR 0.7-2.6) for ADH7 CC genotype and 1.5 muM (IQR 1.4-1.6) for ADH7 CG/GG genotypes.	Acetaldehyde	14-26	latexin	Homo sapiens	90-93
28731573-10	2018	Corresponding acetaldehyde levels were 1.5 muM (IQR 0.7-2.6) for ADH7 CC genotype and 1.5 muM (IQR 1.4-1.6) for ADH7 CG/GG genotypes.	Acetaldehyde	14-26	alcohol dehydrogenase 7 (class IV), mu or sigma polypeptide	Homo sapiens	112-116
29431026-1	2018	INTRODUCTION: Mitochondrial aldehyde dehydrogenase (ALDH-2) plays a major role in the ethanol detoxification pathway by removing acetaldehyde.	Acetaldehyde	129-141	aldehyde dehydrogenase 2 family member	Homo sapiens	52-58
29247577-1	2018	The aldehyde dehydrogenase 2 (ALDH2) polymorphism rs671 (Glu504Lys) causes ALDH2 inactivation and adverse acetaldehyde exposure among Asians, but little is known of the association between alcohol consumption and rs671 and ovarian cancer (OvCa) in Asians.	Acetaldehyde	106-118	aldehyde dehydrogenase 2 family member	Homo sapiens	4-28
29380601-0	2018	Fiber-Optic Bio-sniffer (Biochemical Gas Sensor) Using Reverse Reaction of Alcohol Dehydrogenase for Exhaled Acetaldehyde.	Acetaldehyde	109-121	aldo-keto reductase family 1 member A1	Homo sapiens	75-96
29380601-4	2018	In the AcH bio-sniffer, a reverse reaction of alcohol dehydrogenase (ADH) was employed for reducing AcH to ethanol and simultaneously consuming a coenzyme, reduced form of nicotinamide adenine dinucleotide (NADH).	Acetaldehyde	7-10	aldo-keto reductase family 1 member A1	Homo sapiens	46-67
29359564-0	2018	Fluorometric Sniff-Cam (Gas-Imaging System) Utilizing Alcohol Dehydrogenase for Imaging Concentration Distribution of Acetaldehyde in Breath and Transdermal Vapor after Drinking.	Acetaldehyde	118-130	aldo-keto reductase family 1 member A1	Homo sapiens	54-75
29359564-4	2018	A reverse reaction of ADH was employed for detection of gaseous AcH where a relationship between fluorescence intensity from nicotinamide adenine dinucleotide and the concentration of AcH was inversely proportional; thus, the concentration distribution of AcH was measured by detecting the fluorescence decrease.	Acetaldehyde	64-67	aldo-keto reductase family 1 member A1	Homo sapiens	22-25
29359564-4	2018	A reverse reaction of ADH was employed for detection of gaseous AcH where a relationship between fluorescence intensity from nicotinamide adenine dinucleotide and the concentration of AcH was inversely proportional; thus, the concentration distribution of AcH was measured by detecting the fluorescence decrease.	Acetaldehyde	184-187	aldo-keto reductase family 1 member A1	Homo sapiens	22-25
29380601-4	2018	In the AcH bio-sniffer, a reverse reaction of alcohol dehydrogenase (ADH) was employed for reducing AcH to ethanol and simultaneously consuming a coenzyme, reduced form of nicotinamide adenine dinucleotide (NADH).	Acetaldehyde	7-10	aldo-keto reductase family 1 member A1	Homo sapiens	69-72
29380601-4	2018	In the AcH bio-sniffer, a reverse reaction of alcohol dehydrogenase (ADH) was employed for reducing AcH to ethanol and simultaneously consuming a coenzyme, reduced form of nicotinamide adenine dinucleotide (NADH).	Acetaldehyde	100-103	aldo-keto reductase family 1 member A1	Homo sapiens	46-67
29380601-4	2018	In the AcH bio-sniffer, a reverse reaction of alcohol dehydrogenase (ADH) was employed for reducing AcH to ethanol and simultaneously consuming a coenzyme, reduced form of nicotinamide adenine dinucleotide (NADH).	Acetaldehyde	100-103	aldo-keto reductase family 1 member A1	Homo sapiens	69-72
29380601-5	2018	The concentration of AcH can be quantified by fluorescence detection of NADH that was consumed by reverse reaction of ADH.	Acetaldehyde	21-24	aldo-keto reductase family 1 member A1	Homo sapiens	73-76
29380601-10	2018	Also, the AcH bio-sniffer exhibited a high selectivity to gaseous AcH based on the specificity of ADH.	Acetaldehyde	10-13	aldo-keto reductase family 1 member A1	Homo sapiens	98-101
29380601-13	2018	As a result, a significant difference of AcH concentration between subjects with different aldehyde dehydrogenase type 2 (ALDH2) phenotypes was observed.	Acetaldehyde	41-44	aldehyde dehydrogenase 2 family member	Homo sapiens	91-120
29380601-13	2018	As a result, a significant difference of AcH concentration between subjects with different aldehyde dehydrogenase type 2 (ALDH2) phenotypes was observed.	Acetaldehyde	41-44	aldehyde dehydrogenase 2 family member	Homo sapiens	122-127
29247577-1	2018	The aldehyde dehydrogenase 2 (ALDH2) polymorphism rs671 (Glu504Lys) causes ALDH2 inactivation and adverse acetaldehyde exposure among Asians, but little is known of the association between alcohol consumption and rs671 and ovarian cancer (OvCa) in Asians.	Acetaldehyde	106-118	aldehyde dehydrogenase 2 family member	Homo sapiens	30-35
29247577-9	2018	Because the rs671 Lys allele causes ALDH2 inactivation leading to increased acetaldehyde exposure, the observed inverse genetic association with mucinous ovarian cancer is inferred to mean that alcohol intake may be a risk factor for this histotype.	Acetaldehyde	76-88	aldehyde dehydrogenase 2 family member	Homo sapiens	36-41
29352167-0	2018	SREBP1c mediates the effect of acetaldehyde on Cidea expression in Alcoholic fatty liver Mice.	Acetaldehyde	31-43	sterol regulatory element binding transcription factor 1	Mus musculus	0-7
29348025-4	2018	After multiple rounds of screening against malondialdehyde-acetaldehyde (MAA) epitopes, the Fab LA25 containing minimal nontemplated insertions in the CDR3 region was identified and characterized.	Acetaldehyde	59-71	FA complementation group B	Homo sapiens	92-95
29352167-11	2018	Overall, our findings suggest that Cidea is highly associated with alcoholic fatty liver disease and Cidea expression is specifically induced by acetaldehyde, and this up-regulation is most likely mediated by SREBP1c.	Acetaldehyde	145-157	cell death-inducing DNA fragmentation factor, alpha subunit-like effector A	Mus musculus	101-106
29352167-0	2018	SREBP1c mediates the effect of acetaldehyde on Cidea expression in Alcoholic fatty liver Mice.	Acetaldehyde	31-43	cell death-inducing DNA fragmentation factor, alpha subunit-like effector A	Mus musculus	47-52
29352167-8	2018	Cidea expression was elevated in AML12 cells exposed to 100uM acetaldehyde.	Acetaldehyde	62-74	cell death-inducing DNA fragmentation factor, alpha subunit-like effector A	Mus musculus	0-5
29352167-9	2018	Interestingly, Dual-luciferase reporter gene assay showed that 100 uM acetaldehyde led to the activation of Cidea reporter gene plasmid which containing SRE element.	Acetaldehyde	70-82	cell death-inducing DNA fragmentation factor, alpha subunit-like effector A	Mus musculus	108-113
29352167-10	2018	What"s more, the knockdown of SREBP1c suppressed acetaldehyde-induced Cidea expression.	Acetaldehyde	49-61	sterol regulatory element binding transcription factor 1	Mus musculus	30-37
29182313-1	2018	2-Deoxy-d-ribose-5-phosphate aldolase (DERA) is a biocatalyst that is capable of converting acetaldehyde and a second aldehyde as acceptor into enantiomerically pure mono- and diyhydroxyaldehydes, which are important structural motifs in a number of pharmaceutically active compounds.	Acetaldehyde	92-104	deoxyribose-phosphate aldolase	Homo sapiens	0-37
29352167-10	2018	What"s more, the knockdown of SREBP1c suppressed acetaldehyde-induced Cidea expression.	Acetaldehyde	49-61	cell death-inducing DNA fragmentation factor, alpha subunit-like effector A	Mus musculus	70-75
29352167-11	2018	Overall, our findings suggest that Cidea is highly associated with alcoholic fatty liver disease and Cidea expression is specifically induced by acetaldehyde, and this up-regulation is most likely mediated by SREBP1c.	Acetaldehyde	145-157	cell death-inducing DNA fragmentation factor, alpha subunit-like effector A	Mus musculus	35-40
29321611-7	2018	RA production by hRALDH2 is efficiently inhibited by acetaldehyde but not by ethanol itself.	Acetaldehyde	53-65	aldehyde dehydrogenase 1 family member A2	Homo sapiens	17-24
29321611-4	2018	Pharmacological inhibition of the embryonic alcohol dehydrogenase activity, prevents the oxidation of ethanol to acetaldehyde that in turn functions as a RALDH2 inhibitor.	Acetaldehyde	113-125	aldehyde dehydrogenase 1 family member A2	Homo sapiens	154-160
28803127-4	2017	We have previously demonstrated that protein adducts formed by the interaction of malondialdehyde (MDA) and acetaldehyde (AA), known as MAA-protein adducts, are present in diseased tissues of individuals with rheumatoid arthritis (RA) or CVD.	Acetaldehyde	108-120	MAA	Homo sapiens	136-139
29321611-5	2018	Acetaldehyde-mediated reduction of RA can be rescued by RALDH2 or retinaldehyde supplementation.	Acetaldehyde	0-12	aldehyde dehydrogenase 1 family member A2	Homo sapiens	56-62
29321611-6	2018	Enzymatic kinetic analysis of human RALDH2 shows a preference for acetaldehyde as a substrate over retinaldehyde.	Acetaldehyde	66-78	aldehyde dehydrogenase 1 family member A2	Homo sapiens	36-42
29303995-4	2018	A point mutation in the aldehyde dehydrogenase 2 gene has randomized millions of alcohol consumers to markedly increased local ACH exposure via saliva and gastric juice, which is associated with a manifold risk for upper GI tract cancers.	Acetaldehyde	127-130	aldehyde dehydrogenase 2 family member	Homo sapiens	24-48
29518171-2	2018	Aldehyde dehydrogenase (ALDH) catalyzes the critical step of ethanol metabolism, i.e. transformation of toxic acetaldehyde to acetic acid.	Acetaldehyde	110-122	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	24-28
30362100-3	2018	In tissues, ethanol is metabolized to acetaldehyde (mainly by alcohol dehydrogenase and cytochrome p450 2E1) and subsequently to acetic acid by aldehyde dehydrogenases.	Acetaldehyde	38-50	cytochrome P450, family 2, subfamily e, polypeptide 1	Mus musculus	88-107
28864499-2	2017	Both enzymes metabolize ethanol into acetaldehyde, but CYP2E1 activity also results in the production of reactive oxygen species (ROS) that promote oxidative stress.	Acetaldehyde	37-49	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	55-61
29093526-2	2017	SMOX is induced by a variety of stimuli including bacterial infection, polyamine analogues and acetaldehyde exposure.	Acetaldehyde	95-107	spermine oxidase	Homo sapiens	0-4
29693039-16	2018	Both HCV and acetaldehyde increase JMJD6 levels, thereby impairing STAT1 methylation and innate immunity protection in hepatocytes exposed to the virus and/or alcohol.	Acetaldehyde	13-25	jumonji domain containing 6, arginine demethylase and lysine hydroxylase	Homo sapiens	35-40
29693039-16	2018	Both HCV and acetaldehyde increase JMJD6 levels, thereby impairing STAT1 methylation and innate immunity protection in hepatocytes exposed to the virus and/or alcohol.	Acetaldehyde	13-25	signal transducer and activator of transcription 1	Homo sapiens	67-72
29195668-3	2017	Point mutation in ALDH2 gene proves the causal relationship between acetaldehyde and upper digestive tract cancer in humans.	Acetaldehyde	68-80	aldehyde dehydrogenase 2 family member	Homo sapiens	18-23
28868538-5	2017	The syn conformer of vinyl alcohol is predicted to be lower in energy than the anti conformer by 1.1 kcal mol-1.	Acetaldehyde	21-34	synemin	Homo sapiens	4-7
28729482-0	2017	BRCA1 and BRCA2 tumor suppressors protect against endogenous acetaldehyde toxicity.	Acetaldehyde	61-73	BRCA1 DNA repair associated	Homo sapiens	0-5
28729482-0	2017	BRCA1 and BRCA2 tumor suppressors protect against endogenous acetaldehyde toxicity.	Acetaldehyde	61-73	BRCA2 DNA repair associated	Homo sapiens	10-15
28729482-2	2017	Endogenous acetaldehyde, a product of cellular metabolism, is a potent source of DNA damage, particularly toxic to cells and mice lacking the FA protein FANCD2.	Acetaldehyde	11-23	Fanconi anemia, complementation group D2	Mus musculus	153-159
28729482-4	2017	We demonstrate that inactivation of HR factors BRCA1, BRCA2, or RAD51 hypersensitizes cells to acetaldehyde treatment, in spite of the FA pathway being functional.	Acetaldehyde	95-107	BRCA1 DNA repair associated	Homo sapiens	47-52
28729482-4	2017	We demonstrate that inactivation of HR factors BRCA1, BRCA2, or RAD51 hypersensitizes cells to acetaldehyde treatment, in spite of the FA pathway being functional.	Acetaldehyde	95-107	BRCA2 DNA repair associated	Homo sapiens	54-59
28729482-4	2017	We demonstrate that inactivation of HR factors BRCA1, BRCA2, or RAD51 hypersensitizes cells to acetaldehyde treatment, in spite of the FA pathway being functional.	Acetaldehyde	95-107	RAD51 recombinase	Homo sapiens	64-69
28729482-8	2017	Hypersensitivity of cells lacking BRCA2 to acetaldehyde stems from accumulation of toxic replication-associated DNA damage, leading to checkpoint activation, G2/M arrest, and cell death.	Acetaldehyde	43-55	BRCA2 DNA repair associated	Homo sapiens	34-39
28729482-9	2017	Acetaldehyde-arrested replication forks require BRCA2 and FANCD2 for protection against MRE11-dependent degradation.	Acetaldehyde	0-12	BRCA2 DNA repair associated	Homo sapiens	48-53
28729482-9	2017	Acetaldehyde-arrested replication forks require BRCA2 and FANCD2 for protection against MRE11-dependent degradation.	Acetaldehyde	0-12	FA complementation group D2	Homo sapiens	58-64
28729482-9	2017	Acetaldehyde-arrested replication forks require BRCA2 and FANCD2 for protection against MRE11-dependent degradation.	Acetaldehyde	0-12	MRE11 homolog, double strand break repair nuclease	Homo sapiens	88-93
28729482-10	2017	Importantly, acetaldehyde specifically inhibits in vivo the growth of BRCA1/2-deficient tumors and ex vivo in patient-derived tumor xenograft cells (PDTCs), including those that are resistant to poly (ADP-ribose) polymerase (PARP) inhibitors.	Acetaldehyde	13-25	poly(ADP-ribose) polymerase 1	Homo sapiens	195-223
28729482-10	2017	Importantly, acetaldehyde specifically inhibits in vivo the growth of BRCA1/2-deficient tumors and ex vivo in patient-derived tumor xenograft cells (PDTCs), including those that are resistant to poly (ADP-ribose) polymerase (PARP) inhibitors.	Acetaldehyde	13-25	poly(ADP-ribose) polymerase 1	Homo sapiens	225-229
28729482-11	2017	The work presented here therefore identifies acetaldehyde metabolism as a potential therapeutic target for the selective elimination of BRCA1/2-deficient cells and tumors.	Acetaldehyde	45-57	BRCA1 DNA repair associated	Homo sapiens	136-141
28821405-0	2017	Benzyl isothiocyanate ameliorates acetaldehyde-induced cytotoxicity by enhancing aldehyde dehydrogenase activity in murine hepatoma Hepa1c1c7 cells.	Acetaldehyde	34-46	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	81-103
28821405-7	2017	The pretreatment of BITC completely mitigated the acetaldehyde-induced cytotoxicity, which was impaired by silencing Nrf2.	Acetaldehyde	50-62	nuclear factor, erythroid derived 2, like 2	Mus musculus	117-121
28821405-8	2017	The present study demonstrated that BITC has been identified as a potential inducer of the total ALDH activity to prevent the acetaldehyde-induced cytotoxicity.	Acetaldehyde	126-138	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	97-101
28735060-1	2017	Alcohol dehydrogenases (ADH) are key enzymes of ethanol metabolism that mediate its oxidation to acetaldehyde.	Acetaldehyde	97-109	alcohol dehydrogenase 1C (class I), gamma polypeptide	Rattus norvegicus	0-22
28735060-1	2017	Alcohol dehydrogenases (ADH) are key enzymes of ethanol metabolism that mediate its oxidation to acetaldehyde.	Acetaldehyde	97-109	alcohol dehydrogenase 1C (class I), gamma polypeptide	Rattus norvegicus	24-27
28916784-5	2017	Accumulation of YOX1 mRNA causes aberrant downregulation of a network of genes critical for DNA replication stress resistance and leads to toxic acetaldehyde accumulation.	Acetaldehyde	145-157	Yox1p	Saccharomyces cerevisiae S288C	16-20
28347769-0	2017	Probing the acetaldehyde-sensitivity of 2-deoxy-ribose-5-phosphate aldolase (DERA) leads to resistant variants.	Acetaldehyde	12-24	deoxyribose-phosphate aldolase	Homo sapiens	77-81
28347769-1	2017	The 2-deoxy-d-ribose-5-phosphate aldolase (DERA) is a synthetically attractive enzyme because of its ability to perform CC-couplings stereoselectively, the enzyme uses acetaldehyde as nucleophile and thus produces true aldols rather than ketols, and may add two acetaldehyde molecules onto one electrophile.	Acetaldehyde	168-180	deoxyribose-phosphate aldolase	Homo sapiens	4-41
28347769-1	2017	The 2-deoxy-d-ribose-5-phosphate aldolase (DERA) is a synthetically attractive enzyme because of its ability to perform CC-couplings stereoselectively, the enzyme uses acetaldehyde as nucleophile and thus produces true aldols rather than ketols, and may add two acetaldehyde molecules onto one electrophile.	Acetaldehyde	168-180	deoxyribose-phosphate aldolase	Homo sapiens	43-47
28347769-1	2017	The 2-deoxy-d-ribose-5-phosphate aldolase (DERA) is a synthetically attractive enzyme because of its ability to perform CC-couplings stereoselectively, the enzyme uses acetaldehyde as nucleophile and thus produces true aldols rather than ketols, and may add two acetaldehyde molecules onto one electrophile.	Acetaldehyde	262-274	deoxyribose-phosphate aldolase	Homo sapiens	4-41
28347769-1	2017	The 2-deoxy-d-ribose-5-phosphate aldolase (DERA) is a synthetically attractive enzyme because of its ability to perform CC-couplings stereoselectively, the enzyme uses acetaldehyde as nucleophile and thus produces true aldols rather than ketols, and may add two acetaldehyde molecules onto one electrophile.	Acetaldehyde	262-274	deoxyribose-phosphate aldolase	Homo sapiens	43-47
28347769-2	2017	However, DERA produces crotonaldehyde as side reaction from acetaldehyde which is then an irreversible inhibitor forming a covalent Michael-adduct within the active site in particular with cysteine 47 (Dick et al., 2016).	Acetaldehyde	60-72	deoxyribose-phosphate aldolase	Homo sapiens	9-13
28891965-3	2017	Acetaldehyde is produced endogenously by alcohol metabolism and is catalyzed by aldehyde dehydrogenase 2 (ALDH2).	Acetaldehyde	0-12	aldehyde dehydrogenase 2 family member	Homo sapiens	80-104
28891965-3	2017	Acetaldehyde is produced endogenously by alcohol metabolism and is catalyzed by aldehyde dehydrogenase 2 (ALDH2).	Acetaldehyde	0-12	aldehyde dehydrogenase 2 family member	Homo sapiens	106-111
28891965-4	2017	Alcohol consumption increases blood and salivary acetaldehyde levels, especially in individuals with ALDH2 polymorphisms, which are highly associated with the risk of squamous cell carcinomas in the upper aerodigestive tract.	Acetaldehyde	49-61	aldehyde dehydrogenase 2 family member	Homo sapiens	101-106
27840306-1	2017	Previous studies evidenced the beneficial effects of low-to-moderate alcohol consumption on cardiovascular system by activation of mitochondrial aldehyde dehydrogenase 2 (ALDH2), a key enzyme metabolizing acetaldehyde to innocuous acetic acid, in diabetic mice.	Acetaldehyde	205-217	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	171-176
28578603-1	2017	Most ethanol is broken down in the liver in two steps by alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH2) enzymes, which metabolize down ethanol into acetaldehyde and then acetate.	Acetaldehyde	164-176	aldehyde dehydrogenase 2 family member	Homo sapiens	113-118
28578603-2	2017	Some individuals from the Asian population who carry a mutation in the aldehyde dehydrogenase gene (ALDH2*2) cannot metabolize acetaldehyde as efficiently, producing strong effects, including facial flushing, dizziness, hypotension, and palpitations.	Acetaldehyde	127-139	aldehyde dehydrogenase 2 family member	Homo sapiens	100-105
28098394-6	2017	The inactive ALDH2 provides its protective effect through the accumulation of acetaldehyde after consuming alcohol, resulting in unpleasant effects, and heightened sensitivity to alcohol.	Acetaldehyde	78-90	aldehyde dehydrogenase 2 family member	Homo sapiens	13-18
28655148-3	2017	Moreover, CAT activity contributes to the transformation of ethanol to acetaldehyde, a toxic intermediate product of ethanol metabolism, which has been associated with pancreatic damage.	Acetaldehyde	71-83	catalase	Homo sapiens	10-13
28667748-3	2017	Therefore, we elucidated the roles of alcohol dehydrogenase (ADH), cytochrome P4502E1 (CYP2E1), and catalase, which catalyze alcohol oxidation to acetaldehyde, in these alcohol-evoked biochemical and hemodynamic responses in proestrus rats.	Acetaldehyde	146-158	cytochrome P450, family 2, subfamily e, polypeptide 1	Rattus norvegicus	87-93
28667748-3	2017	Therefore, we elucidated the roles of alcohol dehydrogenase (ADH), cytochrome P4502E1 (CYP2E1), and catalase, which catalyze alcohol oxidation to acetaldehyde, in these alcohol-evoked biochemical and hemodynamic responses in proestrus rats.	Acetaldehyde	146-158	catalase	Rattus norvegicus	100-108
28500264-5	2017	This results from an initial translocation of protein kinase C subtype-epsilon and subsequent activation of aldehyde dehydrogenase type 2 (ALDH2), culminating in the elimination of the MC-degranulating effects of acetaldehyde and other toxic species produced during I/R.	Acetaldehyde	213-225	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	108-137
28584078-13	2017	We found that acetaldehyde and NF-kappaB pathways regulate HDAC11 levels.	Acetaldehyde	14-26	histone deacetylase 11	Mus musculus	59-65
28500264-5	2017	This results from an initial translocation of protein kinase C subtype-epsilon and subsequent activation of aldehyde dehydrogenase type 2 (ALDH2), culminating in the elimination of the MC-degranulating effects of acetaldehyde and other toxic species produced during I/R.	Acetaldehyde	213-225	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	139-144
28540979-2	2017	Aldehyde dehydrogenase 2 (ALDH2) is a key enzyme in alcohol metabolism that degrades acetaldehyde to nontoxic acetic acid.	Acetaldehyde	85-97	aldehyde dehydrogenase 2 family member	Homo sapiens	0-24
28769774-2	2017	Fenofibrate is a peroxisome proliferator-activated receptor alpha (PPARalpha) agonist, which induces the proliferation of peroxisomes in the liver, leading to increases in catalase levels that result in acetaldehyde accumulation at aversive levels in the blood when animals consume ethanol.	Acetaldehyde	203-215	peroxisome proliferator activated receptor alpha	Rattus norvegicus	17-65
28769774-2	2017	Fenofibrate is a peroxisome proliferator-activated receptor alpha (PPARalpha) agonist, which induces the proliferation of peroxisomes in the liver, leading to increases in catalase levels that result in acetaldehyde accumulation at aversive levels in the blood when animals consume ethanol.	Acetaldehyde	203-215	peroxisome proliferator activated receptor alpha	Rattus norvegicus	67-76
28769774-2	2017	Fenofibrate is a peroxisome proliferator-activated receptor alpha (PPARalpha) agonist, which induces the proliferation of peroxisomes in the liver, leading to increases in catalase levels that result in acetaldehyde accumulation at aversive levels in the blood when animals consume ethanol.	Acetaldehyde	203-215	catalase	Rattus norvegicus	172-180
28540979-2	2017	Aldehyde dehydrogenase 2 (ALDH2) is a key enzyme in alcohol metabolism that degrades acetaldehyde to nontoxic acetic acid.	Acetaldehyde	85-97	aldehyde dehydrogenase 2 family member	Homo sapiens	26-31
28540979-4	2017	A point mutation in the ALDH2 gene (the rs671 allele) yields an inactive form of ALDH2 that causes acetaldehyde accumulation in the body after alcohol consumption, thereby inhibiting normal alcohol metabolism.	Acetaldehyde	99-111	aldehyde dehydrogenase 2 family member	Homo sapiens	24-29
28540979-4	2017	A point mutation in the ALDH2 gene (the rs671 allele) yields an inactive form of ALDH2 that causes acetaldehyde accumulation in the body after alcohol consumption, thereby inhibiting normal alcohol metabolism.	Acetaldehyde	99-111	aldehyde dehydrogenase 2 family member	Homo sapiens	81-86
28540979-7	2017	Moreover, recent MR studies suggest that the ALDH2 variant has mechanistic effects on some disease outcomes or mortality through increased blood levels of acetaldehyde, showing differences therein between heterozygotes (ALDH2*2*2) and homozygotes (ALDH2*1*2) in those who consume alcohol.	Acetaldehyde	155-167	aldehyde dehydrogenase 2 family member	Homo sapiens	45-50
28540979-7	2017	Moreover, recent MR studies suggest that the ALDH2 variant has mechanistic effects on some disease outcomes or mortality through increased blood levels of acetaldehyde, showing differences therein between heterozygotes (ALDH2*2*2) and homozygotes (ALDH2*1*2) in those who consume alcohol.	Acetaldehyde	155-167	aldehyde dehydrogenase 2 family member	Homo sapiens	220-225
28540979-7	2017	Moreover, recent MR studies suggest that the ALDH2 variant has mechanistic effects on some disease outcomes or mortality through increased blood levels of acetaldehyde, showing differences therein between heterozygotes (ALDH2*2*2) and homozygotes (ALDH2*1*2) in those who consume alcohol.	Acetaldehyde	155-167	aldehyde dehydrogenase 2 family member	Homo sapiens	220-225
28383062-8	2017	NOX4 promoter was induced in HSC by acetaldehyde treatment, and NOX4 has significantly increased mRNA half-life of CCR2 and CCL2 in conjunction with Ser221 phosphorylation and cytoplasmic shuttling of HuR.	Acetaldehyde	36-48	NADPH oxidase 4	Mus musculus	0-4
28594837-3	2017	One of the most important genetic variants, in this regards, is the single nucleotide polymorphism (SNP) rs671 in ALDH2, the gene encoding the primary acetaldehyde metabolizing enzyme ALDH2.	Acetaldehyde	151-163	aldehyde dehydrogenase 2 family member	Homo sapiens	114-119
28594837-3	2017	One of the most important genetic variants, in this regards, is the single nucleotide polymorphism (SNP) rs671 in ALDH2, the gene encoding the primary acetaldehyde metabolizing enzyme ALDH2.	Acetaldehyde	151-163	aldehyde dehydrogenase 2 family member	Homo sapiens	184-189
28562643-4	2017	We confirmed the dysregulation of these two microRNAs in liver cell lines treated by alcohol and acetaldehyde, and showed that manipulation of miR-223-3p and miR-944 expression induces significant changes in cellular proliferation, sensitivity to doxorubicin, and the expression of both direct-binding and downstream mRNA targets.	Acetaldehyde	97-109	microRNA 944	Homo sapiens	158-165
28538665-2	2017	Ethanol is metabolized by alcohol dehydrogenases (ADH), catalase or cytochrome P450 2E1 (CYP2E1) to acetaldehyde, which is then further oxidized to acetate by aldehyde dehydrogenase (ALDH).	Acetaldehyde	100-112	catalase	Homo sapiens	56-64
28538665-2	2017	Ethanol is metabolized by alcohol dehydrogenases (ADH), catalase or cytochrome P450 2E1 (CYP2E1) to acetaldehyde, which is then further oxidized to acetate by aldehyde dehydrogenase (ALDH).	Acetaldehyde	100-112	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	68-87
28538665-2	2017	Ethanol is metabolized by alcohol dehydrogenases (ADH), catalase or cytochrome P450 2E1 (CYP2E1) to acetaldehyde, which is then further oxidized to acetate by aldehyde dehydrogenase (ALDH).	Acetaldehyde	100-112	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	89-95
28532411-3	2017	ALDH2 has the lowest Km for acetaldehyde among ALDH isozymes and detoxifies acetaldehydes in addition to other reactive aldehydes, such as 4-hydroxy-nonenal, malondialdehyde and acrolein produced from lipid peroxidation by reactive oxygen species (ROS).	Acetaldehyde	28-40	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	0-5
28532411-3	2017	ALDH2 has the lowest Km for acetaldehyde among ALDH isozymes and detoxifies acetaldehydes in addition to other reactive aldehydes, such as 4-hydroxy-nonenal, malondialdehyde and acrolein produced from lipid peroxidation by reactive oxygen species (ROS).	Acetaldehyde	28-40	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	0-4
28532411-3	2017	ALDH2 has the lowest Km for acetaldehyde among ALDH isozymes and detoxifies acetaldehydes in addition to other reactive aldehydes, such as 4-hydroxy-nonenal, malondialdehyde and acrolein produced from lipid peroxidation by reactive oxygen species (ROS).	Acetaldehyde	76-89	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	0-5
28532411-3	2017	ALDH2 has the lowest Km for acetaldehyde among ALDH isozymes and detoxifies acetaldehydes in addition to other reactive aldehydes, such as 4-hydroxy-nonenal, malondialdehyde and acrolein produced from lipid peroxidation by reactive oxygen species (ROS).	Acetaldehyde	76-89	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	0-4
26886278-3	2017	Alcohol is oxidized primarily by alcohol dehydrogenase (ADH) to acetaldehyde, a substance capable of initiating carcinogenesis by forming adducts with proteins and DNA and causing mutations.	Acetaldehyde	64-76	aldo-keto reductase family 1 member A1	Homo sapiens	56-59
26886278-8	2017	ADH and ALDH can play also a crucial regulatory role in initiation and progression of malignant diseases by participation in retinoic acid synthesis and elimination of toxic acetaldehyde.	Acetaldehyde	174-186	aldo-keto reductase family 1 member A1	Homo sapiens	0-3
28027570-7	2017	We also found that ALDH2 altered the redox status of cells by regulating acetaldehyde levels and that it further activated the AMP-activated protein kinase (AMPK) signaling pathway.	Acetaldehyde	73-85	aldehyde dehydrogenase 2 family member	Homo sapiens	19-24
28441416-3	2017	Oxidative metabolism of ethanol by alcohol dehydrogenase or cytochrome P450 2E1 has been implicated in some of ethanol"s teratogenic effects, either via production of acetaldehyde or competitive inhibition of retinoic acid synthesis.	Acetaldehyde	167-179	aldo-keto reductase family 1, member A1 (aldehyde reductase)	Mus musculus	35-56
28441416-3	2017	Oxidative metabolism of ethanol by alcohol dehydrogenase or cytochrome P450 2E1 has been implicated in some of ethanol"s teratogenic effects, either via production of acetaldehyde or competitive inhibition of retinoic acid synthesis.	Acetaldehyde	167-179	cytochrome P450, family 2, subfamily e, polypeptide 1	Mus musculus	60-79
28594397-1	2017	OBJECTIVES: Acetaldehyde, the first metabolite of ethanol, is a definite carcinogen for the esophagus, head, and neck; and aldehyde dehydrogenase 2 (ALDH2) is a mitochondrial enzyme that catalyzes the metabolism of acetaldehyde.	Acetaldehyde	12-24	aldehyde dehydrogenase 2 family member	Homo sapiens	123-147
28594397-1	2017	OBJECTIVES: Acetaldehyde, the first metabolite of ethanol, is a definite carcinogen for the esophagus, head, and neck; and aldehyde dehydrogenase 2 (ALDH2) is a mitochondrial enzyme that catalyzes the metabolism of acetaldehyde.	Acetaldehyde	12-24	aldehyde dehydrogenase 2 family member	Homo sapiens	149-154
28594397-1	2017	OBJECTIVES: Acetaldehyde, the first metabolite of ethanol, is a definite carcinogen for the esophagus, head, and neck; and aldehyde dehydrogenase 2 (ALDH2) is a mitochondrial enzyme that catalyzes the metabolism of acetaldehyde.	Acetaldehyde	215-227	aldehyde dehydrogenase 2 family member	Homo sapiens	123-147
28594397-1	2017	OBJECTIVES: Acetaldehyde, the first metabolite of ethanol, is a definite carcinogen for the esophagus, head, and neck; and aldehyde dehydrogenase 2 (ALDH2) is a mitochondrial enzyme that catalyzes the metabolism of acetaldehyde.	Acetaldehyde	215-227	aldehyde dehydrogenase 2 family member	Homo sapiens	149-154
28594397-11	2017	The breath acetaldehyde levels in ALDH2*2 carriers were significantly higher than for the ALDH2*1/*1 genotype.	Acetaldehyde	11-23	aldehyde dehydrogenase 2 family member	Homo sapiens	34-39
28594397-11	2017	The breath acetaldehyde levels in ALDH2*2 carriers were significantly higher than for the ALDH2*1/*1 genotype.	Acetaldehyde	11-23	aldehyde dehydrogenase 2 family member	Homo sapiens	90-95
28594397-12	2017	Notably, the ratio of breath acetaldehyde level-to-breath ethanol level could identify carriers of the ALDH2*2 allele very accurately (whole accuracy; 96.4%).	Acetaldehyde	29-41	aldehyde dehydrogenase 2 family member	Homo sapiens	103-108
28599714-8	2017	The alcohol group had significantly increased glutathione-S-transferase M1 expression, an antioxidant enzyme that helps detoxify carcinogens, such as acetaldehyde, and significantly increased aldehyde dehydrogenase 2 expression, which allows for greater acetaldehyde clearance.	Acetaldehyde	150-162	glutathione S-transferase mu 1	Rattus norvegicus	46-74
28599714-8	2017	The alcohol group had significantly increased glutathione-S-transferase M1 expression, an antioxidant enzyme that helps detoxify carcinogens, such as acetaldehyde, and significantly increased aldehyde dehydrogenase 2 expression, which allows for greater acetaldehyde clearance.	Acetaldehyde	254-266	aldehyde dehydrogenase 1 family, member A1	Rattus norvegicus	192-216
28599714-9	2017	Increased expression of glutathione-S-transferase M1 and aldehyde dehydrogenase 2 likely contributed to reduce mucosal damage that is caused by acetaldehyde accumulation.	Acetaldehyde	144-156	glutathione S-transferase mu 1	Rattus norvegicus	24-52
28599714-9	2017	Increased expression of glutathione-S-transferase M1 and aldehyde dehydrogenase 2 likely contributed to reduce mucosal damage that is caused by acetaldehyde accumulation.	Acetaldehyde	144-156	aldehyde dehydrogenase 1 family, member A1	Rattus norvegicus	57-81
28575672-5	2017	Acetaldehyde, an alcohol catabolite detoxified by ALDH2, precipitates similar effects.	Acetaldehyde	0-12	aldehyde dehydrogenase 2 family member	Homo sapiens	50-55
28257851-6	2017	The increase in the daily exposure dose to acetaldehyde in alcohol-consuming ALDH2-deficients vs. ALDH2-actives was about twofold.	Acetaldehyde	43-55	aldehyde dehydrogenase 2 family member	Homo sapiens	77-82
28257851-6	2017	The increase in the daily exposure dose to acetaldehyde in alcohol-consuming ALDH2-deficients vs. ALDH2-actives was about twofold.	Acetaldehyde	43-55	aldehyde dehydrogenase 2 family member	Homo sapiens	98-103
28257851-7	2017	The acetaldehyde increase due to ALDH2 inactivity was calculated to be 6.7 mug/kg bw/day for heavy drinkers, which is associated with odds ratios of up to 7 for head and neck as well as oesophageal cancer.	Acetaldehyde	4-16	aldehyde dehydrogenase 2 family member	Homo sapiens	33-38
28430929-1	2017	Aims: Aldehyde dehydrogenase 2 (ALDH2) protects cells from ethanol toxicity by metabolizing acetaldehyde.	Acetaldehyde	92-104	aldehyde dehydrogenase 2 family member	Homo sapiens	6-30
28430929-1	2017	Aims: Aldehyde dehydrogenase 2 (ALDH2) protects cells from ethanol toxicity by metabolizing acetaldehyde.	Acetaldehyde	92-104	aldehyde dehydrogenase 2 family member	Homo sapiens	32-37
28027570-8	2017	CONCLUSION: Decreased levels of ALDH2 may indicate a poor prognosis in HCC patients, while forcing the expression of ALDH2 in HCC cells inhibited their aggressive behavior in vitro and in mice largely by modulating the activity of the ALDH2-acetaldehyde-redox-AMPK axis.	Acetaldehyde	241-253	aldehyde dehydrogenase 2 family member	Homo sapiens	117-122
28027570-8	2017	CONCLUSION: Decreased levels of ALDH2 may indicate a poor prognosis in HCC patients, while forcing the expression of ALDH2 in HCC cells inhibited their aggressive behavior in vitro and in mice largely by modulating the activity of the ALDH2-acetaldehyde-redox-AMPK axis.	Acetaldehyde	241-253	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	117-122
28249782-1	2017	BACKGROUND: Mitochondrial aldehyde dehydrogenase 2 (ALDH2) is highly expressed in heart and skeletal muscles, and is the major enzyme that metabolizes acetaldehyde and toxic aldehydes.	Acetaldehyde	151-163	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	52-57
28026023-7	2017	Aldh1b1 depletion led to increased plasma acetaldehyde levels in ethanol-treated mice, to a significant aggravation of ethanol-induced intestinal hyperproliferation, and to more advanced features of intestinal tumours, but it did not affect intestinal tumour incidence.	Acetaldehyde	42-54	aldehyde dehydrogenase 1 family, member B1	Mus musculus	0-7
28420969-2	2017	Data from several rat strains/lines strongly suggest that catalase-mediated brain oxidation of ethanol into acetaldehyde is an absolute requirement (up 80%-95%) for rats to display ethanol"s reinforcing effects and to initiate chronic ethanol intake.	Acetaldehyde	108-120	catalase	Rattus norvegicus	58-66
28026023-4	2017	In the current study, wild-type mice and mice with depletion of aldehyde dehydrogenase 1b1 (Aldh1b1), an enzyme which has been proposed to play an important role in acetaldehyde detoxification in the intestines, received ethanol in drinking water for 1 year.	Acetaldehyde	165-177	aldehyde dehydrogenase 1 family, member B1	Mus musculus	64-90
28026023-4	2017	In the current study, wild-type mice and mice with depletion of aldehyde dehydrogenase 1b1 (Aldh1b1), an enzyme which has been proposed to play an important role in acetaldehyde detoxification in the intestines, received ethanol in drinking water for 1 year.	Acetaldehyde	165-177	aldehyde dehydrogenase 1 family, member B1	Mus musculus	92-99
28026023-8	2017	These data indicate that ethanol consumption can initiate intestinal tumourigenesis without any additional carcinogen treatment or tumour suppressor gene inactivation, and we provide evidence for a role of Aldh1b1 in protection of the intestines from ethanol-induced damage, as well as for both carcinogenic and tumour-promoting functions of acetaldehyde, including increased progression of ethanol-induced tumours.	Acetaldehyde	342-354	aldehyde dehydrogenase 1 family, member B1	Mus musculus	206-213
28373766-13	2017	Expression of Nrf2 nuclear protein was low in the control group, increased slightly in the model group (or acetaldehyde-stimulated group), and increased more obviously in the IL-22 intervention groups.	Acetaldehyde	107-119	NFE2 like bZIP transcription factor 2	Rattus norvegicus	14-18
28373766-17	2017	CONCLUSION: IL-22 inhibits acetaldehyde-induced HSC activation and proliferation, which may be related to nuclear translocation of Nrf2 and increased activity of the antioxidant axis Nrf2-keap1-ARE.	Acetaldehyde	27-39	interleukin 22	Rattus norvegicus	12-17
28373766-17	2017	CONCLUSION: IL-22 inhibits acetaldehyde-induced HSC activation and proliferation, which may be related to nuclear translocation of Nrf2 and increased activity of the antioxidant axis Nrf2-keap1-ARE.	Acetaldehyde	27-39	NFE2 like bZIP transcription factor 2	Rattus norvegicus	131-135
28373766-17	2017	CONCLUSION: IL-22 inhibits acetaldehyde-induced HSC activation and proliferation, which may be related to nuclear translocation of Nrf2 and increased activity of the antioxidant axis Nrf2-keap1-ARE.	Acetaldehyde	27-39	NFE2 like bZIP transcription factor 2	Rattus norvegicus	183-187
28373766-17	2017	CONCLUSION: IL-22 inhibits acetaldehyde-induced HSC activation and proliferation, which may be related to nuclear translocation of Nrf2 and increased activity of the antioxidant axis Nrf2-keap1-ARE.	Acetaldehyde	27-39	Kelch-like ECH-associated protein 1	Rattus norvegicus	188-193
27533114-10	2017	While examining the role of acetaldehyde, the major alcohol metabolite, in alcohol-associated responses in TNBC cells, we saw that acetaldehyde induced cell migration, invasion, and increased phospho-p38, phospho-JNK, and phospho-IkappaBalpha in a pattern similar to alcohol treatment.	Acetaldehyde	131-143	mitogen-activated protein kinase 14	Homo sapiens	200-203
27865643-7	2017	YNL134C was expressed heterologously in Escherichia coli, and the purified protein catalyzed the formation of HEMF from the mixture of Maillard reaction products, acetaldehydes, and NADPH.	Acetaldehyde	163-176	uncharacterized protein	Saccharomyces cerevisiae S288C	0-7
27533114-10	2017	While examining the role of acetaldehyde, the major alcohol metabolite, in alcohol-associated responses in TNBC cells, we saw that acetaldehyde induced cell migration, invasion, and increased phospho-p38, phospho-JNK, and phospho-IkappaBalpha in a pattern similar to alcohol treatment.	Acetaldehyde	131-143	mitogen-activated protein kinase 8	Homo sapiens	213-216
27533114-10	2017	While examining the role of acetaldehyde, the major alcohol metabolite, in alcohol-associated responses in TNBC cells, we saw that acetaldehyde induced cell migration, invasion, and increased phospho-p38, phospho-JNK, and phospho-IkappaBalpha in a pattern similar to alcohol treatment.	Acetaldehyde	131-143	NFKB inhibitor alpha	Homo sapiens	230-242
27764578-0	2017	Timeless insights into prevention of acetaldehyde genotoxicity?	Acetaldehyde	37-49	timeless circadian regulator	Homo sapiens	0-8
28197082-2	2017	More specifically, it has been hypothesized that acetaldehyde produced in the periphery by the liver is responsible for the aversive effects of ethanol, while the appetitive effects relate to the acetaldehyde produced centrally through the catalase system.	Acetaldehyde	49-61	catalase	Rattus norvegicus	240-248
28061416-0	2017	Purinergic P2X7 receptor mediates acetaldehyde-induced hepatic stellate cells activation via PKC-dependent GSK3beta pathway.	Acetaldehyde	34-46	purinergic receptor P2X 7	Homo sapiens	11-24
28061416-0	2017	Purinergic P2X7 receptor mediates acetaldehyde-induced hepatic stellate cells activation via PKC-dependent GSK3beta pathway.	Acetaldehyde	34-46	glycogen synthase kinase 3 beta	Homo sapiens	107-115
28061416-4	2017	Interestingly, activation of P2X7R by stimulating with P2X7R agonist BzATP significantly promoted acetaldehyde-induced CyclinD1 expression, cell proportion in S phase, inflammatory response, and the protein and mRNA levels of alpha-SMA, collagen I.	Acetaldehyde	98-110	cyclin D1	Homo sapiens	119-127
28061416-8	2017	Taken together, these results suggested that purinergic P2X7R mediated acetaldehyde-induced activation of HSCs via PKC-dependent GSK3beta pathway, which maybe a novel target for limiting HSCs activation.	Acetaldehyde	71-83	glycogen synthase kinase 3 beta	Homo sapiens	129-137
28017615-5	2017	We found that alda-1 increased and acetaldehyde decreased the differentiation of rat primary osteoblasts and expressions of ALDH2 and bone morphogenetic protein-2 (BMP-2).	Acetaldehyde	35-47	aldehyde dehydrogenase 2 family member	Rattus norvegicus	124-129
28017615-5	2017	We found that alda-1 increased and acetaldehyde decreased the differentiation of rat primary osteoblasts and expressions of ALDH2 and bone morphogenetic protein-2 (BMP-2).	Acetaldehyde	35-47	bone morphogenetic protein 2	Rattus norvegicus	134-162
28017615-5	2017	We found that alda-1 increased and acetaldehyde decreased the differentiation of rat primary osteoblasts and expressions of ALDH2 and bone morphogenetic protein-2 (BMP-2).	Acetaldehyde	35-47	bone morphogenetic protein 2	Rattus norvegicus	164-169
28197082-2	2017	More specifically, it has been hypothesized that acetaldehyde produced in the periphery by the liver is responsible for the aversive effects of ethanol, while the appetitive effects relate to the acetaldehyde produced centrally through the catalase system.	Acetaldehyde	196-208	catalase	Rattus norvegicus	240-248
28002588-2	2016	Genetic variations in ADH1B and ALDH2 may alter the function and activity of the corresponding enzymes, leading to differences in acetaldehyde exposure between drinkers.	Acetaldehyde	130-142	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	22-27
28297772-0	2017	[Effect of interleukin-22 on proliferation and activation of hepatic stellate cells induced by acetaldehyde and related mechanism].	Acetaldehyde	95-107	interleukin 22	Rattus norvegicus	11-25
28297772-1	2017	Objective: To investigate the effect of interleukin-22 (IL-22) on the activation and proliferation of hepatic stellate cells (HSCs) induced by acetaldehyde, as well as the role of the antioxidant axis Nrf2-keap1-ARE.	Acetaldehyde	143-155	interleukin 22	Rattus norvegicus	40-54
28297772-1	2017	Objective: To investigate the effect of interleukin-22 (IL-22) on the activation and proliferation of hepatic stellate cells (HSCs) induced by acetaldehyde, as well as the role of the antioxidant axis Nrf2-keap1-ARE.	Acetaldehyde	143-155	interleukin 22	Rattus norvegicus	56-61
28056995-1	2017	BACKGROUND: Mitochondrial aldehyde dehydrogenase 2 (ALDH2) is a key enzyme for the metabolism of many toxic aldehydes such as acetaldehyde, derived from alcohol drinking, and 4HNE, an oxidative stress-derived lipid peroxidation aldehyde.	Acetaldehyde	126-138	aldehyde dehydrogenase 2 family member	Homo sapiens	26-50
28056995-1	2017	BACKGROUND: Mitochondrial aldehyde dehydrogenase 2 (ALDH2) is a key enzyme for the metabolism of many toxic aldehydes such as acetaldehyde, derived from alcohol drinking, and 4HNE, an oxidative stress-derived lipid peroxidation aldehyde.	Acetaldehyde	126-138	aldehyde dehydrogenase 2 family member	Homo sapiens	52-57
28297772-11	2017	There was increased expression of Nrf2 nucleoprotein after acetaldehyde stimulation (compared with the blank control group, P &lt; 0.05), and after the intervention with gradient concentrations of IL-22, the expression of Nrf2 nucleoprotein was further increased (all P &lt; 0.05).	Acetaldehyde	59-71	NFE2 like bZIP transcription factor 2	Rattus norvegicus	34-38
28297772-12	2017	The results of spectrophotometry showed that compared with the blank control group, the model group had increased levels of MDA and GSH in culture supernatant after acetaldehyde stimulation; after the intervention with gradient concentrations of IL-22, there was a significant reduction in the MDA level and a significant increase in the GSH level in a dose-dependent manner (all P &lt; 0.05).	Acetaldehyde	165-177	interleukin 22	Rattus norvegicus	246-251
28297772-14	2017	IL-22 effectively inhibits the activation and proliferation of HSCs induced by acetaldehyde, and its mechanism may be related to promoting Nrf2 nuclear translocation in HSCs and expression of the downstream target gene GSH and increasing the activity of the antioxidant axis Nrf2-keap1-ARE.	Acetaldehyde	79-91	interleukin 22	Rattus norvegicus	0-5
29109756-2	2017	Utilizing a condensation reaction between carbonyls and a hydrazine moeity, we demonstrate that the fluorescent probe (Aldehydefluor-1) AF1 reacts with a range of reactive carbonyl species including formaldehyde, acetaldehyde, glyoxylic acid, and methyl glyoxal.	Acetaldehyde	213-225	interferon gamma receptor 2	Homo sapiens	136-139
26212265-1	2017	BACKGROUND: The human aldehyde dehydrogenase 2 (ALDH2) is the most effective enzyme in the detoxification of alcohol metabolite acetaldehyde.	Acetaldehyde	128-140	aldehyde dehydrogenase 2 family member	Homo sapiens	22-46
26212265-1	2017	BACKGROUND: The human aldehyde dehydrogenase 2 (ALDH2) is the most effective enzyme in the detoxification of alcohol metabolite acetaldehyde.	Acetaldehyde	128-140	aldehyde dehydrogenase 2 family member	Homo sapiens	48-53
26278386-8	2017	We describe experimental data that clearly implicate Egr-1 function in alcohol-induced steatosis and fibrosis, showing that ethanol-elicited regulation of Egr-1 expression depends on the generation of acetaldehyde and that the absence of Egr-1 diminishes alcohol-induced triglyceride accumulation.	Acetaldehyde	201-213	early growth response 1	Homo sapiens	53-58
28002588-2	2016	Genetic variations in ADH1B and ALDH2 may alter the function and activity of the corresponding enzymes, leading to differences in acetaldehyde exposure between drinkers.	Acetaldehyde	130-142	aldehyde dehydrogenase 2 family member	Homo sapiens	32-37
27991430-8	2016	Only DNA sequences from Lactococcus were implicated in the formation of acetaldehyde from acetate through aldehyde dehydrogenase family 9 member A1 (K00149).	Acetaldehyde	72-84	aldehyde dehydrogenase 9 family member A1	Homo sapiens	106-147
27927211-9	2016	Frequency of the ALDH2 SNP allele A which limits acetaldehyde metabolism was lower in patients with AF (18.8%) than in controls (23.5%).	Acetaldehyde	49-61	aldehyde dehydrogenase 2 family member	Homo sapiens	17-22
27958326-5	2016	Src kinase and MLCK inhibitors blocked this synergistic effect of ethanol and acetaldehyde on tight junction.	Acetaldehyde	78-90	myosin light chain kinase 3	Homo sapiens	15-19
27958326-8	2016	Diltiazem and selective knockdown of TRPV6 or CaV1.3 channels, by shRNA blocked ethanol and acetaldehyde-induced tight junction disruption and barrier dysfunction.	Acetaldehyde	92-104	transient receptor potential cation channel subfamily V member 6	Homo sapiens	37-42
27958326-8	2016	Diltiazem and selective knockdown of TRPV6 or CaV1.3 channels, by shRNA blocked ethanol and acetaldehyde-induced tight junction disruption and barrier dysfunction.	Acetaldehyde	92-104	calcium voltage-gated channel subunit alpha1 D	Homo sapiens	46-52
27958326-11	2016	These results demonstrate that ethanol and acetaldehyde synergistically disrupt tight junctions by a mechanism involving calcium, oxidative stress, Src kinase and MLCK.	Acetaldehyde	43-55	myosin light chain kinase 3	Homo sapiens	163-167
27783409-0	2016	Malondialdehyde-Acetaldehyde-Adducted Surfactant Protein Alters Macrophage Functions Through Scavenger Receptor A.	Acetaldehyde	16-28	macrophage scavenger receptor 1	Mus musculus	93-113
27716962-0	2016	Acetaldehyde Disrupts Interferon Alpha Signaling in Hepatitis C Virus-Infected Liver Cells by Up-Regulating USP18.	Acetaldehyde	0-12	ubiquitin specific peptidase 18	Homo sapiens	108-113
27916141-9	2016	Previous studies have shown that polymorphisms in the promoter region of the CYP2E1 gene could cause higher CYP2E1 transcriptional activity, increasing enzyme activity compared with nondrinkers, indicating that the presence of the mutated allele (heterozygous or homozygous) may be associated with higher alcohol metabolic rates and therefore show increased acetaldehyde levels after alcohol consumption, which then can exert its carcinogenic effect.	Acetaldehyde	358-370	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	77-83
27916141-1	2016	DNA damage caused by the accumulation of bio-products generated in the biotransformation of ethanol to acetaldehyde mediated by the CYP2E1 enzyme has been studied.	Acetaldehyde	103-115	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	132-138
27716962-5	2016	To this end, CYP2E1+ Huh7.5 cells were infected with HCV and exposed to the acetaldehyde (Ach) generating system (AGS).	Acetaldehyde	76-88	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	13-19
27716962-5	2016	To this end, CYP2E1+ Huh7.5 cells were infected with HCV and exposed to the acetaldehyde (Ach) generating system (AGS).	Acetaldehyde	90-93	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	13-19
27716962-6	2016	RESULTS: Continuously produced Ach suppressed IFNalpha-induced STAT1 phosphorylation, but increased the level of a protease, USP18 (both measured by Western blot), which interferes with IFNalpha signaling.	Acetaldehyde	31-34	interferon alpha 1	Homo sapiens	46-54
27716962-6	2016	RESULTS: Continuously produced Ach suppressed IFNalpha-induced STAT1 phosphorylation, but increased the level of a protease, USP18 (both measured by Western blot), which interferes with IFNalpha signaling.	Acetaldehyde	31-34	signal transducer and activator of transcription 1	Homo sapiens	63-68
27716962-6	2016	RESULTS: Continuously produced Ach suppressed IFNalpha-induced STAT1 phosphorylation, but increased the level of a protease, USP18 (both measured by Western blot), which interferes with IFNalpha signaling.	Acetaldehyde	31-34	ubiquitin specific peptidase 18	Homo sapiens	125-130
27716962-6	2016	RESULTS: Continuously produced Ach suppressed IFNalpha-induced STAT1 phosphorylation, but increased the level of a protease, USP18 (both measured by Western blot), which interferes with IFNalpha signaling.	Acetaldehyde	31-34	interferon alpha 1	Homo sapiens	186-194
27716962-7	2016	Induction of USP18 by Ach was confirmed in primary human hepatocyte cultures and in livers of ethanol-fed HCV transgenic mice.	Acetaldehyde	22-25	ubiquitin specific peptidase 18	Homo sapiens	13-18
27716962-8	2016	Silencing of USP18 by specific siRNA attenuated the pSTAT1 suppression by Ach.	Acetaldehyde	74-77	ubiquitin specific peptidase 18	Homo sapiens	13-18
27716962-9	2016	The mechanism by which Ach down-regulates pSTAT1 is related to an enhanced interaction between IFNalphaR2 and USP18 that finally dysregulates the cross talk between the IFN receptor on the cell surface and STAT1.	Acetaldehyde	23-26	ubiquitin specific peptidase 18	Homo sapiens	110-115
27716962-9	2016	The mechanism by which Ach down-regulates pSTAT1 is related to an enhanced interaction between IFNalphaR2 and USP18 that finally dysregulates the cross talk between the IFN receptor on the cell surface and STAT1.	Acetaldehyde	23-26	signal transducer and activator of transcription 1	Homo sapiens	43-48
27716962-10	2016	Furthermore, Ach decreases ISGylation of STAT1 (protein conjugation of a small ubiquitin-like modifier, ISG15, Western blot), which preserves STAT1 activation.	Acetaldehyde	13-16	signal transducer and activator of transcription 1	Homo sapiens	41-46
27716962-10	2016	Furthermore, Ach decreases ISGylation of STAT1 (protein conjugation of a small ubiquitin-like modifier, ISG15, Western blot), which preserves STAT1 activation.	Acetaldehyde	13-16	ISG15 ubiquitin like modifier	Homo sapiens	104-109
27716962-10	2016	Furthermore, Ach decreases ISGylation of STAT1 (protein conjugation of a small ubiquitin-like modifier, ISG15, Western blot), which preserves STAT1 activation.	Acetaldehyde	13-16	signal transducer and activator of transcription 1	Homo sapiens	142-147
27716962-12	2016	CONCLUSIONS: We conclude that Ach disrupts IFNalpha-induced STAT1 phosphorylation by the up-regulation of USP18 to block the innate immunity protection in HCV-infected liver cells, thereby contributing to HCV-alcohol pathogenesis.	Acetaldehyde	30-33	interferon alpha 1	Homo sapiens	43-51
27716962-12	2016	CONCLUSIONS: We conclude that Ach disrupts IFNalpha-induced STAT1 phosphorylation by the up-regulation of USP18 to block the innate immunity protection in HCV-infected liver cells, thereby contributing to HCV-alcohol pathogenesis.	Acetaldehyde	30-33	signal transducer and activator of transcription 1	Homo sapiens	60-65
27716962-12	2016	CONCLUSIONS: We conclude that Ach disrupts IFNalpha-induced STAT1 phosphorylation by the up-regulation of USP18 to block the innate immunity protection in HCV-infected liver cells, thereby contributing to HCV-alcohol pathogenesis.	Acetaldehyde	30-33	ubiquitin specific peptidase 18	Homo sapiens	106-111
27325678-8	2016	Unexpectedly, the results indicate that acetaldehyde (and not ethanolamine) serves as the inducer molecule that is sensed by PA4021 and leads to the transcriptional activation of the PA4022-eat-eutBC operon.	Acetaldehyde	40-52	transcriptional regulator	Pseudomonas aeruginosa PAO1	125-131
27580341-5	2016	The active site of NahF is highly hydrophobic, and the enzyme shows higher specificity for less polar substrates than for polar substrates, e.g., acetaldehyde.	Acetaldehyde	146-158	salicyladehyde dehydrogenase	Pseudomonas putida	19-23
27624556-0	2016	NOX2 amplifies acetaldehyde-mediated cardiomyocyte mitochondrial dysfunction in alcoholic cardiomyopathy.	Acetaldehyde	15-27	cytochrome b-245, beta polypeptide	Mus musculus	0-4
27466724-1	2016	Although perhaps better known as an irreversible aldehyde dehydrogenase inhibitor causing increased acetaldehyde levels after concomitant intake of ethanol, disulfiram or one of its metabolites (diethyldithiocarbamate) also inhibit dopamine beta-hydroxylase, an enzyme that converts dopamine to norepinephrine.	Acetaldehyde	100-112	dopamine beta-hydroxylase	Homo sapiens	232-257
27650066-4	2016	ALDH2 is localized in mitochondria and is essential for the metabolism of acetaldehyde, thereby placing it directly downstream of ethanol metabolism.	Acetaldehyde	74-86	aldehyde dehydrogenase 2 family member	Homo sapiens	0-5
27575855-1	2016	The ALDH2 gene encodes the mitochondrial aldehyde dehydrogenase 2 (ALDH2), a critical enzyme involved in ethanol clearance through acetaldehyde metabolism.	Acetaldehyde	131-143	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	4-9
27575855-1	2016	The ALDH2 gene encodes the mitochondrial aldehyde dehydrogenase 2 (ALDH2), a critical enzyme involved in ethanol clearance through acetaldehyde metabolism.	Acetaldehyde	131-143	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	67-72
27325678-14	2016	In contrast, PA4021 (EatR) appears to monitor the intracellular levels of free acetaldehyde and responds through transcriptional activation of the ethanolamine-catabolic genes.	Acetaldehyde	79-91	transcriptional regulator	Pseudomonas aeruginosa PAO1	13-19
27325678-8	2016	Unexpectedly, the results indicate that acetaldehyde (and not ethanolamine) serves as the inducer molecule that is sensed by PA4021 and leads to the transcriptional activation of the PA4022-eat-eutBC operon.	Acetaldehyde	40-52	aldehyde dehydrogenase	Pseudomonas aeruginosa PAO1	183-189
27092375-9	2016	Using the MCM model, only 16% of the modelled acetaldehyde was formed from ethanol oxidation.	Acetaldehyde	46-58	methylmalonyl-CoA mutase	Homo sapiens	10-13
27404720-2	2016	Acetaldehyde generated from alcohol in the liver is metabolized by the mitochondrial aldehyde dehydrogenase (ALDH2) such that diminishing ALDH2 activity leads to the aversive effects of blood acetaldehyde upon alcohol intake.	Acetaldehyde	0-12	aldehyde dehydrogenase 2 family member	Rattus norvegicus	71-107
27404720-2	2016	Acetaldehyde generated from alcohol in the liver is metabolized by the mitochondrial aldehyde dehydrogenase (ALDH2) such that diminishing ALDH2 activity leads to the aversive effects of blood acetaldehyde upon alcohol intake.	Acetaldehyde	0-12	aldehyde dehydrogenase 2 family member	Rattus norvegicus	109-114
27404720-2	2016	Acetaldehyde generated from alcohol in the liver is metabolized by the mitochondrial aldehyde dehydrogenase (ALDH2) such that diminishing ALDH2 activity leads to the aversive effects of blood acetaldehyde upon alcohol intake.	Acetaldehyde	0-12	aldehyde dehydrogenase 2 family member	Rattus norvegicus	138-143
27404720-2	2016	Acetaldehyde generated from alcohol in the liver is metabolized by the mitochondrial aldehyde dehydrogenase (ALDH2) such that diminishing ALDH2 activity leads to the aversive effects of blood acetaldehyde upon alcohol intake.	Acetaldehyde	192-204	aldehyde dehydrogenase 2 family member	Rattus norvegicus	71-107
27404720-2	2016	Acetaldehyde generated from alcohol in the liver is metabolized by the mitochondrial aldehyde dehydrogenase (ALDH2) such that diminishing ALDH2 activity leads to the aversive effects of blood acetaldehyde upon alcohol intake.	Acetaldehyde	192-204	aldehyde dehydrogenase 2 family member	Rattus norvegicus	109-114
27404720-2	2016	Acetaldehyde generated from alcohol in the liver is metabolized by the mitochondrial aldehyde dehydrogenase (ALDH2) such that diminishing ALDH2 activity leads to the aversive effects of blood acetaldehyde upon alcohol intake.	Acetaldehyde	192-204	aldehyde dehydrogenase 2 family member	Rattus norvegicus	138-143
27327271-1	2016	The 2-deoxy-d-ribose-5-phosphate aldolase (DERA) offers access to highly desirable building blocks for organic synthesis by catalyzing a stereoselective C-C bond formation between acetaldehyde and certain electrophilic aldehydes.	Acetaldehyde	180-192	deoxyribose-phosphate aldolase	Homo sapiens	4-41
30155096-1	2016	2-Deoxy-d-ribose-5-phosphate aldolase (DERA) is used in organic synthesis for the enantioselective reaction between acetaldehyde and a broad range of other aldehydes as acceptor molecules.	Acetaldehyde	116-128	deoxyribose-phosphate aldolase	Homo sapiens	0-37
30155096-1	2016	2-Deoxy-d-ribose-5-phosphate aldolase (DERA) is used in organic synthesis for the enantioselective reaction between acetaldehyde and a broad range of other aldehydes as acceptor molecules.	Acetaldehyde	116-128	deoxyribose-phosphate aldolase	Homo sapiens	39-43
30155096-5	2016	The crystal structure of DERA before and after acetaldehyde incubation was determined at high resolution, revealing a covalently bound reaction product bridging the catalytically active lysine (K167) to a nearby cysteine (C47) in the deactivated enzyme.	Acetaldehyde	47-59	deoxyribose-phosphate aldolase	Homo sapiens	25-29
30155096-7	2016	In support of this mechanism, direct incubation of DERA with crotonaldehyde results in a more than 100-fold stronger inhibition, compared to acetaldehyde, whereas mutation of C47 gives rise to a fully acetaldehyde-resistant DERA.	Acetaldehyde	141-153	deoxyribose-phosphate aldolase	Homo sapiens	51-55
30155096-7	2016	In support of this mechanism, direct incubation of DERA with crotonaldehyde results in a more than 100-fold stronger inhibition, compared to acetaldehyde, whereas mutation of C47 gives rise to a fully acetaldehyde-resistant DERA.	Acetaldehyde	201-213	deoxyribose-phosphate aldolase	Homo sapiens	51-55
27362442-6	2016	Serum levels of aspartate transaminase (AST) showed a significant reduction after 2 weeks of ACE consumption (P &lt; .001), in contrast to placebo where no changes were seen; the difference in AST levels between the two groups was significant at 2 weeks (P &lt; .02).	Acetaldehyde	93-96	solute carrier family 17 member 5	Homo sapiens	16-38
27362442-6	2016	Serum levels of aspartate transaminase (AST) showed a significant reduction after 2 weeks of ACE consumption (P &lt; .001), in contrast to placebo where no changes were seen; the difference in AST levels between the two groups was significant at 2 weeks (P &lt; .02).	Acetaldehyde	93-96	solute carrier family 17 member 5	Homo sapiens	40-43
27362442-6	2016	Serum levels of aspartate transaminase (AST) showed a significant reduction after 2 weeks of ACE consumption (P &lt; .001), in contrast to placebo where no changes were seen; the difference in AST levels between the two groups was significant at 2 weeks (P &lt; .02).	Acetaldehyde	93-96	solute carrier family 17 member 5	Homo sapiens	193-196
27348013-16	2016	Increased ROS, IL-1beta, acetaldehyde, and increased hepatic iron, all activate nuclear factor-kappa B (NF-kappaB) transcription factor.	Acetaldehyde	25-37	nuclear factor kappa B subunit 1	Homo sapiens	80-102
27348013-16	2016	Increased ROS, IL-1beta, acetaldehyde, and increased hepatic iron, all activate nuclear factor-kappa B (NF-kappaB) transcription factor.	Acetaldehyde	25-37	nuclear factor kappa B subunit 1	Homo sapiens	104-113
27327271-1	2016	The 2-deoxy-d-ribose-5-phosphate aldolase (DERA) offers access to highly desirable building blocks for organic synthesis by catalyzing a stereoselective C-C bond formation between acetaldehyde and certain electrophilic aldehydes.	Acetaldehyde	180-192	deoxyribose-phosphate aldolase	Homo sapiens	43-47
27511995-0	2016	Effect of ethanol and acetaldehyde at clinically relevant concentrations on atrial inward rectifier potassium current IK1: separate and combined effect.	Acetaldehyde	22-34	potassium calcium-activated channel subfamily N member 4	Rattus norvegicus	118-121
26992901-2	2016	Aldehyde dehydrogenase 2 (ALDH2; rs671, Glu504Lys) and alcohol dehydrogenase 1B (ADH1B; rs1229984, His47Arg) polymorphisms impact the accumulation of acetaldehyde, resulting in an increased risk of various cancers.	Acetaldehyde	150-162	aldehyde dehydrogenase 2 family member	Homo sapiens	0-24
26992901-2	2016	Aldehyde dehydrogenase 2 (ALDH2; rs671, Glu504Lys) and alcohol dehydrogenase 1B (ADH1B; rs1229984, His47Arg) polymorphisms impact the accumulation of acetaldehyde, resulting in an increased risk of various cancers.	Acetaldehyde	150-162	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	55-79
26992901-2	2016	Aldehyde dehydrogenase 2 (ALDH2; rs671, Glu504Lys) and alcohol dehydrogenase 1B (ADH1B; rs1229984, His47Arg) polymorphisms impact the accumulation of acetaldehyde, resulting in an increased risk of various cancers.	Acetaldehyde	150-162	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	81-86
27511995-11	2016	The concurrent application of ethanol (20 mM) and acetaldehyde (3 muM) resulted in the steady-state IK1 activation by 2.1% on average.	Acetaldehyde	50-62	potassium calcium-activated channel subfamily N member 4	Rattus norvegicus	100-103
27511995-12	2016	We conclude that ethanol and even more acetaldehyde affected IK1 at clinically relevant concentrations if applied separately.	Acetaldehyde	39-51	potassium calcium-activated channel subfamily N member 4	Rattus norvegicus	61-64
27511995-3	2016	Both ethanol and acetaldehyde have been demonstrated to considerably modify IK1 in rat ventricular myocytes.	Acetaldehyde	17-29	potassium calcium-activated channel subfamily N member 4	Rattus norvegicus	76-79
27511995-10	2016	Unlike ethanol, acetaldehyde (3 muM) markedly inhibited the rat atrial IK1 (by 15.1%) in a voltage-independent manner, comparably to the rat ventricular IK1.	Acetaldehyde	16-28	potassium calcium-activated channel subfamily N member 4	Rattus norvegicus	71-74
27075303-8	2016	Global inactivation of CES1 aggravated alcohol- or MCD diet-induced liver inflammation and liver injury, likely as a result of increased production of acetaldehyde and reactive oxygen species and mitochondrial dysfunctions.	Acetaldehyde	151-163	carboxylesterase 1	Homo sapiens	23-27
30480906-5	2016	Approximately half of the asthmatic subjects developed bronchoconstriction with concomitant increases in blood acetaldehyde and histamine, which was associated with genetically reduced ALDH2 activities.	Acetaldehyde	111-123	aldehyde dehydrogenase 2 family member	Homo sapiens	185-190
26968209-8	2016	Higher blood acetate, the end product of ethanol metabolism, and lower acetaldehyde levels were evident in the ethanol-challenged SHP(-/-) than WT mice.	Acetaldehyde	71-83	nuclear receptor subfamily 0, group B, member 2	Mus musculus	130-133
26854595-4	2016	Our data showed that both cAMP/PKA and cAMP/EPAC signaling pathways were involved in acetaldehyde-induced HSCs.	Acetaldehyde	85-97	protein kinase cAMP-activated catalytic subunit alpha	Rattus norvegicus	31-34
26854595-4	2016	Our data showed that both cAMP/PKA and cAMP/EPAC signaling pathways were involved in acetaldehyde-induced HSCs.	Acetaldehyde	85-97	Rap guanine nucleotide exchange factor 3	Rattus norvegicus	44-48
26854595-5	2016	Acetaldehyde could reduce the expression of EPAC1 while enhancing the expression of EPAC2.	Acetaldehyde	0-12	Rap guanine nucleotide exchange factor 3	Rattus norvegicus	44-49
26854595-5	2016	Acetaldehyde could reduce the expression of EPAC1 while enhancing the expression of EPAC2.	Acetaldehyde	0-12	Rap guanine nucleotide exchange factor 4	Rattus norvegicus	84-89
26854595-6	2016	The cAMP analog Me-cAMP, which stimulates the EPAC/Rap1 pathway, could significantly decrease the proliferation and collagen synthesis of acetaldehyde-induced HSCs.	Acetaldehyde	138-150	Rap guanine nucleotide exchange factor 3	Rattus norvegicus	46-50
26854595-7	2016	Furthermore, depletion of EPAC2, but not EPAC1, prevented the activation of HSC measured as the production of alpha-SMA and collagen type I and III, indicating that EPAC1 appears to have protective effects on acetaldehyde-induced HSCs.	Acetaldehyde	209-221	Rap guanine nucleotide exchange factor 4	Rattus norvegicus	26-31
26854595-7	2016	Furthermore, depletion of EPAC2, but not EPAC1, prevented the activation of HSC measured as the production of alpha-SMA and collagen type I and III, indicating that EPAC1 appears to have protective effects on acetaldehyde-induced HSCs.	Acetaldehyde	209-221	Rap guanine nucleotide exchange factor 3	Rattus norvegicus	165-170
26854595-9	2016	These results suggested that EPAC activation could inhibit the activation and proliferation of acetaldehyde-induced HSCs via Rap1.	Acetaldehyde	95-107	Rap guanine nucleotide exchange factor 3	Rattus norvegicus	29-33
26646001-0	2016	Ethanol and Acetaldehyde After Intraperitoneal Administration to Aldh2-Knockout Mice-Reflection in Blood and Brain Levels.	Acetaldehyde	12-24	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	65-70
26646001-1	2016	This paper reports, for the first time, on the analysis of ethanol (EtOH) and acetaldehyde (AcH) concentrations in the blood and brains of Aldh2-knockout (Aldh2-KO) and C57B6/6J (WT) mice.	Acetaldehyde	92-95	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	139-144
26646001-6	2016	In the EtOH groups, high AcH levels were found in the blood and brains of Aldh2-KO mice, while only small traces of AcH were seen in the blood and brains of WT mice.	Acetaldehyde	25-28	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	74-79
26646001-9	2016	In the AcH groups, high AcH levels were found in both WT and Aldh2-KO mice.	Acetaldehyde	7-10	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	61-66
26646001-9	2016	In the AcH groups, high AcH levels were found in both WT and Aldh2-KO mice.	Acetaldehyde	24-27	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	61-66
26646001-11	2016	Brain AcH concentrations were almost equal to the concentrations found in the blood, where the AcH concentrations were approximately two times higher in the Aldh2-KO mice than in the WT mice, both in the blood and the brain.	Acetaldehyde	95-98	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	157-162
26646001-12	2016	Our results suggest that systemic EtOH and AcH administration can cause a greater increase in AcH accumulation in the blood and brains of Aldh2-KO mice, where EtOH concentrations in the Aldh2-KO mice were comparable to the EtOH concentrations in the WT mice.	Acetaldehyde	43-46	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	138-143
26646001-12	2016	Our results suggest that systemic EtOH and AcH administration can cause a greater increase in AcH accumulation in the blood and brains of Aldh2-KO mice, where EtOH concentrations in the Aldh2-KO mice were comparable to the EtOH concentrations in the WT mice.	Acetaldehyde	43-46	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	186-191
26542604-9	2016	CONCLUSIONS: The faster metabolism of ethanol and acetaldehyde by the ADH1B*2 allele and ALDH2*1/*1 genotype and higher ketosis levels were associated with higher UA levels in alcoholics, while diabetes and the consumption of sake were negative determinants.	Acetaldehyde	50-62	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	70-75
26854595-0	2016	EPAC activation inhibits acetaldehyde-induced activation and proliferation of hepatic stellate cell via Rap1.	Acetaldehyde	25-37	Rap guanine nucleotide exchange factor 3	Rattus norvegicus	0-4
26854595-2	2016	Previous studies have demonstrated that the rat HSCs could be significantly activated after exposure to 200 mumol/L acetaldehyde for 48 h, and the cAMP/PKA signaling pathways were also dramatically upregulated in activated HSCs isolated from alcoholic fibrotic rat liver.	Acetaldehyde	116-128	protein kinase cAMP-activated catalytic subunit alpha	Rattus norvegicus	152-155
26917006-2	2016	Macrocytosis and macrocytic anemia in alcoholics have been associated with ADH1B and ALDH2 gene variants which increase acetaldehyde (AcH) levels.	Acetaldehyde	120-132	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	75-80
26721332-12	2016	Occludin knockdown significantly enhanced acetaldehyde-induced TJ disruption and barrier dysfunction in Caco-2 cell monolayers.	Acetaldehyde	42-54	occludin	Mus musculus	0-8
26721332-8	2016	The effect of occludin depletion on acetaldehyde-induced TJ disruption was confirmed in Caco-2 cell monolayers.	Acetaldehyde	36-48	occludin	Homo sapiens	14-22
27043646-12	2016	Additionally, culturing the cells in the presence of acetaldehyde alone resulted in increased levels of p-Cdc2 and p21.	Acetaldehyde	53-65	cyclin dependent kinase 1	Homo sapiens	106-110
27043646-12	2016	Additionally, culturing the cells in the presence of acetaldehyde alone resulted in increased levels of p-Cdc2 and p21.	Acetaldehyde	53-65	cyclin dependent kinase inhibitor 1A	Homo sapiens	115-118
27043646-13	2016	CONCLUSIONS: Acetaldehyde produced during ethanol oxidation has a major role in the ethanol metabolism-mediated G2/M cell cycle arrest, and the concurrent accumulation of p21 and p-Cdc2.	Acetaldehyde	13-25	cyclin dependent kinase inhibitor 1A	Homo sapiens	171-174
27043646-13	2016	CONCLUSIONS: Acetaldehyde produced during ethanol oxidation has a major role in the ethanol metabolism-mediated G2/M cell cycle arrest, and the concurrent accumulation of p21 and p-Cdc2.	Acetaldehyde	13-25	cyclin dependent kinase 1	Homo sapiens	181-185
27186430-0	2016	ALDH2 modulates autophagy flux to regulate acetaldehyde-mediated toxicity thresholds.	Acetaldehyde	43-55	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	0-5
27186430-5	2016	Aldh2-deficient cells appeared to be highly susceptible to ethanol- or acetaldehyde-mediated toxicity.	Acetaldehyde	71-83	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	0-5
27186430-6	2016	Alcohol dehydrogenase-mediated acetaldehyde production was implicated in ethanol-induced cell injury in Aldh2 deficient cells as ethanol-induced oxidative stress and cell death was partially inhibited by 4-methylpyrazole.	Acetaldehyde	31-43	aldo-keto reductase family 1, member A1 (aldehyde reductase)	Mus musculus	0-21
27186430-6	2016	Alcohol dehydrogenase-mediated acetaldehyde production was implicated in ethanol-induced cell injury in Aldh2 deficient cells as ethanol-induced oxidative stress and cell death was partially inhibited by 4-methylpyrazole.	Acetaldehyde	31-43	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	104-109
27186430-8	2016	Pharmacological inhibition of autophagy flux by chloroquine stabilized p62/SQSTM1, and increased basal and acetaldehyde-mediate oxidative stress in Aldh2 deficient cells as documented in monolayer culture as well as single-cell derived three-dimensional esophageal organoids, recapitulating a physiological esophageal epithelial proliferation-differentiation gradient.	Acetaldehyde	107-119	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	148-153
26978376-0	2016	Astaxanthin Inhibits Acetaldehyde-Induced Cytotoxicity in SH-SY5Y Cells by Modulating Akt/CREB and p38MAPK/ERK Signaling Pathways.	Acetaldehyde	21-33	AKT serine/threonine kinase 1	Homo sapiens	86-89
26978376-0	2016	Astaxanthin Inhibits Acetaldehyde-Induced Cytotoxicity in SH-SY5Y Cells by Modulating Akt/CREB and p38MAPK/ERK Signaling Pathways.	Acetaldehyde	21-33	cAMP responsive element binding protein 1	Homo sapiens	90-94
26978376-4	2016	It was found that astaxanthin protected cells from apoptosis by ameliorating the effect of acetaldehyde on the expression of Bcl-2 family proteins, preventing the reduction of anti-apoptotic protein Bcl-2 and the increase of pro-apoptotic protein Bak induced by acetaldehyde.	Acetaldehyde	91-103	BCL2 apoptosis regulator	Homo sapiens	125-130
26978376-5	2016	Further analyses showed that astaxanthin treatment inhibited acetaldehyde-induced reduction of the levels of activated Akt and cyclic AMP-responsive element binding protein (CREB).	Acetaldehyde	61-73	AKT serine/threonine kinase 1	Homo sapiens	119-122
26978376-5	2016	Further analyses showed that astaxanthin treatment inhibited acetaldehyde-induced reduction of the levels of activated Akt and cyclic AMP-responsive element binding protein (CREB).	Acetaldehyde	61-73	cAMP responsive element binding protein 1	Homo sapiens	127-172
26978376-5	2016	Further analyses showed that astaxanthin treatment inhibited acetaldehyde-induced reduction of the levels of activated Akt and cyclic AMP-responsive element binding protein (CREB).	Acetaldehyde	61-73	cAMP responsive element binding protein 1	Homo sapiens	174-178
26978376-6	2016	Astaxanthin treatment also prevented acetaldehyde-induced increase of the level of activated p38 mitogen-activated protein kinase (MAPK) and decrease of the level of activated extracellular signal-regulated kinases (ERKs).	Acetaldehyde	37-49	mitogen-activated protein kinase 14	Homo sapiens	93-129
26978376-9	2016	Thus, astaxanthin may inhibit acetaldehyde-induced apoptosis through promoting the activation of Akt/CREB and ERKs and blocking the activation of p38MAPK.	Acetaldehyde	30-42	AKT serine/threonine kinase 1	Homo sapiens	97-100
26978376-9	2016	Thus, astaxanthin may inhibit acetaldehyde-induced apoptosis through promoting the activation of Akt/CREB and ERKs and blocking the activation of p38MAPK.	Acetaldehyde	30-42	cAMP responsive element binding protein 1	Homo sapiens	101-105
26917006-2	2016	Macrocytosis and macrocytic anemia in alcoholics have been associated with ADH1B and ALDH2 gene variants which increase acetaldehyde (AcH) levels.	Acetaldehyde	120-132	aldehyde dehydrogenase 2 family member	Homo sapiens	85-90
26917006-2	2016	Macrocytosis and macrocytic anemia in alcoholics have been associated with ADH1B and ALDH2 gene variants which increase acetaldehyde (AcH) levels.	Acetaldehyde	134-137	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	75-80
26917006-2	2016	Macrocytosis and macrocytic anemia in alcoholics have been associated with ADH1B and ALDH2 gene variants which increase acetaldehyde (AcH) levels.	Acetaldehyde	134-137	aldehyde dehydrogenase 2 family member	Homo sapiens	85-90
26807981-3	2016	ADH is involved in catalyzing ethanol to acetaldehyde although its role in cardiovascular diseases other than ethanol metabolism still remains elusive.	Acetaldehyde	41-53	aldo-keto reductase family 1, member A1 (aldehyde reductase)	Mus musculus	0-3
29910900-1	2016	DERA, 2-deoxyribose-5-phosphate aldolase, catalyzes the retro-aldol cleavage of 2-deoxy-ribose-5-phosphate (dR5P) into glyceraldehyde-3-phosphate (G3P) and acetaldehyde in a branch of the pentose phosphate pathway.	Acetaldehyde	156-168	deoxyribose-phosphate aldolase	Homo sapiens	0-4
29910900-1	2016	DERA, 2-deoxyribose-5-phosphate aldolase, catalyzes the retro-aldol cleavage of 2-deoxy-ribose-5-phosphate (dR5P) into glyceraldehyde-3-phosphate (G3P) and acetaldehyde in a branch of the pentose phosphate pathway.	Acetaldehyde	156-168	deoxyribose-phosphate aldolase	Homo sapiens	6-40
28049208-1	2016	BACKGROUND: In Japanese patients, alcohol-induced asthma is attributed to elevated plasma concentrations of acetaldehyde following alcohol consumption because of an acetaldehyde dehydrogenase 2 gene (ALDH2) polymorphism.	Acetaldehyde	108-120	aldehyde dehydrogenase 2 family member	Homo sapiens	165-193
26692282-3	2016	Acetaldehyde is produced with a Faradaic efficiency of  5% at -0.33 V (vs. RHE).	Acetaldehyde	0-12	factor interacting with PAPOLA and CPSF1	Homo sapiens	75-78
26339786-1	2016	Acetaldehyde, the carcinogenic metabolite of ethanol known to provoke aversive symptoms of alcohol consumption, is predominantly eliminated by aldehyde dehydrogenase 2 (ALDH2).	Acetaldehyde	0-12	aldehyde dehydrogenase 2 family member	Homo sapiens	143-167
26339786-1	2016	Acetaldehyde, the carcinogenic metabolite of ethanol known to provoke aversive symptoms of alcohol consumption, is predominantly eliminated by aldehyde dehydrogenase 2 (ALDH2).	Acetaldehyde	0-12	aldehyde dehydrogenase 2 family member	Homo sapiens	169-174
28049208-1	2016	BACKGROUND: In Japanese patients, alcohol-induced asthma is attributed to elevated plasma concentrations of acetaldehyde following alcohol consumption because of an acetaldehyde dehydrogenase 2 gene (ALDH2) polymorphism.	Acetaldehyde	108-120	aldehyde dehydrogenase 2 family member	Homo sapiens	200-205
26649137-0	2016	Acetaldehyde Induces Cytotoxicity of SH-SY5Y Cells via Inhibition of Akt Activation and Induction of Oxidative Stress.	Acetaldehyde	0-12	AKT serine/threonine kinase 1	Homo sapiens	69-72
26000808-1	2016	AIM: Aldehyde dehydrogenase 2 (ALDH2) is a key enzyme that metabolizes acetaldehyde to acetic acid.	Acetaldehyde	71-83	aldehyde dehydrogenase 2 family member	Homo sapiens	5-29
26000808-1	2016	AIM: Aldehyde dehydrogenase 2 (ALDH2) is a key enzyme that metabolizes acetaldehyde to acetic acid.	Acetaldehyde	71-83	aldehyde dehydrogenase 2 family member	Homo sapiens	31-36
26788255-5	2016	Cyp2E1 content increased with HC diet, as well as in those treated with ethanol or acetaldehyde, while the activity of this enzyme determined in microsomes increased in the HC and in all ethanol treated hepatocytes, HC and CW.	Acetaldehyde	83-95	cytochrome P450, family 2, subfamily e, polypeptide 1	Mus musculus	0-6
26711020-0	2016	Ethanol and acetaldehyde differentially alter extracellular dopamine and serotonin in Aldh2-knockout mouse dorsal striatum: A reverse microdialysis study.	Acetaldehyde	12-24	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	86-91
26711020-9	2016	In contrast, perfusion with 200 and 500muM AcH decreased both DA and 5-HT (p&lt;0.05) in Aldh2-KO mice, but this decrease was not found in WT mice at any AcH dose, indicating an effect of AcH on DA and 5-HT levels.	Acetaldehyde	43-46	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	89-94
26649137-5	2016	In this study, we investigated the cytotoxic effects of acetaldehyde in SH-SY5Y cells and found that acetaldehyde induced apoptosis of SH-SY5Y cells by downregulating the expression of antiapoptotic Bcl-2 and Bcl-xL and upregulating the expression of proapoptotic Bax.	Acetaldehyde	101-113	BCL2 apoptosis regulator	Homo sapiens	199-204
26649137-5	2016	In this study, we investigated the cytotoxic effects of acetaldehyde in SH-SY5Y cells and found that acetaldehyde induced apoptosis of SH-SY5Y cells by downregulating the expression of antiapoptotic Bcl-2 and Bcl-xL and upregulating the expression of proapoptotic Bax.	Acetaldehyde	101-113	BCL2 like 1	Homo sapiens	209-215
26649137-5	2016	In this study, we investigated the cytotoxic effects of acetaldehyde in SH-SY5Y cells and found that acetaldehyde induced apoptosis of SH-SY5Y cells by downregulating the expression of antiapoptotic Bcl-2 and Bcl-xL and upregulating the expression of proapoptotic Bax.	Acetaldehyde	101-113	BCL2 associated X, apoptosis regulator	Homo sapiens	264-267
26649137-6	2016	Acetaldehyde treatment led to a significant decrease in the levels of activated Akt and cyclic AMP-responsive element binding protein (CREB).	Acetaldehyde	0-12	AKT serine/threonine kinase 1	Homo sapiens	80-83
26649137-6	2016	Acetaldehyde treatment led to a significant decrease in the levels of activated Akt and cyclic AMP-responsive element binding protein (CREB).	Acetaldehyde	0-12	cAMP responsive element binding protein 1	Homo sapiens	88-133
26649137-6	2016	Acetaldehyde treatment led to a significant decrease in the levels of activated Akt and cyclic AMP-responsive element binding protein (CREB).	Acetaldehyde	0-12	cAMP responsive element binding protein 1	Homo sapiens	135-139
26649137-7	2016	In addition, acetaldehyde induced the activation of p38 mitogen-activated protein kinase (MAPK) while inhibiting the activation of extracellular signal-regulated kinases (ERKs, p44/p42MAPK).	Acetaldehyde	13-25	mitogen-activated protein kinase 14	Homo sapiens	52-88
26649137-7	2016	In addition, acetaldehyde induced the activation of p38 mitogen-activated protein kinase (MAPK) while inhibiting the activation of extracellular signal-regulated kinases (ERKs, p44/p42MAPK).	Acetaldehyde	13-25	mitogen-activated protein kinase 1	Homo sapiens	90-94
26649137-7	2016	In addition, acetaldehyde induced the activation of p38 mitogen-activated protein kinase (MAPK) while inhibiting the activation of extracellular signal-regulated kinases (ERKs, p44/p42MAPK).	Acetaldehyde	13-25	mitogen-activated protein kinase 1	Homo sapiens	171-175
26649137-7	2016	In addition, acetaldehyde induced the activation of p38 mitogen-activated protein kinase (MAPK) while inhibiting the activation of extracellular signal-regulated kinases (ERKs, p44/p42MAPK).	Acetaldehyde	13-25	interferon induced protein 44	Homo sapiens	177-180
26649137-7	2016	In addition, acetaldehyde induced the activation of p38 mitogen-activated protein kinase (MAPK) while inhibiting the activation of extracellular signal-regulated kinases (ERKs, p44/p42MAPK).	Acetaldehyde	13-25	mitogen-activated protein kinase 1	Homo sapiens	181-188
26142864-1	2015	Many human gastrointestinal facultative anaerobic and aerobic bacteria possess alcohol dehydrogenase (ADH) activity and are therefore capable of oxidizing ethanol to acetaldehyde.	Acetaldehyde	166-178	aldo-keto reductase family 1 member A1	Homo sapiens	79-100
27578490-5	2016	RESULTS: Despite inhibition of the hepatic ALDH, ISO did not result in elevated blood acetaldehyde levels after ETH administration, probably due to the induction of cytochrome P450 2E1 which theoretically leads to an increased elimination rate of acetaldehyde preventing its accumulation.	Acetaldehyde	247-259	cytochrome P450, family 2, subfamily e, polypeptide 1	Rattus norvegicus	165-184
26472042-8	2015	qRT-PCR experiments determined that among these candidates, miR-30a and miR-934 were the most highly upregulated in vitro by alcohol and acetaldehyde.	Acetaldehyde	137-149	microRNA 30a	Homo sapiens	60-67
26472042-8	2015	qRT-PCR experiments determined that among these candidates, miR-30a and miR-934 were the most highly upregulated in vitro by alcohol and acetaldehyde.	Acetaldehyde	137-149	microRNA 934	Homo sapiens	72-79
26701629-5	2015	Mitochondrial aldehyde dehydrogenase (ALDH2) is an enzyme metabolizing acetaldehyde and toxic aldehydes.	Acetaldehyde	71-83	aldehyde dehydrogenase 2 family member	Homo sapiens	38-43
26376349-3	2015	Polymorphisms in the aldehyde dehydrogenase 2 gene, which encodes an enzyme that eliminates acetaldehyde, have been associated with esophageal carcinogenesis.	Acetaldehyde	92-104	aldehyde dehydrogenase 2 family member	Homo sapiens	21-45
26298003-3	2015	The aldehyde dehydrogenase (ALDH) inhibitor cyanamide was used to mimic the effect of prolonged acetaldehyde exposure because acetaldehyde is quickly degraded by ALDH.	Acetaldehyde	96-108	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	4-26
26298003-3	2015	The aldehyde dehydrogenase (ALDH) inhibitor cyanamide was used to mimic the effect of prolonged acetaldehyde exposure because acetaldehyde is quickly degraded by ALDH.	Acetaldehyde	96-108	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	28-32
26298003-3	2015	The aldehyde dehydrogenase (ALDH) inhibitor cyanamide was used to mimic the effect of prolonged acetaldehyde exposure because acetaldehyde is quickly degraded by ALDH.	Acetaldehyde	96-108	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	162-166
26298003-3	2015	The aldehyde dehydrogenase (ALDH) inhibitor cyanamide was used to mimic the effect of prolonged acetaldehyde exposure because acetaldehyde is quickly degraded by ALDH.	Acetaldehyde	126-138	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	4-26
26298003-3	2015	The aldehyde dehydrogenase (ALDH) inhibitor cyanamide was used to mimic the effect of prolonged acetaldehyde exposure because acetaldehyde is quickly degraded by ALDH.	Acetaldehyde	126-138	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	28-32
26298003-3	2015	The aldehyde dehydrogenase (ALDH) inhibitor cyanamide was used to mimic the effect of prolonged acetaldehyde exposure because acetaldehyde is quickly degraded by ALDH.	Acetaldehyde	126-138	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	162-166
26298003-6	2015	Systemic administration of acetaldehyde with cyanamide suppressed blood pressure and increased plasma renin activity.	Acetaldehyde	27-39	renin	Rattus norvegicus	102-107
26298003-7	2015	Blockade of central angiotensin receptor AT1R suppressed the acetaldehyde-induced fluid intake and c-Fos expression in the circumventricular organs (CVOs), which form part of dipsogenic mechanism in the brain.	Acetaldehyde	61-73	angiotensin II receptor, type 1a	Rattus norvegicus	41-45
26298003-11	2015	First acetaldehyde indirectly activates AT1R in the dipsogenic centers via the peripheral renin-angiotensin system following the depressor response and induces both water and salt intake.	Acetaldehyde	6-18	angiotensin II receptor, type 1a	Rattus norvegicus	40-44
26298003-11	2015	First acetaldehyde indirectly activates AT1R in the dipsogenic centers via the peripheral renin-angiotensin system following the depressor response and induces both water and salt intake.	Acetaldehyde	6-18	renin	Rattus norvegicus	90-95
26251470-7	2015	Ach exposure decreased STAT-1 methylation via activation of protein phosphatase 2A and increased the protein inhibitor of activated STAT-1 (PIAS-1)-STAT-1 complex formation in both HCV(+) and HCV(-) cells, preventing ISG activation.	Acetaldehyde	0-3	signal transducer and activator of transcription 1	Homo sapiens	23-29
26251470-7	2015	Ach exposure decreased STAT-1 methylation via activation of protein phosphatase 2A and increased the protein inhibitor of activated STAT-1 (PIAS-1)-STAT-1 complex formation in both HCV(+) and HCV(-) cells, preventing ISG activation.	Acetaldehyde	0-3	signal transducer and activator of transcription 1	Homo sapiens	132-138
26251470-7	2015	Ach exposure decreased STAT-1 methylation via activation of protein phosphatase 2A and increased the protein inhibitor of activated STAT-1 (PIAS-1)-STAT-1 complex formation in both HCV(+) and HCV(-) cells, preventing ISG activation.	Acetaldehyde	0-3	signal transducer and activator of transcription 1	Homo sapiens	132-138
26251470-11	2015	We concluded that Ach potentiates the suppressive effects of HCV on activation of ISGs attributable to methylation-dependent dysregulation of IFN-alpha signaling.	Acetaldehyde	18-21	interferon alpha 1	Homo sapiens	142-151
25761756-6	2015	Importantly, ChREBP silencing in the liver of EtOH-fed mice prevented alcohol-induced triglyceride accumulation through an inhibition of the lipogenic pathway but also led, unexpectedly, to hypothermia, increased blood acetaldehyde concentrations, and enhanced lethality.	Acetaldehyde	219-231	MLX interacting protein-like	Mus musculus	13-19
26374466-0	2015	Protective role of ALDH2 against acetaldehyde-derived DNA damage in oesophageal squamous epithelium.	Acetaldehyde	33-45	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	19-24
26374466-2	2015	Aldehyde dehydrogenase 2 (ALDH2) is a key enzyme that eliminates acetaldehyde, and impairment of ALDH2 increases the risk of ESCC.	Acetaldehyde	65-77	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	0-24
26374466-2	2015	Aldehyde dehydrogenase 2 (ALDH2) is a key enzyme that eliminates acetaldehyde, and impairment of ALDH2 increases the risk of ESCC.	Acetaldehyde	65-77	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	26-31
26374466-5	2015	Notably, levels of acetaldehyde-derived DNA damage represented by N(2)-ethylidene-2"-deoxyguanosine were higher in the oesophagus of Aldh2-knockout mice than in wild-type mice upon ethanol consumption.	Acetaldehyde	19-31	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	133-138
26374466-6	2015	In vitro experiments revealed that acetaldehyde induced ALDH2 production in both mouse and human oesophageal keratinocytes.	Acetaldehyde	35-47	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	56-61
26374466-7	2015	Furthermore, the N(2)-ethylidene-2"-deoxyguanosine levels increased in both Aldh2-knockout mouse keratinocytes and ALDH2-knockdown human keratinocytes treated with acetaldehyde.	Acetaldehyde	164-176	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	76-81
26374466-7	2015	Furthermore, the N(2)-ethylidene-2"-deoxyguanosine levels increased in both Aldh2-knockout mouse keratinocytes and ALDH2-knockdown human keratinocytes treated with acetaldehyde.	Acetaldehyde	164-176	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	115-120
26374466-9	2015	Our findings provide new insight into the preventive role of oesophageal ALDH2 against acetaldehyde-derived DNA damage.	Acetaldehyde	87-99	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	73-78
25857743-9	2015	During the first stage ethanol is oxidized into acetaldehyde, under the action of alcohol dehydrogenase.	Acetaldehyde	48-60	aldo-keto reductase family 1 member A1	Homo sapiens	82-103
26142864-1	2015	Many human gastrointestinal facultative anaerobic and aerobic bacteria possess alcohol dehydrogenase (ADH) activity and are therefore capable of oxidizing ethanol to acetaldehyde.	Acetaldehyde	166-178	aldo-keto reductase family 1 member A1	Homo sapiens	102-105
26187464-1	2015	CutC choline trimethylamine-lyase is an anaerobic bacterial glycyl radical enzyme (GRE) that cleaves choline to produce trimethylamine (TMA) and acetaldehyde.	Acetaldehyde	145-157	cutC copper transporter	Homo sapiens	0-4
26173414-2	2015	Aldehyde dehydrogenase (ALDH) detoxifies acetaldehyde into acetate.	Acetaldehyde	41-53	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	0-22
26086111-4	2015	Our recent in vitro studies using human ALDH1B1 showed that it metabolizes acetaldehyde and retinaldehyde.	Acetaldehyde	75-87	aldehyde dehydrogenase 1 family member B1	Homo sapiens	40-47
26086111-9	2015	Collectively, we show for the first time the functional in vivo role of ALDH1B1 in acetaldehyde metabolism and in maintaining glucose homeostasis.	Acetaldehyde	83-95	aldehyde dehydrogenase 1 family, member B1	Mus musculus	72-79
26173414-2	2015	Aldehyde dehydrogenase (ALDH) detoxifies acetaldehyde into acetate.	Acetaldehyde	41-53	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	24-28
25956975-11	2015	These results suggested that a combination of cAMP/PKA/CREB signals via A2AR and A1R likely mediate the activation of acetaldehyde-induced HSCs, and A1R coupled to the Gi/o-AC signaling pathway may be masked by the more predominant A2AR that coupled to the Gs-AC signaling pathway.	Acetaldehyde	118-130	cAMP responsive element binding protein 1	Rattus norvegicus	55-59
25956975-11	2015	These results suggested that a combination of cAMP/PKA/CREB signals via A2AR and A1R likely mediate the activation of acetaldehyde-induced HSCs, and A1R coupled to the Gi/o-AC signaling pathway may be masked by the more predominant A2AR that coupled to the Gs-AC signaling pathway.	Acetaldehyde	118-130	adenosine A2a receptor	Rattus norvegicus	72-76
25956975-1	2015	The present study was undertaken to investigate the mechanism by which adenosine receptors (ARs)-mediated the cAMP/PKA/CREB signal pathway regulates the activation of acetaldehyde-induced hepatic stellate cells (HSCs).	Acetaldehyde	167-179	cAMP responsive element binding protein 1	Rattus norvegicus	119-123
25827479-11	2015	Kinetic simulations revealed that inhibition by acetaldehyde may largely account for the observed reduction of ADH1 oxidation rates after cyanamide treatment.	Acetaldehyde	48-60	alcohol dehydrogenase 1C (class I), gamma polypeptide	Rattus norvegicus	111-115
25956975-8	2015	The expression of A2AR and A1R was significantly increased in acetaldehyde-induced HSCs as compared with that of control group, whereas the expression of A2BR and A3R remained unaffected by the addition of acetaldehyde.	Acetaldehyde	62-74	adenosine A2a receptor	Rattus norvegicus	18-22
26192017-12	2015	This threshold is combined with the singlet-triplet spacings of O atoms and acetaldehyde to establish the dissociation energy for syn-CH3HOO X(1)A" to the lowest spin-allowed product channel, CH3CHO X(1)A" + O (1)D, of &lt;=55.9 +- 0.4 kcal mol(-1).	Acetaldehyde	76-88	synemin	Homo sapiens	130-133
26150517-1	2015	Mitochondrial aldehyde dehydrogenase 2 (ALDH2) in the liver removes toxic aldehydes including acetaldehyde, an intermediate of ethanol metabolism.	Acetaldehyde	94-106	aldehyde dehydrogenase 2 family member	Homo sapiens	40-45
25641190-4	2015	This specific study was designed to find a novel modulator of ALDH2, a mitochondrial ALDH isoenzyme most well-known for its role in acetaldehyde oxidation.	Acetaldehyde	132-144	aldehyde dehydrogenase 2 family member	Homo sapiens	62-67
25641190-4	2015	This specific study was designed to find a novel modulator of ALDH2, a mitochondrial ALDH isoenzyme most well-known for its role in acetaldehyde oxidation.	Acetaldehyde	132-144	aldehyde dehydrogenase 1 family member A1	Homo sapiens	62-66
25740962-12	2015	However, inhibition of acetaldehyde breakdown attenuated KLF4 induction and promoted M1 polarization.	Acetaldehyde	23-35	Kruppel-like factor 4 (gut)	Mus musculus	57-61
25772736-7	2015	Kinetic inhibition equation-based simulations show at higher therapeutic levels of blood plasma salicylate (1.5 mM) that the decrease of activities at 2-10 mM ethanol for ADH1A/ADH2 and ADH1B2/ADH1B3 are predicted to be 75-86% and 31-52%, respectively, and that the activity decline for ALDH1A1 and ALDH2 at 10-50 muM acetaldehyde to be 62-73%.	Acetaldehyde	318-330	alcohol dehydrogenase 1A (class I), alpha polypeptide	Homo sapiens	171-176
25772736-7	2015	Kinetic inhibition equation-based simulations show at higher therapeutic levels of blood plasma salicylate (1.5 mM) that the decrease of activities at 2-10 mM ethanol for ADH1A/ADH2 and ADH1B2/ADH1B3 are predicted to be 75-86% and 31-52%, respectively, and that the activity decline for ALDH1A1 and ALDH2 at 10-50 muM acetaldehyde to be 62-73%.	Acetaldehyde	318-330	alcohol dehydrogenase 4 (class II), pi polypeptide	Homo sapiens	177-181
25772736-7	2015	Kinetic inhibition equation-based simulations show at higher therapeutic levels of blood plasma salicylate (1.5 mM) that the decrease of activities at 2-10 mM ethanol for ADH1A/ADH2 and ADH1B2/ADH1B3 are predicted to be 75-86% and 31-52%, respectively, and that the activity decline for ALDH1A1 and ALDH2 at 10-50 muM acetaldehyde to be 62-73%.	Acetaldehyde	318-330	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	186-191
25772736-7	2015	Kinetic inhibition equation-based simulations show at higher therapeutic levels of blood plasma salicylate (1.5 mM) that the decrease of activities at 2-10 mM ethanol for ADH1A/ADH2 and ADH1B2/ADH1B3 are predicted to be 75-86% and 31-52%, respectively, and that the activity decline for ALDH1A1 and ALDH2 at 10-50 muM acetaldehyde to be 62-73%.	Acetaldehyde	318-330	aldehyde dehydrogenase 1 family member A1	Homo sapiens	287-294
25772736-7	2015	Kinetic inhibition equation-based simulations show at higher therapeutic levels of blood plasma salicylate (1.5 mM) that the decrease of activities at 2-10 mM ethanol for ADH1A/ADH2 and ADH1B2/ADH1B3 are predicted to be 75-86% and 31-52%, respectively, and that the activity decline for ALDH1A1 and ALDH2 at 10-50 muM acetaldehyde to be 62-73%.	Acetaldehyde	318-330	aldehyde dehydrogenase 2 family member	Homo sapiens	299-304
25740962-14	2015	EtOH promotes KLF4 and M2 phenotype, whereas acetaldehyde attenuates KLF4 and promotes M1 macrophage, which may explain the increased presence of M1 and M2 macrophage populations in ALD.	Acetaldehyde	45-57	Kruppel-like factor 4 (gut)	Mus musculus	69-73
25403981-1	2015	BACKGROUND: Mitochondrial aldehyde dehydrogenase-2 (ALDH2) is an enzyme that oxidizes acetaldehyde into acetic acid during alcohol metabolism.	Acetaldehyde	86-98	aldehyde dehydrogenase 2 family member	Homo sapiens	52-57
25413692-0	2015	Human ALDH1B1 polymorphisms may affect the metabolism of acetaldehyde and all-trans retinaldehyde--in vitro studies and computational modeling.	Acetaldehyde	57-69	aldehyde dehydrogenase 1 family member B1	Homo sapiens	6-13
26087623-10	2015	We also for the first time demonstrated that the evolutionarily young ADH1B*48His allele (which determines a high rate of ethanol metabolism into acetaldehyde) is presented with a large frequency in those populations where filariasis is endemic.	Acetaldehyde	146-158	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	70-75
25683389-7	2015	ALDH2 enzyme is primarily responsible for oxidation of acetaldehyde derived from ethanol metabolism, as well as oxidation of various other endogenous and exogenous aldehydes.	Acetaldehyde	55-67	aldehyde dehydrogenase 2 family member	Homo sapiens	0-5
25683389-14	2015	As a result, high amounts of acetaldehyde will circulate for longer time in the blood, until the liver CYP2E1(p450) enzyme system finally metabilizes the acetaldehyde, during that period of time the patients will experience a flushing as well as the people with the "Asian flushing syndrome" suffer when they drink ethanol.	Acetaldehyde	29-41	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	103-109
25683389-14	2015	As a result, high amounts of acetaldehyde will circulate for longer time in the blood, until the liver CYP2E1(p450) enzyme system finally metabilizes the acetaldehyde, during that period of time the patients will experience a flushing as well as the people with the "Asian flushing syndrome" suffer when they drink ethanol.	Acetaldehyde	29-41	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	110-114
25683389-14	2015	As a result, high amounts of acetaldehyde will circulate for longer time in the blood, until the liver CYP2E1(p450) enzyme system finally metabilizes the acetaldehyde, during that period of time the patients will experience a flushing as well as the people with the "Asian flushing syndrome" suffer when they drink ethanol.	Acetaldehyde	154-166	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	103-109
25683389-14	2015	As a result, high amounts of acetaldehyde will circulate for longer time in the blood, until the liver CYP2E1(p450) enzyme system finally metabilizes the acetaldehyde, during that period of time the patients will experience a flushing as well as the people with the "Asian flushing syndrome" suffer when they drink ethanol.	Acetaldehyde	154-166	cytochrome P450 family 2 subfamily B member 6	Homo sapiens	110-114
25831092-2	2015	Aldehyde dehydrogenase (ALDH2), a major ACH eliminating enzyme, is genetically deficient in 30-50% of Eastern Asians.	Acetaldehyde	40-43	aldehyde dehydrogenase 2 family member	Homo sapiens	24-29
25831092-9	2015	The gastric mucosa also possesses the acetaldehyde-eliminating ALDH2 enzyme.	Acetaldehyde	38-50	aldehyde dehydrogenase 2 family member	Homo sapiens	63-68
25831092-10	2015	Due to decreased mucosal ALDH2 activity, the elimination of ethanol-derived acetaldehyde is decreased, which results in its accumulation in the gastric juice.	Acetaldehyde	76-88	aldehyde dehydrogenase 2 family member	Homo sapiens	25-30
25831092-11	2015	We also demonstrate that ALDH2 deficiency, proton pump inhibitor (PPI) treatment, and L-cysteine cause independent changes in gastric juice and salivary acetaldehyde levels, indicating that intragastric acetaldehyde is locally regulated by gastric mucosal ADH and ALDH2 enzymes, and by oral microbes colonizing an achlorhydric stomach.	Acetaldehyde	153-165	aldehyde dehydrogenase 2 family member	Homo sapiens	25-30
25831092-11	2015	We also demonstrate that ALDH2 deficiency, proton pump inhibitor (PPI) treatment, and L-cysteine cause independent changes in gastric juice and salivary acetaldehyde levels, indicating that intragastric acetaldehyde is locally regulated by gastric mucosal ADH and ALDH2 enzymes, and by oral microbes colonizing an achlorhydric stomach.	Acetaldehyde	203-215	aldehyde dehydrogenase 2 family member	Homo sapiens	25-30
25831092-13	2015	A capsule that slowly releases L-cysteine effectively eliminated acetaldehyde from the gastric juice of PPI-treated ALDH2-active and ALDH2-deficient subjects.	Acetaldehyde	65-77	aldehyde dehydrogenase 2 family member	Homo sapiens	116-121
25831092-13	2015	A capsule that slowly releases L-cysteine effectively eliminated acetaldehyde from the gastric juice of PPI-treated ALDH2-active and ALDH2-deficient subjects.	Acetaldehyde	65-77	aldehyde dehydrogenase 2 family member	Homo sapiens	133-138
25713355-0	2015	Pharmacological recruitment of aldehyde dehydrogenase 3A1 (ALDH3A1) to assist ALDH2 in acetaldehyde and ethanol metabolism in vivo.	Acetaldehyde	87-99	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	31-57
25713355-0	2015	Pharmacological recruitment of aldehyde dehydrogenase 3A1 (ALDH3A1) to assist ALDH2 in acetaldehyde and ethanol metabolism in vivo.	Acetaldehyde	87-99	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	59-66
25713355-0	2015	Pharmacological recruitment of aldehyde dehydrogenase 3A1 (ALDH3A1) to assist ALDH2 in acetaldehyde and ethanol metabolism in vivo.	Acetaldehyde	87-99	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	78-83
25713355-4	2015	To temporarily increase metabolism of acetaldehyde in vivo, we describe an approach in which a pharmacologic agent recruited another ALDH to metabolize acetaldehyde.	Acetaldehyde	38-50	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	133-137
25713355-4	2015	To temporarily increase metabolism of acetaldehyde in vivo, we describe an approach in which a pharmacologic agent recruited another ALDH to metabolize acetaldehyde.	Acetaldehyde	152-164	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	133-137
25713355-5	2015	We focused on ALDH3A1, which is enriched in the upper aerodigestive track, and identified Alda-89 as a small molecule that enables ALDH3A1 to metabolize acetaldehyde.	Acetaldehyde	153-165	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	131-138
25713355-6	2015	When given together with the ALDH2-specific activator, Alda-1, Alda-89 reduced acetaldehyde-induced behavioral impairment by causing a rapid reduction in blood ethanol and acetaldehyde levels after acute ethanol intoxication in both wild-type and ALDH2-deficient, ALDH2*1/*2, heterozygotic knock-in mice.	Acetaldehyde	79-91	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	29-34
25713355-6	2015	When given together with the ALDH2-specific activator, Alda-1, Alda-89 reduced acetaldehyde-induced behavioral impairment by causing a rapid reduction in blood ethanol and acetaldehyde levels after acute ethanol intoxication in both wild-type and ALDH2-deficient, ALDH2*1/*2, heterozygotic knock-in mice.	Acetaldehyde	172-184	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	29-34
25662247-9	2015	The emission ratios relative to toluene for formaldehyde, acetaldehyde, and acetone were determined to be 0.10, 0.20 and 0.40 ppb/ppb, respectively.	Acetaldehyde	58-70	histatin 1	Homo sapiens	130-133
25457208-1	2015	BACKGROUND &amp; AIMS: Mitochondrial aldehyde dehydrogenase (ALDH2) plays a critical role in the detoxification of the ethanol metabolite acetaldehyde.	Acetaldehyde	138-150	aldehyde dehydrogenase 2 family member	Homo sapiens	61-66
25457208-8	2015	Moreover, ethanol (100 mM) and acetaldehyde (100 and 500 muM) increased levels of IL-6 and IFN-gamma, and suppressed autophagy in VA-13 cells, effects which were markedly alleviated by rapamycin.	Acetaldehyde	31-43	interleukin 6	Homo sapiens	82-86
25457208-8	2015	Moreover, ethanol (100 mM) and acetaldehyde (100 and 500 muM) increased levels of IL-6 and IFN-gamma, and suppressed autophagy in VA-13 cells, effects which were markedly alleviated by rapamycin.	Acetaldehyde	31-43	interferon gamma	Homo sapiens	91-100
25662247-9	2015	The emission ratios relative to toluene for formaldehyde, acetaldehyde, and acetone were determined to be 0.10, 0.20 and 0.40 ppb/ppb, respectively.	Acetaldehyde	58-70	histatin 1	Homo sapiens	126-129
25636114-1	2015	Aldehyde dehydrogenase 2 (ALDH2), as one of the most important alcohol metabolizing enzymes, plays a significant role in the detoxification process of acetaldehyde which is a main carcinogenic product of alcoholic metabolism.	Acetaldehyde	151-163	aldehyde dehydrogenase 2 family member	Homo sapiens	0-24
25636114-1	2015	Aldehyde dehydrogenase 2 (ALDH2), as one of the most important alcohol metabolizing enzymes, plays a significant role in the detoxification process of acetaldehyde which is a main carcinogenic product of alcoholic metabolism.	Acetaldehyde	151-163	aldehyde dehydrogenase 2 family member	Homo sapiens	26-31
25448285-1	2015	Aldehyde dehydrogenase 2 (ALDH2) detoxifies toxic aldehydes, e.g. acetaldehyde in cigarette smoke; however, the interactive effects between smoking status and the ALDH2 genotype on coronary artery disease (CAD) have not been reported.	Acetaldehyde	66-78	aldehyde dehydrogenase 2 family member	Homo sapiens	0-24
25495913-4	2015	With the mimicking sandwich-type reaction, the cascade catalysis amplification strategy was carried out by AOx catalyzing ethanol to acetaldehyde with the concomitant formation of high concentration of H2O2, which was further electrocatalyzed by PtNPs and Cyt c.	Acetaldehyde	133-145	acyl-CoA oxidase 1	Homo sapiens	107-110
25495913-4	2015	With the mimicking sandwich-type reaction, the cascade catalysis amplification strategy was carried out by AOx catalyzing ethanol to acetaldehyde with the concomitant formation of high concentration of H2O2, which was further electrocatalyzed by PtNPs and Cyt c.	Acetaldehyde	133-145	cytochrome c, somatic	Homo sapiens	256-261
25448285-1	2015	Aldehyde dehydrogenase 2 (ALDH2) detoxifies toxic aldehydes, e.g. acetaldehyde in cigarette smoke; however, the interactive effects between smoking status and the ALDH2 genotype on coronary artery disease (CAD) have not been reported.	Acetaldehyde	66-78	aldehyde dehydrogenase 2 family member	Homo sapiens	26-31
25448285-1	2015	Aldehyde dehydrogenase 2 (ALDH2) detoxifies toxic aldehydes, e.g. acetaldehyde in cigarette smoke; however, the interactive effects between smoking status and the ALDH2 genotype on coronary artery disease (CAD) have not been reported.	Acetaldehyde	66-78	aldehyde dehydrogenase 2 family member	Homo sapiens	163-168
25427900-8	2015	This is probably just the tip of the iceberg, since more recent epidemiological studies have also shown significant positive associations between the aldehyde dehydrogenase ALDH2 (rs671)*2 allele (encoding inactive enzyme causing high acetaldehyde elevations) and gastric, colorectal, lung, and hepatocellular cancers.	Acetaldehyde	235-247	aldehyde dehydrogenase 2 family member	Homo sapiens	173-178
24103023-3	2015	Evidence indicates that catalase-mediated conversion of ethanol into acetaldehyde in pVTA plays a critical role in this effect.	Acetaldehyde	69-81	catalase	Mus musculus	24-32
24103023-9	2015	This effect requires ethanol oxidation into acetaldehyde given that, when H2 O2 -catalase system was impaired by either 3-amino-1,2,4-triazole or in vivo administration of alpha-lipoic acid, ethanol did not enhance DA cell activity.	Acetaldehyde	44-56	catalase	Mus musculus	81-89
25946330-9	2015	ldlr(-/-) syk(-/-) mice fed a high-fat diet produced lower levels of IgG to malondialdehyde (MDA)-LDL, malondialdehyde-acetaldehyde (MAA)-LDL, and OxLDL compared to ldlr(-/-) mice.	Acetaldehyde	119-131	spleen tyrosine kinase	Mus musculus	10-13
26233911-5	2015	In addition, aldehyde dehydrogenases including the mitochondrial low Km aldehyde dehydrogenase-2 (ALDH2), responsible for the metabolism of acetaldehyde and lipid aldehydes, can be inactivated by various hepatotoxic agents.	Acetaldehyde	140-152	aldehyde dehydrogenase 2 family member	Homo sapiens	72-96
26233911-5	2015	In addition, aldehyde dehydrogenases including the mitochondrial low Km aldehyde dehydrogenase-2 (ALDH2), responsible for the metabolism of acetaldehyde and lipid aldehydes, can be inactivated by various hepatotoxic agents.	Acetaldehyde	140-152	aldehyde dehydrogenase 2 family member	Homo sapiens	98-103
26233911-6	2015	These highly reactive acetaldehyde and lipid peroxides, accumulated due to ALDH2 suppression, can interact with cellular macromolecules DNA/RNA, lipids, and proteins, leading to suppression of their normal function, contributing to DNA mutations, endoplasmic reticulum stress, mitochondrial dysfunction, steatosis, and cell death.	Acetaldehyde	22-34	aldehyde dehydrogenase 2 family member	Homo sapiens	75-80
25427912-1	2015	Genetic polymorphisms of alcohol dehydrogenase-1B (ADH1B) and aldehyde dehydrogenase-2 (ALDH2) modulate exposure levels to ethanol/acetaldehyde.	Acetaldehyde	131-143	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	25-49
25427912-1	2015	Genetic polymorphisms of alcohol dehydrogenase-1B (ADH1B) and aldehyde dehydrogenase-2 (ALDH2) modulate exposure levels to ethanol/acetaldehyde.	Acetaldehyde	131-143	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	51-56
25427912-1	2015	Genetic polymorphisms of alcohol dehydrogenase-1B (ADH1B) and aldehyde dehydrogenase-2 (ALDH2) modulate exposure levels to ethanol/acetaldehyde.	Acetaldehyde	131-143	aldehyde dehydrogenase 2 family member	Homo sapiens	62-86
25427912-1	2015	Genetic polymorphisms of alcohol dehydrogenase-1B (ADH1B) and aldehyde dehydrogenase-2 (ALDH2) modulate exposure levels to ethanol/acetaldehyde.	Acetaldehyde	131-143	aldehyde dehydrogenase 2 family member	Homo sapiens	88-93
25427912-3	2015	The risks of upper aerodigestive tract SCC/dysplasia, especially of multiple SCC/dysplasia, were increased in a multiplicative fashion by the presence of a combination of slow-metabolizing ADH1B*1/*1 and inactive heterozygous ALDH2*1/*2 because of prolonged exposure to higher concentrations of ethanol/acetaldehyde.	Acetaldehyde	303-315	serpin family B member 3	Homo sapiens	39-42
25427912-3	2015	The risks of upper aerodigestive tract SCC/dysplasia, especially of multiple SCC/dysplasia, were increased in a multiplicative fashion by the presence of a combination of slow-metabolizing ADH1B*1/*1 and inactive heterozygous ALDH2*1/*2 because of prolonged exposure to higher concentrations of ethanol/acetaldehyde.	Acetaldehyde	303-315	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	189-194
25427913-4	2015	Acetaldehyde is metabolized by ALDH2, ALDH1B1, and ALDH1A1 to acetate.	Acetaldehyde	0-12	aldehyde dehydrogenase 2 family member	Homo sapiens	31-36
25427913-4	2015	Acetaldehyde is metabolized by ALDH2, ALDH1B1, and ALDH1A1 to acetate.	Acetaldehyde	0-12	aldehyde dehydrogenase 1 family member B1	Homo sapiens	38-45
25427913-4	2015	Acetaldehyde is metabolized by ALDH2, ALDH1B1, and ALDH1A1 to acetate.	Acetaldehyde	0-12	aldehyde dehydrogenase 1 family member A1	Homo sapiens	51-58
25243355-11	2014	These results suggest that temperature-induced redox imbalances could be compensated by increased glycerol accumulation or production of cytosolic acetaldehyde through the deletion of GUT2 or ADH3, respectively.	Acetaldehyde	147-159	glycerol-3-phosphate dehydrogenase	Saccharomyces cerevisiae S288C	184-188
25548474-4	2014	Acetaldehyde is known to be toxic to the liver and alters lipid homeostasis, decreasing peroxisome proliferator-activated receptors and increasing sterol regulatory element binding protein activity via an AMP-activated protein kinase (AMPK)-dependent mechanism.	Acetaldehyde	0-12	CCHC-type zinc finger nucleic acid binding protein	Homo sapiens	147-188
26491656-1	2015	Aldehyde dehydrogenase (ALDH) 2 is a mitochondrial enzyme that is known for its important role in oxidation and detoxification of ethanol metabolite acetaldehyde.	Acetaldehyde	149-161	aldehyde dehydrogenase 2 family member	Homo sapiens	0-31
26491656-3	2015	The Glu504Lys single nucleotide polymorphism (SNP) of ALDH2 gene, which is found in approximately 40% of the East Asian populations, causes defect in the enzyme activity of ALDH2, leading to alterations in acetaldehyde metabolism and alcohol-induced "flushing" syndrome.	Acetaldehyde	206-218	aldehyde dehydrogenase 2 family member	Homo sapiens	54-59
26491656-3	2015	The Glu504Lys single nucleotide polymorphism (SNP) of ALDH2 gene, which is found in approximately 40% of the East Asian populations, causes defect in the enzyme activity of ALDH2, leading to alterations in acetaldehyde metabolism and alcohol-induced "flushing" syndrome.	Acetaldehyde	206-218	aldehyde dehydrogenase 2 family member	Homo sapiens	173-178
25318477-7	2015	Moreover, P2X7R silencing prevented ATP- and acetaldehyde-induced renin release.	Acetaldehyde	45-57	purinergic receptor P2X, ligand-gated ion channel, 7	Mus musculus	10-15
25327712-1	2015	Human O-phosphoethanolamine (PEA) phospho-lyase is a pyridoxal 5"-phosphate (PLP) dependent enzyme that catalyzes the degradation of PEA to acetaldehyde, phosphate and ammonia.	Acetaldehyde	140-152	pyridoxal phosphatase	Homo sapiens	77-80
25229427-1	2014	Deoxyribose-phosphate aldolase (EC 4.1.2.4), which converts 2-deoxy-d-ribose-5-phosphate into glyceraldehyde-3-phosphate and acetaldehyde, belongs to the core metabolism of living organisms.	Acetaldehyde	125-137	deoxyribose-phosphate aldolase	Homo sapiens	0-30
25365528-5	2014	RESULTS: The ALDH2*1/*2 heterozygotes carrying three ADH1B allelotypes showed significantly higher peak levels and areas under the concentration curve (AUCs) of the blood acetaldehyde as well as significantly greater increases in the peak pulse rate and peak FSBF compared with the ALDH2*1/*1 homozygotes.	Acetaldehyde	171-183	aldehyde dehydrogenase 2 family member	Homo sapiens	13-18
25365528-5	2014	RESULTS: The ALDH2*1/*2 heterozygotes carrying three ADH1B allelotypes showed significantly higher peak levels and areas under the concentration curve (AUCs) of the blood acetaldehyde as well as significantly greater increases in the peak pulse rate and peak FSBF compared with the ALDH2*1/*1 homozygotes.	Acetaldehyde	171-183	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	53-58
25365528-8	2014	CONCLUSION: Findings indicate that ALDH2*2, rather than ADH1B2*2, is a causal variant allele for the accumulation of blood acetaldehyde and the resultant facial flushing during low alcohol consumption.	Acetaldehyde	123-135	aldehyde dehydrogenase 2 family member	Homo sapiens	35-40
25213698-3	2014	Accumulating evidences demonstrated that ALDH7A1, one of ALDH superfamily members, degrades and detoxifies acetaldehyde generated by alcohol metabolism and have been associated with development and prognosis of multiple cancers.	Acetaldehyde	107-119	aldehyde dehydrogenase 7 family member A1	Homo sapiens	41-48
25241056-3	2014	Fenofibrate reduces blood triglyceride levels by increasing fatty acid oxidation by liver peroxisomes, along with an increase in the activity of catalase, which can oxidize ethanol to acetaldehyde.	Acetaldehyde	184-196	catalase	Rattus norvegicus	145-153
25243355-11	2014	These results suggest that temperature-induced redox imbalances could be compensated by increased glycerol accumulation or production of cytosolic acetaldehyde through the deletion of GUT2 or ADH3, respectively.	Acetaldehyde	147-159	alcohol dehydrogenase ADH3	Saccharomyces cerevisiae S288C	192-196
25008481-12	2014	Our study established MIR146A rs2431697 as a prognostic biomarker for ACE in anticoagulated AF patients.	Acetaldehyde	70-73	microRNA 146a	Homo sapiens	22-29
25764900-4	2014	These data put in question the opinion of the independent specialist about disturbances in the alcohol dehydrogenase activity in blood manifested as a considerable increase of the rate of acetaldehyde reduction to ethanol with the decreasing ethanol dehydration rate.	Acetaldehyde	188-200	aldo-keto reductase family 1 member A1	Homo sapiens	95-116
25084483-5	2014	Aldehyde dehydrogenase 2 (ALDH2) metabolizes acetaldehyde into nontoxic acetate.	Acetaldehyde	45-57	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	0-24
25084483-5	2014	Aldehyde dehydrogenase 2 (ALDH2) metabolizes acetaldehyde into nontoxic acetate.	Acetaldehyde	45-57	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	26-31
24863043-10	2014	These results indicate that cerebral CYP 2E1 activity could contribute to the locomotor-stimulating effects of EtOH, and therefore we suggest that centrally produced acetaldehyde might be a possible mediator of some EtOH-induced pharmacological effects.	Acetaldehyde	166-178	cytochrome P450, family 2, subfamily e, polypeptide 1	Mus musculus	37-44
24880893-2	2014	We have previously shown that exposure of bronchial epithelial cells to malondialdehyde-acetaldehyde (MAA) adducted protein increases protein kinase C (PKC) activity and proinflammatory cytokine release.	Acetaldehyde	88-100	protein kinase C, epsilon	Mus musculus	152-155
25111957-8	2014	Moreover, OA co-administration can significantly reduce the activity and expressions of CYP2E1 and ADH, which has characteristic of generation ROS mediated oxidative stress and acetaldehyde respectively.	Acetaldehyde	177-189	cytochrome P450, family 2, subfamily e, polypeptide 1	Rattus norvegicus	88-102
25157460-1	2014	Yeast (Saccharomyces cerevisiae) alcohol dehydrogenase I (ADH1) is the constitutive enzyme that reduces acetaldehyde to ethanol during the fermentation of glucose.	Acetaldehyde	104-116	alcohol dehydrogenase ADH1	Saccharomyces cerevisiae S288C	58-62
25064658-8	2014	The lower values of salivary ADH in smoking than non-smoking alcoholics might also be partly due to the reversed/inhibited ADH reaction by high levels of accumulated acetaldehyde.	Acetaldehyde	166-178	aldo-keto reductase family 1 member A1	Homo sapiens	29-32
25064658-8	2014	The lower values of salivary ADH in smoking than non-smoking alcoholics might also be partly due to the reversed/inhibited ADH reaction by high levels of accumulated acetaldehyde.	Acetaldehyde	166-178	aldo-keto reductase family 1 member A1	Homo sapiens	123-126
25163478-6	2014	Further, acetaldehyde- and formalin-induced nociceptive behavior was greater in the ALDH2*1/*2 mice than in the wild-type mice.	Acetaldehyde	9-21	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	84-89
24978604-6	2014	Together, the RVLM phosphatase activity acts tonically to attenuate the ERK-dependent pressor effect of ethanol or acetaldehyde in normotensive rats.	Acetaldehyde	115-127	Eph receptor B1	Rattus norvegicus	72-75
25084704-2	2014	Never users have more inactive aldehyde dehydrogenase 2 (ALDH2) alleles (A) potentially generating confounding because inactive alleles may increase acetaldehyde exposure and reduce lung function.	Acetaldehyde	149-161	aldehyde dehydrogenase 2 family member	Homo sapiens	31-55
24904079-11	2014	Furthermore, acetaldehyde induced LDH release and increased caspase3/7 activity and percentage of cells expressing cleaved CK18 and increased MUC2 protein expression compared with negative controls (P &lt; 0.0001).	Acetaldehyde	13-25	caspase 3	Homo sapiens	60-68
25084704-2	2014	Never users have more inactive aldehyde dehydrogenase 2 (ALDH2) alleles (A) potentially generating confounding because inactive alleles may increase acetaldehyde exposure and reduce lung function.	Acetaldehyde	149-161	aldehyde dehydrogenase 2 family member	Homo sapiens	57-62
25084704-8	2014	High frequency of inactive ALDH2 alleles in East Asia may exacerbate the effect of environmental acetaldehyde exposure on lung function and potentially on chronic obstructive pulmonary disease.	Acetaldehyde	97-109	aldehyde dehydrogenase 2 family member	Homo sapiens	27-32
24904079-11	2014	Furthermore, acetaldehyde induced LDH release and increased caspase3/7 activity and percentage of cells expressing cleaved CK18 and increased MUC2 protein expression compared with negative controls (P &lt; 0.0001).	Acetaldehyde	13-25	keratin 18	Homo sapiens	123-127
24492981-5	2014	Compared with wild-type mice, ethanol-fed ALDH2(-/-) mice had higher levels of malondialdehyde-acetaldehyde (MAA) adduct and greater hepatic inflammation, with higher hepatic interleukin (IL)-6 expression but surprisingly lower levels of steatosis and serum alanine aminotransferase (ALT).	Acetaldehyde	95-107	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	42-47
24904079-11	2014	Furthermore, acetaldehyde induced LDH release and increased caspase3/7 activity and percentage of cells expressing cleaved CK18 and increased MUC2 protein expression compared with negative controls (P &lt; 0.0001).	Acetaldehyde	13-25	mucin 2, oligomeric mucus/gel-forming	Homo sapiens	142-146
24220877-5	2014	Expression of dehydrogenase (formaldehyde dehydrogenase (FDH)) in the formaldehyde (10.40) and methanol (10.60) groups increased significantly compared with the control (1), while it was similar to the control in formic acid (0.90) and acetaldehyde (1.10) groups.	Acetaldehyde	236-248	alcohol dehydrogenase 5 (class III), chi polypeptide	Homo sapiens	29-55
24220877-5	2014	Expression of dehydrogenase (formaldehyde dehydrogenase (FDH)) in the formaldehyde (10.40) and methanol (10.60) groups increased significantly compared with the control (1), while it was similar to the control in formic acid (0.90) and acetaldehyde (1.10) groups.	Acetaldehyde	236-248	alcohol dehydrogenase 5 (class III), chi polypeptide	Homo sapiens	57-60
24492981-1	2014	UNLABELLED: Aldehyde dehydrogenase 2 (ALDH2) is the major enzyme that metabolizes acetaldehyde produced from alcohol metabolism.	Acetaldehyde	82-94	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	12-36
24854437-4	2014	We have observed CutD-mediated formation of a glycyl radical on CutC using EPR spectroscopy and have demonstrated that activated CutC processes choline to trimethylamine and acetaldehyde.	Acetaldehyde	174-186	cutC copper transporter	Homo sapiens	64-68
24854437-4	2014	We have observed CutD-mediated formation of a glycyl radical on CutC using EPR spectroscopy and have demonstrated that activated CutC processes choline to trimethylamine and acetaldehyde.	Acetaldehyde	174-186	cutC copper transporter	Homo sapiens	129-133
24746671-4	2014	In the present study we demonstrate that acetaldehyde transiently impairs SOD2 activity in HepG2 cells, the decrease in the enzyme activity was associated to a reduction in the protein content, which was rapidly recovered, to basal values, by synthesis de novo in a mechanism mediated by NF-kappaB and PKC.	Acetaldehyde	41-53	superoxide dismutase 2	Homo sapiens	74-78
24492981-1	2014	UNLABELLED: Aldehyde dehydrogenase 2 (ALDH2) is the major enzyme that metabolizes acetaldehyde produced from alcohol metabolism.	Acetaldehyde	82-94	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	38-43
24988262-1	2014	OBJECTIVE: A single nucleotide variation in the alcohol dehydrogenase 1B (ADH1B) gene, rs1229984, produces an ADH1B enzyme with faster acetaldehyde production.	Acetaldehyde	135-147	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	48-72
24988262-1	2014	OBJECTIVE: A single nucleotide variation in the alcohol dehydrogenase 1B (ADH1B) gene, rs1229984, produces an ADH1B enzyme with faster acetaldehyde production.	Acetaldehyde	135-147	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	74-79
24988262-1	2014	OBJECTIVE: A single nucleotide variation in the alcohol dehydrogenase 1B (ADH1B) gene, rs1229984, produces an ADH1B enzyme with faster acetaldehyde production.	Acetaldehyde	135-147	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	110-115
24588059-1	2014	BACKGROUND: Oxidation of ethanol by alcohol dehydrogenase (ADH) generates acetaldehyde (AcH), which is converted to acetate by aldehyde dehydrogenase-2 (ALDH2).	Acetaldehyde	74-86	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	59-62
24959382-1	2014	Ethanol and its metabolite, acetaldehyde, are the definite carcinogens for esophageal squamous cell carcinoma (ESCC), and reduced catalytic activity of aldehyde dehydrogenase 2 (ALDH2), which detoxifies acetaldehyde, increases the risk for ESCC.	Acetaldehyde	28-40	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	152-176
24959382-1	2014	Ethanol and its metabolite, acetaldehyde, are the definite carcinogens for esophageal squamous cell carcinoma (ESCC), and reduced catalytic activity of aldehyde dehydrogenase 2 (ALDH2), which detoxifies acetaldehyde, increases the risk for ESCC.	Acetaldehyde	28-40	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	178-183
24959382-1	2014	Ethanol and its metabolite, acetaldehyde, are the definite carcinogens for esophageal squamous cell carcinoma (ESCC), and reduced catalytic activity of aldehyde dehydrogenase 2 (ALDH2), which detoxifies acetaldehyde, increases the risk for ESCC.	Acetaldehyde	203-215	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	152-176
24959382-1	2014	Ethanol and its metabolite, acetaldehyde, are the definite carcinogens for esophageal squamous cell carcinoma (ESCC), and reduced catalytic activity of aldehyde dehydrogenase 2 (ALDH2), which detoxifies acetaldehyde, increases the risk for ESCC.	Acetaldehyde	203-215	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	178-183
24959382-7	2014	Taken together, our findings strongly suggest the importance of acetaldehyde-derived DNA damage which is induced in the esophagus of individuals with ALDH2 gene impairment.	Acetaldehyde	64-76	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	150-155
24811712-6	2014	Individual quantum yields of acetaldehyde are 0.030 +- 0.007 for CuL and 0.024 +- 0.007 for CuL2.	Acetaldehyde	29-41	cullin 2	Homo sapiens	92-96
24811712-8	2014	For both CuL and CuL2, the individual quantum yields of Cu(I), ammonia, and acetaldehyde are in the ratio of 1.8:1:0.7.	Acetaldehyde	76-88	cullin 2	Homo sapiens	17-21
24797321-10	2014	In the case of acetaldehyde, the AUC0-4 and Cmax of acetaldehyde of ADH1B*2/*2 after administration of 0.25 g/kg alcohol and the AUC0-4 of acetaldehyde of ADH1B*2/*2 at 0.5 g/kg were significantly higher than corresponding values of ADH1B*1/*2 only in the group of ALDH2*1/*2.	Acetaldehyde	15-27	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	68-73
24797321-10	2014	In the case of acetaldehyde, the AUC0-4 and Cmax of acetaldehyde of ADH1B*2/*2 after administration of 0.25 g/kg alcohol and the AUC0-4 of acetaldehyde of ADH1B*2/*2 at 0.5 g/kg were significantly higher than corresponding values of ADH1B*1/*2 only in the group of ALDH2*1/*2.	Acetaldehyde	15-27	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	155-160
24797321-10	2014	In the case of acetaldehyde, the AUC0-4 and Cmax of acetaldehyde of ADH1B*2/*2 after administration of 0.25 g/kg alcohol and the AUC0-4 of acetaldehyde of ADH1B*2/*2 at 0.5 g/kg were significantly higher than corresponding values of ADH1B*1/*2 only in the group of ALDH2*1/*2.	Acetaldehyde	15-27	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	155-160
24797321-10	2014	In the case of acetaldehyde, the AUC0-4 and Cmax of acetaldehyde of ADH1B*2/*2 after administration of 0.25 g/kg alcohol and the AUC0-4 of acetaldehyde of ADH1B*2/*2 at 0.5 g/kg were significantly higher than corresponding values of ADH1B*1/*2 only in the group of ALDH2*1/*2.	Acetaldehyde	15-27	aldehyde dehydrogenase 2 family member	Homo sapiens	265-270
24797321-10	2014	In the case of acetaldehyde, the AUC0-4 and Cmax of acetaldehyde of ADH1B*2/*2 after administration of 0.25 g/kg alcohol and the AUC0-4 of acetaldehyde of ADH1B*2/*2 at 0.5 g/kg were significantly higher than corresponding values of ADH1B*1/*2 only in the group of ALDH2*1/*2.	Acetaldehyde	52-64	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	68-73
24797321-10	2014	In the case of acetaldehyde, the AUC0-4 and Cmax of acetaldehyde of ADH1B*2/*2 after administration of 0.25 g/kg alcohol and the AUC0-4 of acetaldehyde of ADH1B*2/*2 at 0.5 g/kg were significantly higher than corresponding values of ADH1B*1/*2 only in the group of ALDH2*1/*2.	Acetaldehyde	52-64	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	68-73
24797321-11	2014	CONCLUSIONS: Our findings indicate that the blood EtOH concentrations of ADH1B*2/*2 group are higher than those of ADH1B*1/*2 group regardless of ALDH2 genotype, and the blood acetaldehyde concentrations of ADH1B*2/*2 are also higher than those of ADH1B*1/*2 only in the ALDH2*1/*2 group.	Acetaldehyde	176-188	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	73-78
24797321-12	2014	To our knowledge, this is the first report to demonstrate the association of ADH1B*2 allele with blood EtOH and acetaldehyde levels in humans, and these results suggest that higher blood EtOH and acetaldehyde concentrations in ADH1B*2/*2 may constitute the mechanism of protection against alcoholism by ADH1B*2/*2.	Acetaldehyde	112-124	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	77-82
24797321-12	2014	To our knowledge, this is the first report to demonstrate the association of ADH1B*2 allele with blood EtOH and acetaldehyde levels in humans, and these results suggest that higher blood EtOH and acetaldehyde concentrations in ADH1B*2/*2 may constitute the mechanism of protection against alcoholism by ADH1B*2/*2.	Acetaldehyde	112-124	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	227-232
24797321-12	2014	To our knowledge, this is the first report to demonstrate the association of ADH1B*2 allele with blood EtOH and acetaldehyde levels in humans, and these results suggest that higher blood EtOH and acetaldehyde concentrations in ADH1B*2/*2 may constitute the mechanism of protection against alcoholism by ADH1B*2/*2.	Acetaldehyde	112-124	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	227-232
24797321-12	2014	To our knowledge, this is the first report to demonstrate the association of ADH1B*2 allele with blood EtOH and acetaldehyde levels in humans, and these results suggest that higher blood EtOH and acetaldehyde concentrations in ADH1B*2/*2 may constitute the mechanism of protection against alcoholism by ADH1B*2/*2.	Acetaldehyde	196-208	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	77-82
24797321-12	2014	To our knowledge, this is the first report to demonstrate the association of ADH1B*2 allele with blood EtOH and acetaldehyde levels in humans, and these results suggest that higher blood EtOH and acetaldehyde concentrations in ADH1B*2/*2 may constitute the mechanism of protection against alcoholism by ADH1B*2/*2.	Acetaldehyde	196-208	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	227-232
24797321-12	2014	To our knowledge, this is the first report to demonstrate the association of ADH1B*2 allele with blood EtOH and acetaldehyde levels in humans, and these results suggest that higher blood EtOH and acetaldehyde concentrations in ADH1B*2/*2 may constitute the mechanism of protection against alcoholism by ADH1B*2/*2.	Acetaldehyde	196-208	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	227-232
24567230-5	2014	We investigated whether variation in genes encoding cytochrome P450 2E1 (CYP2E1) or acetaldehyde-metabolising enzymes (ALDH1A1, ALDH2) might alter the risk of AD, with and without symptoms of anxiety, in a Cape population with mixed ancestry.	Acetaldehyde	84-96	aldehyde dehydrogenase 1 family member A1	Homo sapiens	119-126
24944770-10	2014	RESULTS: Compared to untreated cells, LPS-stimulated RAW 264.7 cells treated with ACE showed reduced NO generation and reduced iNOS and COX-2 expression.	Acetaldehyde	82-85	nitric oxide synthase 2, inducible	Mus musculus	127-131
24944770-12	2014	CONCLUSION: Taken together, these results suggest that ACE can inhibit inflammation and modulate NO generation via downregulation of iNOS levels and NF-kappaB signaling in vitro and in vivo.	Acetaldehyde	55-58	nitric oxide synthase 2, inducible	Mus musculus	133-137
24959382-0	2014	Impairment of aldehyde dehydrogenase 2 increases accumulation of acetaldehyde-derived DNA damage in the esophagus after ethanol ingestion.	Acetaldehyde	65-77	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	14-38
24754626-4	2014	Catalytic activity of acetaldehyde (ACA)-generating (alcohol dehydrogenase [ADH] and catalase) and eliminating aldehyde dehydrogenase [ALDH2] enzymes along with mediators of oxidative stress were measured in myocardial tissues collected at 30, 60, or 90 minutes after EtOH or water.	Acetaldehyde	22-34	catalase	Rattus norvegicus	53-133
24754626-4	2014	Catalytic activity of acetaldehyde (ACA)-generating (alcohol dehydrogenase [ADH] and catalase) and eliminating aldehyde dehydrogenase [ALDH2] enzymes along with mediators of oxidative stress were measured in myocardial tissues collected at 30, 60, or 90 minutes after EtOH or water.	Acetaldehyde	22-34	aldehyde dehydrogenase 2 family member	Rattus norvegicus	135-140
24754626-4	2014	Catalytic activity of acetaldehyde (ACA)-generating (alcohol dehydrogenase [ADH] and catalase) and eliminating aldehyde dehydrogenase [ALDH2] enzymes along with mediators of oxidative stress were measured in myocardial tissues collected at 30, 60, or 90 minutes after EtOH or water.	Acetaldehyde	36-39	catalase	Rattus norvegicus	53-133
24754626-4	2014	Catalytic activity of acetaldehyde (ACA)-generating (alcohol dehydrogenase [ADH] and catalase) and eliminating aldehyde dehydrogenase [ALDH2] enzymes along with mediators of oxidative stress were measured in myocardial tissues collected at 30, 60, or 90 minutes after EtOH or water.	Acetaldehyde	36-39	aldehyde dehydrogenase 2 family member	Rattus norvegicus	135-140
24588059-1	2014	BACKGROUND: Oxidation of ethanol by alcohol dehydrogenase (ADH) generates acetaldehyde (AcH), which is converted to acetate by aldehyde dehydrogenase-2 (ALDH2).	Acetaldehyde	74-86	aldehyde dehydrogenase 2 family member	Homo sapiens	127-151
24588059-1	2014	BACKGROUND: Oxidation of ethanol by alcohol dehydrogenase (ADH) generates acetaldehyde (AcH), which is converted to acetate by aldehyde dehydrogenase-2 (ALDH2).	Acetaldehyde	74-86	aldehyde dehydrogenase 2 family member	Homo sapiens	153-158
24588059-1	2014	BACKGROUND: Oxidation of ethanol by alcohol dehydrogenase (ADH) generates acetaldehyde (AcH), which is converted to acetate by aldehyde dehydrogenase-2 (ALDH2).	Acetaldehyde	88-91	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	59-62
24588059-1	2014	BACKGROUND: Oxidation of ethanol by alcohol dehydrogenase (ADH) generates acetaldehyde (AcH), which is converted to acetate by aldehyde dehydrogenase-2 (ALDH2).	Acetaldehyde	88-91	aldehyde dehydrogenase 2 family member	Homo sapiens	127-151
24641900-0	2014	Mechanisms of action of acetaldehyde in the up-regulation of the human alpha2(I) collagen gene in hepatic stellate cells: key roles of Ski, SMAD3, SMAD4, and SMAD7.	Acetaldehyde	24-36	collagen type I alpha 2 chain	Homo sapiens	71-89
24588059-1	2014	BACKGROUND: Oxidation of ethanol by alcohol dehydrogenase (ADH) generates acetaldehyde (AcH), which is converted to acetate by aldehyde dehydrogenase-2 (ALDH2).	Acetaldehyde	88-91	aldehyde dehydrogenase 2 family member	Homo sapiens	153-158
24641900-0	2014	Mechanisms of action of acetaldehyde in the up-regulation of the human alpha2(I) collagen gene in hepatic stellate cells: key roles of Ski, SMAD3, SMAD4, and SMAD7.	Acetaldehyde	24-36	SMAD family member 3	Homo sapiens	140-145
24492484-10	2014	LC3B lipidation increased with acetaldehyde treatment and increased further with the addition of cyanamide.	Acetaldehyde	31-43	microtubule associated protein 1 light chain 3 beta	Homo sapiens	0-4
24641900-2	2014	Acetaldehyde, the first metabolite of ethanol, up-regulates expression of the human alpha2(I) collagen gene (COL1A2).	Acetaldehyde	0-12	collagen type I alpha 2 chain	Homo sapiens	84-102
24641900-2	2014	Acetaldehyde, the first metabolite of ethanol, up-regulates expression of the human alpha2(I) collagen gene (COL1A2).	Acetaldehyde	0-12	collagen type I alpha 2 chain	Homo sapiens	109-115
24641900-3	2014	Early acetaldehyde-mediated effects involve phosphorylation and nuclear translocation of SMAD3/4-containing complexes that bind to COL1A2 promoter to induce fibrogenesis.	Acetaldehyde	6-18	SMAD family member 3	Homo sapiens	89-94
24641900-3	2014	Early acetaldehyde-mediated effects involve phosphorylation and nuclear translocation of SMAD3/4-containing complexes that bind to COL1A2 promoter to induce fibrogenesis.	Acetaldehyde	6-18	collagen type I alpha 2 chain	Homo sapiens	131-137
24641900-4	2014	We used human and mouse hepatic stellate cells to elucidate the mechanisms whereby acetaldehyde up-regulates COL1A2 by modulating the role of Ski and the expression of SMADs 3, 4, and 7.	Acetaldehyde	83-95	collagen, type I, alpha 2	Mus musculus	109-115
24641900-4	2014	We used human and mouse hepatic stellate cells to elucidate the mechanisms whereby acetaldehyde up-regulates COL1A2 by modulating the role of Ski and the expression of SMADs 3, 4, and 7.	Acetaldehyde	83-95	ski sarcoma viral oncogene homolog (avian)	Mus musculus	142-145
24641900-5	2014	Acetaldehyde induced up-regulation of COL1A2 by 3.5-fold, with concomitant increases in the mRNA (threefold) and protein (4.2- and 3.5-fold) levels of SMAD3 and SMAD4, respectively.	Acetaldehyde	0-12	collagen type I alpha 2 chain	Homo sapiens	38-44
24641900-5	2014	Acetaldehyde induced up-regulation of COL1A2 by 3.5-fold, with concomitant increases in the mRNA (threefold) and protein (4.2- and 3.5-fold) levels of SMAD3 and SMAD4, respectively.	Acetaldehyde	0-12	SMAD family member 3	Homo sapiens	151-156
24641900-5	2014	Acetaldehyde induced up-regulation of COL1A2 by 3.5-fold, with concomitant increases in the mRNA (threefold) and protein (4.2- and 3.5-fold) levels of SMAD3 and SMAD4, respectively.	Acetaldehyde	0-12	SMAD family member 4	Homo sapiens	161-166
24641900-8	2014	Acetaldehyde induces translocation of Ski and SMAD4 to the cytoplasm, where Ski undergoes proteasomal degradation, as confirmed by the ability of the proteasomal inhibitor lactacystin to blunt up-regulation of acetaldehyde-dependent COL1A2, but not of the nonspecific fibronectin gene (FN1).	Acetaldehyde	0-12	SKI proto-oncogene	Homo sapiens	38-41
24641900-8	2014	Acetaldehyde induces translocation of Ski and SMAD4 to the cytoplasm, where Ski undergoes proteasomal degradation, as confirmed by the ability of the proteasomal inhibitor lactacystin to blunt up-regulation of acetaldehyde-dependent COL1A2, but not of the nonspecific fibronectin gene (FN1).	Acetaldehyde	0-12	SMAD family member 4	Homo sapiens	46-51
24641900-8	2014	Acetaldehyde induces translocation of Ski and SMAD4 to the cytoplasm, where Ski undergoes proteasomal degradation, as confirmed by the ability of the proteasomal inhibitor lactacystin to blunt up-regulation of acetaldehyde-dependent COL1A2, but not of the nonspecific fibronectin gene (FN1).	Acetaldehyde	0-12	SKI proto-oncogene	Homo sapiens	76-79
24641900-8	2014	Acetaldehyde induces translocation of Ski and SMAD4 to the cytoplasm, where Ski undergoes proteasomal degradation, as confirmed by the ability of the proteasomal inhibitor lactacystin to blunt up-regulation of acetaldehyde-dependent COL1A2, but not of the nonspecific fibronectin gene (FN1).	Acetaldehyde	0-12	collagen type I alpha 2 chain	Homo sapiens	233-239
24641900-8	2014	Acetaldehyde induces translocation of Ski and SMAD4 to the cytoplasm, where Ski undergoes proteasomal degradation, as confirmed by the ability of the proteasomal inhibitor lactacystin to blunt up-regulation of acetaldehyde-dependent COL1A2, but not of the nonspecific fibronectin gene (FN1).	Acetaldehyde	0-12	fibronectin 1	Homo sapiens	268-279
24641900-8	2014	Acetaldehyde induces translocation of Ski and SMAD4 to the cytoplasm, where Ski undergoes proteasomal degradation, as confirmed by the ability of the proteasomal inhibitor lactacystin to blunt up-regulation of acetaldehyde-dependent COL1A2, but not of the nonspecific fibronectin gene (FN1).	Acetaldehyde	0-12	fibronectin 1	Homo sapiens	286-289
24641900-8	2014	Acetaldehyde induces translocation of Ski and SMAD4 to the cytoplasm, where Ski undergoes proteasomal degradation, as confirmed by the ability of the proteasomal inhibitor lactacystin to blunt up-regulation of acetaldehyde-dependent COL1A2, but not of the nonspecific fibronectin gene (FN1).	Acetaldehyde	210-222	SKI proto-oncogene	Homo sapiens	38-41
24641900-8	2014	Acetaldehyde induces translocation of Ski and SMAD4 to the cytoplasm, where Ski undergoes proteasomal degradation, as confirmed by the ability of the proteasomal inhibitor lactacystin to blunt up-regulation of acetaldehyde-dependent COL1A2, but not of the nonspecific fibronectin gene (FN1).	Acetaldehyde	210-222	SMAD family member 4	Homo sapiens	46-51
24641900-8	2014	Acetaldehyde induces translocation of Ski and SMAD4 to the cytoplasm, where Ski undergoes proteasomal degradation, as confirmed by the ability of the proteasomal inhibitor lactacystin to blunt up-regulation of acetaldehyde-dependent COL1A2, but not of the nonspecific fibronectin gene (FN1).	Acetaldehyde	210-222	SKI proto-oncogene	Homo sapiens	76-79
24641900-9	2014	We conclude that acetaldehyde up-regulates COL1A2 by enhancing expression of the transactivators SMAD3 and SMAD4 while inhibiting the repressor SMAD7, along with promoting Ski translocation from the nucleus to cytoplasm.	Acetaldehyde	17-29	collagen type I alpha 2 chain	Homo sapiens	43-49
24641900-9	2014	We conclude that acetaldehyde up-regulates COL1A2 by enhancing expression of the transactivators SMAD3 and SMAD4 while inhibiting the repressor SMAD7, along with promoting Ski translocation from the nucleus to cytoplasm.	Acetaldehyde	17-29	SMAD family member 3	Homo sapiens	97-102
24641900-9	2014	We conclude that acetaldehyde up-regulates COL1A2 by enhancing expression of the transactivators SMAD3 and SMAD4 while inhibiting the repressor SMAD7, along with promoting Ski translocation from the nucleus to cytoplasm.	Acetaldehyde	17-29	SMAD family member 4	Homo sapiens	107-112
24641900-9	2014	We conclude that acetaldehyde up-regulates COL1A2 by enhancing expression of the transactivators SMAD3 and SMAD4 while inhibiting the repressor SMAD7, along with promoting Ski translocation from the nucleus to cytoplasm.	Acetaldehyde	17-29	SMAD family member 7	Homo sapiens	144-149
24641900-9	2014	We conclude that acetaldehyde up-regulates COL1A2 by enhancing expression of the transactivators SMAD3 and SMAD4 while inhibiting the repressor SMAD7, along with promoting Ski translocation from the nucleus to cytoplasm.	Acetaldehyde	17-29	SKI proto-oncogene	Homo sapiens	172-175
24690209-1	2014	BACKGROUND: The well-known genetic polymorphisms in ADH1B(His47Arg) and ALDH2(Glu487Lys) have dramatic effects on the rate of metabolizing alcohol and acetaldehyde.	Acetaldehyde	151-163	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	52-57
24690209-1	2014	BACKGROUND: The well-known genetic polymorphisms in ADH1B(His47Arg) and ALDH2(Glu487Lys) have dramatic effects on the rate of metabolizing alcohol and acetaldehyde.	Acetaldehyde	151-163	aldehyde dehydrogenase 2 family member	Homo sapiens	72-77
24448831-5	2014	Our findings suggested that only exposure to high concentrations of ETBE might result in reproductive toxicity in mice with normal active ALDH2, while low active and inactive ALDH2 enzyme significantly enhanced the ETBE-induced reproductive toxicity in mice, even exposed to low concentrations of ETBE, mainly due to the accumulation of acetaldehyde as a primary metabolite of ETBE.	Acetaldehyde	337-349	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	175-180
24682220-6	2014	Caffeine and the A2AR antagonist ZM241385 decreased the cell viability and inhibited the expression of procollagen type I and type III in acetaldehyde-induced HSC-T6 cells.	Acetaldehyde	138-150	adenosine A2a receptor	Rattus norvegicus	17-21
23934054-5	2014	In vivo the pretreatment of rats with RAN (100 mg/kg) and 50, 100, and 200 mg/kg doses of ACE significantly reduced the ulcer index in a dose-dependant manner in both the models by blocking lipid peroxidation and by significant increases in superoxide dismutase and catalase activity.	Acetaldehyde	90-93	catalase	Rattus norvegicus	266-274
24201835-2	2014	Mitochondrial aldehyde dehydrogenase 2 (ALDH2) metabolizes acetaldehyde into acetate and also protects against oxidative stress, playing an important role in the development of AD.	Acetaldehyde	59-71	aldehyde dehydrogenase 2 family member	Homo sapiens	40-45
24682220-9	2014	CONCLUSIONS: Caffeine significantly inhibited acetaldehyde-induced HSC-T6 cells activation by distinct A2AR mediated signal pathway via inhibition of cAMP-PKA-SRC-ERK1/2 for procollagen type I and via P38 MAPK for procollagen type III.	Acetaldehyde	46-58	adenosine A2a receptor	Rattus norvegicus	103-107
24682220-0	2014	Caffeine inhibits the activation of hepatic stellate cells induced by acetaldehyde via adenosine A2A receptor mediated by the cAMP/PKA/SRC/ERK1/2/P38 MAPK signal pathway.	Acetaldehyde	70-82	adenosine A2a receptor	Rattus norvegicus	87-109
24682220-0	2014	Caffeine inhibits the activation of hepatic stellate cells induced by acetaldehyde via adenosine A2A receptor mediated by the cAMP/PKA/SRC/ERK1/2/P38 MAPK signal pathway.	Acetaldehyde	70-82	SRC proto-oncogene, non-receptor tyrosine kinase	Rattus norvegicus	135-138
24682220-9	2014	CONCLUSIONS: Caffeine significantly inhibited acetaldehyde-induced HSC-T6 cells activation by distinct A2AR mediated signal pathway via inhibition of cAMP-PKA-SRC-ERK1/2 for procollagen type I and via P38 MAPK for procollagen type III.	Acetaldehyde	46-58	SRC proto-oncogene, non-receptor tyrosine kinase	Rattus norvegicus	159-162
24682220-0	2014	Caffeine inhibits the activation of hepatic stellate cells induced by acetaldehyde via adenosine A2A receptor mediated by the cAMP/PKA/SRC/ERK1/2/P38 MAPK signal pathway.	Acetaldehyde	70-82	mitogen activated protein kinase 3	Rattus norvegicus	139-145
24682220-9	2014	CONCLUSIONS: Caffeine significantly inhibited acetaldehyde-induced HSC-T6 cells activation by distinct A2AR mediated signal pathway via inhibition of cAMP-PKA-SRC-ERK1/2 for procollagen type I and via P38 MAPK for procollagen type III.	Acetaldehyde	46-58	mitogen activated protein kinase 3	Rattus norvegicus	163-169
24682220-0	2014	Caffeine inhibits the activation of hepatic stellate cells induced by acetaldehyde via adenosine A2A receptor mediated by the cAMP/PKA/SRC/ERK1/2/P38 MAPK signal pathway.	Acetaldehyde	70-82	mitogen activated protein kinase 14	Rattus norvegicus	146-149
24682220-0	2014	Caffeine inhibits the activation of hepatic stellate cells induced by acetaldehyde via adenosine A2A receptor mediated by the cAMP/PKA/SRC/ERK1/2/P38 MAPK signal pathway.	Acetaldehyde	70-82	mitogen activated protein kinase 3	Rattus norvegicus	150-154
24682220-9	2014	CONCLUSIONS: Caffeine significantly inhibited acetaldehyde-induced HSC-T6 cells activation by distinct A2AR mediated signal pathway via inhibition of cAMP-PKA-SRC-ERK1/2 for procollagen type I and via P38 MAPK for procollagen type III.	Acetaldehyde	46-58	mitogen activated protein kinase 14	Rattus norvegicus	201-204
24682220-4	2014	In this study, we attempted to validate the hypothesis that caffeine influences acetaldehyde-induced HSC activation by acting on A2AR.	Acetaldehyde	80-92	adenosine A2a receptor	Rattus norvegicus	129-133
24489834-5	2014	Newly generated mutant lacking Crz Receptor (CrzR(01) ) and CrzR-knockdown flies showed even more severe hangover-like phenotype, which is causally associated with fast accumulation of acetaldehyde in the CrzR(01) mutant following ethanol exposure.	Acetaldehyde	185-197	Corazonin receptor	Drosophila melanogaster	31-43
24282063-6	2014	Finally, we note the lack of information regarding acetaldehyde effects on the mitochondrial genome, which is notable since aldehyde dehydrogenase 2 (ALDH2), the primary acetaldehyde metabolic enzyme, is located in the mitochondrion, and roughly 30% of East Asian individuals are deficient in ALDH2 activity due to a genetic variant in the ALDH2 gene.	Acetaldehyde	170-182	aldehyde dehydrogenase 2 family member	Homo sapiens	124-148
24282063-6	2014	Finally, we note the lack of information regarding acetaldehyde effects on the mitochondrial genome, which is notable since aldehyde dehydrogenase 2 (ALDH2), the primary acetaldehyde metabolic enzyme, is located in the mitochondrion, and roughly 30% of East Asian individuals are deficient in ALDH2 activity due to a genetic variant in the ALDH2 gene.	Acetaldehyde	170-182	aldehyde dehydrogenase 2 family member	Homo sapiens	150-155
24236752-1	2014	Elamin and colleagues in this issue report that acetaldehyde activates Snail, a transcription factor involved in epithelial-to-mesenchymal transition, in an intestinal epithelium.	Acetaldehyde	48-60	snail family transcriptional repressor 1	Homo sapiens	71-76
24236752-2	2014	Snail mediates acetaldehyde-induced tight junction disruption and increase in paracellular permeability.	Acetaldehyde	15-27	snail family transcriptional repressor 1	Homo sapiens	0-5
24033729-0	2014	Activation of the epithelial-to-mesenchymal transition factor snail mediates acetaldehyde-induced intestinal epithelial barrier disruption.	Acetaldehyde	77-89	snail family transcriptional repressor 1	Homo sapiens	62-67
24033729-3	2014	As AcH is mutagenic, the role of Snail in the AcH-induced disruption of intestinal epithelial TJs deserves further investigation.	Acetaldehyde	46-49	snail family transcriptional repressor 1	Homo sapiens	33-38
24033729-4	2014	Our aim was to investigate the role of oxidative stress and Snail activation in AcH-induced barrier disruption in Caco-2 monolayers.	Acetaldehyde	80-83	snail family transcriptional repressor 1	Homo sapiens	60-65
24033729-9	2014	RESULTS: Exposure to 25 muM AcH increased ROS generation and ROS-dependently induced Snail phosphorylation.	Acetaldehyde	28-31	snail family transcriptional repressor 1	Homo sapiens	85-90
24033729-11	2014	Knockdown of Snail by siRNA attenuated the AcH-induced redistribution and decrease in the TJ and AJ proteins, in association with improvement of the barrier function.	Acetaldehyde	43-46	snail family transcriptional repressor 1	Homo sapiens	13-18
24033729-12	2014	CONCLUSIONS: Our data demonstrate that oxidative stress-mediated Snail phosphorylation is likely a novel mechanism contributing to the deleterious effects of AcH on the TJ and AJ, and intestinal barrier function.	Acetaldehyde	158-161	snail family transcriptional repressor 1	Homo sapiens	65-70
24804381-0	2014	[Relationship among ALDH2 gene polymorphism, alcohol metabolism and acetaldehyde level in peripheral blood].	Acetaldehyde	68-80	aldehyde dehydrogenase 2 family member	Homo sapiens	20-25
24804381-1	2014	OBJECTIVE: To explore alcohol pharmacokinetics as well as acetaldehyde level in peripheral blood in human subjects with different ALDH2 genotypes after drinking.	Acetaldehyde	58-70	aldehyde dehydrogenase 2 family member	Homo sapiens	130-135
24804381-11	2014	CONCLUSION: After the consumption of alcohol, alcohol and acetaldehyde metabolism in blood slow down in ALDH2*1/*2 mutation group influenced by the inhibition of enzyme activity, leading to the accumulation of acetaldehyde in peripheral blood, thus reinforcing their effects in the body.	Acetaldehyde	58-70	aldehyde dehydrogenase 2 family member	Homo sapiens	104-109
24804381-11	2014	CONCLUSION: After the consumption of alcohol, alcohol and acetaldehyde metabolism in blood slow down in ALDH2*1/*2 mutation group influenced by the inhibition of enzyme activity, leading to the accumulation of acetaldehyde in peripheral blood, thus reinforcing their effects in the body.	Acetaldehyde	210-222	aldehyde dehydrogenase 2 family member	Homo sapiens	104-109
24489834-5	2014	Newly generated mutant lacking Crz Receptor (CrzR(01) ) and CrzR-knockdown flies showed even more severe hangover-like phenotype, which is causally associated with fast accumulation of acetaldehyde in the CrzR(01) mutant following ethanol exposure.	Acetaldehyde	185-197	Corazonin receptor	Drosophila melanogaster	45-49
24489834-5	2014	Newly generated mutant lacking Crz Receptor (CrzR(01) ) and CrzR-knockdown flies showed even more severe hangover-like phenotype, which is causally associated with fast accumulation of acetaldehyde in the CrzR(01) mutant following ethanol exposure.	Acetaldehyde	185-197	Corazonin receptor	Drosophila melanogaster	60-64
24489834-5	2014	Newly generated mutant lacking Crz Receptor (CrzR(01) ) and CrzR-knockdown flies showed even more severe hangover-like phenotype, which is causally associated with fast accumulation of acetaldehyde in the CrzR(01) mutant following ethanol exposure.	Acetaldehyde	185-197	Corazonin receptor	Drosophila melanogaster	60-64
24489834-6	2014	Higher levels of acetaldehyde are likely due to 30% reduced ALDH activity in the mutants.	Acetaldehyde	17-29	Aldehyde dehydrogenase	Drosophila melanogaster	60-64
23909789-6	2014	The ALDH2 activity was determined at a sufficient low acetaldehyde concentration (3 muM) and the isozyme protein amount by immunotitration using purified class-specific antibodies.	Acetaldehyde	54-66	aldehyde dehydrogenase 2 family member	Homo sapiens	4-9
25354396-3	2014	Although oxidative stress and endothelial injury have been postulated to play a major contributing role to alcoholism-induced hypertension, recent evidence depicted a rather unique role for the genotype of the acetaldehyde-metabolizing enzyme mitochondrial aldehyde dehydrogenase (ALDH2), which is mainly responsible for detoxifying ethanol consumed, in alcoholism-induced elevation of blood pressure.	Acetaldehyde	210-222	aldehyde dehydrogenase 2 family member	Homo sapiens	281-286
24200853-6	2014	Some compounds, however, had contrasting magnitudes of sensitivity; a strikingly high (19- to 22-fold) hypersensitivity was seen among PALB2-null and BRCA2-null cells for the ethanol metabolite, acetaldehyde, associated with widespread chromosomal breakage at a concentration not producing breaks in parental cells.	Acetaldehyde	195-207	partner and localizer of BRCA2	Mus musculus	135-140
24200853-6	2014	Some compounds, however, had contrasting magnitudes of sensitivity; a strikingly high (19- to 22-fold) hypersensitivity was seen among PALB2-null and BRCA2-null cells for the ethanol metabolite, acetaldehyde, associated with widespread chromosomal breakage at a concentration not producing breaks in parental cells.	Acetaldehyde	195-207	breast cancer 2, early onset	Mus musculus	150-155
24333098-1	2014	BACKGROUND AND AIMS: Emerging evidences have shown that the Glu504Lys variant in ALDH2 gene may greatly reduce the ability of ALDH2 to metabolize acetaldehyde, which could increase the risk of coronary artery disease (CAD) and myocardial infarction (MI).	Acetaldehyde	146-158	aldehyde dehydrogenase 2 family member	Homo sapiens	81-86
24333098-1	2014	BACKGROUND AND AIMS: Emerging evidences have shown that the Glu504Lys variant in ALDH2 gene may greatly reduce the ability of ALDH2 to metabolize acetaldehyde, which could increase the risk of coronary artery disease (CAD) and myocardial infarction (MI).	Acetaldehyde	146-158	aldehyde dehydrogenase 2 family member	Homo sapiens	126-131
25354396-4	2014	Genetic polymorphism of ALDH2 in human results in altered ethanol pharmacokinetic properties and ethanol metabolism, leading to accumulation of the ethanol metabolite acetaldehyde following alcohol intake.	Acetaldehyde	167-179	aldehyde dehydrogenase 2 family member	Homo sapiens	24-29
25354396-5	2014	The unfavorable consequence of the ALDH2 variants is believed to be governed by the accumulation of the ethanol metabolite acetaldehyde.	Acetaldehyde	123-135	aldehyde dehydrogenase 2 family member	Homo sapiens	35-40
23892315-3	2013	The generated aqueous Co(III) is then applied to simultaneous deodorization of simulated odor gases, namely, ammonia, trimethylamine, hydrogen sulfide, methyl mercaptan, and acetaldehyde, for municipal waste treatment plant emissions.	Acetaldehyde	174-186	mitochondrially encoded cytochrome c oxidase III	Homo sapiens	22-29
24244749-7	2013	Acetaldehyde, a metabolic product of alcohol dehydrogenase, induced significant cell death, depolarization of MMP, and caspase-3 activation as ethanol and this damage was also averted by NAC.	Acetaldehyde	0-12	aldo-keto reductase family 1 member A1	Homo sapiens	37-58
24244749-7	2013	Acetaldehyde, a metabolic product of alcohol dehydrogenase, induced significant cell death, depolarization of MMP, and caspase-3 activation as ethanol and this damage was also averted by NAC.	Acetaldehyde	0-12	caspase 3	Homo sapiens	119-128
23905689-0	2013	Role of rostral ventrolateral medullary ERK/JNK/p38 MAPK signaling in the pressor effects of ethanol and its oxidative product acetaldehyde.	Acetaldehyde	127-139	Eph receptor B1	Rattus norvegicus	40-43
23905689-0	2013	Role of rostral ventrolateral medullary ERK/JNK/p38 MAPK signaling in the pressor effects of ethanol and its oxidative product acetaldehyde.	Acetaldehyde	127-139	mitogen-activated protein kinase 8	Rattus norvegicus	44-47
23905689-0	2013	Role of rostral ventrolateral medullary ERK/JNK/p38 MAPK signaling in the pressor effects of ethanol and its oxidative product acetaldehyde.	Acetaldehyde	127-139	mitogen activated protein kinase 14	Rattus norvegicus	48-51
23905689-0	2013	Role of rostral ventrolateral medullary ERK/JNK/p38 MAPK signaling in the pressor effects of ethanol and its oxidative product acetaldehyde.	Acetaldehyde	127-139	mitogen activated protein kinase 1	Rattus norvegicus	52-56
23905689-4	2013	RESULTS: Intra-RVLM EtOH (10 mug/rat) or ACA (2 mug/rat) caused a similar ERK2-dependent pressor response because EtOH or ACA-evoked increases in BP and in RVLM p-ERK2 level were abolished after pharmacologic inhibition of ERK phosphorylation.	Acetaldehyde	41-44	mitogen activated protein kinase 1	Rattus norvegicus	74-78
23905689-4	2013	RESULTS: Intra-RVLM EtOH (10 mug/rat) or ACA (2 mug/rat) caused a similar ERK2-dependent pressor response because EtOH or ACA-evoked increases in BP and in RVLM p-ERK2 level were abolished after pharmacologic inhibition of ERK phosphorylation.	Acetaldehyde	41-44	mitogen activated protein kinase 1	Rattus norvegicus	163-167
23905689-4	2013	RESULTS: Intra-RVLM EtOH (10 mug/rat) or ACA (2 mug/rat) caused a similar ERK2-dependent pressor response because EtOH or ACA-evoked increases in BP and in RVLM p-ERK2 level were abolished after pharmacologic inhibition of ERK phosphorylation.	Acetaldehyde	41-44	Eph receptor B1	Rattus norvegicus	74-77
23905689-9	2013	CONCLUSIONS: Enhancement of RVLM ERK2 phosphorylation constitutes a major molecular mechanism for the pressor response elicited by intra-RVLM EtOH or its metabolite, ACA, in conscious SHRs.	Acetaldehyde	166-169	mitogen activated protein kinase 1	Rattus norvegicus	33-37
23808586-3	2013	Ethanol"s (EtOH) motivational effects are postulated to be mediated by the CAT-dependent acetaldehyde generated in the brain.	Acetaldehyde	89-101	catalase	Rattus norvegicus	75-78
23892315-7	2013	Also, acetaldehyde deodorization results obtained by pH, total acidity and CO2 analyses evidence the process follow Co(III)-MEO.	Acetaldehyde	6-18	mitochondrially encoded cytochrome c oxidase III	Homo sapiens	119-122
23880292-0	2013	Fibrogenic actions of acetaldehyde are beta-catenin dependent but Wingless independent: a critical role of nucleoredoxin and reactive oxygen species in human hepatic stellate cells.	Acetaldehyde	22-34	catenin beta 1	Homo sapiens	39-51
23880292-4	2013	Acetaldehyde induced MYC and collagen type-1 alpha-2 mRNA and protein expressions were WNT independent because DKK1, an antagonist of the canonical WNT/beta-catenin pathway, completely failed to block these inductions.	Acetaldehyde	0-12	MYC proto-oncogene, bHLH transcription factor	Homo sapiens	21-52
23880292-4	2013	Acetaldehyde induced MYC and collagen type-1 alpha-2 mRNA and protein expressions were WNT independent because DKK1, an antagonist of the canonical WNT/beta-catenin pathway, completely failed to block these inductions.	Acetaldehyde	0-12	catenin beta 1	Homo sapiens	152-164
23880292-5	2013	Acetaldehyde increased phospho-glycogen synthase kinase-3 beta (GSK3B) protein by 31% (P&lt;0.01), whereas phospho-beta-catenin protein decreased by 50% (P &lt;= 0.01).	Acetaldehyde	0-12	glycogen synthase kinase 3 beta	Homo sapiens	64-69
23880292-6	2013	Significantly, in contrast to 43% (P&lt;0.01) inhibition of beta-catenin nuclear translocation in nucleoredoxin (NXN)-overexpressed HSC, acetaldehyde profoundly stimulated beta-catenin nuclear translocation by 51%, (P&lt;0.01).	Acetaldehyde	137-149	nucleoredoxin	Homo sapiens	113-116
23880292-6	2013	Significantly, in contrast to 43% (P&lt;0.01) inhibition of beta-catenin nuclear translocation in nucleoredoxin (NXN)-overexpressed HSC, acetaldehyde profoundly stimulated beta-catenin nuclear translocation by 51%, (P&lt;0.01).	Acetaldehyde	137-149	catenin beta 1	Homo sapiens	172-184
23880292-9	2013	Based on these findings, we conclude that actions of acetaldehyde are mediated by a mechanism that inactivates NXN by releasing DVL, leading to the inactivation of GSK3B, and thereby blocks beta-catenin phosphorylation and degradation.	Acetaldehyde	53-65	nucleoredoxin	Homo sapiens	111-114
23880292-9	2013	Based on these findings, we conclude that actions of acetaldehyde are mediated by a mechanism that inactivates NXN by releasing DVL, leading to the inactivation of GSK3B, and thereby blocks beta-catenin phosphorylation and degradation.	Acetaldehyde	53-65	glycogen synthase kinase 3 beta	Homo sapiens	164-169
23880292-9	2013	Based on these findings, we conclude that actions of acetaldehyde are mediated by a mechanism that inactivates NXN by releasing DVL, leading to the inactivation of GSK3B, and thereby blocks beta-catenin phosphorylation and degradation.	Acetaldehyde	53-65	catenin beta 1	Homo sapiens	190-202
24096209-0	2013	Ethanol- and acetaldehyde-induced cholinergic imbalance in the hippocampus of Aldh2-knockout mice does not affect nerve growth factor or brain-derived neurotrophic factor.	Acetaldehyde	13-25	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	78-83
24096209-6	2013	We show that treatment with 2.0 g/kg of EtOH decreased ChAT mRNA and protein levels in Aldh2-KO mice but not in wild-type (WT) mice, which suggests a role for AcH in the mechanism of action of EtOH.	Acetaldehyde	159-162	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	87-92
23318456-7	2013	Finally, we demonstrate that both PD20 and UM are sensitive to acetaldehyde, supporting a role for FANCD2 in repair of lesions induced by such endogenous metabolites.	Acetaldehyde	63-75	FA complementation group D2	Homo sapiens	99-105
23800500-4	2013	In contrast, doxycycline treatment prevented upregulation of MMP-9 protein expression and activity in brains and aortas in response to ACE and significantly decreased stroke incidence.	Acetaldehyde	135-138	matrix metallopeptidase 9	Rattus norvegicus	61-66
23847486-4	2013	Similarly aversive is an increased acetaldehyde level resulting from the inhibition of liver aldehyde dehydrogenase-2 (ALDH2) synthesis (by an antisense coding gene against aldh2 mRNA).	Acetaldehyde	35-47	aldehyde dehydrogenase 1 family, member A1	Rattus norvegicus	93-117
23825090-2	2013	These individuals accumulate acetaldehyde, the primary metabolite of ethanol, because of a genetic polymorphism of aldehyde dehydrogenase (ALDH) that metabolizes acetaldehyde to nontoxic acetate.	Acetaldehyde	29-41	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	115-137
23825090-2	2013	These individuals accumulate acetaldehyde, the primary metabolite of ethanol, because of a genetic polymorphism of aldehyde dehydrogenase (ALDH) that metabolizes acetaldehyde to nontoxic acetate.	Acetaldehyde	29-41	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	139-143
23825090-2	2013	These individuals accumulate acetaldehyde, the primary metabolite of ethanol, because of a genetic polymorphism of aldehyde dehydrogenase (ALDH) that metabolizes acetaldehyde to nontoxic acetate.	Acetaldehyde	162-174	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	115-137
23825090-2	2013	These individuals accumulate acetaldehyde, the primary metabolite of ethanol, because of a genetic polymorphism of aldehyde dehydrogenase (ALDH) that metabolizes acetaldehyde to nontoxic acetate.	Acetaldehyde	162-174	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	139-143
23825090-3	2013	The aim of these studies is to upregulate ALDH by dietary means, thereby reducing acetaldehyde toxicity.	Acetaldehyde	82-94	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	42-46
23759430-0	2013	Highly efficient Michael-type addition of acetaldehyde to beta-nitrostyrenes by whole resting cells of Escherichia coli expressing 4-oxalocrotonate tautomerase.	Acetaldehyde	42-54	4-oxalocrotonate tautomerase	Escherichia coli	131-159
23759430-1	2013	A novel whole cell system based on recombinantly expressed 4-oxalocrotonate tautomerase (4-OT) was developed and shown to be an effective biocatalyst for the asymmetric Michael addition of acetaldehyde to beta-nitrostyrenes.	Acetaldehyde	189-201	4-oxalocrotonate tautomerase	Escherichia coli	59-87
24058561-2	2013	ALDH2 (aldehyde dehydrogenase 2) deficient alcohol consumers are exposed to high concentrations of salivary acetaldehyde and have an increased risk of upper digestive tract cancer.	Acetaldehyde	108-120	aldehyde dehydrogenase 2 family member	Homo sapiens	0-5
24058561-2	2013	ALDH2 (aldehyde dehydrogenase 2) deficient alcohol consumers are exposed to high concentrations of salivary acetaldehyde and have an increased risk of upper digestive tract cancer.	Acetaldehyde	108-120	aldehyde dehydrogenase 2 family member	Homo sapiens	7-31
24058561-4	2013	Therefore, the aim of this study was to examine the effect of the ALDH2 genotype on the exposure to locally formed acetaldehyde via the saliva without ethanol ingestion.	Acetaldehyde	115-127	aldehyde dehydrogenase 2 family member	Homo sapiens	66-71
24058561-10	2013	CONCLUSIONS: For ALDH2 deficient subjects, an elevated exposure to endogenously formed acetaldehyde requires the presence of ethanol in the systemic circulation.	Acetaldehyde	87-99	aldehyde dehydrogenase 2 family member	Homo sapiens	17-22
24058561-12	2013	Thus, ALDH2 deficient alcohol drinkers provide a human model for increased local exposure to acetaldehyde derived from the salivary glands.	Acetaldehyde	93-105	aldehyde dehydrogenase 2 family member	Homo sapiens	6-11
23732484-0	2013	Immune response to acetaldehyde-human serum albumin adduct among healthy subjects related to alcohol intake.	Acetaldehyde	19-31	albumin	Homo sapiens	38-51
23707493-0	2013	Acetaldehyde-induced cytotoxicity involves induction of spermine oxidase at the transcriptional level.	Acetaldehyde	0-12	spermine oxidase	Homo sapiens	56-72
23707493-4	2013	We found that acetaldehyde induced spermine oxidase (SMO) at the transcriptional level in HepG2 cells.	Acetaldehyde	14-26	spermine oxidase	Homo sapiens	35-51
23707493-4	2013	We found that acetaldehyde induced spermine oxidase (SMO) at the transcriptional level in HepG2 cells.	Acetaldehyde	14-26	spermine oxidase	Homo sapiens	53-56
23707493-7	2013	Knockdown of SMO expression using siRNA reduced acetaldehyde toxicity.	Acetaldehyde	48-60	spermine oxidase	Homo sapiens	13-16
23707493-9	2013	An increase of acrolein by acetaldehyde was SMO dependent.	Acetaldehyde	27-39	spermine oxidase	Homo sapiens	44-47
23707493-10	2013	Our results indicate that cytotoxicity of acetaldehyde involves, at least in part, oxidation of spermine to spermidine by SMO, which is induced by acetaldehyde.	Acetaldehyde	42-54	spermine oxidase	Homo sapiens	122-125
23707493-10	2013	Our results indicate that cytotoxicity of acetaldehyde involves, at least in part, oxidation of spermine to spermidine by SMO, which is induced by acetaldehyde.	Acetaldehyde	147-159	spermine oxidase	Homo sapiens	122-125
23692528-4	2013	We demonstrated that a wine yeast strain deleted for AAF1 reduced acetic acid levels in wine by up to 39.2% without increasing the acetaldehyde levels, revealing a potential for industrial application.	Acetaldehyde	131-143	Tda9p	Saccharomyces cerevisiae S288C	53-57
23692528-5	2013	Deletion of the cytosolic aldehyde dehydrogenase gene ALD6 also reduced acetic acid levels dramatically, but increased the acetaldehyde levels by 41.4%, which is not desired by the wine industry.	Acetaldehyde	123-135	aldehyde dehydrogenase (NADP(+)) ALD6	Saccharomyces cerevisiae S288C	54-58
23847486-2	2013	Aldehyde dehydrogenase-2 metabolizes acetaldehyde into acetate in both organs.	Acetaldehyde	37-49	aldehyde dehydrogenase 1 family, member A1	Rattus norvegicus	0-24
23847486-3	2013	Gene specific modifications reviewed here show that an increased liver generation of acetaldehyde (by transduction of a gene coding for a high-activity liver alcohol dehydrogenase ADH1(*)B2) leads to increased blood acetaldehyde levels and aversion to ethanol in animals.	Acetaldehyde	85-97	UDP glucuronosyltransferase 1 family, polypeptide A2	Rattus norvegicus	180-189
23847486-3	2013	Gene specific modifications reviewed here show that an increased liver generation of acetaldehyde (by transduction of a gene coding for a high-activity liver alcohol dehydrogenase ADH1(*)B2) leads to increased blood acetaldehyde levels and aversion to ethanol in animals.	Acetaldehyde	216-228	UDP glucuronosyltransferase 1 family, polypeptide A2	Rattus norvegicus	180-189
23847486-4	2013	Similarly aversive is an increased acetaldehyde level resulting from the inhibition of liver aldehyde dehydrogenase-2 (ALDH2) synthesis (by an antisense coding gene against aldh2 mRNA).	Acetaldehyde	35-47	aldehyde dehydrogenase 1 family, member A1	Rattus norvegicus	119-124
23847486-4	2013	Similarly aversive is an increased acetaldehyde level resulting from the inhibition of liver aldehyde dehydrogenase-2 (ALDH2) synthesis (by an antisense coding gene against aldh2 mRNA).	Acetaldehyde	35-47	aldehyde dehydrogenase 2 family member	Rattus norvegicus	173-178
23847486-6	2013	When the brain ventral tegmental area (VTA) is endowed with an increased ability to generate acetaldehyde (by transfection of liver rADH) the reinforcing effects of ethanol are increased, while a highly specific inhibition of catalase synthesis (by transduction of a shRNA anti catalase mRNA) virtually abolishes the reinforcing effects of ethanol as seen by a complete abolition of ethanol intake in rats bred for generations as high ethanol drinkers.	Acetaldehyde	93-105	alcohol dehydrogenase 1C (class I), gamma polypeptide	Rattus norvegicus	132-136
24273684-4	2013	Decreased drinking due to ALDH-2 inhibition is attributed to aversive properties of acetaldehyde accumulated during alcohol consumption.	Acetaldehyde	84-96	aldehyde dehydrogenase 2 family member	Homo sapiens	26-32
24455167-5	2013	RESULTS: Like 60 mM ethanol, we found that exogenous acetaldehyde enhanced neurosteroid immunostaining in CA1 pyramidal neurons, and that augmented neurosteroid immunostaining by high ethanol alone was blocked by 4MP but not by inhibitors of other ethanol metabolism pathways.	Acetaldehyde	53-65	carbonic anhydrase 1	Rattus norvegicus	106-109
23624825-11	2013	The differences in the activity of total alcohol dehydrogenase, and class I isoenzyme between cancer tissues and healthy brain cells might be a factor for metabolic changes and disturbances in low mature cancer cells and additionally might be a reason for higher level of acetaldehyde which can intensify the carcinogenesis.	Acetaldehyde	272-284	aldo-keto reductase family 1 member A1	Homo sapiens	41-62
23406661-0	2013	The influence of B-complex vitamins upon the prolongation of prothrombin time by acetaldehyde.	Acetaldehyde	81-93	coagulation factor II, thrombin	Homo sapiens	61-72
23406661-3	2013	In this current study, it is reported that prothrombin time (PT), which is prolonged in a fraction of the alcoholic population, can be modified (in the laboratory) when several B-complex vitamins and AcH are added successively to human plasma or are premixed prior to the addition to plasma.	Acetaldehyde	200-203	coagulation factor II, thrombin	Homo sapiens	43-54
23619349-6	2013	RESULTS: The majority (68%) of cultures produced carcinogenic levels of acetaldehyde (&gt;100 muM) when incubated with ethanol (22 mM).	Acetaldehyde	72-84	latexin	Homo sapiens	94-97
23619349-7	2013	The mean acetaldehyde production by microbes cultured from smoker samples was significantly higher (213 muM) than from non-smoker samples (141 muM) (P=.0326).	Acetaldehyde	9-21	latexin	Homo sapiens	104-107
23619349-7	2013	The mean acetaldehyde production by microbes cultured from smoker samples was significantly higher (213 muM) than from non-smoker samples (141 muM) (P=.0326).	Acetaldehyde	9-21	latexin	Homo sapiens	143-146
23801948-8	2013	ACE is a good substrate for CYP 2E1 enzyme as the other substrate-inhibitors and by this way may facilitate the susceptibility of dopaminergic neurons to toxic events.	Acetaldehyde	0-3	cytochrome P450, family 2, subfamily e, polypeptide 1	Mus musculus	28-35
23380360-4	2013	Moreover, certain nutraceuticals, including taurine, pantethine, and lipoic acid, may have the potential to boost the activity of the mitochondrial isoform of aldehyde dehydrogenase, ALDH-2, accelerating conversion of acetaldehyde to acetate (which arguably has protective health effects).	Acetaldehyde	218-230	aldehyde dehydrogenase 2 family member	Homo sapiens	183-189
23840319-0	2013	IGHV1-69-encoded antibodies expressed in chronic lymphocytic leukemia react with malondialdehyde-acetaldehyde adduct, an immunodominant oxidation-specific epitope.	Acetaldehyde	97-109	immunoglobulin heavy variable 1-69	Homo sapiens	0-8
23313283-1	2013	INTRODUCTION: Aldehyde dehydrogenase 2 (ALDH2) degrades acetaldehyde produced by the metabolism of alcohol.	Acetaldehyde	56-68	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	14-38
23313283-1	2013	INTRODUCTION: Aldehyde dehydrogenase 2 (ALDH2) degrades acetaldehyde produced by the metabolism of alcohol.	Acetaldehyde	56-68	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	40-45
23468340-2	2013	C48/80 was quantified at 570 nm after reaction with acetaldehyde and sodium nitroprusside in an alkaline solution (pH 9.6).	Acetaldehyde	52-64	CDK5 regulatory subunit associated protein 2	Homo sapiens	0-3
23225495-4	2013	In this work, we show that dynamic MRSI of hyperpolarized [1-(13) C]pyruvate and its conversion to [1-(13) C]lactate can provide an indirect in vivo measurement of ALDH2 activity via the concentration of NADH (nicotinamide adenine dinucleotide, reduced form), a co-factor common to both the reduction of pyruvate to lactate and the oxidation of acetaldehyde to acetate.	Acetaldehyde	345-357	aldehyde dehydrogenase 1 family, member A1	Rattus norvegicus	164-169
23745109-0	2013	c-Fos immunoreactivity in prefrontal, basal ganglia and limbic areas of the rat brain after central and peripheral administration of ethanol and its metabolite acetaldehyde.	Acetaldehyde	160-172	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	0-5
23745109-7	2013	IP administration of EtOH minimally induced c-Fos in some regions of the prefrontal cortex and basal ganglia, mainly at the low dose (0.5 g/kg), while IP acetaldehyde induced c-Fos in virtually all the structures studied at both doses.	Acetaldehyde	154-166	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	175-180
23745109-8	2013	Acetaldehyde administered centrally increased c-Fos in all areas studied, a pattern that was very similar to EtOH.	Acetaldehyde	0-12	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	46-51
23745109-9	2013	Thus, IP administered acetaldehyde was more efficacious than EtOH at inducing c-Fos expression.	Acetaldehyde	22-34	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	78-83
23745109-10	2013	However, the general pattern of c-Fos induction promoted by ICV EtOH and acetaldehyde was similar.	Acetaldehyde	73-85	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	32-37
22615054-2	2013	Strains deleted in the genes encoding the enzymes involved in glutathione synthesis and reduction, GSH1, GSH2 and GLR1, exhibited severe growth defects compared to wild-type under acetaldehyde stress, although strains deleted in the genes encoding glutathione peroxidases or glutathione transferases did not show any growth defects.	Acetaldehyde	180-192	glutamate--cysteine ligase	Saccharomyces cerevisiae S288C	99-103
23220590-6	2013	At therapeutic drug levels (0.015 mM) and physiologically relevant concentrations of ethanol (10 mM) and acetaldehyde (10 muM) in target tissues, cimetidine could weakly inhibit (&lt;5%) the activities of ADH1B2 and ADH1B3 in liver, ADH2 in liver and small intestine, ADH4 in stomach, and ALDH1A1 in the three tissues, but not significantly affect ADH1A, ADH1B1, ADH1C1/2, or ALDH2.	Acetaldehyde	105-117	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	205-210
23247008-1	2013	Vertebrate ALDH2 genes encode mitochondrial enzymes capable of metabolizing acetaldehyde and other biological aldehydes in the body.	Acetaldehyde	76-88	aldehyde dehydrogenase 2 family member	Homo sapiens	11-16
23247008-2	2013	Mammalian ALDH1B1, another mitochondrial enzyme sharing 72% identity with ALDH2, is also capable of metabolizing acetaldehyde but has a tissue distribution and pattern of activity distinct from that of ALDH2.	Acetaldehyde	113-125	aldehyde dehydrogenase 1 family member B1	Homo sapiens	10-17
23247008-2	2013	Mammalian ALDH1B1, another mitochondrial enzyme sharing 72% identity with ALDH2, is also capable of metabolizing acetaldehyde but has a tissue distribution and pattern of activity distinct from that of ALDH2.	Acetaldehyde	113-125	aldehyde dehydrogenase 2 family member	Homo sapiens	74-79
23519123-1	2013	CYP2E1 metabolizes ethanol leading to production of reactive oxygen species (ROS) and acetaldehyde, which are known to cause not only liver damage but also toxicity to other organs.	Acetaldehyde	86-98	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	0-6
23352969-0	2013	Inhibition of CYP2E1 leads to decreased malondialdehyde-acetaldehyde adduct formation in VL-17A cells under chronic alcohol exposure.	Acetaldehyde	56-68	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	14-20
23103837-3	2013	Here, using recombinant hepatoma (HepG2; VL-17A) cells that metabolize ethanol, we show that alcohol dehydrogenase catalysis of ethanol oxidation and subsequent acetaldehyde production controls Egr-1 expression.	Acetaldehyde	161-173	early growth response 1	Homo sapiens	194-199
23103837-10	2013	However, direct exposure of HepG2 cells to acetaldehyde induced both Egr-1 protein and triglycerides.	Acetaldehyde	43-55	early growth response 1	Homo sapiens	69-74
23223230-1	2013	In yeast, Adh1 (alcohol dehydrogenase 1) is an abundant zinc-binding protein that is required for the conversion of acetaldehyde to ethanol.	Acetaldehyde	116-128	alcohol dehydrogenase ADH1	Saccharomyces cerevisiae S288C	10-14
23223230-1	2013	In yeast, Adh1 (alcohol dehydrogenase 1) is an abundant zinc-binding protein that is required for the conversion of acetaldehyde to ethanol.	Acetaldehyde	116-128	alcohol dehydrogenase ADH1	Saccharomyces cerevisiae S288C	16-39
22615054-2	2013	Strains deleted in the genes encoding the enzymes involved in glutathione synthesis and reduction, GSH1, GSH2 and GLR1, exhibited severe growth defects compared to wild-type under acetaldehyde stress, although strains deleted in the genes encoding glutathione peroxidases or glutathione transferases did not show any growth defects.	Acetaldehyde	180-192	glutathione synthase	Saccharomyces cerevisiae S288C	105-109
22615054-2	2013	Strains deleted in the genes encoding the enzymes involved in glutathione synthesis and reduction, GSH1, GSH2 and GLR1, exhibited severe growth defects compared to wild-type under acetaldehyde stress, although strains deleted in the genes encoding glutathione peroxidases or glutathione transferases did not show any growth defects.	Acetaldehyde	180-192	glutathione-disulfide reductase GLR1	Saccharomyces cerevisiae S288C	114-118
23064762-9	2012	Coimmunoprecipitation studies showed that acetaldehyde increased the interaction of PP2A with occludin and induced dephosphorylation of occludin on threonine residues.	Acetaldehyde	42-54	occludin	Homo sapiens	136-144
24151610-4	2013	In addition, via CYP450 (CYP2E1) oxidase, alcohol is metabolized to acetaldehyde, a highly toxic compound, which plays an important role in carcinogenesis.	Acetaldehyde	68-80	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	25-31
23238616-1	2013	Aldehyde dehydrogenase-2 (ALDH2) is the main enzyme responsible for acetaldehyde oxidation in ethanol metabolism and also provides protection against oxidative stress.	Acetaldehyde	68-80	aldehyde dehydrogenase 2 family member	Homo sapiens	0-24
23238616-1	2013	Aldehyde dehydrogenase-2 (ALDH2) is the main enzyme responsible for acetaldehyde oxidation in ethanol metabolism and also provides protection against oxidative stress.	Acetaldehyde	68-80	aldehyde dehydrogenase 2 family member	Homo sapiens	26-31
23064762-3	2012	In the present study, we investigated the role of PP2A in the acetaldehyde-induced disruption of intestinal epithelial tight junctions.	Acetaldehyde	62-74	protein phosphatase 2 phosphatase activator	Homo sapiens	50-54
23064762-5	2012	Acetaldehyde treatment resulted in a time-dependent increase in inulin permeability and redistribution of occludin and ZO-1 from the intercellular junctions.	Acetaldehyde	0-12	occludin	Homo sapiens	106-114
23064762-10	2012	Fostriecin and TPDYFL significantly reduced acetaldehyde-induced threonine dephosphorylation of occludin.	Acetaldehyde	44-56	occludin	Homo sapiens	96-104
23064762-5	2012	Acetaldehyde treatment resulted in a time-dependent increase in inulin permeability and redistribution of occludin and ZO-1 from the intercellular junctions.	Acetaldehyde	0-12	tight junction protein 1	Homo sapiens	119-123
23064762-6	2012	Treatment of cells with fostriecin (a PP2A-selective inhibitor) or knockdown of PP2A by siRNA blocked acetaldehyde-induced increase in inulin permeability and redistribution of occludin and ZO-1.	Acetaldehyde	102-114	protein phosphatase 2 phosphatase activator	Homo sapiens	38-42
23064762-6	2012	Treatment of cells with fostriecin (a PP2A-selective inhibitor) or knockdown of PP2A by siRNA blocked acetaldehyde-induced increase in inulin permeability and redistribution of occludin and ZO-1.	Acetaldehyde	102-114	protein phosphatase 2 phosphatase activator	Homo sapiens	80-84
23064762-6	2012	Treatment of cells with fostriecin (a PP2A-selective inhibitor) or knockdown of PP2A by siRNA blocked acetaldehyde-induced increase in inulin permeability and redistribution of occludin and ZO-1.	Acetaldehyde	102-114	occludin	Homo sapiens	177-185
23064762-6	2012	Treatment of cells with fostriecin (a PP2A-selective inhibitor) or knockdown of PP2A by siRNA blocked acetaldehyde-induced increase in inulin permeability and redistribution of occludin and ZO-1.	Acetaldehyde	102-114	tight junction protein 1	Homo sapiens	190-194
23064762-8	2012	Acetaldehyde-induced tight junction disruption and barrier dysfunction were also attenuated by a PP2A-specific inhibitory peptide, TPDYFL.	Acetaldehyde	0-12	protein phosphatase 2 phosphatase activator	Homo sapiens	97-101
23064762-9	2012	Coimmunoprecipitation studies showed that acetaldehyde increased the interaction of PP2A with occludin and induced dephosphorylation of occludin on threonine residues.	Acetaldehyde	42-54	protein phosphatase 2 phosphatase activator	Homo sapiens	84-88
23064762-12	2012	However, genistein (a tyrosine kinase inhibitor) blocked acetaldehyde-induced association of PP2A with occludin and threonine dephosphorylation of occludin.	Acetaldehyde	57-69	protein phosphatase 2 phosphatase activator	Homo sapiens	93-97
23064762-9	2012	Coimmunoprecipitation studies showed that acetaldehyde increased the interaction of PP2A with occludin and induced dephosphorylation of occludin on threonine residues.	Acetaldehyde	42-54	occludin	Homo sapiens	94-102
23064762-12	2012	However, genistein (a tyrosine kinase inhibitor) blocked acetaldehyde-induced association of PP2A with occludin and threonine dephosphorylation of occludin.	Acetaldehyde	57-69	occludin	Homo sapiens	103-111
23064762-12	2012	However, genistein (a tyrosine kinase inhibitor) blocked acetaldehyde-induced association of PP2A with occludin and threonine dephosphorylation of occludin.	Acetaldehyde	57-69	occludin	Homo sapiens	147-155
23064762-13	2012	These results demonstrate that acetaldehyde-induced disruption of tight junctions is mediated by PP2A translocation to tight junctions and dephosphorylation of occludin on threonine residues.	Acetaldehyde	31-43	protein phosphatase 2 phosphatase activator	Homo sapiens	97-101
23064762-13	2012	These results demonstrate that acetaldehyde-induced disruption of tight junctions is mediated by PP2A translocation to tight junctions and dephosphorylation of occludin on threonine residues.	Acetaldehyde	31-43	occludin	Homo sapiens	160-168
22486589-1	2012	BACKGROUND: Ethanol (EtOH) is metabolized by a 2-step process in which alcohol dehydrogenase (ADH) oxidizes EtOH to acetaldehyde, which is further oxidized to acetate by aldehyde dehydrogenase (ALDH).	Acetaldehyde	116-128	Aldehyde dehydrogenase	Caenorhabditis elegans	170-192
23217322-4	2012	Therefore, for the first time, the hyphenated ACE with a high-sensitivity cell was developed and employed to investigate the binding of retinol and retinoic acid in nanomolars with human serum albumin (HSA) and bovine serum albumin (BSA) under physiological conditions.	Acetaldehyde	46-49	albumin	Homo sapiens	187-200
23217322-4	2012	Therefore, for the first time, the hyphenated ACE with a high-sensitivity cell was developed and employed to investigate the binding of retinol and retinoic acid in nanomolars with human serum albumin (HSA) and bovine serum albumin (BSA) under physiological conditions.	Acetaldehyde	46-49	albumin	Homo sapiens	218-231
23130947-4	2012	Based on such principles, the fabricated acetaldehyde sensor exhibited excellent selectivity with wide linear range (5-200 muM) and low detection limit (1 muM), which conforms to the criteria provided by the World Health Organisation (WHO).	Acetaldehyde	41-53	latexin	Homo sapiens	123-126
23130947-4	2012	Based on such principles, the fabricated acetaldehyde sensor exhibited excellent selectivity with wide linear range (5-200 muM) and low detection limit (1 muM), which conforms to the criteria provided by the World Health Organisation (WHO).	Acetaldehyde	41-53	latexin	Homo sapiens	155-158
22486589-1	2012	BACKGROUND: Ethanol (EtOH) is metabolized by a 2-step process in which alcohol dehydrogenase (ADH) oxidizes EtOH to acetaldehyde, which is further oxidized to acetate by aldehyde dehydrogenase (ALDH).	Acetaldehyde	116-128	Aldehyde dehydrogenase	Caenorhabditis elegans	194-198
22451246-11	2012	Third, the pear increased the acetaldehyde level in blood in Aldh2 deficient mice but not in Aldh2 normal mice.	Acetaldehyde	30-42	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	61-66
23126711-1	2012	A heated SiC microtubular reactor has been used to decompose acetaldehyde and its isotopomers (CH(3)CDO, CD(3)CHO, and CD(3)CDO).	Acetaldehyde	61-73	cell adhesion associated, oncogene regulated	Homo sapiens	100-103
22761303-6	2012	ALDH2 activation substantially reduced acetaldehyde- and hypoxia-induced norepinephrine release, an action prevented by inhibition of ALDH2 or protein kinase Cepsilon (PKCepsilon).	Acetaldehyde	39-51	protein kinase C, epsilon	Rattus norvegicus	168-178
22761303-6	2012	ALDH2 activation substantially reduced acetaldehyde- and hypoxia-induced norepinephrine release, an action prevented by inhibition of ALDH2 or protein kinase Cepsilon (PKCepsilon).	Acetaldehyde	39-51	aldehyde dehydrogenase 2 family member	Rattus norvegicus	0-5
22761303-6	2012	ALDH2 activation substantially reduced acetaldehyde- and hypoxia-induced norepinephrine release, an action prevented by inhibition of ALDH2 or protein kinase Cepsilon (PKCepsilon).	Acetaldehyde	39-51	aldehyde dehydrogenase 2 family member	Rattus norvegicus	134-139
22241472-8	2012	AGXT2L1 catalyzed a similar reaction on phosphoethanolamine, converting it to ammonia, inorganic phosphate, and acetaldehyde.	Acetaldehyde	112-124	ethanolamine-phosphate phospho-lyase	Homo sapiens	0-7
22761303-6	2012	ALDH2 activation substantially reduced acetaldehyde- and hypoxia-induced norepinephrine release, an action prevented by inhibition of ALDH2 or protein kinase Cepsilon (PKCepsilon).	Acetaldehyde	39-51	protein kinase C, epsilon	Rattus norvegicus	143-166
22508505-3	2012	Aldh2 plays a role in alcohol-detoxification by acetaldehyde-detoxification; however, transgenic mice expressing Aldh2*2 (Aldh2*2 Tg) exhibited severe osteoporosis with increased levels of blood acetaldehyde without alcohol consumption, indicating that Aldh2 regulates physiological bone homeostasis.	Acetaldehyde	48-60	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	0-5
22508505-3	2012	Aldh2 plays a role in alcohol-detoxification by acetaldehyde-detoxification; however, transgenic mice expressing Aldh2*2 (Aldh2*2 Tg) exhibited severe osteoporosis with increased levels of blood acetaldehyde without alcohol consumption, indicating that Aldh2 regulates physiological bone homeostasis.	Acetaldehyde	195-207	aldehyde dehydrogenase 2 family member	Homo sapiens	113-118
22508505-3	2012	Aldh2 plays a role in alcohol-detoxification by acetaldehyde-detoxification; however, transgenic mice expressing Aldh2*2 (Aldh2*2 Tg) exhibited severe osteoporosis with increased levels of blood acetaldehyde without alcohol consumption, indicating that Aldh2 regulates physiological bone homeostasis.	Acetaldehyde	195-207	aldehyde dehydrogenase 2 family member	Homo sapiens	113-118
22508505-3	2012	Aldh2 plays a role in alcohol-detoxification by acetaldehyde-detoxification; however, transgenic mice expressing Aldh2*2 (Aldh2*2 Tg) exhibited severe osteoporosis with increased levels of blood acetaldehyde without alcohol consumption, indicating that Aldh2 regulates physiological bone homeostasis.	Acetaldehyde	195-207	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	113-118
22508505-6	2012	The Aldh2*2 transgene or acetaldehyde treatment induced accumulation of the lipid-oxidant 4-hydroxy-2-nonenal (4HNE) and expression of peroxisome proliferator-activated receptor gamma (PPARgamma), a transcription factor that promotes adipogenesis and inhibits osteoblastogenesis.	Acetaldehyde	25-37	peroxisome proliferator activated receptor gamma	Homo sapiens	135-183
22508505-6	2012	The Aldh2*2 transgene or acetaldehyde treatment induced accumulation of the lipid-oxidant 4-hydroxy-2-nonenal (4HNE) and expression of peroxisome proliferator-activated receptor gamma (PPARgamma), a transcription factor that promotes adipogenesis and inhibits osteoblastogenesis.	Acetaldehyde	25-37	peroxisome proliferator activated receptor gamma	Homo sapiens	185-194
22508505-7	2012	Antioxidant treatment inhibited acetaldehyde-induced proliferation-loss, apoptosis, and PPARgamma expression and restored osteoblastogenesis inhibited by acetaldehyde.	Acetaldehyde	32-44	peroxisome proliferator activated receptor gamma	Homo sapiens	88-97
22508505-8	2012	Treatment with a PPARgamma inhibitor also restored acetaldehyde-mediated osteoblastogenesis inhibition.	Acetaldehyde	51-63	peroxisome proliferator activated receptor gamma	Homo sapiens	17-26
22711426-3	2012	In this study, branch emissions of GLVs and a group of oxygenated metabolites (acetaldehyde, ethanol, acetic acid, and acetone) derived from the pyruvate dehydrogenase (PDH) bypass pathway were quantified from mesquite plants following light-dark transitions using a coupled GC-MS, PTR-MS, and photosynthesis system.	Acetaldehyde	79-91	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	145-167
22711426-3	2012	In this study, branch emissions of GLVs and a group of oxygenated metabolites (acetaldehyde, ethanol, acetic acid, and acetone) derived from the pyruvate dehydrogenase (PDH) bypass pathway were quantified from mesquite plants following light-dark transitions using a coupled GC-MS, PTR-MS, and photosynthesis system.	Acetaldehyde	79-91	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	169-172
22407337-0	2012	Polyamines detoxify the anticoagulant effect of acetaldehyde on prothrombin time.	Acetaldehyde	48-60	coagulation factor II, thrombin	Homo sapiens	64-75
22551057-0	2012	Mineralization of gaseous acetaldehyde by electrochemically generated Co(III) in H2SO4 with wet scrubber combinatorial system.	Acetaldehyde	26-38	mitochondrially encoded cytochrome c oxidase III	Homo sapiens	70-77
22551057-1	2012	Electrochemically generated Co(III) mediated catalytic room temperature incineration of acetaldehyde, which is one of volatile organic compounds (VOCs), combined with wet scrubbing system was developed and investigated.	Acetaldehyde	88-100	mitochondrially encoded cytochrome c oxidase III	Homo sapiens	28-34
22551057-3	2012	In presence of electrogenerated Co(III) in sulfuric acid, acetaldehyde was mineralized to CO2 and not like only absorption in pure sulfuric acid.	Acetaldehyde	58-70	mitochondrially encoded cytochrome c oxidase III	Homo sapiens	32-38
22551057-6	2012	By the optimization of the experimental conditions, the complete mineralization of acetaldehyde was realized at a room temperature using electrochemically generated Co(III) with wet scrubber combinatorial system.	Acetaldehyde	83-95	mitochondrially encoded cytochrome c oxidase III	Homo sapiens	165-172
22318456-4	2012	Immobilised DERA maintained maximal activity in 2-deoxyribose-5-phosphate (DR5P) synthesis up to 600 mM of acetaldehyde, which was much higher than the amount of acetaldehyde tolerated by free enzyme (300 mM).	Acetaldehyde	107-119	deoxyribose-phosphate aldolase	Homo sapiens	12-16
22318456-4	2012	Immobilised DERA maintained maximal activity in 2-deoxyribose-5-phosphate (DR5P) synthesis up to 600 mM of acetaldehyde, which was much higher than the amount of acetaldehyde tolerated by free enzyme (300 mM).	Acetaldehyde	162-174	deoxyribose-phosphate aldolase	Homo sapiens	12-16
22285649-4	2012	By 48 h, the level of acetaldehyde decreased in association with the induction of aldehyde dehydrogenase (ALDH) type 1 family members.	Acetaldehyde	22-34	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	82-104
22285649-4	2012	By 48 h, the level of acetaldehyde decreased in association with the induction of aldehyde dehydrogenase (ALDH) type 1 family members.	Acetaldehyde	22-34	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	106-110
22361447-10	2012	The 2.0 g/kg EtOH-induced memory impairment in Aldh2-KO mice was greater, suggesting an AcH effect.	Acetaldehyde	88-91	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	47-52
22931071-1	2012	BACKGROUND: Ethanol is primarily metabolized in the liver by two rate-limiting reactions: conversion of ethanol to acetaldehyde by alcohol dehydrogenase (ADH) and subsequent conversion of acetaldehyde to acetate by aldehyde dehydrogenase (ALDH).	Acetaldehyde	115-127	aldo-keto reductase family 1 member A1	Homo sapiens	131-152
22703580-0	2012	Combination of ADH1B*2/ALDH2*2 polymorphisms alters acetaldehyde-derived DNA damage in the blood of Japanese alcoholics.	Acetaldehyde	52-64	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	15-20
22703580-0	2012	Combination of ADH1B*2/ALDH2*2 polymorphisms alters acetaldehyde-derived DNA damage in the blood of Japanese alcoholics.	Acetaldehyde	52-64	aldehyde dehydrogenase 2 family member	Homo sapiens	23-28
22703580-4	2012	ADH1B*2 is involved in overproduction of acetaldehyde due to increased ethanol metabolism into acetaldehyde, and ALDH2*2 is involved in accumulation of acetaldehyde due to the deficiency of acetaldehyde metabolism.	Acetaldehyde	41-53	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	0-5
22703580-4	2012	ADH1B*2 is involved in overproduction of acetaldehyde due to increased ethanol metabolism into acetaldehyde, and ALDH2*2 is involved in accumulation of acetaldehyde due to the deficiency of acetaldehyde metabolism.	Acetaldehyde	95-107	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	0-5
22703580-4	2012	ADH1B*2 is involved in overproduction of acetaldehyde due to increased ethanol metabolism into acetaldehyde, and ALDH2*2 is involved in accumulation of acetaldehyde due to the deficiency of acetaldehyde metabolism.	Acetaldehyde	95-107	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	0-5
22710192-7	2012	RESULTS: The ethanol metabolites acetaldehyde, ethyl palmitate, and ethyl oleate reduced CCK-8-stimulated apical exocytosis and formation of apical exocytotic complexes (between Munc18b and Syntaxin-2, synaptosomal-associated protein of 23 kilodaltons [SNAP23], and VAMP2) in rat pancreatic acini.	Acetaldehyde	33-45	syntaxin binding protein 2	Rattus norvegicus	178-185
22710192-7	2012	RESULTS: The ethanol metabolites acetaldehyde, ethyl palmitate, and ethyl oleate reduced CCK-8-stimulated apical exocytosis and formation of apical exocytotic complexes (between Munc18b and Syntaxin-2, synaptosomal-associated protein of 23 kilodaltons [SNAP23], and VAMP2) in rat pancreatic acini.	Acetaldehyde	33-45	syntaxin 2	Rattus norvegicus	190-200
22710192-7	2012	RESULTS: The ethanol metabolites acetaldehyde, ethyl palmitate, and ethyl oleate reduced CCK-8-stimulated apical exocytosis and formation of apical exocytotic complexes (between Munc18b and Syntaxin-2, synaptosomal-associated protein of 23 kilodaltons [SNAP23], and VAMP2) in rat pancreatic acini.	Acetaldehyde	33-45	synaptosome associated protein 23	Rattus norvegicus	253-259
22710192-7	2012	RESULTS: The ethanol metabolites acetaldehyde, ethyl palmitate, and ethyl oleate reduced CCK-8-stimulated apical exocytosis and formation of apical exocytotic complexes (between Munc18b and Syntaxin-2, synaptosomal-associated protein of 23 kilodaltons [SNAP23], and VAMP2) in rat pancreatic acini.	Acetaldehyde	33-45	vesicle-associated membrane protein 2	Rattus norvegicus	266-271
22710192-8	2012	Acetaldehyde and ethyl oleate redirected CCK-8-stimulated exocytosis to the basal and lateral plasma membranes and translocation of VAMP8-containing ZGs toward the basolateral plasma membrane.	Acetaldehyde	0-12	vesicle-associated membrane protein 8	Rattus norvegicus	132-137
22710192-11	2012	Acetaldehyde, like ethanol, promoted fusion between ZGs by the formation of ZG-ZG exocytotic complexes (between Munc18b and Syntaxin-3, SNAP23, and VAMP8), whereas ethyl palmitate and ethyl oleate reduced ZG-ZG fusion and formation of these complexes.	Acetaldehyde	0-12	syntaxin binding protein 2	Rattus norvegicus	112-119
22710192-11	2012	Acetaldehyde, like ethanol, promoted fusion between ZGs by the formation of ZG-ZG exocytotic complexes (between Munc18b and Syntaxin-3, SNAP23, and VAMP8), whereas ethyl palmitate and ethyl oleate reduced ZG-ZG fusion and formation of these complexes.	Acetaldehyde	0-12	syntaxin 3	Rattus norvegicus	124-134
22710192-11	2012	Acetaldehyde, like ethanol, promoted fusion between ZGs by the formation of ZG-ZG exocytotic complexes (between Munc18b and Syntaxin-3, SNAP23, and VAMP8), whereas ethyl palmitate and ethyl oleate reduced ZG-ZG fusion and formation of these complexes.	Acetaldehyde	0-12	synaptosome associated protein 23	Rattus norvegicus	136-142
22710192-11	2012	Acetaldehyde, like ethanol, promoted fusion between ZGs by the formation of ZG-ZG exocytotic complexes (between Munc18b and Syntaxin-3, SNAP23, and VAMP8), whereas ethyl palmitate and ethyl oleate reduced ZG-ZG fusion and formation of these complexes.	Acetaldehyde	0-12	vesicle-associated membrane protein 8	Rattus norvegicus	148-153
22353233-1	2012	PURPOSE: Recent epidemiological studies demonstrated that alcohol dehydrogenase 1C (ADH1C) alleles that result in acetaldehyde accumulation in the cells can enhance a drinker"s risk of developing alcohol related cancer in a variety of tissues.	Acetaldehyde	114-126	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	58-82
22353233-1	2012	PURPOSE: Recent epidemiological studies demonstrated that alcohol dehydrogenase 1C (ADH1C) alleles that result in acetaldehyde accumulation in the cells can enhance a drinker"s risk of developing alcohol related cancer in a variety of tissues.	Acetaldehyde	114-126	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	84-89
22544865-4	2012	ALDH2, as a key enzyme that oxidizes acetaldehyde, is crucial for alcohol metabolism.	Acetaldehyde	37-49	aldehyde dehydrogenase 2 family member	Homo sapiens	0-5
22615048-1	2012	An unconventional dehalogenase: An engineered variant (I64V/V106L) of the mouse cytokine macrophage migration inhibitory factor (MIF) promiscuously catalyzes the hydrolytic dehalogenation of the xenobiotic organohalogen trans-3-chloroacrylic acid to acetaldehyde.	Acetaldehyde	250-262	macrophage migration inhibitory factor (glycosylation-inhibiting factor)	Mus musculus	129-132
22102315-2	2012	The aldehyde dehydrogenase 2 gene (ALDH2) is the most important gene responsible for acetaldehyde metabolism.	Acetaldehyde	85-97	aldehyde dehydrogenase 2 family member	Homo sapiens	4-28
22102315-2	2012	The aldehyde dehydrogenase 2 gene (ALDH2) is the most important gene responsible for acetaldehyde metabolism.	Acetaldehyde	85-97	aldehyde dehydrogenase 2 family member	Homo sapiens	35-40
22102315-3	2012	Individuals heterozygous or homozygous for the lys (A or *2) allele at the single nucleotide polymorphism (SNP) glu504lys (rs671) of ALDH2 have greatly reduced ability to metabolize acetaldehyde, which greatly decreases their risk for alcohol dependence (AD).	Acetaldehyde	182-194	aldehyde dehydrogenase 2 family member	Homo sapiens	133-138
22042713-2	2012	This risk may be modified by alcohol dehydrogenase (ADH) genes, particularly ADH1B and ADH1C, that oxidise ethanol to its carcinogenic metabolite, acetaldehyde.	Acetaldehyde	147-159	aldo-keto reductase family 1 member A1	Homo sapiens	29-50
22042713-2	2012	This risk may be modified by alcohol dehydrogenase (ADH) genes, particularly ADH1B and ADH1C, that oxidise ethanol to its carcinogenic metabolite, acetaldehyde.	Acetaldehyde	147-159	aldo-keto reductase family 1 member A1	Homo sapiens	52-55
22042713-2	2012	This risk may be modified by alcohol dehydrogenase (ADH) genes, particularly ADH1B and ADH1C, that oxidise ethanol to its carcinogenic metabolite, acetaldehyde.	Acetaldehyde	147-159	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	77-82
22042713-2	2012	This risk may be modified by alcohol dehydrogenase (ADH) genes, particularly ADH1B and ADH1C, that oxidise ethanol to its carcinogenic metabolite, acetaldehyde.	Acetaldehyde	147-159	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	87-92
22042713-6	2012	A reduced risk for HNC was associated with carrying the ADH1B*2 and ADH1C*1 alleles that confer faster metabolism of ethanol to acetaldehyde [meta-OR ADH1B, 0.50; 95% confidence interval (CI): 0.37-0.68, 13 studies; meta-OR ADH1C, 0.87; 95% CI: 0.76-0.99, 22 studies].	Acetaldehyde	128-140	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	56-61
22042713-6	2012	A reduced risk for HNC was associated with carrying the ADH1B*2 and ADH1C*1 alleles that confer faster metabolism of ethanol to acetaldehyde [meta-OR ADH1B, 0.50; 95% confidence interval (CI): 0.37-0.68, 13 studies; meta-OR ADH1C, 0.87; 95% CI: 0.76-0.99, 22 studies].	Acetaldehyde	128-140	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	68-73
22042713-6	2012	A reduced risk for HNC was associated with carrying the ADH1B*2 and ADH1C*1 alleles that confer faster metabolism of ethanol to acetaldehyde [meta-OR ADH1B, 0.50; 95% confidence interval (CI): 0.37-0.68, 13 studies; meta-OR ADH1C, 0.87; 95% CI: 0.76-0.99, 22 studies].	Acetaldehyde	128-140	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	150-155
22042713-7	2012	ADH1B*2 and ADH1C*1 alleles appear to be protective for HNC, possibly due to: (i) decreasing the opportunity for oral microflora to produce acetaldehyde locally from a prolonged systemic circulation of ethanol, (ii) preventing ethanol from acting as a solvent for other carcinogens, and (iii) decreasing the amount of ethanol a person consumes since a consequent peak in systemic acetaldehyde could cause discomfort.	Acetaldehyde	140-152	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	0-5
22042713-7	2012	ADH1B*2 and ADH1C*1 alleles appear to be protective for HNC, possibly due to: (i) decreasing the opportunity for oral microflora to produce acetaldehyde locally from a prolonged systemic circulation of ethanol, (ii) preventing ethanol from acting as a solvent for other carcinogens, and (iii) decreasing the amount of ethanol a person consumes since a consequent peak in systemic acetaldehyde could cause discomfort.	Acetaldehyde	140-152	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	12-17
22042713-7	2012	ADH1B*2 and ADH1C*1 alleles appear to be protective for HNC, possibly due to: (i) decreasing the opportunity for oral microflora to produce acetaldehyde locally from a prolonged systemic circulation of ethanol, (ii) preventing ethanol from acting as a solvent for other carcinogens, and (iii) decreasing the amount of ethanol a person consumes since a consequent peak in systemic acetaldehyde could cause discomfort.	Acetaldehyde	380-392	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	0-5
22042713-7	2012	ADH1B*2 and ADH1C*1 alleles appear to be protective for HNC, possibly due to: (i) decreasing the opportunity for oral microflora to produce acetaldehyde locally from a prolonged systemic circulation of ethanol, (ii) preventing ethanol from acting as a solvent for other carcinogens, and (iii) decreasing the amount of ethanol a person consumes since a consequent peak in systemic acetaldehyde could cause discomfort.	Acetaldehyde	380-392	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	12-17
22455355-8	2012	CONCLUSIONS: Facial redness and pulse rate after ethanol ingestion were significantly higher in the ALDH2*1/*2 genotype, and were significantly associated with blood acetaldehyde concentrations.	Acetaldehyde	166-178	aldehyde dehydrogenase 2 family member	Homo sapiens	100-105
22703173-4	2012	The most well-established genetic factors associated with alcohol dependence are in the genes encoding alcohol dehydrogenase (ADH), which oxidizes alcohol to acetaldehyde, and aldehyde dehydrogenase (ALDH2), which oxidizes acetaldehyde to acetate.	Acetaldehyde	158-170	aldehyde dehydrogenase 2 family member	Homo sapiens	200-205
22100631-5	2012	Chronic and high alcohol use has been implicated in the induction of CYP2E1, which oxidizes ethanol to acetaldehyde.	Acetaldehyde	103-115	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	69-75
22100631-9	2012	Our first hypothesis is that as increased levels of folate lead to higher concentrations of SAM, SAM antagonizes the expression of CYP2E1, which results in decreased conversion of ethanol into acetaldehyde.	Acetaldehyde	193-205	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	131-137
22100631-12	2012	The first, ALDH1A1, converts acetaldehyde into its non-carcinogenic byproduct, acetate, as part of the second step in the ethanol metabolism pathway.	Acetaldehyde	29-41	aldehyde dehydrogenase 1 family member A1	Homo sapiens	11-18
22100631-16	2012	Our second hypothesis is that folate interacts with one of these response elements to upregulate ALDH1A1 and ALDH1L1 expression in order to decrease acetaldehyde concentrations and promote DNA stability, thereby decreasing cancer susceptibility.	Acetaldehyde	149-161	aldehyde dehydrogenase 1 family member A1	Homo sapiens	97-104
22100631-16	2012	Our second hypothesis is that folate interacts with one of these response elements to upregulate ALDH1A1 and ALDH1L1 expression in order to decrease acetaldehyde concentrations and promote DNA stability, thereby decreasing cancer susceptibility.	Acetaldehyde	149-161	aldehyde dehydrogenase 1 family member L1	Homo sapiens	109-116
21940137-9	2012	The activity of ALDH2-active phenotypes of rectal mucosa was 33% greater than ALDH2-inactive phenotypes at 200muM acetaldehyde.	Acetaldehyde	114-126	aldehyde dehydrogenase 2 family member	Homo sapiens	16-21
21940137-9	2012	The activity of ALDH2-active phenotypes of rectal mucosa was 33% greater than ALDH2-inactive phenotypes at 200muM acetaldehyde.	Acetaldehyde	114-126	aldehyde dehydrogenase 2 family member	Homo sapiens	78-83
22159996-6	2012	The first oxidation product, acetaldehyde, played a critical role in ethanol-evoked hypertension because 1) catalase inhibition (3-aminotriazole treatment) virtually abolished the ethanol-evoked pressor response in SHRs, 2) intra-RVLM acetaldehyde (2 mug/rat) reproduced the strain-dependent hypertensive effect of intra-RVLM ethanol, and 3) ALDH inhibition (cyanamide treatment) uncovered a pressor response to intra-RVLM acetaldehyde in WKY rats similar to the response observed in SHRs.	Acetaldehyde	29-41	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	342-346
22094012-3	2012	Cultivation with glucose or ethanol as carbon substrate revealed that Adh1 was the only alcohol dehydrogenase capable of efficiently catalysing the reduction of acetaldehyde to ethanol.	Acetaldehyde	161-173	alcohol dehydrogenase ADH1	Saccharomyces cerevisiae S288C	70-74
22094012-5	2012	Growth of strains lacking the ADH1 gene resulted in the production of glycerol as a major fermentation product, concomitant with the production of a significant amount of acetaldehyde.	Acetaldehyde	171-183	alcohol dehydrogenase ADH1	Saccharomyces cerevisiae S288C	30-34
22004471-10	2012	The SNP rs1789891 is in complete linkage disequilibrium with the functional Arg272Gln variant (P = 1.24E-7, OR = 1.31) of the ADH1C gene, which has been reported to modify the rate of ethanol oxidation to acetaldehyde in vitro.	Acetaldehyde	205-217	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	126-131
23134050-6	2012	For example, certain ADH1B and ADH1C variants that are commonly found in East Asian populations lead to more rapid ethanol breakdown and acetaldehyde accumulation in the body.	Acetaldehyde	137-149	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	21-26
23134050-6	2012	For example, certain ADH1B and ADH1C variants that are commonly found in East Asian populations lead to more rapid ethanol breakdown and acetaldehyde accumulation in the body.	Acetaldehyde	137-149	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	31-36
23134050-8	2012	Likewise, an ALDH2 variant with reduced activity results in acetaldehyde buildup and also has a protective effect against alcoholism.	Acetaldehyde	60-72	aldehyde dehydrogenase 2 family member	Homo sapiens	13-18
22703173-4	2012	The most well-established genetic factors associated with alcohol dependence are in the genes encoding alcohol dehydrogenase (ADH), which oxidizes alcohol to acetaldehyde, and aldehyde dehydrogenase (ALDH2), which oxidizes acetaldehyde to acetate.	Acetaldehyde	223-235	aldehyde dehydrogenase 2 family member	Homo sapiens	200-205
22675424-1	2012	BACKGROUND: Alcohol dehydrogenase 1C (ADH1C) is the key enzyme catalyze oxidation of alcohol to acetaldehyde, which plays vital roles in the etiology of various cancer.	Acetaldehyde	96-108	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	12-36
21989637-7	2012	This reduced expression of PDC1, an enzyme which converts pyruvate to acetaldehyde, may cause low ethanol productivity in xylose medium.	Acetaldehyde	70-82	indolepyruvate decarboxylase 1	Saccharomyces cerevisiae S288C	27-31
22919469-1	2012	Catalase (EC 1.11.1.6) oxidizes ethanol to acetaldehyde within the brain and variations in catalase activity may underlie some consequences of ethanol consumption.	Acetaldehyde	43-55	catalase	Rattus norvegicus	0-8
22005600-7	2012	METHODS: CD1 male mice received acetaldehyde (0, 25, 50, 75 or 100 mg/kg) at different time intervals and were assessed in the elevated plus maze and in the dark-light box.	Acetaldehyde	32-44	CD1 antigen complex	Mus musculus	9-12
22675424-1	2012	BACKGROUND: Alcohol dehydrogenase 1C (ADH1C) is the key enzyme catalyze oxidation of alcohol to acetaldehyde, which plays vital roles in the etiology of various cancer.	Acetaldehyde	96-108	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	38-43
22563376-8	2012	Exposure to ethanol (10-40 mM) or acetaldehyde (25-200 microM) for 3 h, dose-dependently and additively increased the paracellular permeability and induced redistribution of ZO-1 and occludin without affecting cell viability or tight junction-encoding gene expression.	Acetaldehyde	34-46	tight junction protein 1	Homo sapiens	174-178
22563376-8	2012	Exposure to ethanol (10-40 mM) or acetaldehyde (25-200 microM) for 3 h, dose-dependently and additively increased the paracellular permeability and induced redistribution of ZO-1 and occludin without affecting cell viability or tight junction-encoding gene expression.	Acetaldehyde	34-46	occludin	Homo sapiens	183-191
22538484-10	2012	Mite allergen sensitization significantly increased interleukin-5 and granulocyte macrophage colony-stimulating factor, and decreased interferon-gamma levels in the airways; injecting acetaldehyde into airways with allergic inflammation significantly increased the levels of these inflammatory cytokines.	Acetaldehyde	184-196	interleukin 5	Mus musculus	52-118
22319594-0	2012	Benzo[a]pyrene, aflatoxine B1 and acetaldehyde mutational patterns in TP53 gene using a functional assay: relevance to human cancer aetiology.	Acetaldehyde	34-46	tumor protein p53	Homo sapiens	70-74
22319594-6	2012	By using a functional assay, the Functional Analysis of Separated Alleles in Yeast (FASAY), the present study depicts the mutational pattern of TP53 in normal human fibroblasts after in vitro exposure to well-known carcinogens: benzo[a]pyrene, aflatoxin B(1) and acetaldehyde.	Acetaldehyde	263-275	tumor protein p53	Homo sapiens	144-148
22538484-10	2012	Mite allergen sensitization significantly increased interleukin-5 and granulocyte macrophage colony-stimulating factor, and decreased interferon-gamma levels in the airways; injecting acetaldehyde into airways with allergic inflammation significantly increased the levels of these inflammatory cytokines.	Acetaldehyde	184-196	interferon gamma	Mus musculus	134-150
21803531-10	2011	Moreover, NTX decreased ACD-elicited ERK activation in the Acb shell and core.	Acetaldehyde	24-27	Eph receptor B1	Rattus norvegicus	37-40
21609791-3	2011	Consequently, inhibition of ALDH2 would lead to elevated levels of acetaldehyde and other reactive lipid peroxides following ethanol intake and/or exposure to toxic chemicals.	Acetaldehyde	67-79	aldehyde dehydrogenase 2 family member	Homo sapiens	28-33
21919919-4	2011	Ethanol treatment of HeLa-ADH1B cells produced a 4-fold increase in the acetaldehyde-DNA adduct and N(2)-ethylidene-dGuo and also resulted in the activation of the FA-BRCA DNA damage response network, as indicated by a monoubiquitination of FANCD2 and phosphorylation of BRCA1.	Acetaldehyde	72-84	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	26-31
21679053-1	2011	Acetaldehyde can generate modifications in several proteins, such as carbonic anhydrase (CA) II.	Acetaldehyde	0-12	carbonic anhydrase 2	Homo sapiens	69-95
21679053-3	2011	High-resolution mass spectrometric analysis indicated that acetaldehyde most efficiently formed covalent adducts with CA II and XIII.	Acetaldehyde	59-71	carbonic anhydrase 2	Homo sapiens	118-123
21679053-4	2011	The binding of up to 19 acetaldehydes in CA II is probably attributable to the high number of lysine residues (n = 24) located mainly on the surface of the enzyme molecule.	Acetaldehyde	24-37	carbonic anhydrase 2	Homo sapiens	41-46
21609791-2	2011	Among 19 ALDH isozymes, mitochondrial ALDH2 is a low Km enzyme responsible for the metabolism of acetaldehyde and lipid peroxides such as malondialdehyde and 4-hydroxynonenal, both of which are highly reactive and toxic.	Acetaldehyde	97-109	aldehyde dehydrogenase 2 family member	Homo sapiens	9-13
21609791-2	2011	Among 19 ALDH isozymes, mitochondrial ALDH2 is a low Km enzyme responsible for the metabolism of acetaldehyde and lipid peroxides such as malondialdehyde and 4-hydroxynonenal, both of which are highly reactive and toxic.	Acetaldehyde	97-109	aldehyde dehydrogenase 2 family member	Homo sapiens	38-43
21919919-2	2011	METHODS: To determine whether intracellular generation of acetaldehyde from ethanol metabolism can cause DNA damage and activate the FA-BRCA network, we engineered HeLa cells to metabolize alcohol by expression of human alcohol dehydrogenase (ADH) 1B.	Acetaldehyde	58-70	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	220-250
21919919-3	2011	RESULTS: Incubation of HeLa-ADH1B cells with ethanol (20 mM) resulted in acetaldehyde accumulation in the media, which was prevented by co-incubation with 4-methyl pyrazole (4-MP), a specific inhibitor of ADH.	Acetaldehyde	73-85	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	28-33
21988148-2	2011	A diarylprolinol silyl ether-catalyzed reaction of acetaldehyde with an imine and di-tert-butyl azodicarboxylate affords syn-2,3-diaminoalcohols with excellent ee values of up to 98%.	Acetaldehyde	51-63	synapsin II	Homo sapiens	121-126
21257642-4	2011	Accordingly, we found a metabolism of alcohol to acetaldehyde in the rat uterine horn tissue cytosolic fraction mediated by xanthine oxidoreductase, requiring a purine cosubstrate and inhibited by allopurinol.	Acetaldehyde	49-61	xanthine dehydrogenase	Rattus norvegicus	124-147
21782022-4	2011	Computational docking studies suggested that the lack of the ethanone substituent in G15 could minimize key steric conflicts, present in G-1, that limit binding within the ERalpha ligand binding pocket.	Acetaldehyde	61-69	RNA binding motif protein 5	Homo sapiens	85-88
21782022-4	2011	Computational docking studies suggested that the lack of the ethanone substituent in G15 could minimize key steric conflicts, present in G-1, that limit binding within the ERalpha ligand binding pocket.	Acetaldehyde	61-69	estrogen receptor 1	Homo sapiens	172-179
21687930-1	2011	In the present study, we examined whether Acer okamotoanum (A. okamotoanum) sap decreased the serum alcohol and acetaldehyde levels after acute ethanol treatment in a rat model.	Acetaldehyde	112-124	amyloid P component, serum	Rattus norvegicus	76-79
21687930-3	2011	Pre-treatment with the sap significantly decreased the blood ethanol and acetaldehyde concentrations after 5 h when compared with ethanol treatment alone (a negative control).	Acetaldehyde	73-85	amyloid P component, serum	Rattus norvegicus	23-26
21056952-3	2011	The aim of the present study was to investigate the influence of ethanol and its primary metabolite, acetaldehyde, on TNF-alpha and IL-6 production in a rat cortical astrocyte primary culture.	Acetaldehyde	101-113	tumor necrosis factor	Rattus norvegicus	118-127
21664374-3	2011	Findings from our group and others have revealed that the mitochondrial isoform of aldehyde dehydrogenase (ALDH2), which metabolizes acetaldehyde, governs the detoxification of acetaldehyde formed following alcohol consumption and the ultimate elimination of alcohol from the body.	Acetaldehyde	133-145	aldehyde dehydrogenase 2 family member	Homo sapiens	107-112
21664374-3	2011	Findings from our group and others have revealed that the mitochondrial isoform of aldehyde dehydrogenase (ALDH2), which metabolizes acetaldehyde, governs the detoxification of acetaldehyde formed following alcohol consumption and the ultimate elimination of alcohol from the body.	Acetaldehyde	177-189	aldehyde dehydrogenase 2 family member	Homo sapiens	107-112
21664374-6	2011	The pathophysiological effects of ALDH2 polymorphism may be mediated by accumulation of acetaldehyde and other reactive aldehydes.	Acetaldehyde	88-100	aldehyde dehydrogenase 2 family member	Homo sapiens	34-39
21056952-0	2011	Ethanol and acetaldehyde disturb TNF-alpha and IL-6 production in cultured astrocytes.	Acetaldehyde	12-24	tumor necrosis factor	Rattus norvegicus	33-42
21056952-3	2011	The aim of the present study was to investigate the influence of ethanol and its primary metabolite, acetaldehyde, on TNF-alpha and IL-6 production in a rat cortical astrocyte primary culture.	Acetaldehyde	101-113	interleukin 6	Rattus norvegicus	132-136
21056952-0	2011	Ethanol and acetaldehyde disturb TNF-alpha and IL-6 production in cultured astrocytes.	Acetaldehyde	12-24	interleukin 6	Rattus norvegicus	47-51
21056952-4	2011	We are the first to report that both ethanol and acetaldehyde can modulate TNF-alpha and IL-6 secretion from cultured astrocytes.	Acetaldehyde	49-61	tumor necrosis factor	Rattus norvegicus	75-84
21056952-4	2011	We are the first to report that both ethanol and acetaldehyde can modulate TNF-alpha and IL-6 secretion from cultured astrocytes.	Acetaldehyde	49-61	interleukin 6	Rattus norvegicus	89-93
21056952-6	2011	However, both compounds showed a biphasic, hormestic effect on the IL-6 secretion after the acute as well as the long-term exposure, and the maximum stimulation was reached for 50-mM ethanol and 1-mM acetaldehyde after 7-day exposure.	Acetaldehyde	200-212	interleukin 6	Rattus norvegicus	67-71
21056952-9	2011	In conclusion, both ethanol and acetaldehyde affect the production of IL-6 and TNF-alpha in cultured astrocytes.	Acetaldehyde	32-44	interleukin 6	Rattus norvegicus	70-74
21056952-9	2011	In conclusion, both ethanol and acetaldehyde affect the production of IL-6 and TNF-alpha in cultured astrocytes.	Acetaldehyde	32-44	tumor necrosis factor	Rattus norvegicus	79-88
21474650-0	2011	ERK is involved in EGF-mediated protection of tight junctions, but not adherens junctions, in acetaldehyde-treated Caco-2 cell monolayers.	Acetaldehyde	94-106	mitogen-activated protein kinase 1	Homo sapiens	0-3
21734703-5	2011	Our results show that the acetaldehyde-catabolising enzyme Aldh2 is essential for the development of Fancd2(-/-) embryos.	Acetaldehyde	26-38	Fanconi anemia, complementation group D2	Mus musculus	101-107
21734703-6	2011	Nevertheless, acetaldehyde-catabolism-competent mothers (Aldh2(+/-)) can support the development of double-mutant (Aldh2(-/-)Fancd2(-/-)) mice.	Acetaldehyde	14-26	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	57-62
21734703-6	2011	Nevertheless, acetaldehyde-catabolism-competent mothers (Aldh2(+/-)) can support the development of double-mutant (Aldh2(-/-)Fancd2(-/-)) mice.	Acetaldehyde	14-26	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	115-120
21734703-6	2011	Nevertheless, acetaldehyde-catabolism-competent mothers (Aldh2(+/-)) can support the development of double-mutant (Aldh2(-/-)Fancd2(-/-)) mice.	Acetaldehyde	14-26	Fanconi anemia, complementation group D2	Mus musculus	125-131
21474650-11	2011	These results indicate that EGF-mediated protection of tight junctions from acetaldehyde requires the activity of ERK1/2, but not p38 MAPK or JNK1/2, and that EGF-mediated protection of adherens junctions is independent of MAPK activities.	Acetaldehyde	76-88	epidermal growth factor	Homo sapiens	28-31
21734703-5	2011	Our results show that the acetaldehyde-catabolising enzyme Aldh2 is essential for the development of Fancd2(-/-) embryos.	Acetaldehyde	26-38	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	59-64
21474650-4	2011	Pretreatment of cell monolayers with U-0126 (inhibitor of ERK activation), but not SB-202190 and SP-600125 (p38 MAPK and JNK inhibitors), significantly attenuated EGF-mediated prevention of acetaldehyde-induced changes in resistance, inulin permeability, and redistribution of occludin and ZO-1.	Acetaldehyde	190-202	epidermal growth factor	Homo sapiens	163-166
21474650-5	2011	U-0126, but not SB-202190 and SP-600125, also attenuated EGF-mediated prevention of acetaldehyde effect on the midregion F-actin ring.	Acetaldehyde	84-96	epidermal growth factor	Homo sapiens	57-60
21474650-7	2011	Expression of wild-type or constitutively active MEK1 attenuated acetaldehyde-induced redistribution of occludin and ZO-1, whereas dominant-negative MEK1 prevented EGF-mediated preservation of occludin and ZO-1 in acetaldehyde-treated cells.	Acetaldehyde	65-77	mitogen-activated protein kinase kinase 1	Homo sapiens	49-53
21474650-7	2011	Expression of wild-type or constitutively active MEK1 attenuated acetaldehyde-induced redistribution of occludin and ZO-1, whereas dominant-negative MEK1 prevented EGF-mediated preservation of occludin and ZO-1 in acetaldehyde-treated cells.	Acetaldehyde	65-77	occludin	Homo sapiens	104-112
21474650-7	2011	Expression of wild-type or constitutively active MEK1 attenuated acetaldehyde-induced redistribution of occludin and ZO-1, whereas dominant-negative MEK1 prevented EGF-mediated preservation of occludin and ZO-1 in acetaldehyde-treated cells.	Acetaldehyde	65-77	tight junction protein 1	Homo sapiens	117-121
21474650-0	2011	ERK is involved in EGF-mediated protection of tight junctions, but not adherens junctions, in acetaldehyde-treated Caco-2 cell monolayers.	Acetaldehyde	94-106	epidermal growth factor	Homo sapiens	19-22
21474650-1	2011	The role of mitogen-activated protein kinases (MAPK) in the mechanism of EGF-mediated prevention of acetaldehyde-induced tight junction disruption was evaluated in Caco-2 cell monolayers.	Acetaldehyde	100-112	mitogen-activated protein kinase 3	Homo sapiens	47-51
21474650-7	2011	Expression of wild-type or constitutively active MEK1 attenuated acetaldehyde-induced redistribution of occludin and ZO-1, whereas dominant-negative MEK1 prevented EGF-mediated preservation of occludin and ZO-1 in acetaldehyde-treated cells.	Acetaldehyde	65-77	epidermal growth factor	Homo sapiens	164-167
21474650-1	2011	The role of mitogen-activated protein kinases (MAPK) in the mechanism of EGF-mediated prevention of acetaldehyde-induced tight junction disruption was evaluated in Caco-2 cell monolayers.	Acetaldehyde	100-112	epidermal growth factor	Homo sapiens	73-76
21474650-7	2011	Expression of wild-type or constitutively active MEK1 attenuated acetaldehyde-induced redistribution of occludin and ZO-1, whereas dominant-negative MEK1 prevented EGF-mediated preservation of occludin and ZO-1 in acetaldehyde-treated cells.	Acetaldehyde	65-77	occludin	Homo sapiens	193-201
21474650-7	2011	Expression of wild-type or constitutively active MEK1 attenuated acetaldehyde-induced redistribution of occludin and ZO-1, whereas dominant-negative MEK1 prevented EGF-mediated preservation of occludin and ZO-1 in acetaldehyde-treated cells.	Acetaldehyde	65-77	tight junction protein 1	Homo sapiens	206-210
21474650-2	2011	Pretreatment of cell monolayers with EGF attenuated acetaldehyde-induced decrease in resistance and increase in inulin permeability and redistribution of occludin, zona occludens-1 (ZO-1), E-cadherin, and beta-catenin from the intercellular junctions.	Acetaldehyde	52-64	epidermal growth factor	Homo sapiens	37-40
21474650-7	2011	Expression of wild-type or constitutively active MEK1 attenuated acetaldehyde-induced redistribution of occludin and ZO-1, whereas dominant-negative MEK1 prevented EGF-mediated preservation of occludin and ZO-1 in acetaldehyde-treated cells.	Acetaldehyde	214-226	mitogen-activated protein kinase kinase 1	Homo sapiens	49-53
21474650-2	2011	Pretreatment of cell monolayers with EGF attenuated acetaldehyde-induced decrease in resistance and increase in inulin permeability and redistribution of occludin, zona occludens-1 (ZO-1), E-cadherin, and beta-catenin from the intercellular junctions.	Acetaldehyde	52-64	tight junction protein 1	Homo sapiens	182-186
21474650-7	2011	Expression of wild-type or constitutively active MEK1 attenuated acetaldehyde-induced redistribution of occludin and ZO-1, whereas dominant-negative MEK1 prevented EGF-mediated preservation of occludin and ZO-1 in acetaldehyde-treated cells.	Acetaldehyde	214-226	epidermal growth factor	Homo sapiens	164-167
21474650-9	2011	Furthermore, EGF attenuated acetaldehyde-induced tyrosine-phosphorylation of occludin, ZO-1, claudin-3, and E-cadherin.	Acetaldehyde	28-40	epidermal growth factor	Homo sapiens	13-16
21474650-2	2011	Pretreatment of cell monolayers with EGF attenuated acetaldehyde-induced decrease in resistance and increase in inulin permeability and redistribution of occludin, zona occludens-1 (ZO-1), E-cadherin, and beta-catenin from the intercellular junctions.	Acetaldehyde	52-64	cadherin 1	Homo sapiens	189-199
21474650-9	2011	Furthermore, EGF attenuated acetaldehyde-induced tyrosine-phosphorylation of occludin, ZO-1, claudin-3, and E-cadherin.	Acetaldehyde	28-40	occludin	Homo sapiens	77-85
21474650-2	2011	Pretreatment of cell monolayers with EGF attenuated acetaldehyde-induced decrease in resistance and increase in inulin permeability and redistribution of occludin, zona occludens-1 (ZO-1), E-cadherin, and beta-catenin from the intercellular junctions.	Acetaldehyde	52-64	catenin beta 1	Homo sapiens	205-217
21474650-9	2011	Furthermore, EGF attenuated acetaldehyde-induced tyrosine-phosphorylation of occludin, ZO-1, claudin-3, and E-cadherin.	Acetaldehyde	28-40	tight junction protein 1	Homo sapiens	87-91
21474650-9	2011	Furthermore, EGF attenuated acetaldehyde-induced tyrosine-phosphorylation of occludin, ZO-1, claudin-3, and E-cadherin.	Acetaldehyde	28-40	claudin 3	Homo sapiens	93-102
21861333-9	2011	The concentrations of blood acetaldehyde in ALDH2*1/*2 type were higher in prandial condition than in fasted condition with shochu.	Acetaldehyde	28-40	aldehyde dehydrogenase 2 family member	Homo sapiens	44-49
21474650-9	2011	Furthermore, EGF attenuated acetaldehyde-induced tyrosine-phosphorylation of occludin, ZO-1, claudin-3, and E-cadherin.	Acetaldehyde	28-40	cadherin 1	Homo sapiens	108-118
21294755-9	2011	However, combined treatment of leptin with acetaldehyde synergistically enhanced the protein expression of smooth muscle actin (alphaSMA), an activation marker of HSCs, and of Interleukin-6 (IL-6).	Acetaldehyde	43-55	interleukin 6	Rattus norvegicus	191-195
21294755-10	2011	The combination of leptin and acetaldehyde also augmented MAPK/p38 and MAPK/ERK1/2 phosphoprotein expression.	Acetaldehyde	30-42	mitogen activated protein kinase 14	Rattus norvegicus	63-66
21284671-0	2011	Acetaldehyde burst protection of ADH1B*2 against alcoholism: an additional hormesis protection against esophageal cancers following alcohol consumption?	Acetaldehyde	0-12	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	33-38
21284671-1	2011	This account of recent work presented at the 4th International Symposium on Alcohol Pancreatitis and Cirrhosis reports animal studies aimed at determining the role of the "acetaldehyde burst," generated shortly upon ethanol intake, as the mechanism of protection against alcoholism conferred by the ADH1B*2 polymorphism.	Acetaldehyde	172-184	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	299-304
21284671-2	2011	Literature studies discussed suggest an additional role of the acetaldehyde burst on the paradoxical (hormesis) protection of the ADH1B*2 polymorphism against esophageal cancers in alcoholics.	Acetaldehyde	63-75	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	130-135
21294755-10	2011	The combination of leptin and acetaldehyde also augmented MAPK/p38 and MAPK/ERK1/2 phosphoprotein expression.	Acetaldehyde	30-42	mitogen activated protein kinase 3	Rattus norvegicus	76-82
21294755-0	2011	Leptin and acetaldehyde synergistically promotes alphaSMA expression in hepatic stellate cells by an interleukin 6-dependent mechanism.	Acetaldehyde	11-23	interleukin 6	Rattus norvegicus	101-114
21294755-14	2011	CONCLUSIONS: We conclude that leptin potentiates acetaldehyde-induced HSC activation and alphaSMA expression by an IL-6-dependent mechanism.	Acetaldehyde	49-61	leptin	Rattus norvegicus	30-36
21294755-9	2011	However, combined treatment of leptin with acetaldehyde synergistically enhanced the protein expression of smooth muscle actin (alphaSMA), an activation marker of HSCs, and of Interleukin-6 (IL-6).	Acetaldehyde	43-55	interleukin 6	Rattus norvegicus	176-189
21294755-14	2011	CONCLUSIONS: We conclude that leptin potentiates acetaldehyde-induced HSC activation and alphaSMA expression by an IL-6-dependent mechanism.	Acetaldehyde	49-61	interleukin 6	Rattus norvegicus	115-119
21294757-7	2011	This was not observed in hepatocytes from AQP9 knockout mice, nor observed by direct application of acetaldehyde to AQP9 expressed in Xenopus Laevis oocytes.	Acetaldehyde	100-112	aquaporin 9	Mus musculus	116-120
21294757-9	2011	Acetaldehyde decreased AQP9 mRNA and AQP9 protein, while ethanol decreased AQP9 mRNA but not AQP9 protein.	Acetaldehyde	0-12	aquaporin 9	Rattus norvegicus	23-27
21294757-9	2011	Acetaldehyde decreased AQP9 mRNA and AQP9 protein, while ethanol decreased AQP9 mRNA but not AQP9 protein.	Acetaldehyde	0-12	aquaporin 9	Rattus norvegicus	37-41
21294757-9	2011	Acetaldehyde decreased AQP9 mRNA and AQP9 protein, while ethanol decreased AQP9 mRNA but not AQP9 protein.	Acetaldehyde	0-12	aquaporin 9	Rattus norvegicus	37-41
21294757-9	2011	Acetaldehyde decreased AQP9 mRNA and AQP9 protein, while ethanol decreased AQP9 mRNA but not AQP9 protein.	Acetaldehyde	0-12	aquaporin 9	Rattus norvegicus	37-41
21294757-11	2011	CONCLUSIONS: The acute effects of acetaldehyde, while mediated by AQP9, are probably influenced by binding of acetaldehyde to hepatocyte membranes and changes in cell permeability.	Acetaldehyde	34-46	aquaporin 9	Rattus norvegicus	66-70
21360751-2	2011	Adh1p is responsible for the reduction of acetaldehyde to ethanol, while Adh2p catalyses the reverse reaction, the oxidation of ethanol to acetaldehyde.	Acetaldehyde	42-54	alcohol dehydrogenase ADH1	Saccharomyces cerevisiae S288C	0-5
21360751-2	2011	Adh1p is responsible for the reduction of acetaldehyde to ethanol, while Adh2p catalyses the reverse reaction, the oxidation of ethanol to acetaldehyde.	Acetaldehyde	139-151	alcohol dehydrogenase ADH1	Saccharomyces cerevisiae S288C	0-5
21360751-2	2011	Adh1p is responsible for the reduction of acetaldehyde to ethanol, while Adh2p catalyses the reverse reaction, the oxidation of ethanol to acetaldehyde.	Acetaldehyde	139-151	alcohol dehydrogenase ADH2	Saccharomyces cerevisiae S288C	73-78
21360751-3	2011	Lack of Adh1p shifts the cellular redox balance towards excess NADH/NADPH and acetaldehyde, while absence of Adh2p does the opposite.	Acetaldehyde	78-90	alcohol dehydrogenase ADH1	Saccharomyces cerevisiae S288C	8-13
21352247-4	2011	This is accomplished by manipulating the brain levels of acetaldehyde produced from ethanol by the injection of lentivirus containing either an anti-catalase shRNA construct or a rat liver alcohol dehydrogenase into the central nervous system and observing the effects on alcohol preference by high ethanol-consuming rats.	Acetaldehyde	57-69	aldo-keto reductase family 1 member A1	Rattus norvegicus	189-210
21320498-0	2011	Modification of mouse A2M B (620-792) and A2M N (168-230) by malondialdehyde and acetaldehyde attenuates the proteinase and TGF-beta1 binding ability of A2MB.	Acetaldehyde	81-93	transforming growth factor, beta 1	Mus musculus	124-133
21106935-9	2011	A link has been observed between gene expression alterations and selective epigenetic modulation in the prodynorphin promoter region, demonstrating a specificity of the changes induced by ethanol and acetaldehyde.	Acetaldehyde	200-212	prodynorphin	Homo sapiens	104-116
21106935-0	2011	Ethanol and acetaldehyde exposure induces specific epigenetic modifications in the prodynorphin gene promoter in a human neuroblastoma cell line.	Acetaldehyde	12-24	prodynorphin	Homo sapiens	83-95
21083667-1	2011	BACKGROUND: Ethanol is metabolized by 2 rate-limiting reactions: alcohol dehydrogenases (ADH) convert ethanol to acetaldehyde that is subsequently metabolized to acetate by aldehyde dehydrogenases (ALDH).	Acetaldehyde	113-125	alcohol dehydrogenase 1A (class I), alpha polypeptide	Homo sapiens	89-92
21216231-5	2011	ALDH1B1 is a mitochondrial ALDH that metabolizes a wide range of aldehyde substrates including acetaldehyde and products of lipid peroxidation (LPO).	Acetaldehyde	95-107	aldehyde dehydrogenase 1 family member B1	Homo sapiens	0-7
21216231-5	2011	ALDH1B1 is a mitochondrial ALDH that metabolizes a wide range of aldehyde substrates including acetaldehyde and products of lipid peroxidation (LPO).	Acetaldehyde	95-107	aldehyde dehydrogenase 1 family member A1	Homo sapiens	0-4
21083667-1	2011	BACKGROUND: Ethanol is metabolized by 2 rate-limiting reactions: alcohol dehydrogenases (ADH) convert ethanol to acetaldehyde that is subsequently metabolized to acetate by aldehyde dehydrogenases (ALDH).	Acetaldehyde	113-125	aldehyde dehydrogenase 1 family member A1	Homo sapiens	198-202
22320964-2	2011	Individuals homozygous for the *2 variant allele of aldehyde dehydrogenase 2 (ALDH2) are unable to metabolize acetaldehyde, which prevents them from alcohol drinking, whereas those with *1/*2 have a 6-fold higher blood acetaldehyde concentration postalcohol consumption with respect to *1*1.	Acetaldehyde	110-122	aldehyde dehydrogenase 2 family member	Homo sapiens	52-76
21211027-7	2011	In general, the highest salivary acetaldehyde concentration was found in all cases in the saliva 30 sec after using the beverages (average 353 muM).	Acetaldehyde	33-45	latexin	Homo sapiens	143-146
21166830-0	2011	Ethanol metabolism by HeLa cells transduced with human alcohol dehydrogenase isoenzymes: control of the pathway by acetaldehyde concentration.	Acetaldehyde	115-127	aldo-keto reductase family 1 member A1	Homo sapiens	55-76
21166830-7	2011	This was not explained by high cellular NADH levels or endogenous inhibitors; but rather because the activity of the beta1 and beta2 ADHs was constrained by the accumulation of acetaldehyde, as shown by the increased rate of ethanol oxidation by cell lines expressing beta2 ADH plus ALDH2.	Acetaldehyde	177-189	potassium calcium-activated channel subfamily M regulatory beta subunit 1	Homo sapiens	117-122
21166830-7	2011	This was not explained by high cellular NADH levels or endogenous inhibitors; but rather because the activity of the beta1 and beta2 ADHs was constrained by the accumulation of acetaldehyde, as shown by the increased rate of ethanol oxidation by cell lines expressing beta2 ADH plus ALDH2.	Acetaldehyde	177-189	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	127-132
21166830-8	2011	CONCLUSION: The activity of the human beta2 ADH isoenzyme is sensitive to inhibition by acetaldehyde, which likely limits its activity in vivo.	Acetaldehyde	88-100	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	38-43
21166830-8	2011	CONCLUSION: The activity of the human beta2 ADH isoenzyme is sensitive to inhibition by acetaldehyde, which likely limits its activity in vivo.	Acetaldehyde	88-100	alcohol dehydrogenase 1C (class I), gamma polypeptide	Rattus norvegicus	44-47
22292652-1	2011	AIM: Alcohol dehydrogenase-IB (ADH1B) and aldehyde dehydrogenase-2 (ALDH2) are the key enzymes for elimination of ethanol and acetaldehyde, the latter being an established animal carcinogen produced after drinking.	Acetaldehyde	126-138	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	31-36
22292652-1	2011	AIM: Alcohol dehydrogenase-IB (ADH1B) and aldehyde dehydrogenase-2 (ALDH2) are the key enzymes for elimination of ethanol and acetaldehyde, the latter being an established animal carcinogen produced after drinking.	Acetaldehyde	126-138	aldehyde dehydrogenase 2 family member	Homo sapiens	42-66
22292652-1	2011	AIM: Alcohol dehydrogenase-IB (ADH1B) and aldehyde dehydrogenase-2 (ALDH2) are the key enzymes for elimination of ethanol and acetaldehyde, the latter being an established animal carcinogen produced after drinking.	Acetaldehyde	126-138	aldehyde dehydrogenase 2 family member	Homo sapiens	68-73
22320964-2	2011	Individuals homozygous for the *2 variant allele of aldehyde dehydrogenase 2 (ALDH2) are unable to metabolize acetaldehyde, which prevents them from alcohol drinking, whereas those with *1/*2 have a 6-fold higher blood acetaldehyde concentration postalcohol consumption with respect to *1*1.	Acetaldehyde	110-122	aldehyde dehydrogenase 2 family member	Homo sapiens	78-83
22320964-2	2011	Individuals homozygous for the *2 variant allele of aldehyde dehydrogenase 2 (ALDH2) are unable to metabolize acetaldehyde, which prevents them from alcohol drinking, whereas those with *1/*2 have a 6-fold higher blood acetaldehyde concentration postalcohol consumption with respect to *1*1.	Acetaldehyde	219-231	aldehyde dehydrogenase 2 family member	Homo sapiens	52-76
22320964-2	2011	Individuals homozygous for the *2 variant allele of aldehyde dehydrogenase 2 (ALDH2) are unable to metabolize acetaldehyde, which prevents them from alcohol drinking, whereas those with *1/*2 have a 6-fold higher blood acetaldehyde concentration postalcohol consumption with respect to *1*1.	Acetaldehyde	219-231	aldehyde dehydrogenase 2 family member	Homo sapiens	78-83
22180353-10	2011	Butein also inhibited acetaldehyde-induced TGF-beta1 production.	Acetaldehyde	22-34	transforming growth factor, beta 1	Rattus norvegicus	43-52
20847004-0	2011	Acetaldehyde/alcohol dehydrogenase-2 (EhADH2) and clathrin are involved in internalization of human transferrin by Entamoeba histolytica.	Acetaldehyde	0-12	transferrin	Homo sapiens	100-111
21863215-8	2011	In vitro, acetaldehyde, H2O2, as well as 2-AG and THC, alone or in combination with acetaldehyde, induced CB1 mRNA expression, whereas CB1 blockage with SR141716 dose-dependently inhibited HSC proliferation and downregulated mRNA expression of fibrosis-mediated genes PCalpha1(I), TIMP-1 and MMP-13.	Acetaldehyde	10-22	cannabinoid receptor 1	Homo sapiens	106-109
21863215-8	2011	In vitro, acetaldehyde, H2O2, as well as 2-AG and THC, alone or in combination with acetaldehyde, induced CB1 mRNA expression, whereas CB1 blockage with SR141716 dose-dependently inhibited HSC proliferation and downregulated mRNA expression of fibrosis-mediated genes PCalpha1(I), TIMP-1 and MMP-13.	Acetaldehyde	10-22	cannabinoid receptor 1	Homo sapiens	135-138
21863215-8	2011	In vitro, acetaldehyde, H2O2, as well as 2-AG and THC, alone or in combination with acetaldehyde, induced CB1 mRNA expression, whereas CB1 blockage with SR141716 dose-dependently inhibited HSC proliferation and downregulated mRNA expression of fibrosis-mediated genes PCalpha1(I), TIMP-1 and MMP-13.	Acetaldehyde	10-22	TIMP metallopeptidase inhibitor 1	Homo sapiens	281-287
21863215-8	2011	In vitro, acetaldehyde, H2O2, as well as 2-AG and THC, alone or in combination with acetaldehyde, induced CB1 mRNA expression, whereas CB1 blockage with SR141716 dose-dependently inhibited HSC proliferation and downregulated mRNA expression of fibrosis-mediated genes PCalpha1(I), TIMP-1 and MMP-13.	Acetaldehyde	10-22	matrix metallopeptidase 13	Homo sapiens	292-298
21863215-8	2011	In vitro, acetaldehyde, H2O2, as well as 2-AG and THC, alone or in combination with acetaldehyde, induced CB1 mRNA expression, whereas CB1 blockage with SR141716 dose-dependently inhibited HSC proliferation and downregulated mRNA expression of fibrosis-mediated genes PCalpha1(I), TIMP-1 and MMP-13.	Acetaldehyde	84-96	cannabinoid receptor 1	Homo sapiens	106-109
21863215-8	2011	In vitro, acetaldehyde, H2O2, as well as 2-AG and THC, alone or in combination with acetaldehyde, induced CB1 mRNA expression, whereas CB1 blockage with SR141716 dose-dependently inhibited HSC proliferation and downregulated mRNA expression of fibrosis-mediated genes PCalpha1(I), TIMP-1 and MMP-13.	Acetaldehyde	84-96	TIMP metallopeptidase inhibitor 1	Homo sapiens	281-287
21863215-8	2011	In vitro, acetaldehyde, H2O2, as well as 2-AG and THC, alone or in combination with acetaldehyde, induced CB1 mRNA expression, whereas CB1 blockage with SR141716 dose-dependently inhibited HSC proliferation and downregulated mRNA expression of fibrosis-mediated genes PCalpha1(I), TIMP-1 and MMP-13.	Acetaldehyde	84-96	matrix metallopeptidase 13	Homo sapiens	292-298
21863215-11	2011	In conclusion, CB1 expression is upregulated in human ALF, which is at least in part triggered by acetaldehyde (AA) and oxidative stress.	Acetaldehyde	98-110	cannabinoid receptor 1	Homo sapiens	15-18
22180353-11	2011	Butein, betulin, and betulinic acid down-regulated acetaldehyde-induced production of TIMP-1 and TIMP-2.	Acetaldehyde	51-63	TIMP metallopeptidase inhibitor 1	Rattus norvegicus	86-92
22180353-11	2011	Butein, betulin, and betulinic acid down-regulated acetaldehyde-induced production of TIMP-1 and TIMP-2.	Acetaldehyde	51-63	TIMP metallopeptidase inhibitor 2	Rattus norvegicus	97-103
22180353-12	2011	Betulin decreased the acetaldehyde-induced activity of MMP-2, but butein and betulinic acid did not.	Acetaldehyde	22-34	matrix metallopeptidase 2	Rattus norvegicus	55-60
21687683-0	2011	Down regulation of a matrix degrading cysteine protease cathepsin L, by acetaldehyde: role of C/EBPalpha.	Acetaldehyde	72-84	cathepsin L	Homo sapiens	56-67
21687683-2	2011	This study was carried out to investigate the effect of acetaldehyde on expression of an extra cellular matrix degrading protease cathepsin L (CTSL) in HepG2 cells.	Acetaldehyde	56-68	cathepsin L	Homo sapiens	130-141
21687683-2	2011	This study was carried out to investigate the effect of acetaldehyde on expression of an extra cellular matrix degrading protease cathepsin L (CTSL) in HepG2 cells.	Acetaldehyde	56-68	cathepsin L	Homo sapiens	143-147
21687683-3	2011	METHODOLOGY AND RESULTS: We measured the enzymatic activity, protein and, mRNA levels of CTSL in acetaldehyde treated and untreated cells.	Acetaldehyde	97-109	cathepsin L	Homo sapiens	89-93
21687683-4	2011	The binding of CAAT enhancer binding protein alpha (C/EBP alpha) to CTSL promoter and its key role in the transcription from this promoter and conferring responsiveness to acetaldehyde was established by site directed mutagenesis, electrophoretic mobility shift assay (EMSA), chromatin immunoprecipitation (ChIP) assays and siRNA technology.	Acetaldehyde	172-184	CCAAT enhancer binding protein alpha	Homo sapiens	52-63
21687683-4	2011	The binding of CAAT enhancer binding protein alpha (C/EBP alpha) to CTSL promoter and its key role in the transcription from this promoter and conferring responsiveness to acetaldehyde was established by site directed mutagenesis, electrophoretic mobility shift assay (EMSA), chromatin immunoprecipitation (ChIP) assays and siRNA technology.	Acetaldehyde	172-184	cathepsin L	Homo sapiens	68-72
21687683-5	2011	Acetaldehyde treatment significantly decreased CTSL activity and protein levels in HepG2 cells.	Acetaldehyde	0-12	cathepsin L	Homo sapiens	47-51
21687683-7	2011	This decrease by acetaldehyde was attributed to the fall in the liver enriched transcription factor C/EBP alpha levels and it"s binding to the CTSL promoter.	Acetaldehyde	17-29	CCAAT enhancer binding protein alpha	Homo sapiens	100-111
21687683-7	2011	This decrease by acetaldehyde was attributed to the fall in the liver enriched transcription factor C/EBP alpha levels and it"s binding to the CTSL promoter.	Acetaldehyde	17-29	cathepsin L	Homo sapiens	143-147
21687683-8	2011	Mutagenesis of C/EBP alpha binding motifs revealed the key role of this factor in CTSL transcription as well as conferring responsiveness to acetaldehyde.	Acetaldehyde	141-153	CCAAT enhancer binding protein alpha	Homo sapiens	15-26
21687683-9	2011	The siRNA mediated silencing of the C/EBP alpha expression mimicked the effect of acetaldehyde on CTSL levels and its promoter activity.	Acetaldehyde	82-94	CCAAT enhancer binding protein alpha	Homo sapiens	36-47
21687683-9	2011	The siRNA mediated silencing of the C/EBP alpha expression mimicked the effect of acetaldehyde on CTSL levels and its promoter activity.	Acetaldehyde	82-94	cathepsin L	Homo sapiens	98-102
21687683-11	2011	CONCLUSION: Acetaldehyde down regulates the C/EBP alpha mediated CTSL expression in hepatic cell lines.	Acetaldehyde	12-24	CCAAT enhancer binding protein alpha	Homo sapiens	44-55
21687683-11	2011	CONCLUSION: Acetaldehyde down regulates the C/EBP alpha mediated CTSL expression in hepatic cell lines.	Acetaldehyde	12-24	cathepsin L	Homo sapiens	65-69
20924567-5	2010	Molecular specificity of the SERS technique was studied by comparing the SERS spectrum of TBA-MDA with those acquired with TBA adducts of other TBA-reactive compounds (TBARCs) that includes formaldehyde, acetaldehyde, butyraldehyde, trans-2-hexenal, and pyrimidine.	Acetaldehyde	204-216	seryl-tRNA synthetase 2, mitochondrial	Homo sapiens	29-33
20813101-2	2010	Ingested ethanol is mainly oxidized by the enzymes alcohol dehydrogenase (ADH), cytochrome P-450 2E1 (CYP2E1), and catalase to form acetaldehyde, which is subsequently oxidized by aldehyde dehydrogenase 2 (ALDH2) to produce acetate.	Acetaldehyde	132-144	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	74-77
20813101-2	2010	Ingested ethanol is mainly oxidized by the enzymes alcohol dehydrogenase (ADH), cytochrome P-450 2E1 (CYP2E1), and catalase to form acetaldehyde, which is subsequently oxidized by aldehyde dehydrogenase 2 (ALDH2) to produce acetate.	Acetaldehyde	132-144	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	80-100
20813101-2	2010	Ingested ethanol is mainly oxidized by the enzymes alcohol dehydrogenase (ADH), cytochrome P-450 2E1 (CYP2E1), and catalase to form acetaldehyde, which is subsequently oxidized by aldehyde dehydrogenase 2 (ALDH2) to produce acetate.	Acetaldehyde	132-144	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	102-108
20813101-2	2010	Ingested ethanol is mainly oxidized by the enzymes alcohol dehydrogenase (ADH), cytochrome P-450 2E1 (CYP2E1), and catalase to form acetaldehyde, which is subsequently oxidized by aldehyde dehydrogenase 2 (ALDH2) to produce acetate.	Acetaldehyde	132-144	catalase	Homo sapiens	115-123
20813101-2	2010	Ingested ethanol is mainly oxidized by the enzymes alcohol dehydrogenase (ADH), cytochrome P-450 2E1 (CYP2E1), and catalase to form acetaldehyde, which is subsequently oxidized by aldehyde dehydrogenase 2 (ALDH2) to produce acetate.	Acetaldehyde	132-144	aldehyde dehydrogenase 2 family member	Homo sapiens	180-204
20813101-2	2010	Ingested ethanol is mainly oxidized by the enzymes alcohol dehydrogenase (ADH), cytochrome P-450 2E1 (CYP2E1), and catalase to form acetaldehyde, which is subsequently oxidized by aldehyde dehydrogenase 2 (ALDH2) to produce acetate.	Acetaldehyde	132-144	aldehyde dehydrogenase 2 family member	Homo sapiens	206-211
20506324-0	2010	Acetaldehyde elicits ERK phosphorylation in the rat nucleus accumbens and extended amygdala.	Acetaldehyde	0-12	Eph receptor B1	Rattus norvegicus	21-24
20506324-3	2010	The aim of this study was to determine whether acetaldehyde and ethanol-derived acetaldehyde elicit the activation of ERK in the nucleus accumbens and extended amygdala.	Acetaldehyde	47-59	Eph receptor B1	Rattus norvegicus	118-121
20506324-3	2010	The aim of this study was to determine whether acetaldehyde and ethanol-derived acetaldehyde elicit the activation of ERK in the nucleus accumbens and extended amygdala.	Acetaldehyde	80-92	Eph receptor B1	Rattus norvegicus	118-121
20506324-7	2010	Inhibition of ethanol metabolism and sequestration of newly synthesized acetaldehyde completely prevented ERK activation by ethanol.	Acetaldehyde	72-84	Eph receptor B1	Rattus norvegicus	106-109
20506324-8	2010	In addition, to establish the role of D(1) receptors stimulation in acetaldehyde-elicited ERK phosphorylation, we studied the effect of the D(1) receptor antagonist, SCH 39166.	Acetaldehyde	68-80	Eph receptor B1	Rattus norvegicus	90-93
20506324-9	2010	Pretreatment with the D(1) receptor antagonist (50 mug/kg) fully prevented acetaldehyde-elicited ERK activation.	Acetaldehyde	75-87	Eph receptor B1	Rattus norvegicus	97-100
20506324-10	2010	Overall, these results indicate that ethanol activates ERK by means of its metabolic conversion into acetaldehyde and strengthen the view that acetaldehyde is a centrally acting compound with a pharmacological profile similar to ethanol.	Acetaldehyde	101-113	Eph receptor B1	Rattus norvegicus	55-58
20506324-10	2010	Overall, these results indicate that ethanol activates ERK by means of its metabolic conversion into acetaldehyde and strengthen the view that acetaldehyde is a centrally acting compound with a pharmacological profile similar to ethanol.	Acetaldehyde	143-155	Eph receptor B1	Rattus norvegicus	55-58
20598738-5	2010	An overall good correlation between acetaldehyde (C(2)) and propanal (C(3)) indicates the contribution of vehicular emission to the carbonyl budget.	Acetaldehyde	36-48	complement C2	Homo sapiens	50-54
20616185-2	2010	Clearance of acetaldehyde is achieved by its oxidation, primarily catalyzed by the mitochondrial class II aldehyde dehydrogenase (ALDH2).	Acetaldehyde	13-25	aldehyde dehydrogenase 2 family member	Homo sapiens	130-135
20616185-10	2010	Most importantly, human ALDH1B1 exhibited an apparent K(m) of 55 muM for acetaldehyde, making it the second low K(m) ALDH for metabolism of this substrate.	Acetaldehyde	73-85	aldehyde dehydrogenase 1 family member B1	Homo sapiens	24-31
20668055-8	2010	Substance P, norepinephrine, and renin were also released by acetaldehyde, a known product of ischemia/reperfusion, from cardiac synaptosomes and cultured mast cells, respectively.	Acetaldehyde	61-73	tachykinin precursor 1	Homo sapiens	0-11
20668055-8	2010	Substance P, norepinephrine, and renin were also released by acetaldehyde, a known product of ischemia/reperfusion, from cardiac synaptosomes and cultured mast cells, respectively.	Acetaldehyde	61-73	renin	Homo sapiens	33-38
20350778-2	2010	We wanted to determine if ADH polymorphisms which modify the rate of ethanol oxidation to acetaldehyde, were associated with breast cancer risk.	Acetaldehyde	90-102	alcohol dehydrogenase 1A (class I), alpha polypeptide	Homo sapiens	26-29
20935489-1	2010	The mitochondrial isoform of aldehyde dehydrogenase (ALDH2) plays a key role in the metabolism of acetaldehyde and other toxic aldehydes.	Acetaldehyde	98-110	aldehyde dehydrogenase 2 family member	Homo sapiens	53-58
20736996-1	2010	The antialcoholism medication disulfiram (Antabuse) inhibits aldehyde dehydrogenase (ALDH), which results in the accumulation of acetaldehyde upon ethanol ingestion and produces the aversive "Antabuse reaction" that deters alcohol consumption.	Acetaldehyde	129-141	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	61-83
20736996-1	2010	The antialcoholism medication disulfiram (Antabuse) inhibits aldehyde dehydrogenase (ALDH), which results in the accumulation of acetaldehyde upon ethanol ingestion and produces the aversive "Antabuse reaction" that deters alcohol consumption.	Acetaldehyde	129-141	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	85-89
20521872-11	2010	CONCLUSION: Microbial production of carcinogen acetaldehyde in the presence of gastric hypochlorhydria is most probably involved in the mechanism of ALDH2-related susceptibility to ESCC.	Acetaldehyde	47-59	aldehyde dehydrogenase 2 family member	Homo sapiens	149-154
20806246-0	2010	Transcription factor Stb5p is essential for acetaldehyde tolerance in Saccharomyces cerevisiae.	Acetaldehyde	44-56	Stb5p	Saccharomyces cerevisiae S288C	21-26
20806246-1	2010	Transcription factor Stb5p, previously known as one of the multidrug resistance gene regulators in Saccharomyces cerevisiae, was shown here to play an essential role in acetaldehyde tolerance.	Acetaldehyde	169-181	Stb5p	Saccharomyces cerevisiae S288C	21-26
20806246-3	2010	Using this strain it was revealed that Stb5p acts as a repressor for PGI1 encoding glucose-6-phosphate isomerase under acetaldehyde stress.	Acetaldehyde	119-131	Stb5p	Saccharomyces cerevisiae S288C	39-44
20806246-3	2010	Using this strain it was revealed that Stb5p acts as a repressor for PGI1 encoding glucose-6-phosphate isomerase under acetaldehyde stress.	Acetaldehyde	119-131	glucose-6-phosphate isomerase	Saccharomyces cerevisiae S288C	83-112
20806246-4	2010	In reverse, over-expression of Stb5p reinforced acetaldehyde tolerance to the yeast.	Acetaldehyde	48-60	Stb5p	Saccharomyces cerevisiae S288C	31-36
20806246-6	2010	From these results, it was suggested that Stb5p participates in acetaldehyde tolerance by regulating expression of the PPP genes and PGI1, and that down-regulation of glycolytic pathway may lead to vitalization of PPP and to increased acetaldehyde tolerance.	Acetaldehyde	64-76	Stb5p	Saccharomyces cerevisiae S288C	42-47
20806246-6	2010	From these results, it was suggested that Stb5p participates in acetaldehyde tolerance by regulating expression of the PPP genes and PGI1, and that down-regulation of glycolytic pathway may lead to vitalization of PPP and to increased acetaldehyde tolerance.	Acetaldehyde	235-247	Stb5p	Saccharomyces cerevisiae S288C	42-47
20724102-1	2010	Alcohol dehydrogenase (ADH) catalyzes oxidation of ingested ethanol to acetaldehyde, the first step in hepatic metabolism.	Acetaldehyde	71-83	aldo-keto reductase family 1 member A1	Rattus norvegicus	0-21
20724102-1	2010	Alcohol dehydrogenase (ADH) catalyzes oxidation of ingested ethanol to acetaldehyde, the first step in hepatic metabolism.	Acetaldehyde	71-83	aldo-keto reductase family 1 member A1	Rattus norvegicus	23-26
20598484-1	2010	The most well-known metabolic pathways from ethanol to acetaldehyde include alcohol dehydrogenase (ADH) and the microsomal ethanol oxidizing system that involves cytochrome P450 2E1 (CYP2E1).	Acetaldehyde	55-67	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	99-102
20598484-1	2010	The most well-known metabolic pathways from ethanol to acetaldehyde include alcohol dehydrogenase (ADH) and the microsomal ethanol oxidizing system that involves cytochrome P450 2E1 (CYP2E1).	Acetaldehyde	55-67	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	162-181
20598484-1	2010	The most well-known metabolic pathways from ethanol to acetaldehyde include alcohol dehydrogenase (ADH) and the microsomal ethanol oxidizing system that involves cytochrome P450 2E1 (CYP2E1).	Acetaldehyde	55-67	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	183-189
20362583-6	2010	ALDH2 KO accentuated ethanol-induced elevation in cardiac acetaldehyde levels.	Acetaldehyde	58-70	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	0-5
20374217-4	2010	A highly active ADH protects against alcoholism, an effect related to a presteady state burst in arterial acetaldehyde.	Acetaldehyde	106-118	aldo-keto reductase family 1 member A1	Homo sapiens	16-19
20477767-6	2010	High blood acetaldehyde levels were found even in the active ALDH2*1/*1 alcoholics, which were comparable with the levels of the inactive heterozygous ALDH2*1/*2 alcoholics with less active ADH1B*1/*1.	Acetaldehyde	11-23	aldehyde dehydrogenase 2 family member	Homo sapiens	61-66
20477767-6	2010	High blood acetaldehyde levels were found even in the active ALDH2*1/*1 alcoholics, which were comparable with the levels of the inactive heterozygous ALDH2*1/*2 alcoholics with less active ADH1B*1/*1.	Acetaldehyde	11-23	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	190-195
20477767-7	2010	The slope of the increase in blood acetaldehyde level as the blood ethanol level increased was significantly steeper in alcoholics with inactive heterozygous ALDH2*1/*2 plus ADH1B*2 allele than with any other genotype combinations, but the slopes of the increase in salivary acetaldehyde level as the salivary ethanol level increased did not differ between the groups of subjects with any combinations of ALDH2 and ADH1B genotypes.	Acetaldehyde	35-47	aldehyde dehydrogenase 2 family member	Homo sapiens	158-163
20477767-7	2010	The slope of the increase in blood acetaldehyde level as the blood ethanol level increased was significantly steeper in alcoholics with inactive heterozygous ALDH2*1/*2 plus ADH1B*2 allele than with any other genotype combinations, but the slopes of the increase in salivary acetaldehyde level as the salivary ethanol level increased did not differ between the groups of subjects with any combinations of ALDH2 and ADH1B genotypes.	Acetaldehyde	35-47	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	174-179
20477767-7	2010	The slope of the increase in blood acetaldehyde level as the blood ethanol level increased was significantly steeper in alcoholics with inactive heterozygous ALDH2*1/*2 plus ADH1B*2 allele than with any other genotype combinations, but the slopes of the increase in salivary acetaldehyde level as the salivary ethanol level increased did not differ between the groups of subjects with any combinations of ALDH2 and ADH1B genotypes.	Acetaldehyde	35-47	aldehyde dehydrogenase 2 family member	Homo sapiens	405-410
20477767-7	2010	The slope of the increase in blood acetaldehyde level as the blood ethanol level increased was significantly steeper in alcoholics with inactive heterozygous ALDH2*1/*2 plus ADH1B*2 allele than with any other genotype combinations, but the slopes of the increase in salivary acetaldehyde level as the salivary ethanol level increased did not differ between the groups of subjects with any combinations of ALDH2 and ADH1B genotypes.	Acetaldehyde	35-47	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	415-420
20477767-8	2010	CONCLUSIONS: The ADH1B/ALDH2 genotype affected the blood and salivary ethanol and acetaldehyde levels of nonabstinent alcoholics in a different manner from nonalcoholics, and clear effects of ADH1B genotype and less clear effects of ALDH2 were observed in the alcoholics.	Acetaldehyde	82-94	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	17-22
20477767-8	2010	CONCLUSIONS: The ADH1B/ALDH2 genotype affected the blood and salivary ethanol and acetaldehyde levels of nonabstinent alcoholics in a different manner from nonalcoholics, and clear effects of ADH1B genotype and less clear effects of ALDH2 were observed in the alcoholics.	Acetaldehyde	82-94	aldehyde dehydrogenase 2 family member	Homo sapiens	23-28
20590827-1	2010	AIMS: Most of the acetaldehyde, a recognized animal carcinogen, generated during alcohol metabolism is eliminated by liver mitochondrial aldehyde dehydrogenase 2 (ALDH2).	Acetaldehyde	18-30	aldehyde dehydrogenase 2 family member	Homo sapiens	137-161
20590827-1	2010	AIMS: Most of the acetaldehyde, a recognized animal carcinogen, generated during alcohol metabolism is eliminated by liver mitochondrial aldehyde dehydrogenase 2 (ALDH2).	Acetaldehyde	18-30	aldehyde dehydrogenase 2 family member	Homo sapiens	163-168
20594261-2	2010	Since Bcl-2 overexpression preserves viability against OS, our objective was to address the effect of Bcl-2 overexpression in the hepatic stellate cells (HSC) cell-line CFSC-2G under acetaldehyde and H(2)O(2) challenge, and explore if it protects these cells against OS, induces replicative senescence and/or modify extracellular matrix (ECM) remodeling potential.	Acetaldehyde	183-195	BCL2, apoptosis regulator	Rattus norvegicus	102-107
20594261-9	2010	Bcl-2 overexpression did not change alpha-SMA levels, but it increased TIMP-1 (55%), tissue transglutaminases (tTG) (25%) and TGF-beta mRNA (49%), when exposed to acetaldehyde, while MMP-13 content decreased (47%).	Acetaldehyde	163-175	BCL2, apoptosis regulator	Rattus norvegicus	0-5
20102564-0	2010	Role of dopamine D1 receptors and extracellular signal regulated kinase in the motivational properties of acetaldehyde as assessed by place preference conditioning.	Acetaldehyde	106-118	Eph receptor B1	Rattus norvegicus	34-71
20515806-2	2010	Aldehyde dehydrogenase 2 (ALDH2) is the major enzyme that contribute to the detoxification of acetaldehyde in human body.	Acetaldehyde	94-106	aldehyde dehydrogenase 2 family member	Homo sapiens	0-24
20515806-2	2010	Aldehyde dehydrogenase 2 (ALDH2) is the major enzyme that contribute to the detoxification of acetaldehyde in human body.	Acetaldehyde	94-106	aldehyde dehydrogenase 2 family member	Homo sapiens	26-31
20515806-5	2010	N2-ethylidene-dG levels in livers of Aldh2-/- mice were always lower than those of Aldh2+/+ mice, suggesting that Aldh2 deficiency might cause the induction of acetaldehyde metabolizing enzymes in the liver such as P450s.	Acetaldehyde	160-172	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	37-42
20515806-6	2010	The differences between Aldh2-/- and Aldh2+/+ mice were greater in the order of nasal epithelium &gt; lung &gt; dorsal skin, suggesting that nasal epithelium and lung are the major target sites for acetaldehyde.	Acetaldehyde	198-210	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	24-29
20515806-7	2010	Acetaldehyde inhalation may cause a high risk in nasal epithelium and lung cancers for individuals with inactive ALDH2.	Acetaldehyde	0-12	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	113-118
20306188-1	2010	Pyrroquinoline quinone-dependent alcohol dehydrogenase (PQQ-ADH) of acetic acid bacteria is a membrane-bound enzyme involved in the acetic acid fermentation by oxidizing ethanol to acetaldehyde coupling with reduction of membranous ubiquinone (Q), which is, in turn, re-oxidized by ubiquinol oxidase, reducing oxygen to water.	Acetaldehyde	181-193	aldo-keto reductase family 1 member A1	Homo sapiens	33-54
20449332-1	2010	The asymmetric inverse-electron-demand aza-Diels-Alder reaction of N-Ts-1-aza-1,3-butadienes derived from 3-argiocarbonylcoumarins and acetaldehyde has been developed using chiral secondary aminocatalysis, giving tricyclic chroman-2-one derivatives in high enantioselectivities (up to 95% ee).	Acetaldehyde	135-147	neurotensin	Homo sapiens	67-73
20102564-3	2010	To date, the role of D1 receptors and ERK activation in acetaldehyde-elicited place preference has not been determined.	Acetaldehyde	56-68	Eph receptor B1	Rattus norvegicus	38-41
20102564-16	2010	Furthermore, the finding that PD98059 prevents the acquisition of acetaldehyde-elicited conditioned place preference highlights the importance of the D1 receptor-ERK pathway in its motivational effects.	Acetaldehyde	66-78	Eph receptor B1	Rattus norvegicus	162-165
20467251-5	2010	Due to the disruption of ADH2 gene in TQ1, the off-flavor acetaldehyde concentration in the fermentation broth were 9.43% and 13.28% respectively lower than that of T1 and YSF5.	Acetaldehyde	58-70	alcohol dehydrogenase ADH2	Saccharomyces cerevisiae S288C	25-29
20051035-9	2010	Stimulation of LEC2 expression in mature tobacco plants by acetaldehyde led to the accumulation of up to 6.8% per dry weight of total extracted FA.	Acetaldehyde	59-71	AP2/B3-like transcriptional factor family protein	Arabidopsis thaliana	15-19
20062057-4	2010	The accumulation of acetaldehyde following the consumption of even a single alcoholic beverage leads to the Asian alcohol-induced flushing syndrome in ALDH2*2 homozygotes.	Acetaldehyde	20-32	aldehyde dehydrogenase 2 family member	Homo sapiens	151-156
20155960-0	2010	Boryl substitution of acetaldehyde makes it an enol: inconsistency between Gn/CBS and ab initio/DFT data.	Acetaldehyde	22-34	cystathionine beta-synthase	Homo sapiens	78-81
20042735-1	2010	The progression of periodontitis may be affected by ALDH2 genotypes with respect to the oxidation of acetaldehyde to acetate, which leads to the accumulation of acetaldehyde in plasma and potential toxic effects.	Acetaldehyde	101-113	aldehyde dehydrogenase 2 family member	Homo sapiens	52-57
20042735-1	2010	The progression of periodontitis may be affected by ALDH2 genotypes with respect to the oxidation of acetaldehyde to acetate, which leads to the accumulation of acetaldehyde in plasma and potential toxic effects.	Acetaldehyde	161-173	aldehyde dehydrogenase 2 family member	Homo sapiens	52-57
20082270-0	2010	DNA repair mutant pso2 of Saccharomyces cerevisiae is sensitive to intracellular acetaldehyde accumulated by disulfiram-mediated inhibition of acetaldehyde dehydrogenase.	Acetaldehyde	81-93	DNA cross-link repair protein PSO2	Saccharomyces cerevisiae S288C	18-22
19914339-2	2010	Furthermore, another gene mitochondrial aldehyde dehydrogenase (ALDH2) has also been proposed to be potentially associated with AD, based on its possible relations toward acetaldehyde accumulation which further damage brain cells.	Acetaldehyde	171-183	aldehyde dehydrogenase 2 family member	Homo sapiens	64-69
20090911-11	2010	CONCLUSIONS: Taken together, these data suggest that enhanced acetaldehyde production through ADH overexpression following acute ethanol exposure exacerbated ethanol-induced myocardial contractile dysfunction, cardiomyocyte enlargement, mitochondrial damage and apoptosis, indicating a pivotal role of ADH in ethanol-induced cardiac dysfunction possibly through mitochondrial death pathway of apoptosis.	Acetaldehyde	62-74	aldo-keto reductase family 1, member A1 (aldehyde reductase)	Mus musculus	94-97
20090911-11	2010	CONCLUSIONS: Taken together, these data suggest that enhanced acetaldehyde production through ADH overexpression following acute ethanol exposure exacerbated ethanol-induced myocardial contractile dysfunction, cardiomyocyte enlargement, mitochondrial damage and apoptosis, indicating a pivotal role of ADH in ethanol-induced cardiac dysfunction possibly through mitochondrial death pathway of apoptosis.	Acetaldehyde	62-74	aldo-keto reductase family 1, member A1 (aldehyde reductase)	Mus musculus	302-305
20082270-4	2010	Acetaldehyde induced the expression of a PSO2-lacZ reporter construct that is specifically inducible by bi- or poly-functional mutagens, e.g., nitrogen mustard and photo-activated psoralens.	Acetaldehyde	0-12	DNA cross-link repair protein PSO2	Saccharomyces cerevisiae S288C	41-45
20082270-5	2010	Chronic exposure of yeast cells to disulfiram and acute exposure to acetaldehyde induced forward mutagenesis in the yeast CAN1 gene.	Acetaldehyde	68-80	arginine permease CAN1	Saccharomyces cerevisiae S288C	122-126
20872569-11	2010	CONCLUSION: The increased activity of total ADH in endometrial cancer, especially the class I isoenzyme and normal activity of ALDH, may be the cause of disorders in metabolic pathways that use these isoenzymes and could increase the concentration of acetaldehyde, which is cancerogenic substance.	Acetaldehyde	251-263	aldo-keto reductase family 1 member A1	Homo sapiens	44-47
21525760-9	2010	This ethanol-induced upregulation of CB1 receptors was partly dependent on the ethanol metabolite acetaldehyde.	Acetaldehyde	98-110	cannabinoid receptor 1 (brain)	Mus musculus	37-40
19710201-9	2010	This brief increase (burst) in arterial acetaldehyde concentration after ethanol ingestion may constitute the mechanism by which humans carrying the ADH1B*2 allele are protected against alcoholism.	Acetaldehyde	40-52	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	149-154
20714161-3	2010	METHODS: We develop a pharmacokinetic model describing how genetic variations in ADH1B, ADH1C, ADH7, ALDH2, and TAS2R38 affect consumption behavior, and alcohol and acetaldehyde levels over time in various tissues of individuals with a particular genotype to predict their susceptibility to alcohol dependence.	Acetaldehyde	165-177	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	81-86
19906643-4	2010	Alda-1 increased acetaldehyde oxidation by ALDH2*1 and ALDH2*2 approximately 1.5- and 6-fold, respectively, and stimulated the esterase activities of both enzymes to similar extent as the coenzyme NAD.	Acetaldehyde	17-29	aldolase, fructose-bisphosphate A	Homo sapiens	0-4
19906643-4	2010	Alda-1 increased acetaldehyde oxidation by ALDH2*1 and ALDH2*2 approximately 1.5- and 6-fold, respectively, and stimulated the esterase activities of both enzymes to similar extent as the coenzyme NAD.	Acetaldehyde	17-29	aldehyde dehydrogenase 2 family member	Homo sapiens	43-48
20072603-9	2010	ALDH7A1 degrades and detoxifies acetaldehyde, which inhibits osteoblast proliferation and results in decreased bone formation.	Acetaldehyde	32-44	aldehyde dehydrogenase 7 family member A1	Homo sapiens	0-7
20205700-2	2010	In contrast, in Asians, alcohol-induced asthma and flushing have been shown to be because of a single nucleotide polymorphism (SNP), the acetaldehyde dehydrogenase 2 (ALDH2) 487lys, causing decreased acetaldehyde (the metabolite of ethanol) metabolism and high levels of histamine.	Acetaldehyde	137-149	aldehyde dehydrogenase 2 family member	Homo sapiens	167-172
19925625-2	2010	The alcohol dehydrogenase (ADH) pathway, which converts alcohol to the toxic substance acetaldehyde, is responsible for most of the alcohol breakdown in the liver.	Acetaldehyde	87-99	alcohol dehydrogenase 4 (class II), pi polypeptide	Homo sapiens	27-30
19942091-1	2009	OBJECTIVES: This study was designed to evaluate the role of facilitated detoxification of acetaldehyde, the main metabolic product of ethanol, through systemic overexpression of mitochondrial aldehyde dehydrogenase-2 (ALDH2) on acute ethanol exposure-induced myocardial damage.	Acetaldehyde	90-102	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	218-223
21187698-4	2010	The inefficient degradation of acetaldehyde by weakly expressed ALDH2 in the UADT may be cri!	Acetaldehyde	31-43	aldehyde dehydrogenase 2 family member	Homo sapiens	64-69
21187698-5	2010	tical to the local accumulation of acetaldehyde, especially in ALDH2*1/*2 carriers.	Acetaldehyde	35-47	aldehyde dehydrogenase 2 family member	Homo sapiens	63-68
21187698-7	2010	Heavy drinking by persons with the less-active ADH1B*1/*1 leads to longer exposure of the UADT to salivary ethanol and acetaldehyde.	Acetaldehyde	119-131	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	47-52
19942091-6	2009	RESULTS: ALDH2 reduced ethanol-induced elevation in cardiac acetaldehyde levels.	Acetaldehyde	60-72	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	9-14
19673742-4	2009	Decreased drinking due to ALDH-2 inhibition is attributed to aversive properties of acetaldehyde accumulated during alcohol consumption.	Acetaldehyde	84-96	aldehyde dehydrogenase 2 family member	Rattus norvegicus	26-32
19719790-9	2009	The inhibition of ALDH enzymes by cyanamide induced a strong potentiation of both ethanol- and acetaldehyde-induced hypothermia.	Acetaldehyde	95-107	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	18-22
19719790-12	2009	Furthermore, the accumulation of acetaldehyde following ALDH inhibition strongly enhanced the hypothermic effects of ethanol.	Acetaldehyde	33-45	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	56-60
19874182-3	2009	Aldehyde dehydrogenase 2 (ALDH2) is an important enzyme that oxidizes acetaldehyde.	Acetaldehyde	70-82	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	0-24
19874182-3	2009	Aldehyde dehydrogenase 2 (ALDH2) is an important enzyme that oxidizes acetaldehyde.	Acetaldehyde	70-82	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	26-31
19874182-5	2009	This review gives an overview of published studies on Aldh2 knockout mice, which were treated with ethanol or acetaldehyde.	Acetaldehyde	110-122	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	54-59
19874182-6	2009	According to these studies, it was found that Aldh2 -/- mice (Aldh2 knockout mice) are more susceptible to ethanol and acetaldehyde-induced toxicity than Aldh2 +/+ mice (wild type mice).	Acetaldehyde	119-131	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	46-51
19874182-6	2009	According to these studies, it was found that Aldh2 -/- mice (Aldh2 knockout mice) are more susceptible to ethanol and acetaldehyde-induced toxicity than Aldh2 +/+ mice (wild type mice).	Acetaldehyde	119-131	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	62-67
19874182-6	2009	According to these studies, it was found that Aldh2 -/- mice (Aldh2 knockout mice) are more susceptible to ethanol and acetaldehyde-induced toxicity than Aldh2 +/+ mice (wild type mice).	Acetaldehyde	119-131	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	62-67
19874182-8	2009	When they were exposed to atmospheres containing acetaldehyde, the Aldh2 -/- mice showed more severe toxic symptoms, like weight loss and higher blood acetaldehyde levels, as compared with the Aldh2 +/+ mice.	Acetaldehyde	49-61	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	67-72
19874182-8	2009	When they were exposed to atmospheres containing acetaldehyde, the Aldh2 -/- mice showed more severe toxic symptoms, like weight loss and higher blood acetaldehyde levels, as compared with the Aldh2 +/+ mice.	Acetaldehyde	49-61	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	193-198
19874182-8	2009	When they were exposed to atmospheres containing acetaldehyde, the Aldh2 -/- mice showed more severe toxic symptoms, like weight loss and higher blood acetaldehyde levels, as compared with the Aldh2 +/+ mice.	Acetaldehyde	151-163	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	67-72
19874182-9	2009	Thus, ethanol and acetaldehyde treatment affects Aldh2 knockout mice more than wild type mice.	Acetaldehyde	18-30	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	49-54
19874182-10	2009	Based on these findings, it is suggested that ethanol consumption and acetaldehyde inhalation are inferred to pose a higher risk to ALDH2-inactive humans.	Acetaldehyde	70-82	aldehyde dehydrogenase 2 family member	Homo sapiens	132-137
19911129-1	2009	Human mitochondrial acetaldehyde dehydrogenase 2 (ALDH2) catalyzes the oxidation of acetaldehyde to acetic acid.	Acetaldehyde	20-32	aldehyde dehydrogenase 2 family member	Homo sapiens	50-55
19794996-1	2009	Ethanol and its metabolite acetaldehyde increase transforming growth factor beta1 (TGF-beta1) expression in animal studies.	Acetaldehyde	27-39	transforming growth factor beta 1	Homo sapiens	49-81
19794996-1	2009	Ethanol and its metabolite acetaldehyde increase transforming growth factor beta1 (TGF-beta1) expression in animal studies.	Acetaldehyde	27-39	transforming growth factor beta 1	Homo sapiens	83-92
19664611-1	2009	We investigated the effects of alcohol (EtOH) and acetaldehyde (ACe) on choline acetyltransferase (ChAT) and acetylcholinesterase (AChE) in the frontal cortex of Aldh2-/- (KO) mice.	Acetaldehyde	50-62	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	162-167
19664611-1	2009	We investigated the effects of alcohol (EtOH) and acetaldehyde (ACe) on choline acetyltransferase (ChAT) and acetylcholinesterase (AChE) in the frontal cortex of Aldh2-/- (KO) mice.	Acetaldehyde	64-67	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	162-167
19908471-2	2009	The results indicate that Au/TiO2 core-shell catalyst shows higher activity for the oxidation of acetaldehyde into CO2 under both UV and visible light irradiation comparing with P-25 and metal-deposited TiO2 photocatalysts.	Acetaldehyde	97-109	tubulin polymerization promoting protein	Homo sapiens	178-182
19911129-2	2009	Therefore, ALDH2 has therapeutic potential in detoxification of acetaldehyde.	Acetaldehyde	64-76	aldehyde dehydrogenase 2 family member	Homo sapiens	11-16
19449376-1	2009	Genetic variants in alcohol dehydrogenase-1B (ADH1B) and aldehyde dehydrogenase-2 (ALDH2) genes modulate acetaldehyde removal upon alcohol ingestion.	Acetaldehyde	105-117	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	46-51
19449376-1	2009	Genetic variants in alcohol dehydrogenase-1B (ADH1B) and aldehyde dehydrogenase-2 (ALDH2) genes modulate acetaldehyde removal upon alcohol ingestion.	Acetaldehyde	105-117	aldehyde dehydrogenase 2 family member	Homo sapiens	83-88
19449376-10	2009	In conclusion, consumption of tobacco and alcohol, coupled with genetic susceptibilities associated with acetaldehyde elimination, as modulated by ADH1B and ALDH2 genotypes, determines a substantial magnitude of tumorigenetic effect on earlier age ESCC diagnosis.	Acetaldehyde	105-117	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	147-152
19449376-10	2009	In conclusion, consumption of tobacco and alcohol, coupled with genetic susceptibilities associated with acetaldehyde elimination, as modulated by ADH1B and ALDH2 genotypes, determines a substantial magnitude of tumorigenetic effect on earlier age ESCC diagnosis.	Acetaldehyde	105-117	aldehyde dehydrogenase 2 family member	Homo sapiens	157-162
19376089-7	2009	Zinc also inhibited ethanol- and acetaldehyde-induced TGF-beta1 and TNF-alpha production.	Acetaldehyde	33-45	transforming growth factor, beta 1	Rattus norvegicus	54-63
19376089-9	2009	In ethanol- and acetaldehyde-induced HSCs, zinc inhibited the activation of the p38 MAPK as well as the JNK transduction pathways and phosphorylation of IkappaB and Smad 3.	Acetaldehyde	16-28	mitogen activated protein kinase 14	Rattus norvegicus	80-88
19376089-7	2009	Zinc also inhibited ethanol- and acetaldehyde-induced TGF-beta1 and TNF-alpha production.	Acetaldehyde	33-45	tumor necrosis factor	Rattus norvegicus	68-77
19376089-9	2009	In ethanol- and acetaldehyde-induced HSCs, zinc inhibited the activation of the p38 MAPK as well as the JNK transduction pathways and phosphorylation of IkappaB and Smad 3.	Acetaldehyde	16-28	mitogen-activated protein kinase 8	Rattus norvegicus	104-107
19376089-8	2009	Zinc down-regulated ethanol- and acetaldehyde-induced production of TIMP-1 and TIMP-2 and decreased the activity of MMP-2.	Acetaldehyde	33-45	TIMP metallopeptidase inhibitor 1	Rattus norvegicus	68-74
19376089-9	2009	In ethanol- and acetaldehyde-induced HSCs, zinc inhibited the activation of the p38 MAPK as well as the JNK transduction pathways and phosphorylation of IkappaB and Smad 3.	Acetaldehyde	16-28	SMAD family member 3	Rattus norvegicus	165-171
19376089-8	2009	Zinc down-regulated ethanol- and acetaldehyde-induced production of TIMP-1 and TIMP-2 and decreased the activity of MMP-2.	Acetaldehyde	33-45	TIMP metallopeptidase inhibitor 2	Rattus norvegicus	79-85
19376089-10	2009	CONCLUSION: The results indicated that zinc supplementation inhibited ethanol- and acetaldehyde-induced activation of HSCs on different levels, acting as an antioxidant and inhibitor of MAPK, TGF-beta and NFkappaB/IkappaB transduction signaling.	Acetaldehyde	83-95	transforming growth factor, beta 1	Rattus norvegicus	192-200
19376089-8	2009	Zinc down-regulated ethanol- and acetaldehyde-induced production of TIMP-1 and TIMP-2 and decreased the activity of MMP-2.	Acetaldehyde	33-45	matrix metallopeptidase 2	Rattus norvegicus	116-121
19389190-9	2009	CONCLUSIONS: These data indicate high levels of IgA antibodies against acetaldehyde-derived antigens in IgAGN patients, which may hamper the use of the immune responses as markers of alcohol consumption among such patients.	Acetaldehyde	71-83	CD79a molecule	Homo sapiens	48-51
19344727-11	2009	Transfection of H9C2 myoblast cells with Foxo3a adenovirus mimicked acetaldehyde-induced JNK activation and glucose uptake defect whereas the dominant negative Foxo3a ablated acetaldehyde-elicited insulin insensitivity.	Acetaldehyde	68-80	forkhead box O3	Rattus norvegicus	41-47
19344727-11	2009	Transfection of H9C2 myoblast cells with Foxo3a adenovirus mimicked acetaldehyde-induced JNK activation and glucose uptake defect whereas the dominant negative Foxo3a ablated acetaldehyde-elicited insulin insensitivity.	Acetaldehyde	68-80	mitogen-activated protein kinase 8	Rattus norvegicus	89-92
19344727-11	2009	Transfection of H9C2 myoblast cells with Foxo3a adenovirus mimicked acetaldehyde-induced JNK activation and glucose uptake defect whereas the dominant negative Foxo3a ablated acetaldehyde-elicited insulin insensitivity.	Acetaldehyde	175-187	forkhead box O3	Rattus norvegicus	160-166
19584771-0	2009	Pharmacokinetic and pharmacodynamic basis for overcoming acetaldehyde-induced adverse reaction in Asian alcoholics, heterozygous for the variant ALDH2*2 gene allele.	Acetaldehyde	57-69	aldehyde dehydrogenase 2 family member	Homo sapiens	145-150
19584771-2	2009	The partial protection against alcoholism has been ascribed to the faster elimination of acetaldehyde by residual hepatic ALDH2 activity and the lower accumulation in circulation in nonalcoholic heterozygotes.	Acetaldehyde	89-101	aldehyde dehydrogenase 2 family member	Homo sapiens	122-127
19584771-7	2009	RESULTS: ALDH2*1/*2 alcoholics exhibited significantly higher blood acetaldehyde levels as well as prominent cardiovascular effects and the subjective perceptions, compared with the ALDH2*1/*1 alcoholics.	Acetaldehyde	68-80	aldehyde dehydrogenase 2 family member	Homo sapiens	9-14
19446252-2	2009	In our previous study, we showed that MDMA exposure inhibits the activity of the acetaldehyde (ACH) metabolizing enzyme, aldehyde dehydrogenase2 (ALDH2).	Acetaldehyde	81-93	aldehyde dehydrogenase 1 family, member A1	Rattus norvegicus	121-144
19446252-2	2009	In our previous study, we showed that MDMA exposure inhibits the activity of the acetaldehyde (ACH) metabolizing enzyme, aldehyde dehydrogenase2 (ALDH2).	Acetaldehyde	81-93	aldehyde dehydrogenase 1 family, member A1	Rattus norvegicus	146-151
19446252-2	2009	In our previous study, we showed that MDMA exposure inhibits the activity of the acetaldehyde (ACH) metabolizing enzyme, aldehyde dehydrogenase2 (ALDH2).	Acetaldehyde	95-98	aldehyde dehydrogenase 1 family, member A1	Rattus norvegicus	121-144
19446252-2	2009	In our previous study, we showed that MDMA exposure inhibits the activity of the acetaldehyde (ACH) metabolizing enzyme, aldehyde dehydrogenase2 (ALDH2).	Acetaldehyde	95-98	aldehyde dehydrogenase 1 family, member A1	Rattus norvegicus	146-151
19389190-0	2009	IgA immune responses against acetaldehyde adducts and biomarkers of alcohol consumption in patients with IgA glomerulonephritis.	Acetaldehyde	29-41	CD79a molecule	Homo sapiens	0-3
19389190-0	2009	IgA immune responses against acetaldehyde adducts and biomarkers of alcohol consumption in patients with IgA glomerulonephritis.	Acetaldehyde	29-41	CD79a molecule	Homo sapiens	105-108
19382905-10	2009	The activity of ALDH2-inactive phenotypes was slightly lower than ALDH2-active phenotypes at 200 microM acetaldehyde.	Acetaldehyde	104-116	aldehyde dehydrogenase 2 family member	Homo sapiens	16-21
20005475-2	2009	ALDH2 mediates both the detoxification of reactive aldehydes such as acetaldehyde and 4-hydroxy-2-nonenal and the bioactivation of nitroglycerin to nitric oxide.	Acetaldehyde	69-81	aldehyde dehydrogenase 2 family member	Homo sapiens	0-5
19429258-2	2009	This study was designed to examine the impact of facilitated acetaldehyde breakdown via transgenic overexpression of mitochondrial aldehyde dehydrogenase-2 (ALDH2) on alcohol-induced cerebral cortical injury.	Acetaldehyde	61-73	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	157-162
19382905-10	2009	The activity of ALDH2-inactive phenotypes was slightly lower than ALDH2-active phenotypes at 200 microM acetaldehyde.	Acetaldehyde	104-116	aldehyde dehydrogenase 2 family member	Homo sapiens	66-71
19144977-0	2009	A promoter polymorphism in the ALDH2 gene affects its basal and acetaldehyde/ethanol-induced gene expression in human peripheral blood leukocytes and HepG2 cells.	Acetaldehyde	64-76	aldehyde dehydrogenase 2 family member	Homo sapiens	31-36
19036374-0	2009	Acetaldehyde stimulates monocyte adhesion in a P-selectin- and TNFalpha-dependent manner.	Acetaldehyde	0-12	selectin P	Homo sapiens	47-71
19036374-5	2009	RESULTS: Acetaldehyde dose-dependently increased the number of CCR2 positive THP-1 monocytes, with a maximal increase of approximately 50% observed in the presence of 10 microM acetaldehyde.	Acetaldehyde	9-21	C-C motif chemokine receptor 2	Homo sapiens	63-67
19036374-5	2009	RESULTS: Acetaldehyde dose-dependently increased the number of CCR2 positive THP-1 monocytes, with a maximal increase of approximately 50% observed in the presence of 10 microM acetaldehyde.	Acetaldehyde	9-21	GLI family zinc finger 2	Homo sapiens	77-82
19036374-5	2009	RESULTS: Acetaldehyde dose-dependently increased the number of CCR2 positive THP-1 monocytes, with a maximal increase of approximately 50% observed in the presence of 10 microM acetaldehyde.	Acetaldehyde	177-189	C-C motif chemokine receptor 2	Homo sapiens	63-67
19036374-5	2009	RESULTS: Acetaldehyde dose-dependently increased the number of CCR2 positive THP-1 monocytes, with a maximal increase of approximately 50% observed in the presence of 10 microM acetaldehyde.	Acetaldehyde	177-189	GLI family zinc finger 2	Homo sapiens	77-82
19036374-6	2009	There was a significant increase in both the number of P-selectin positive cells and P-selectin receptor density when HUVEC were incubated with acetaldehyde.	Acetaldehyde	144-156	selectin P	Homo sapiens	55-65
19036374-6	2009	There was a significant increase in both the number of P-selectin positive cells and P-selectin receptor density when HUVEC were incubated with acetaldehyde.	Acetaldehyde	144-156	selectin P	Homo sapiens	85-95
19036374-7	2009	HUVEC TNFalpha mRNA expression and secretion were enhanced by acetaldehyde.	Acetaldehyde	62-74	tumor necrosis factor	Homo sapiens	6-14
19036374-8	2009	Moreover, acetaldehyde increased THP-1 and PBM adhesion to HUVEC.	Acetaldehyde	10-22	GLI family zinc finger 2	Homo sapiens	33-38
19036374-9	2009	Inhibition of P-selectin or TNFalpha, using antibodies or siRNA-directed gene knockdown, attenuated acetaldehyde-induced monocyte adhesion.	Acetaldehyde	100-112	selectin P	Homo sapiens	14-24
19036374-9	2009	Inhibition of P-selectin or TNFalpha, using antibodies or siRNA-directed gene knockdown, attenuated acetaldehyde-induced monocyte adhesion.	Acetaldehyde	100-112	tumor necrosis factor	Homo sapiens	28-36
19036374-10	2009	In conclusion, acetaldehyde increased the number of CCR2 positive monocytes and stimulated endothelial cell P-selectin and TNFalpha expression.	Acetaldehyde	15-27	C-C motif chemokine receptor 2	Homo sapiens	52-56
19036374-10	2009	In conclusion, acetaldehyde increased the number of CCR2 positive monocytes and stimulated endothelial cell P-selectin and TNFalpha expression.	Acetaldehyde	15-27	selectin P	Homo sapiens	108-118
19036374-10	2009	In conclusion, acetaldehyde increased the number of CCR2 positive monocytes and stimulated endothelial cell P-selectin and TNFalpha expression.	Acetaldehyde	15-27	tumor necrosis factor	Homo sapiens	123-131
19036374-11	2009	Moreover, acetaldehyde increased monocyte adhesion to endothelial cells, an effect that was both P-selectin- and TNFalpha-dependent.	Acetaldehyde	10-22	selectin P	Homo sapiens	97-121
19326463-10	2009	To confirm or to refute the hypothesis that ethanol, acetaldehyde or other alcohol-related substances might influence the acquisition or persistence of K-ras mutations in the pancreatic epithelium, large and unselected studies are warranted.	Acetaldehyde	53-65	KRAS proto-oncogene, GTPase	Homo sapiens	152-157
19428384-0	2009	Acetaldehyde stimulates FANCD2 monoubiquitination, H2AX phosphorylation, and BRCA1 phosphorylation in human cells in vitro: implications for alcohol-related carcinogenesis.	Acetaldehyde	0-12	FA complementation group D2	Homo sapiens	24-30
19428384-0	2009	Acetaldehyde stimulates FANCD2 monoubiquitination, H2AX phosphorylation, and BRCA1 phosphorylation in human cells in vitro: implications for alcohol-related carcinogenesis.	Acetaldehyde	0-12	H2A.X variant histone	Homo sapiens	51-55
19428384-0	2009	Acetaldehyde stimulates FANCD2 monoubiquitination, H2AX phosphorylation, and BRCA1 phosphorylation in human cells in vitro: implications for alcohol-related carcinogenesis.	Acetaldehyde	0-12	BRCA1 DNA repair associated	Homo sapiens	77-82
19298328-9	2009	CONCLUSIONS: These results suggest that high NS and low HA scores in alcoholics with inactive ALDH2 are associated with an increased risk for developing alcoholism, despite a low enzymatic ability to eliminate toxic acetaldehyde in these subjects.	Acetaldehyde	216-228	aldehyde dehydrogenase 2 family member	Homo sapiens	94-99
19144977-1	2009	AIMS: To assess the effect of the -360G/A polymorphism in the promoter region of the human aldehyde dehydrogenase-2 (ALDH2) gene on its transcription, basal and acetaldehyde/ethanol-induced gene expression was examined by in vivo and in vitro experiments.	Acetaldehyde	161-173	aldehyde dehydrogenase 2 family member	Homo sapiens	91-115
19144977-1	2009	AIMS: To assess the effect of the -360G/A polymorphism in the promoter region of the human aldehyde dehydrogenase-2 (ALDH2) gene on its transcription, basal and acetaldehyde/ethanol-induced gene expression was examined by in vivo and in vitro experiments.	Acetaldehyde	161-173	aldehyde dehydrogenase 2 family member	Homo sapiens	117-122
19144977-3	2009	The transcriptional activity of the ALDH2 promoter was investigated by a reporter assay using HepG2 cells in the presence or absence of acetaldehyde/ethanol.	Acetaldehyde	136-148	aldehyde dehydrogenase 2 family member	Homo sapiens	36-41
19456322-9	2009	Esophageal cancer, with its highest incidence in East Asia, may be associated with ALDH2*504Lys because of a toxic effect of increased acetaldehyde in the tissue where ingested ethanol has its highest concentration.	Acetaldehyde	135-147	aldehyde dehydrogenase 2 family member	Homo sapiens	83-88
19299582-3	2009	In the present study, we examined the role of SIRT1 signaling in TNF-alpha generation stimulated by either lipopolysaccharide (LPS), acetaldehyde (AcH), or acetate (two major metabolites of ethanol) in two cultured macrophage cell lines.	Acetaldehyde	133-145	sirtuin 1	Rattus norvegicus	46-51
19299582-3	2009	In the present study, we examined the role of SIRT1 signaling in TNF-alpha generation stimulated by either lipopolysaccharide (LPS), acetaldehyde (AcH), or acetate (two major metabolites of ethanol) in two cultured macrophage cell lines.	Acetaldehyde	133-145	tumor necrosis factor	Rattus norvegicus	65-74
19299582-3	2009	In the present study, we examined the role of SIRT1 signaling in TNF-alpha generation stimulated by either lipopolysaccharide (LPS), acetaldehyde (AcH), or acetate (two major metabolites of ethanol) in two cultured macrophage cell lines.	Acetaldehyde	147-150	tumor necrosis factor	Rattus norvegicus	65-74
19299582-4	2009	In both rat Kupffer cell line 1 (RKC1) and murine RAW 264.7 macrophages, treatment with either LPS, AcH, or acetate caused significant decreases in SIRT1 transcription, translation, and activation, which essentially demonstrated an inverse relationship with TNF-alpha levels.	Acetaldehyde	100-103	sirtuin 1	Mus musculus	148-153
19332462-7	2009	ALDH2 reduced the chronic alcohol ingestion-induced elevation in plasma and tissue acetaldehyde levels.	Acetaldehyde	83-95	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	0-5
19299582-4	2009	In both rat Kupffer cell line 1 (RKC1) and murine RAW 264.7 macrophages, treatment with either LPS, AcH, or acetate caused significant decreases in SIRT1 transcription, translation, and activation, which essentially demonstrated an inverse relationship with TNF-alpha levels.	Acetaldehyde	100-103	tumor necrosis factor	Mus musculus	258-267
19299582-5	2009	LPS, AcH, and acetate each provoked the release of TNF-alpha from RKC1 cells, whereas coincubation with resveratrol (a potent SIRT1 agonist) inhibited this effect.	Acetaldehyde	5-8	tumor necrosis factor	Rattus norvegicus	51-60
19299582-7	2009	Further mechanistic studies revealed that inhibition of SIRT1 by LPS, AcH, or acetate was associated with a marked increase in the acetylation of the RelA/p65 subunit of nuclear transcription factor (NF-kappaB) and promotion of NF-kappaB transcriptional activity.	Acetaldehyde	70-73	sirtuin 1	Rattus norvegicus	56-61
19215238-5	2009	The present study was designed to examine the impact of facilitated acetaldehyde metabolism via overexpression of aldehyde dehydrogenase-2 (ALDH2) on chronic alcohol ingestion-induced hepatic damage.	Acetaldehyde	68-80	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	114-138
19215238-5	2009	The present study was designed to examine the impact of facilitated acetaldehyde metabolism via overexpression of aldehyde dehydrogenase-2 (ALDH2) on chronic alcohol ingestion-induced hepatic damage.	Acetaldehyde	68-80	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	140-145
19393179-2	2009	The alcohol sensitivity in Orientals is due to a delayed oxidation of acetaldehyde by an atypical aldehyde dehydrogenase ALDH2487Lys, which is resulted from a structural mutation in gene ALDH2.	Acetaldehyde	70-82	aldehyde dehydrogenase 2 family member	Homo sapiens	121-126
18688716-3	2009	Alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) are the main enzymes involved in ethanol metabolism, which leads to generation of acetaldehyde.	Acetaldehyde	144-156	aldo-keto reductase family 1 member A1	Homo sapiens	0-21
19290633-0	2009	Reductive half-reaction of aldehyde oxidoreductase toward acetaldehyde: a combined QM/MM study.	Acetaldehyde	58-70	thioredoxin reductase 1	Homo sapiens	36-50
18688716-3	2009	Alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH) are the main enzymes involved in ethanol metabolism, which leads to generation of acetaldehyde.	Acetaldehyde	144-156	aldo-keto reductase family 1 member A1	Homo sapiens	23-26
18688716-11	2009	CONCLUSION: Increased ADH IV activity may be a factor intensifying carcinogenesis, because of the increased ability to form acetaldehyde from ethanol.	Acetaldehyde	124-136	aldo-keto reductase family 1 member A1	Homo sapiens	22-25
19280452-2	2009	In view of the central role of connective tissue growth factor (CCN2) in fibrosis, we investigated the mechanisms by which CCN2 is regulated in PSC following their exposure to ethanol or acetaldehyde.	Acetaldehyde	187-199	cellular communication network factor 2	Mus musculus	123-127
19280452-6	2009	These results show the production of acetaldehyde and oxidant stress in mouse PSC are the cause of increased CCN2 mRNA and protein production after exposure of the cells to ethanol.	Acetaldehyde	37-49	cellular communication network factor 2	Mus musculus	109-113
19734271-5	2009	In this study, we report that in the ventral prostate cytosolic fraction, xanthine oxidoreductase is able to metabolize acetaldehyde to acetyl radical.	Acetaldehyde	120-132	xanthine dehydrogenase	Rattus norvegicus	74-97
19356968-3	2009	We found that blood acetate levels in ALDH2 KO mice were slightly lower than those in wild type (WT), whereas EtOH and AcH levels in ALDH2 KO were significantly higher than those in WT.	Acetaldehyde	119-122	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	133-138
19356968-4	2009	These observations indicate that high EtOH, AcH and low acetate in the blood of ALDH2 KO are due to the deficient effect of ALDH2 enzyme activity.	Acetaldehyde	44-47	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	80-85
19356968-4	2009	These observations indicate that high EtOH, AcH and low acetate in the blood of ALDH2 KO are due to the deficient effect of ALDH2 enzyme activity.	Acetaldehyde	44-47	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	124-129
19014920-7	2009	The pharmacokinetic and pharmacodynamic consequences indicate that acetaldehyde, rather than ethanol, is primarily responsible for the observed alcohol sensitivity reactions, suggesting that the full protection by ALDH2*2/*2 can be ascribed to the intense unpleasant physiological and psychological reactions caused by persistently elevated blood acetaldehyde after ingesting a small amount of alcohol and that the partial protection by ALDH2*1/*2 can be attributed to a faster elimination of acetaldehyde and the lower accumulation in circulation.	Acetaldehyde	67-79	aldehyde dehydrogenase 2 family member	Homo sapiens	214-219
19023563-10	2009	In conclusion, MCT1-mediated transport of (14)C-BT in Caco-2 cells is modulated by either acute or chronic exposure to some pharmacological agents and drugs of abuse (acetaldehyde, acetylsalicylic acid, indomethacin, caffeine, theophylline and the drugs of abuse tetrahydrocannabinol and MDMA).	Acetaldehyde	167-179	solute carrier family 16 member 1	Homo sapiens	15-19
19014920-7	2009	The pharmacokinetic and pharmacodynamic consequences indicate that acetaldehyde, rather than ethanol, is primarily responsible for the observed alcohol sensitivity reactions, suggesting that the full protection by ALDH2*2/*2 can be ascribed to the intense unpleasant physiological and psychological reactions caused by persistently elevated blood acetaldehyde after ingesting a small amount of alcohol and that the partial protection by ALDH2*1/*2 can be attributed to a faster elimination of acetaldehyde and the lower accumulation in circulation.	Acetaldehyde	67-79	aldehyde dehydrogenase 2 family member	Homo sapiens	437-442
19014920-7	2009	The pharmacokinetic and pharmacodynamic consequences indicate that acetaldehyde, rather than ethanol, is primarily responsible for the observed alcohol sensitivity reactions, suggesting that the full protection by ALDH2*2/*2 can be ascribed to the intense unpleasant physiological and psychological reactions caused by persistently elevated blood acetaldehyde after ingesting a small amount of alcohol and that the partial protection by ALDH2*1/*2 can be attributed to a faster elimination of acetaldehyde and the lower accumulation in circulation.	Acetaldehyde	347-359	aldehyde dehydrogenase 2 family member	Homo sapiens	214-219
19014920-7	2009	The pharmacokinetic and pharmacodynamic consequences indicate that acetaldehyde, rather than ethanol, is primarily responsible for the observed alcohol sensitivity reactions, suggesting that the full protection by ALDH2*2/*2 can be ascribed to the intense unpleasant physiological and psychological reactions caused by persistently elevated blood acetaldehyde after ingesting a small amount of alcohol and that the partial protection by ALDH2*1/*2 can be attributed to a faster elimination of acetaldehyde and the lower accumulation in circulation.	Acetaldehyde	347-359	aldehyde dehydrogenase 2 family member	Homo sapiens	214-219
19014920-9	2009	Physiological tolerance or innate insensitivity to acetaldehyde may be crucial for development of alcohol dependence in alcoholics carrying ALDH2*2.	Acetaldehyde	51-63	aldehyde dehydrogenase 2 family member	Homo sapiens	140-145
19146861-2	2009	Acetaldehyde, metabolized from ethanol in the CNS through the actions of catalase, has a role in the behavioral effects observed after ethanol administration.	Acetaldehyde	0-12	catalase	Rattus norvegicus	73-81
19146861-10	2009	Some brain nuclei rich in catalase (i.e.; SNR and ARH) could be mediating some of the locomotor stimulant effects of ethanol through its conversion to acetaldehyde.	Acetaldehyde	151-163	catalase	Rattus norvegicus	26-34
19120062-3	2009	In Caucasians, a polymorphism of alcohol dehydrogenase 1C (ADH1C) exists resulting in different acetaldehyde concentrations following ethanol oxidation.	Acetaldehyde	96-108	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	33-57
19120062-3	2009	In Caucasians, a polymorphism of alcohol dehydrogenase 1C (ADH1C) exists resulting in different acetaldehyde concentrations following ethanol oxidation.	Acetaldehyde	96-108	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	59-64
19177030-2	2009	Catalase has been proposed as the main enzyme responsible for the synthesis of acetaldehyde from ethanol in the brain.	Acetaldehyde	79-91	catalase	Mus musculus	0-8
19251111-1	2009	Liver alcohol dehydrogenase oxidizes ethanol to acetaldehyde, which is further oxidized to acetate by aldehyde dehydrogenase-2 (ALDH2*1).	Acetaldehyde	48-60	aldehyde dehydrogenase 2 family member	Homo sapiens	102-126
19251111-1	2009	Liver alcohol dehydrogenase oxidizes ethanol to acetaldehyde, which is further oxidized to acetate by aldehyde dehydrogenase-2 (ALDH2*1).	Acetaldehyde	48-60	aldehyde dehydrogenase 2 family member	Homo sapiens	128-133
19251111-2	2009	Individuals who carry a low-activity ALDH2 (ALDH2*2) display high blood acetaldehyde levels after ethanol consumption, which leads to dysphoric effects, such as facial flushing, nausea, dizziness, and headache ("Asian alcohol phenotype"), which result in an aversion to alcohol and protection against alcohol abuse and alcoholism.	Acetaldehyde	72-84	aldehyde dehydrogenase 2 family member	Homo sapiens	37-42
19251111-2	2009	Individuals who carry a low-activity ALDH2 (ALDH2*2) display high blood acetaldehyde levels after ethanol consumption, which leads to dysphoric effects, such as facial flushing, nausea, dizziness, and headache ("Asian alcohol phenotype"), which result in an aversion to alcohol and protection against alcohol abuse and alcoholism.	Acetaldehyde	72-84	aldehyde dehydrogenase 2 family member	Homo sapiens	44-49
18925476-4	2009	Acetaldehyde, an important metabolite of ethanol detoxified by aldehyde dehydrogenase (ALDH2) is more toxic that ethanol.	Acetaldehyde	0-12	aldehyde dehydrogenase 2 family member	Rattus norvegicus	87-92
19101651-1	2009	We analyzed an acetaldehyde-derived DNA adduct, N(2)-ethylidene-2"-deoxyguanosine (N(2)-Eti-dG) in stomach DNA of aldehyde dehydrogenase (Aldh)-2-knockout mice that were fed with alcohol to determine effects of alcohol consumption and Aldh2 genotype on the level of DNA damage in stomach.	Acetaldehyde	15-27	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	235-240
19101651-1	2009	We analyzed an acetaldehyde-derived DNA adduct, N(2)-ethylidene-2"-deoxyguanosine (N(2)-Eti-dG) in stomach DNA of aldehyde dehydrogenase (Aldh)-2-knockout mice that were fed with alcohol to determine effects of alcohol consumption and Aldh2 genotype on the level of DNA damage in stomach.	Acetaldehyde	15-27	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	114-136
19101651-1	2009	We analyzed an acetaldehyde-derived DNA adduct, N(2)-ethylidene-2"-deoxyguanosine (N(2)-Eti-dG) in stomach DNA of aldehyde dehydrogenase (Aldh)-2-knockout mice that were fed with alcohol to determine effects of alcohol consumption and Aldh2 genotype on the level of DNA damage in stomach.	Acetaldehyde	15-27	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	138-142
19110045-0	2009	Hesperidin inhibited acetaldehyde-induced matrix metalloproteinase-9 gene expression in human hepatocellular carcinoma cells.	Acetaldehyde	21-33	matrix metallopeptidase 9	Homo sapiens	42-68
19110045-1	2009	Previous studies have revealed that acetaldehyde-induced cell invasion and matrix metalloproteinase-9 (MMP-9) activation and are directly involved in hepatic tumorigenesis and metastasis.	Acetaldehyde	36-48	matrix metallopeptidase 9	Homo sapiens	75-101
19110045-1	2009	Previous studies have revealed that acetaldehyde-induced cell invasion and matrix metalloproteinase-9 (MMP-9) activation and are directly involved in hepatic tumorigenesis and metastasis.	Acetaldehyde	36-48	matrix metallopeptidase 9	Homo sapiens	103-108
19110045-6	2009	Hesperidin suppressed acetaldehyde-induced cell invasion and inhibited the secreted and cytosolic MMP-9 forms in HepG2 cells with acetaldehyde.	Acetaldehyde	130-142	matrix metallopeptidase 9	Homo sapiens	98-103
19110045-7	2009	Hesperidin suppressed acetaldehyde-induced MMP-9 expression through the inhibition of nuclear factor-kappaB (NF-kappaB) and AP-1, and suppressed acetaldehyde-stimulated NF-kappaB translocation into the nucleus through IkappaB inhibitory signaling pathways.	Acetaldehyde	22-34	matrix metallopeptidase 9	Homo sapiens	43-48
19110045-7	2009	Hesperidin suppressed acetaldehyde-induced MMP-9 expression through the inhibition of nuclear factor-kappaB (NF-kappaB) and AP-1, and suppressed acetaldehyde-stimulated NF-kappaB translocation into the nucleus through IkappaB inhibitory signaling pathways.	Acetaldehyde	22-34	Jun proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	124-128
19110045-8	2009	Hesperidin also inhibited acetaldehyde-induced AP-1 activity by the inhibitory phosphorylation of p38 kinase and c-Jun N-terminal kinase (JNK) signaling pathways.	Acetaldehyde	26-38	Jun proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	47-51
19110045-8	2009	Hesperidin also inhibited acetaldehyde-induced AP-1 activity by the inhibitory phosphorylation of p38 kinase and c-Jun N-terminal kinase (JNK) signaling pathways.	Acetaldehyde	26-38	mitogen-activated protein kinase 14	Homo sapiens	98-101
19110045-8	2009	Hesperidin also inhibited acetaldehyde-induced AP-1 activity by the inhibitory phosphorylation of p38 kinase and c-Jun N-terminal kinase (JNK) signaling pathways.	Acetaldehyde	26-38	mitogen-activated protein kinase 8	Homo sapiens	113-136
19110045-8	2009	Hesperidin also inhibited acetaldehyde-induced AP-1 activity by the inhibitory phosphorylation of p38 kinase and c-Jun N-terminal kinase (JNK) signaling pathways.	Acetaldehyde	26-38	mitogen-activated protein kinase 8	Homo sapiens	138-141
19110045-9	2009	Results from our study revealed that hesperidin suppressed both acetaldehyde-activated NF-kappaB and activator protein 1 (AP-1) activity by IkappaB, JNK, and p38 signaling pathways.	Acetaldehyde	64-76	mitogen-activated protein kinase 8	Homo sapiens	149-152
19110045-9	2009	Results from our study revealed that hesperidin suppressed both acetaldehyde-activated NF-kappaB and activator protein 1 (AP-1) activity by IkappaB, JNK, and p38 signaling pathways.	Acetaldehyde	64-76	mitogen-activated protein kinase 14	Homo sapiens	158-161
18304535-10	2009	Treatment with acetaldehyde resulted in a relative reduction of ALDH1 level in the myoma cells.	Acetaldehyde	15-27	aldehyde dehydrogenase 1 family member A1	Homo sapiens	64-69
18304535-12	2009	The reduced level of ADH1 and the increased level of ALDH1 proteins observed in myoma cell culture reduces the acetaldehyde level and thus may be involved in myoma cell growth.	Acetaldehyde	111-123	alcohol dehydrogenase 1A (class I), alpha polypeptide	Homo sapiens	21-25
18304535-12	2009	The reduced level of ADH1 and the increased level of ALDH1 proteins observed in myoma cell culture reduces the acetaldehyde level and thus may be involved in myoma cell growth.	Acetaldehyde	111-123	aldehyde dehydrogenase 1 family member A1	Homo sapiens	53-58
19113843-1	2009	The logic network composed of three enzymes (alcohol dehydrogenase, glucose dehydrogenase, and glucose oxidase) operating in concert as four concatenated logic gates (AND/OR), was designed to process four different chemical input signals (NADH, acetaldehyde, glucose, and oxygen).	Acetaldehyde	245-257	aldo-keto reductase family 1 member A1	Homo sapiens	45-66
19113843-1	2009	The logic network composed of three enzymes (alcohol dehydrogenase, glucose dehydrogenase, and glucose oxidase) operating in concert as four concatenated logic gates (AND/OR), was designed to process four different chemical input signals (NADH, acetaldehyde, glucose, and oxygen).	Acetaldehyde	245-257	hexose-6-phosphate dehydrogenase/glucose 1-dehydrogenase	Homo sapiens	68-89
19199308-0	2009	The proline-catalyzed double Mannich reaction of acetaldehyde with N-Boc imines.	Acetaldehyde	49-61	BOC cell adhesion associated, oncogene regulated	Homo sapiens	69-72
19124505-2	2009	Individuals homozygous for the 2 variant allele of aldehyde dehydrogenase 2 (ALDH2) are unable to metabolize acetaldehyde, which prevents them from alcohol drinking, whereas 1 2 have 6-fold higher blood acetaldehyde concentration postalcohol consumption with respect to 1 1.	Acetaldehyde	109-121	aldehyde dehydrogenase 2 family member	Homo sapiens	51-75
19124505-2	2009	Individuals homozygous for the 2 variant allele of aldehyde dehydrogenase 2 (ALDH2) are unable to metabolize acetaldehyde, which prevents them from alcohol drinking, whereas 1 2 have 6-fold higher blood acetaldehyde concentration postalcohol consumption with respect to 1 1.	Acetaldehyde	109-121	aldehyde dehydrogenase 2 family member	Homo sapiens	77-82
19124505-2	2009	Individuals homozygous for the 2 variant allele of aldehyde dehydrogenase 2 (ALDH2) are unable to metabolize acetaldehyde, which prevents them from alcohol drinking, whereas 1 2 have 6-fold higher blood acetaldehyde concentration postalcohol consumption with respect to 1 1.	Acetaldehyde	203-215	aldehyde dehydrogenase 2 family member	Homo sapiens	51-75
19124505-2	2009	Individuals homozygous for the 2 variant allele of aldehyde dehydrogenase 2 (ALDH2) are unable to metabolize acetaldehyde, which prevents them from alcohol drinking, whereas 1 2 have 6-fold higher blood acetaldehyde concentration postalcohol consumption with respect to 1 1.	Acetaldehyde	203-215	aldehyde dehydrogenase 2 family member	Homo sapiens	77-82
19199308-1	2009	Double-cross: Proline catalyzes the double Mannich reaction of acetaldehyde with N-Boc imines in excellent yields (up to 99 %; Boc = tert-butoxycarbonyl) and close to perfect diastereo- and enantioselectivities.	Acetaldehyde	63-75	BOC cell adhesion associated, oncogene regulated	Homo sapiens	83-86
19199308-1	2009	Double-cross: Proline catalyzes the double Mannich reaction of acetaldehyde with N-Boc imines in excellent yields (up to 99 %; Boc = tert-butoxycarbonyl) and close to perfect diastereo- and enantioselectivities.	Acetaldehyde	63-75	BOC cell adhesion associated, oncogene regulated	Homo sapiens	127-130
19164089-0	2009	Effect of the allelic variants of aldehyde dehydrogenase ALDH2*2 and alcohol dehydrogenase ADH1B*2 on blood acetaldehyde concentrations.	Acetaldehyde	108-120	aldehyde dehydrogenase 2 family member	Homo sapiens	57-62
19164089-0	2009	Effect of the allelic variants of aldehyde dehydrogenase ALDH2*2 and alcohol dehydrogenase ADH1B*2 on blood acetaldehyde concentrations.	Acetaldehyde	108-120	aldo-keto reductase family 1 member A1	Homo sapiens	69-90
19164089-6	2009	Here, we briefly review recent advances in genomic studies of human ADH/ALDH families and alcoholism, with an emphasis on the pharmacogenetic consequences of venous blood acetaldehyde in the different ALDH2 genotypes following the intake of various doses of ethanol.	Acetaldehyde	171-183	aldehyde dehydrogenase 2 family member	Homo sapiens	201-206
19164089-0	2009	Effect of the allelic variants of aldehyde dehydrogenase ALDH2*2 and alcohol dehydrogenase ADH1B*2 on blood acetaldehyde concentrations.	Acetaldehyde	108-120	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	91-96
19396661-3	2009	ADH and ALDH2 gene mutations provide an exceptional human model to estimate the long-term effects of acetaldehyde exposure in man.	Acetaldehyde	101-113	alcohol dehydrogenase 1A (class I), alpha polypeptide	Homo sapiens	0-3
19667493-3	2009	Many of the epidemiological studies have investigated genetic polymorphisms of alcohol dehydrogenase-1B (ADH1B) His48Arg and aldehyde dehydrogenase-2 (ALDH2) Glu504Lys, because of the strong impact these polymorphisms have on exposure to and accumulation of acetaldehyde.	Acetaldehyde	258-270	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	79-103
19667493-3	2009	Many of the epidemiological studies have investigated genetic polymorphisms of alcohol dehydrogenase-1B (ADH1B) His48Arg and aldehyde dehydrogenase-2 (ALDH2) Glu504Lys, because of the strong impact these polymorphisms have on exposure to and accumulation of acetaldehyde.	Acetaldehyde	258-270	aldehyde dehydrogenase 2 family member	Homo sapiens	125-149
19667493-3	2009	Many of the epidemiological studies have investigated genetic polymorphisms of alcohol dehydrogenase-1B (ADH1B) His48Arg and aldehyde dehydrogenase-2 (ALDH2) Glu504Lys, because of the strong impact these polymorphisms have on exposure to and accumulation of acetaldehyde.	Acetaldehyde	258-270	aldehyde dehydrogenase 2 family member	Homo sapiens	151-156
20183527-2	2009	CYP2E1 is also one of the enzymes that metabolizes ethanol to acetaldehyde, and is induced by recent ethanol ingestion.	Acetaldehyde	62-74	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	0-6
19756185-4	2009	The increased ethanol metabolism, in turn, leads to alteration of the redox balance of the cells and impairment of RXR/PPAR functions by direct and indirect effects of acetaldehyde, resulting in deranged lipid metabolism, oxidative stress, and release of proinflammatory cytokines.	Acetaldehyde	168-180	retinoid X receptor alpha	Homo sapiens	115-118
19756185-4	2009	The increased ethanol metabolism, in turn, leads to alteration of the redox balance of the cells and impairment of RXR/PPAR functions by direct and indirect effects of acetaldehyde, resulting in deranged lipid metabolism, oxidative stress, and release of proinflammatory cytokines.	Acetaldehyde	168-180	peroxisome proliferator activated receptor alpha	Homo sapiens	119-123
19396661-3	2009	ADH and ALDH2 gene mutations provide an exceptional human model to estimate the long-term effects of acetaldehyde exposure in man.	Acetaldehyde	101-113	aldehyde dehydrogenase 2 family member	Homo sapiens	8-13
19396661-11	2009	Screening of the risk groups with enhanced acetaldehyde exposure, e.g. people with ADH and ALDH2 gene polymorphisms and hypochlorhydric atrophic gastritis, should also be seriously considered.	Acetaldehyde	43-55	alcohol dehydrogenase 1A (class I), alpha polypeptide	Homo sapiens	83-86
19396661-11	2009	Screening of the risk groups with enhanced acetaldehyde exposure, e.g. people with ADH and ALDH2 gene polymorphisms and hypochlorhydric atrophic gastritis, should also be seriously considered.	Acetaldehyde	43-55	aldehyde dehydrogenase 2 family member	Homo sapiens	91-96
19013301-0	2008	Phytophenols in whisky lower blood acetaldehyde level by depressing alcohol metabolism through inhibition of alcohol dehydrogenase 1 (class I) in mice.	Acetaldehyde	35-47	alcohol dehydrogenase 1 (class I)	Mus musculus	109-132
18673087-3	2008	Using lentivirus-derived particles to regulate the bone morphogenetic protein-2 (BMP-2) gene expression in a pristinamycin- or gaseous acetaldehyde-inducible manner, we demonstrated the adjustment of cardiomyocyte electrophysiological characteristics.	Acetaldehyde	135-147	bone morphogenetic protein 2	Rattus norvegicus	51-79
18673087-3	2008	Using lentivirus-derived particles to regulate the bone morphogenetic protein-2 (BMP-2) gene expression in a pristinamycin- or gaseous acetaldehyde-inducible manner, we demonstrated the adjustment of cardiomyocyte electrophysiological characteristics.	Acetaldehyde	135-147	bone morphogenetic protein 2	Rattus norvegicus	81-86
19036170-0	2008	Modification of carbonic anhydrase II with acetaldehyde, the first metabolite of ethanol, leads to decreased enzyme activity.	Acetaldehyde	43-55	carbonic anhydrase 2	Homo sapiens	16-37
19036170-4	2008	RESULTS: Acetaldehyde treatment in the absence and presence of a reducing agent (NaBH3(CN)) caused shifts in the pI values of CA II.	Acetaldehyde	9-21	carbonic anhydrase 2	Homo sapiens	126-131
19036170-7	2008	Mass spectra of CA II treated with acetaldehyde revealed a modified protein form (+26 Da), consistent with a "Schiff base" formation between acetaldehyde and one of the primary NH2 groups (e.g., in lysine side chain) in the protein structure.	Acetaldehyde	35-47	carbonic anhydrase 2	Homo sapiens	16-21
19036170-7	2008	Mass spectra of CA II treated with acetaldehyde revealed a modified protein form (+26 Da), consistent with a "Schiff base" formation between acetaldehyde and one of the primary NH2 groups (e.g., in lysine side chain) in the protein structure.	Acetaldehyde	141-153	carbonic anhydrase 2	Homo sapiens	16-21
19036170-9	2008	In reducing conditions, each CA II molecule had reacted with 9-19 (14 on average) acetaldehyde molecules (+28 Da), consistent with further reduction of the "Schiff bases" to substituted amines (N-ethyllysine residues).	Acetaldehyde	82-94	carbonic anhydrase 2	Homo sapiens	29-34
19036170-11	2008	CONCLUSION: The acetaldehyde-derived modifications in CA II molecule may have physiological consequences in alcoholic patients.	Acetaldehyde	16-28	carbonic anhydrase 2	Homo sapiens	54-59
19013301-0	2008	Phytophenols in whisky lower blood acetaldehyde level by depressing alcohol metabolism through inhibition of alcohol dehydrogenase 1 (class I) in mice.	Acetaldehyde	35-47	ATPase, aminophospholipid transporter (APLT), class I, type 8A, member 1	Mus musculus	134-141
19013301-3	2008	In this study, administration of the nonvolatile fraction of whisky was found to lower the concentration of acetaldehyde in the blood of mice by depressing alcohol metabolism through the inhibition of liver alcohol dehydrogenase (ADH).	Acetaldehyde	108-120	aldo-keto reductase family 1, member A1 (aldehyde reductase)	Mus musculus	207-228
19013301-3	2008	In this study, administration of the nonvolatile fraction of whisky was found to lower the concentration of acetaldehyde in the blood of mice by depressing alcohol metabolism through the inhibition of liver alcohol dehydrogenase (ADH).	Acetaldehyde	108-120	aldo-keto reductase family 1, member A1 (aldehyde reductase)	Mus musculus	230-233
19013301-8	2008	Thus, it was demonstrated that the enhanced inhibition of liver ADH 1 due to the increased amounts of these phytophenols in mature whisky caused the depression of alcohol metabolism and a consequent lowering of blood acetaldehyde level.	Acetaldehyde	217-229	alcohol dehydrogenase 1 (class I)	Mus musculus	64-69
18554307-3	2008	Acetaldehyde induces BTN2 transcription in laboratory strains.	Acetaldehyde	0-12	Btn2p	Saccharomyces cerevisiae S288C	21-25
18554307-5	2008	The BTN2 gene shows a complex expression pattern in wine yeast, increasing its expression by acetaldehyde, but repressing it by ethanol.	Acetaldehyde	93-105	Btn2p	Saccharomyces cerevisiae S288C	4-8
18587667-1	2008	RATIONALE: Considerable evidence indicates that brain ethanol metabolism mediated by catalase is involved in modulating some of the behavioral and physiological effects of this drug, which suggests that the first metabolite of ethanol, acetaldehyde, may have central actions.	Acetaldehyde	236-248	catalase	Rattus norvegicus	85-93
18587667-8	2008	CONCLUSIONS: Thus, when cerebral metabolism of ethanol into acetaldehyde is blocked by catalase inhibitors, or acetaldehyde is inactivated, there is a suppressive effect on the anxiolytic actions of ethanol.	Acetaldehyde	60-72	catalase	Rattus norvegicus	87-95
18703563-3	2008	Experiments were designed to evaluate the influence of ethanol (EtOH), lipopolysaccharide (LPS), and acetaldehyde (ACA) on OPN and PPAR-alpha expression levels in vivo (rats and mice) and in vitro (hepatocytes and biliary epithelium).	Acetaldehyde	101-113	secreted phosphoprotein 1	Mus musculus	123-126
18703563-3	2008	Experiments were designed to evaluate the influence of ethanol (EtOH), lipopolysaccharide (LPS), and acetaldehyde (ACA) on OPN and PPAR-alpha expression levels in vivo (rats and mice) and in vitro (hepatocytes and biliary epithelium).	Acetaldehyde	101-113	peroxisome proliferator activated receptor alpha	Rattus norvegicus	131-141
18703563-3	2008	Experiments were designed to evaluate the influence of ethanol (EtOH), lipopolysaccharide (LPS), and acetaldehyde (ACA) on OPN and PPAR-alpha expression levels in vivo (rats and mice) and in vitro (hepatocytes and biliary epithelium).	Acetaldehyde	115-118	secreted phosphoprotein 1	Mus musculus	123-126
18703563-3	2008	Experiments were designed to evaluate the influence of ethanol (EtOH), lipopolysaccharide (LPS), and acetaldehyde (ACA) on OPN and PPAR-alpha expression levels in vivo (rats and mice) and in vitro (hepatocytes and biliary epithelium).	Acetaldehyde	115-118	peroxisome proliferator activated receptor alpha	Rattus norvegicus	131-141
18616675-0	2008	Salivary acetaldehyde concentration according to alcoholic beverage consumed and aldehyde dehydrogenase-2 genotype.	Acetaldehyde	9-21	aldehyde dehydrogenase 2 family member	Homo sapiens	81-105
19061187-3	2008	We focused on six of these genes required for acetaldehyde tolerance, ZWF1, GND1, RPE1, TKL1 and TAL1, which encode enzymes in the pentose phosphate pathway (PPP), and OAR1, which encodes for NADPH-dependent 3-oxoacyl-(acyl-carrier-protein) reductase.	Acetaldehyde	46-58	glucose-6-phosphate dehydrogenase	Saccharomyces cerevisiae S288C	70-74
19061187-3	2008	We focused on six of these genes required for acetaldehyde tolerance, ZWF1, GND1, RPE1, TKL1 and TAL1, which encode enzymes in the pentose phosphate pathway (PPP), and OAR1, which encodes for NADPH-dependent 3-oxoacyl-(acyl-carrier-protein) reductase.	Acetaldehyde	46-58	ribulose-phosphate 3-epimerase RPE1	Saccharomyces cerevisiae S288C	82-86
19061187-3	2008	We focused on six of these genes required for acetaldehyde tolerance, ZWF1, GND1, RPE1, TKL1 and TAL1, which encode enzymes in the pentose phosphate pathway (PPP), and OAR1, which encodes for NADPH-dependent 3-oxoacyl-(acyl-carrier-protein) reductase.	Acetaldehyde	46-58	transketolase TKL1	Saccharomyces cerevisiae S288C	88-92
19061187-3	2008	We focused on six of these genes required for acetaldehyde tolerance, ZWF1, GND1, RPE1, TKL1 and TAL1, which encode enzymes in the pentose phosphate pathway (PPP), and OAR1, which encodes for NADPH-dependent 3-oxoacyl-(acyl-carrier-protein) reductase.	Acetaldehyde	46-58	sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate transaldolase TAL1	Saccharomyces cerevisiae S288C	97-101
19061187-3	2008	We focused on six of these genes required for acetaldehyde tolerance, ZWF1, GND1, RPE1, TKL1 and TAL1, which encode enzymes in the pentose phosphate pathway (PPP), and OAR1, which encodes for NADPH-dependent 3-oxoacyl-(acyl-carrier-protein) reductase.	Acetaldehyde	46-58	3-oxoacyl-[acyl-carrier-protein] reductase (NADPH)	Saccharomyces cerevisiae S288C	168-172
18797246-8	2008	In addition, our data suggest that brain structures that, as the ArcN, are rich in catalase may support the formation of ethanol-derived pharmacologically relevant concentrations of acetaldehyde and, thus be of particular importance for the behavioral effects of ethanol.	Acetaldehyde	182-194	catalase	Rattus norvegicus	83-91
19141570-10	2008	The powerful carcinogenesis caused by these halohydrocarbons may have been caused by excessive and metabolically unresolved acetaldehyde (AC) which is directly generated by Cyp2E1 in the oxidative elimination of CE.	Acetaldehyde	124-136	cytochrome P450, family 2, subfamily e, polypeptide 1	Mus musculus	173-179
19141570-10	2008	The powerful carcinogenesis caused by these halohydrocarbons may have been caused by excessive and metabolically unresolved acetaldehyde (AC) which is directly generated by Cyp2E1 in the oxidative elimination of CE.	Acetaldehyde	138-140	cytochrome P450, family 2, subfamily e, polypeptide 1	Mus musculus	173-179
18974956-7	2008	Cells treated with sulfite generated more than 70% of acetaldehyde than untreated cells, suggesting that the increased acetaldehyde production is correlated with the induction of PDC1 gene encoding pyruvate decarboxylase.	Acetaldehyde	54-66	indolepyruvate decarboxylase 1	Saccharomyces cerevisiae S288C	179-183
18974956-7	2008	Cells treated with sulfite generated more than 70% of acetaldehyde than untreated cells, suggesting that the increased acetaldehyde production is correlated with the induction of PDC1 gene encoding pyruvate decarboxylase.	Acetaldehyde	119-131	indolepyruvate decarboxylase 1	Saccharomyces cerevisiae S288C	179-183
18704003-1	2008	OBJECTIVE: The polymorphism of aldehyde dehydrogenase 2 (ALDH2), denoted ALDH2*2, is very common in East Asian countries, and the mutated ALDH2 protein derived from ALDH2*2 lacks the ability of acetaldehyde metabolization.	Acetaldehyde	194-206	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	31-55
18704003-1	2008	OBJECTIVE: The polymorphism of aldehyde dehydrogenase 2 (ALDH2), denoted ALDH2*2, is very common in East Asian countries, and the mutated ALDH2 protein derived from ALDH2*2 lacks the ability of acetaldehyde metabolization.	Acetaldehyde	194-206	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	57-62
18704003-1	2008	OBJECTIVE: The polymorphism of aldehyde dehydrogenase 2 (ALDH2), denoted ALDH2*2, is very common in East Asian countries, and the mutated ALDH2 protein derived from ALDH2*2 lacks the ability of acetaldehyde metabolization.	Acetaldehyde	194-206	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	73-78
18704003-1	2008	OBJECTIVE: The polymorphism of aldehyde dehydrogenase 2 (ALDH2), denoted ALDH2*2, is very common in East Asian countries, and the mutated ALDH2 protein derived from ALDH2*2 lacks the ability of acetaldehyde metabolization.	Acetaldehyde	194-206	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	73-78
18704003-1	2008	OBJECTIVE: The polymorphism of aldehyde dehydrogenase 2 (ALDH2), denoted ALDH2*2, is very common in East Asian countries, and the mutated ALDH2 protein derived from ALDH2*2 lacks the ability of acetaldehyde metabolization.	Acetaldehyde	194-206	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	73-78
18616675-11	2008	The values after subtracting the blood acetaldehyde concentration from the salivary acetaldehyde concentration were also higher in the ALDH2 heterozygotes than in the ALDH2 homozygotes.	Acetaldehyde	39-51	aldehyde dehydrogenase 2 family member	Homo sapiens	135-140
18616675-11	2008	The values after subtracting the blood acetaldehyde concentration from the salivary acetaldehyde concentration were also higher in the ALDH2 heterozygotes than in the ALDH2 homozygotes.	Acetaldehyde	39-51	aldehyde dehydrogenase 2 family member	Homo sapiens	167-172
18616675-11	2008	The values after subtracting the blood acetaldehyde concentration from the salivary acetaldehyde concentration were also higher in the ALDH2 heterozygotes than in the ALDH2 homozygotes.	Acetaldehyde	84-96	aldehyde dehydrogenase 2 family member	Homo sapiens	135-140
18616675-11	2008	The values after subtracting the blood acetaldehyde concentration from the salivary acetaldehyde concentration were also higher in the ALDH2 heterozygotes than in the ALDH2 homozygotes.	Acetaldehyde	84-96	aldehyde dehydrogenase 2 family member	Homo sapiens	167-172
18616675-12	2008	CONCLUSIONS: There are differences in exposure of the UADT to high salivary acetaldehyde concentrations according to the type of alcoholic beverage and ALDH2 genotype, and the differences partly explain the differences in the cancer susceptibility of the UADT according to alcoholic beverage and ALDH2 genotype.	Acetaldehyde	76-88	aldehyde dehydrogenase 2 family member	Homo sapiens	152-157
18616675-12	2008	CONCLUSIONS: There are differences in exposure of the UADT to high salivary acetaldehyde concentrations according to the type of alcoholic beverage and ALDH2 genotype, and the differences partly explain the differences in the cancer susceptibility of the UADT according to alcoholic beverage and ALDH2 genotype.	Acetaldehyde	76-88	aldehyde dehydrogenase 2 family member	Homo sapiens	296-301
18505683-5	2008	Ethanol is metabolized to acetaldehyde by alcohol dehydrogenase (ADH).	Acetaldehyde	26-38	aldo-keto reductase family 1 member A1	Homo sapiens	42-63
18505683-5	2008	Ethanol is metabolized to acetaldehyde by alcohol dehydrogenase (ADH).	Acetaldehyde	26-38	aldo-keto reductase family 1 member A1	Homo sapiens	65-68
18505683-11	2008	In addition significant differences of ADH isoenzymes activities between cancer tissues and healthy organs may be a factor intensifying carcinogenesis by the increased ability to acetaldehyde formation from ethanol and disorders in metabolism of some biologically important substances (e.g. retinoic acid).	Acetaldehyde	179-191	aldo-keto reductase family 1 member A1	Homo sapiens	39-42
17952619-9	2008	IL-6 expression decreased significantly in acetaldehyde-pentoxifylline-treated cells.	Acetaldehyde	43-55	interleukin 6	Rattus norvegicus	0-4
18599023-4	2008	More importantly, the major enzymes of ethanol detoxification; alcohol dehydrogenase, aldehyde dehydrogenase, and cytochrome P4502E1, remained active and PCLS readily metabolized ethanol and produced acetaldehyde.	Acetaldehyde	200-212	aldo-keto reductase family 1 member A1	Rattus norvegicus	63-84
18224440-1	2008	BACKGROUND: Alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH), which are most abundant in the liver, are the main enzymes involved in ethanol and acetaldehyde metabolism.	Acetaldehyde	158-170	aldo-keto reductase family 1 member A1	Homo sapiens	12-33
18224440-1	2008	BACKGROUND: Alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH), which are most abundant in the liver, are the main enzymes involved in ethanol and acetaldehyde metabolism.	Acetaldehyde	158-170	aldo-keto reductase family 1 member A1	Homo sapiens	35-38
17952619-10	2008	Acetaldehyde-treated cells pretreated with an anti-IL-6 monoclonal antibody did not show any increase in alpha (I) collagen expression.	Acetaldehyde	0-12	interleukin 6	Rattus norvegicus	51-55
17952619-14	2008	IkappaBalpha protein level decreased 50% in acetaldehyde-treated cells, while acetaldehyde-pentoxifylline-treated cells showed IkappaBalpha control cells value.	Acetaldehyde	44-56	NFKB inhibitor alpha	Rattus norvegicus	0-12
17952619-14	2008	IkappaBalpha protein level decreased 50% in acetaldehyde-treated cells, while acetaldehyde-pentoxifylline-treated cells showed IkappaBalpha control cells value.	Acetaldehyde	78-90	NFKB inhibitor alpha	Rattus norvegicus	127-139
17952619-15	2008	The data suggest that acetaldehyde induced alpha(I) collagen and IL-6 expression via NFkappaB activation.	Acetaldehyde	22-34	interleukin 6	Rattus norvegicus	65-69
17952619-16	2008	Pentoxifylline prevents acetaldehyde-induced alpha(I) collagen and IL-6 expression by a mechanism dependent on IkappaBalpha degradation, which in turn blocks NFkappaB activation.	Acetaldehyde	24-36	interleukin 6	Rattus norvegicus	67-71
17952619-16	2008	Pentoxifylline prevents acetaldehyde-induced alpha(I) collagen and IL-6 expression by a mechanism dependent on IkappaBalpha degradation, which in turn blocks NFkappaB activation.	Acetaldehyde	24-36	NFKB inhibitor alpha	Rattus norvegicus	111-123
18377926-2	2008	This study examined the impact of augmented acetaldehyde exposure on myocardial function, geometry, and insulin signaling via cardiac-specific overexpression of alcohol dehydrogenase (ADH).	Acetaldehyde	44-56	aldo-keto reductase family 1, member A1 (aldehyde reductase)	Mus musculus	161-182
18552233-5	2008	The role of ACS in destroying fermentative intermediates is supported by the increased sensitivity of the acs1 mutant to exogenous acetate, ethanol, and acetaldehyde compared to wild-type plants.	Acetaldehyde	153-165	acetyl-CoA synthetase	Arabidopsis thaliana	12-15
18552233-5	2008	The role of ACS in destroying fermentative intermediates is supported by the increased sensitivity of the acs1 mutant to exogenous acetate, ethanol, and acetaldehyde compared to wild-type plants.	Acetaldehyde	153-165	ACC synthase 1	Arabidopsis thaliana	106-110
18385209-5	2008	Chloroethane is eliminated from the body by pulmonary exhalation and metabolically by oxidation via cytochrome P-450 (likely producing acetaldehyde) and conjugation with glutathione (GSH).	Acetaldehyde	135-147	cytochrome P450, family 21, subfamily a, polypeptide 1	Mus musculus	100-116
18377926-13	2008	These data suggest that elevated cardiac acetaldehyde exposure via ADH may exacerbate alcohol-induced myocardial dysfunction, hypertrophy, insulin insensitivity and ER stress, indicating a key role of ADH gene in alcohol-induced cardiac dysfunction and insulin resistance.	Acetaldehyde	41-53	aldo-keto reductase family 1, member A1 (aldehyde reductase)	Mus musculus	67-70
18377926-13	2008	These data suggest that elevated cardiac acetaldehyde exposure via ADH may exacerbate alcohol-induced myocardial dysfunction, hypertrophy, insulin insensitivity and ER stress, indicating a key role of ADH gene in alcohol-induced cardiac dysfunction and insulin resistance.	Acetaldehyde	41-53	aldo-keto reductase family 1, member A1 (aldehyde reductase)	Mus musculus	201-204
18482162-10	2008	Acetaldehyde also induced nonubiquitinated FANCD2 protein, and we were able to demonstrate the ability of acetaldehyde to generate DNA double strand breaks, lesions which normally induce ubiquitination of FANCD2.	Acetaldehyde	0-12	FA complementation group D2	Homo sapiens	43-49
18482162-10	2008	Acetaldehyde also induced nonubiquitinated FANCD2 protein, and we were able to demonstrate the ability of acetaldehyde to generate DNA double strand breaks, lesions which normally induce ubiquitination of FANCD2.	Acetaldehyde	0-12	FA complementation group D2	Homo sapiens	205-211
18482162-10	2008	Acetaldehyde also induced nonubiquitinated FANCD2 protein, and we were able to demonstrate the ability of acetaldehyde to generate DNA double strand breaks, lesions which normally induce ubiquitination of FANCD2.	Acetaldehyde	106-118	FA complementation group D2	Homo sapiens	205-211
18377926-2	2008	This study examined the impact of augmented acetaldehyde exposure on myocardial function, geometry, and insulin signaling via cardiac-specific overexpression of alcohol dehydrogenase (ADH).	Acetaldehyde	44-56	aldo-keto reductase family 1, member A1 (aldehyde reductase)	Mus musculus	184-187
17932766-0	2008	Captopril and lisinopril decrease acetaldehyde effects upon the prothrombin time.	Acetaldehyde	34-46	coagulation factor II, thrombin	Homo sapiens	64-75
18702345-3	2008	Formation and degradation of acetaldehyde in the body is modified by activity of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH).	Acetaldehyde	29-41	aldo-keto reductase family 1 member A1	Homo sapiens	81-102
18702345-3	2008	Formation and degradation of acetaldehyde in the body is modified by activity of alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH).	Acetaldehyde	29-41	aldo-keto reductase family 1 member A1	Homo sapiens	104-107
18439018-7	2008	The presence of alanine, threonine, or serine promoted furan formation by the recombination of C(2) fragments, such as acetaldehyde and glycolaldehyde, which may originate from both sugars and amino acids.	Acetaldehyde	119-131	complement C2	Homo sapiens	95-99
18201725-1	2008	A functional polymorphism of mitochondrial aldehyde dehydrogenase gene (ALDH2 1/2 polymorphism) can influence the accumulation of acetaldehyde which may have a role in Alzheimer"s disease (AD), and is widely prevalent among Mongoloids.	Acetaldehyde	130-142	aldehyde dehydrogenase 2 family member	Homo sapiens	72-81
17932768-0	2008	Effect of acetaldehyde upon cathepsin G and chymase.	Acetaldehyde	10-22	cathepsin G	Homo sapiens	28-51
17932768-5	2008	We report here the results of a study on the effect of acetaldehyde upon cathepsin G and mast cell chymase.	Acetaldehyde	55-67	cathepsin G	Homo sapiens	73-84
17932768-5	2008	We report here the results of a study on the effect of acetaldehyde upon cathepsin G and mast cell chymase.	Acetaldehyde	55-67	chymase 1	Homo sapiens	99-106
17932768-6	2008	Acetaldehyde enhanced cathepsin G activity at all of the concentrations tested between 11.2 and 223.5 mM in a statistically significant manner.	Acetaldehyde	0-12	cathepsin G	Homo sapiens	22-33
17932768-7	2008	Since cathepsin G is one of several enzymes transforming ANG I into ANG II and is also capable of cleaving ANG II directly from angiotensinogen, we suggest that alcoholism, which will generate exogenous acetaldehyde from ingested alcohol, may be a contributory factor for an elevated cathepsin G activity and, consequently, hypertension via the NRAS.	Acetaldehyde	203-215	cathepsin G	Homo sapiens	6-17
17932768-7	2008	Since cathepsin G is one of several enzymes transforming ANG I into ANG II and is also capable of cleaving ANG II directly from angiotensinogen, we suggest that alcoholism, which will generate exogenous acetaldehyde from ingested alcohol, may be a contributory factor for an elevated cathepsin G activity and, consequently, hypertension via the NRAS.	Acetaldehyde	203-215	cathepsin G	Homo sapiens	284-295
17932768-8	2008	Chymase activity also is elevated in the presence of 440 mM acetaldehyde and diminished in the presence of 27 mM acetaldehyde.	Acetaldehyde	60-72	chymase 1	Homo sapiens	0-7
17932768-8	2008	Chymase activity also is elevated in the presence of 440 mM acetaldehyde and diminished in the presence of 27 mM acetaldehyde.	Acetaldehyde	113-125	chymase 1	Homo sapiens	0-7
18395094-6	2008	Nrf2(-/-) mice showed a significantly reduced ability to detoxify acetaldehyde, leading to an accumulation of the toxic metabolite.	Acetaldehyde	66-78	nuclear factor, erythroid derived 2, like 2	Mus musculus	0-4
18653909-18	2008	INTERPRETATION &amp; CONCLUSION: PartySmart enhanced acetaldehyde metabolism by increasing ADH and ALDH activity without any side effects.	Acetaldehyde	53-65	alcohol dehydrogenase 1C (class I), gamma polypeptide	Rattus norvegicus	91-94
18653909-18	2008	INTERPRETATION &amp; CONCLUSION: PartySmart enhanced acetaldehyde metabolism by increasing ADH and ALDH activity without any side effects.	Acetaldehyde	53-65	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	99-103
18705328-0	2008	Effect of interferon-gamma on hepatic stellate cells stimulated by acetaldehyde.	Acetaldehyde	67-79	interferon gamma	Homo sapiens	10-26
18705328-2	2008	Although, it is considered that IFN-gamma inhibits the transcription of matrix, it has not been well defined whether IFN-gamma could inhibit the expression of matrix induced by acetaldehyde in METHODOLOGY: HSC were divided into 5 groups, 4 groups were treated with different doses (0, 1000, 1500, 2000 IU/mL) of IFN-gamma and acetaldehyde (200pM) for 24 and 48 h. For the control group, HSC were treated only with medium.	Acetaldehyde	177-189	interferon gamma	Homo sapiens	117-126
18705328-2	2008	Although, it is considered that IFN-gamma inhibits the transcription of matrix, it has not been well defined whether IFN-gamma could inhibit the expression of matrix induced by acetaldehyde in METHODOLOGY: HSC were divided into 5 groups, 4 groups were treated with different doses (0, 1000, 1500, 2000 IU/mL) of IFN-gamma and acetaldehyde (200pM) for 24 and 48 h. For the control group, HSC were treated only with medium.	Acetaldehyde	177-189	interferon gamma	Homo sapiens	117-126
18705328-7	2008	CONCLUSIONS: The present data indicated that IFN-gamma could inhibit the collagen expression in HSC stimulated by acetaldehyde.	Acetaldehyde	114-126	interferon gamma	Homo sapiens	45-54
18705328-8	2008	IFN-gamma could down-regulate the TGF-beta1, Smad4 and especially TGFbetaRI in HSC after acetaldehyde stimulation.	Acetaldehyde	89-101	interferon gamma	Homo sapiens	0-9
18705328-8	2008	IFN-gamma could down-regulate the TGF-beta1, Smad4 and especially TGFbetaRI in HSC after acetaldehyde stimulation.	Acetaldehyde	89-101	transforming growth factor beta 1	Homo sapiens	34-43
18705328-8	2008	IFN-gamma could down-regulate the TGF-beta1, Smad4 and especially TGFbetaRI in HSC after acetaldehyde stimulation.	Acetaldehyde	89-101	SMAD family member 4	Homo sapiens	45-50
18705328-8	2008	IFN-gamma could down-regulate the TGF-beta1, Smad4 and especially TGFbetaRI in HSC after acetaldehyde stimulation.	Acetaldehyde	89-101	transforming growth factor beta receptor 1	Homo sapiens	66-75
18705328-9	2008	This experiment showed 1000, 1500, 2000 IU/mL IFN-gamma were effective and safe to down-regulate the extracellular matrix induced by acetaldehyde in vitro.	Acetaldehyde	133-145	interferon gamma	Homo sapiens	46-55
18288105-5	2008	Here we show that acetaldehyde is a powerful nucleophile in asymmetric, proline-catalysed Mannich reactions with N-tert-butoxycarbonyl (N-Boc)-imines, yielding beta-amino aldehydes with extremely high enantioselectivities-desirable products as drug intermediates and in the synthesis of other biologically active molecules.	Acetaldehyde	18-30	BOC cell adhesion associated, oncogene regulated	Homo sapiens	138-141
18242117-0	2008	Acetaldehyde-induced mutational pattern in the tumour suppressor gene TP53 analysed by use of a functional assay, the FASAY (functional analysis of separated alleles in yeast).	Acetaldehyde	0-12	tumor protein p53	Homo sapiens	70-74
18242117-2	2008	Whereas alcohol as such is not thought to be directly carcinogenic, acetaldehyde, its first metabolite, has been proven genotoxic and mutagenic in the HPRT gene.	Acetaldehyde	68-80	hypoxanthine phosphoribosyltransferase 1	Homo sapiens	151-155
18242117-3	2008	As mutations in the tumour suppressor gene TP53 are the most common genetic alterations involved in human cancers, especially esophageal tumours, the aim of this work was to establish the mutational pattern induced by acetaldehyde in vitro on the TP53 gene, and to compare this pattern with that found in human alcohol-related tumours.	Acetaldehyde	218-230	tumor protein p53	Homo sapiens	43-47
18242117-3	2008	As mutations in the tumour suppressor gene TP53 are the most common genetic alterations involved in human cancers, especially esophageal tumours, the aim of this work was to establish the mutational pattern induced by acetaldehyde in vitro on the TP53 gene, and to compare this pattern with that found in human alcohol-related tumours.	Acetaldehyde	218-230	tumor protein p53	Homo sapiens	247-251
18242117-10	2008	These results support the notion that acetaldehyde plays a role in TP53 mutations in esophageal cancers.	Acetaldehyde	38-50	tumor protein p53	Homo sapiens	67-71
18155096-2	2008	The present research addressed the hypothesis that catalase-dependent metabolism of ethanol to acetaldehyde in the brain is an important step in the production of ethanol-related affective properties.	Acetaldehyde	95-107	catalase	Mus musculus	51-59
18155096-9	2008	Taken together, the results of the present study indicate that the brain catalase-H(2)O(2) system contributes to the acquisition of affective-dependent learning induced by ethanol, and support the involvement of centrally-formed acetaldehyde in the formation of positive affective memories produced by ethanol.	Acetaldehyde	229-241	catalase	Mus musculus	73-81
18252249-4	2008	For D. melanogaster MalE-ALDH the K(M) of the putative in vivo substrate acetaldehyde was 0.9 microM while for NAD+, a K(M) of 62.7 microM was determined.	Acetaldehyde	73-85	Aldehyde dehydrogenase	Drosophila melanogaster	25-29
18056758-2	2008	Alcohol dehydrogenase (ADH) converts alcohol to acetaldehyde, and aldehyde dehydrogenase (ALDH) converts acetaldehyde to acetate.	Acetaldehyde	48-60	aldo-keto reductase family 1 member A1	Homo sapiens	0-21
18056758-2	2008	Alcohol dehydrogenase (ADH) converts alcohol to acetaldehyde, and aldehyde dehydrogenase (ALDH) converts acetaldehyde to acetate.	Acetaldehyde	48-60	aldo-keto reductase family 1 member A1	Homo sapiens	23-26
18056758-2	2008	Alcohol dehydrogenase (ADH) converts alcohol to acetaldehyde, and aldehyde dehydrogenase (ALDH) converts acetaldehyde to acetate.	Acetaldehyde	105-117	aldo-keto reductase family 1 member A1	Homo sapiens	0-21
18056758-2	2008	Alcohol dehydrogenase (ADH) converts alcohol to acetaldehyde, and aldehyde dehydrogenase (ALDH) converts acetaldehyde to acetate.	Acetaldehyde	105-117	aldo-keto reductase family 1 member A1	Homo sapiens	23-26
18056758-3	2008	The well-known genetic polymorphisms in ADH1B(His47Arg) and ALDH2(Glu487Lys) have dramatic effects on the rate of metabolizing alcohol and acetaldehyde, respectively.	Acetaldehyde	139-151	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	40-45
18056758-3	2008	The well-known genetic polymorphisms in ADH1B(His47Arg) and ALDH2(Glu487Lys) have dramatic effects on the rate of metabolizing alcohol and acetaldehyde, respectively.	Acetaldehyde	139-151	aldehyde dehydrogenase 2 family member	Homo sapiens	60-65
18056758-4	2008	The protective allele of ADH1B (ADH1B*47His) encodes for a rapid ethanol-metabolizing enzyme, and the susceptible allele of the ALDH2 (ALDH2*487Lys) is strongly associated with decreased rate of metabolizing acetaldehyde.	Acetaldehyde	208-220	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	25-30
18056758-4	2008	The protective allele of ADH1B (ADH1B*47His) encodes for a rapid ethanol-metabolizing enzyme, and the susceptible allele of the ALDH2 (ALDH2*487Lys) is strongly associated with decreased rate of metabolizing acetaldehyde.	Acetaldehyde	208-220	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	32-37
18056758-4	2008	The protective allele of ADH1B (ADH1B*47His) encodes for a rapid ethanol-metabolizing enzyme, and the susceptible allele of the ALDH2 (ALDH2*487Lys) is strongly associated with decreased rate of metabolizing acetaldehyde.	Acetaldehyde	208-220	aldehyde dehydrogenase 2 family member	Homo sapiens	128-133
18056758-4	2008	The protective allele of ADH1B (ADH1B*47His) encodes for a rapid ethanol-metabolizing enzyme, and the susceptible allele of the ALDH2 (ALDH2*487Lys) is strongly associated with decreased rate of metabolizing acetaldehyde.	Acetaldehyde	208-220	aldehyde dehydrogenase 2 family member	Homo sapiens	135-140
17991733-3	2008	EGF-mediated prevention of acetaldehyde-induced decrease in transepithelial electrical resistance and an increase in inulin permeability, and subcellular redistribution of occludin and ZO-1 was attenuated by reduced expression of PLCgamma1 by short hairpin RNA.	Acetaldehyde	27-39	tight junction protein 1	Homo sapiens	185-189
18003597-0	2008	PPARalpha and PPARbeta are differentially affected by ethanol and the ethanol metabolite acetaldehyde in the MCF-7 breast cancer cell line.	Acetaldehyde	89-101	peroxisome proliferator activated receptor alpha	Homo sapiens	0-9
18003597-0	2008	PPARalpha and PPARbeta are differentially affected by ethanol and the ethanol metabolite acetaldehyde in the MCF-7 breast cancer cell line.	Acetaldehyde	89-101	peroxisome proliferator activated receptor delta	Homo sapiens	14-22
18003597-3	2008	Using the MCF-7 breast cancer cell line, we examined the relationship between ethanol and its metabolite acetaldehyde on PPARalpha and PPARbeta transactivation.	Acetaldehyde	105-117	peroxisome proliferator activated receptor alpha	Homo sapiens	121-130
18003597-3	2008	Using the MCF-7 breast cancer cell line, we examined the relationship between ethanol and its metabolite acetaldehyde on PPARalpha and PPARbeta transactivation.	Acetaldehyde	105-117	peroxisome proliferator activated receptor delta	Homo sapiens	135-143
18003597-5	2008	Using the enzyme inhibitors 4-methylpyrazole and cyanamide and the metabolite acetaldehyde, we showed that PPARalpha and PPARbeta are differentially modulated by ethanol and acetaldehyde.	Acetaldehyde	78-90	peroxisome proliferator activated receptor alpha	Homo sapiens	107-116
18003597-5	2008	Using the enzyme inhibitors 4-methylpyrazole and cyanamide and the metabolite acetaldehyde, we showed that PPARalpha and PPARbeta are differentially modulated by ethanol and acetaldehyde.	Acetaldehyde	78-90	peroxisome proliferator activated receptor delta	Homo sapiens	121-129
18003597-5	2008	Using the enzyme inhibitors 4-methylpyrazole and cyanamide and the metabolite acetaldehyde, we showed that PPARalpha and PPARbeta are differentially modulated by ethanol and acetaldehyde.	Acetaldehyde	174-186	peroxisome proliferator activated receptor alpha	Homo sapiens	107-116
18003597-5	2008	Using the enzyme inhibitors 4-methylpyrazole and cyanamide and the metabolite acetaldehyde, we showed that PPARalpha and PPARbeta are differentially modulated by ethanol and acetaldehyde.	Acetaldehyde	174-186	peroxisome proliferator activated receptor delta	Homo sapiens	121-129
18003597-6	2008	While acetaldehyde is responsible for the inhibition of PPARalpha ligand inhibition with a concentration that inhibits 50% of activity (IC50) of 111 nM, acetaldehyde has no effect on PPARbeta or its ligand activation.	Acetaldehyde	6-18	peroxisome proliferator activated receptor alpha	Homo sapiens	56-65
18003597-8	2008	The differential effect of ethanol and acetaldehyde on PPARalpha and PPARbeta further underscores the differences between these receptors and may indicate the relevance of PPARs in the effects of ethanol in the human breast.	Acetaldehyde	39-51	peroxisome proliferator activated receptor alpha	Homo sapiens	55-64
18003597-8	2008	The differential effect of ethanol and acetaldehyde on PPARalpha and PPARbeta further underscores the differences between these receptors and may indicate the relevance of PPARs in the effects of ethanol in the human breast.	Acetaldehyde	39-51	peroxisome proliferator activated receptor delta	Homo sapiens	69-77
17991733-3	2008	EGF-mediated prevention of acetaldehyde-induced decrease in transepithelial electrical resistance and an increase in inulin permeability, and subcellular redistribution of occludin and ZO-1 was attenuated by reduced expression of PLCgamma1 by short hairpin RNA.	Acetaldehyde	27-39	phospholipase C gamma 1	Homo sapiens	230-239
17991733-5	2008	Inhibition of PKC activity or selective interference of membrane translocation of PKCepsilon and PKCbetaI by RACK interference peptides attenuated EGF-mediated prevention of acetaldehyde-induced increase in inulin permeability and redistribution of occludin and ZO-1.	Acetaldehyde	174-186	protein kinase C epsilon	Homo sapiens	82-92
17991733-5	2008	Inhibition of PKC activity or selective interference of membrane translocation of PKCepsilon and PKCbetaI by RACK interference peptides attenuated EGF-mediated prevention of acetaldehyde-induced increase in inulin permeability and redistribution of occludin and ZO-1.	Acetaldehyde	174-186	occludin	Homo sapiens	249-257
17991733-5	2008	Inhibition of PKC activity or selective interference of membrane translocation of PKCepsilon and PKCbetaI by RACK interference peptides attenuated EGF-mediated prevention of acetaldehyde-induced increase in inulin permeability and redistribution of occludin and ZO-1.	Acetaldehyde	174-186	tight junction protein 1	Homo sapiens	262-266
17991733-8	2008	This study shows that PLCgamma-mediated activation of PKCepsilon and PKCbetaI and intracellular calcium is involved in EGF-mediated protection of tight junctions from acetaldehyde-induced insult.	Acetaldehyde	167-179	protein kinase C epsilon	Homo sapiens	54-64
18302046-3	2008	Differences in the anatomy and biochemistry of the rodent and human nose, including polymorphisms in human high-affinity acetaldehyde dehydrogenase (ALDH2), are important considerations for interspecies extrapolations in the risk assessment of acetaldehyde.	Acetaldehyde	121-133	aldehyde dehydrogenase 2 family member	Homo sapiens	149-154
17597408-3	2008	Here, measurements of specific IgAs against tissue transglutaminase and proteins modified by acetaldehyde, the first metabolite of ethanol, showed significantly higher levels of both antibodies in alcoholic liver disease patients than in healthy controls or heavy drinkers without liver disease.	Acetaldehyde	93-105	transglutaminase 2	Homo sapiens	44-67
18234639-10	2008	The secretion of type I collagen and the expression of cyclin D1, CDK4 and TGF-beta1 mRNA in acetaldehyde-induced HSCs were markedly inhibited by 50 and 100 micromol/L PD98059, respectively.	Acetaldehyde	93-105	cyclin D1	Rattus norvegicus	55-64
18234639-10	2008	The secretion of type I collagen and the expression of cyclin D1, CDK4 and TGF-beta1 mRNA in acetaldehyde-induced HSCs were markedly inhibited by 50 and 100 micromol/L PD98059, respectively.	Acetaldehyde	93-105	cyclin-dependent kinase 4	Rattus norvegicus	66-70
18234639-10	2008	The secretion of type I collagen and the expression of cyclin D1, CDK4 and TGF-beta1 mRNA in acetaldehyde-induced HSCs were markedly inhibited by 50 and 100 micromol/L PD98059, respectively.	Acetaldehyde	93-105	transforming growth factor, beta 1	Rattus norvegicus	75-84
18234639-11	2008	CONCLUSIONS: The ERK pathway regulates the cell proliferation, secretion of type I collagen and the expression of TGF-beta1 mRNA in rat HSCs stimulated by acetaldehyde, which is likely related to its regulative effect on the cell cycle.	Acetaldehyde	155-167	Eph receptor B1	Rattus norvegicus	17-20
18234639-11	2008	CONCLUSIONS: The ERK pathway regulates the cell proliferation, secretion of type I collagen and the expression of TGF-beta1 mRNA in rat HSCs stimulated by acetaldehyde, which is likely related to its regulative effect on the cell cycle.	Acetaldehyde	155-167	transforming growth factor, beta 1	Rattus norvegicus	114-123
18302046-7	2008	ALDH2 polymorphisms were represented in the human model as reduced rates of acetaldehyde metabolism.	Acetaldehyde	76-88	aldehyde dehydrogenase 2 family member	Homo sapiens	0-5
18303182-0	2008	Increased frequencies of micronucleated reticulocytes and T-cell receptor mutation in Aldh2 knockout mice exposed to acetaldehyde.	Acetaldehyde	117-129	T cell receptor alpha variable 6-3	Mus musculus	58-73
18303182-0	2008	Increased frequencies of micronucleated reticulocytes and T-cell receptor mutation in Aldh2 knockout mice exposed to acetaldehyde.	Acetaldehyde	117-129	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	86-91
18303182-1	2008	Aldehyde dehydrogenase-2 (ALDH2) metabolizes acetaldehyde produced from ethanol into acetate and plays a major role in the oxidation of acetaldehyde in vivo.	Acetaldehyde	45-57	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	0-24
18303182-1	2008	Aldehyde dehydrogenase-2 (ALDH2) metabolizes acetaldehyde produced from ethanol into acetate and plays a major role in the oxidation of acetaldehyde in vivo.	Acetaldehyde	45-57	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	26-31
18303182-1	2008	Aldehyde dehydrogenase-2 (ALDH2) metabolizes acetaldehyde produced from ethanol into acetate and plays a major role in the oxidation of acetaldehyde in vivo.	Acetaldehyde	136-148	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	0-24
18303182-1	2008	Aldehyde dehydrogenase-2 (ALDH2) metabolizes acetaldehyde produced from ethanol into acetate and plays a major role in the oxidation of acetaldehyde in vivo.	Acetaldehyde	136-148	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	26-31
18303182-9	2008	The frequency of micronucleated reticulocytes induced by acetaldehyde was significantly increased in Aldh2 -/- mice, but not in Aldh2 +/+ mice.	Acetaldehyde	57-69	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	101-106
18303182-10	2008	TCR mutant frequency was also associated with acetaldehyde exposure in Aldh2-/ - mice, especially after oral administration; however, it was not associated with acetaldehyde exposure in Aldh2 +/+ mice.	Acetaldehyde	46-58	T cell receptor alpha variable 6-3	Mus musculus	0-3
18303182-10	2008	TCR mutant frequency was also associated with acetaldehyde exposure in Aldh2-/ - mice, especially after oral administration; however, it was not associated with acetaldehyde exposure in Aldh2 +/+ mice.	Acetaldehyde	46-58	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	71-76
18303182-11	2008	In conclusion, Aldh2 -/- mice showed high sensitivity in the micronuclei and TCR mutation assays compared with Aldh2 +/+ mice after exposure to acetaldehyde.	Acetaldehyde	144-156	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	15-20
18303182-11	2008	In conclusion, Aldh2 -/- mice showed high sensitivity in the micronuclei and TCR mutation assays compared with Aldh2 +/+ mice after exposure to acetaldehyde.	Acetaldehyde	144-156	T cell receptor alpha variable 6-3	Mus musculus	77-80
18369923-2	2008	Alcohol dehydrogenase is the enzyme that is most important in the oxidation of ethanol to acetaldehyde.	Acetaldehyde	90-102	aldo-keto reductase family 1 member A1	Homo sapiens	0-21
17982019-8	2008	Channel activity of the RyR2 with slightly reduced cytoplasmic redox potential from near resting state (-213 mV) or without redox fixation was augmented by all concentrations of acetaldehyde (1-100 microM) used here.	Acetaldehyde	178-190	ryanodine receptor 2	Rattus norvegicus	24-28
17982019-11	2008	The present results suggest that acetaldehyde acts as an RyR2 activator to disturb cardiac muscle function, and redox potential protects the heart from acetaldehyde-induced alterations in myocytes.	Acetaldehyde	33-45	ryanodine receptor 2	Rattus norvegicus	57-61
18254707-7	2008	CONCLUSIONS: It was observed that ADH variants, ADH2*1 and ADH3*2, were associated with increased risk for oesophageal cancer, possibly due to the tolerance of the carriers of these alleles to alcohol consumption compared to those with high activity alleles (ADH2*2 and ADH2*3) which are associated with higher production of the unpleasant acetaldehyde intermediate.	Acetaldehyde	340-352	aldo-keto reductase family 1 member A1	Homo sapiens	34-37
18254707-7	2008	CONCLUSIONS: It was observed that ADH variants, ADH2*1 and ADH3*2, were associated with increased risk for oesophageal cancer, possibly due to the tolerance of the carriers of these alleles to alcohol consumption compared to those with high activity alleles (ADH2*2 and ADH2*3) which are associated with higher production of the unpleasant acetaldehyde intermediate.	Acetaldehyde	340-352	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	59-63
18070084-6	2008	Moreover, strains with the derived allele have significantly higher ALDH enzyme activity with acetaldehyde (the breakdown product of ethanol) as a substrate than strains with the ancestral allele.	Acetaldehyde	94-106	Aldehyde dehydrogenase	Drosophila melanogaster	68-72
18028524-0	2008	Evaluation of the effect of ethanol"s toxic metabolite acetaldehyde on the gastrointestinal oligopeptide transporter, PEPT1: in vitro and in vivo studies.	Acetaldehyde	55-67	solute carrier family 15 member 1	Rattus norvegicus	118-123
18028524-2	2008	This study examines the effects of the ethanol metabolite, acetaldehyde, on the clinically relevant drug transporter, PEPT1.	Acetaldehyde	59-71	solute carrier family 15 member 1	Rattus norvegicus	118-123
18028524-3	2008	The metabolism of ethanol and the following acetaldehyde formation is thought to modulate the uptake capacity of PEPT1 within the gastrointestinal tract for a variety of clinically important peptidomimetic drug compounds.	Acetaldehyde	44-56	solute carrier family 15 member 1	Rattus norvegicus	113-118
18028524-8	2008	RESULTS: In vitro uptake of [(3)H]-GlySar in CHO-hPEPT1 cells treated with 1 mM acetaldehyde was significantly decreased (p &lt; 0.05) as compared to untreated controls.	Acetaldehyde	80-92	solute carrier family 15 member 1	Homo sapiens	49-55
18028524-11	2008	CONCLUSION: The effects of acetaldehyde due to consumption of ethanol on the uptake and bioavailability of therapeutic drug compounds transported by the PEPT1 oligopeptide transporter have not been documented.	Acetaldehyde	27-39	solute carrier family 15 member 1	Rattus norvegicus	153-158
18028524-12	2008	In the present studies, we demonstrate that acetaldehyde significantly modulates PEPT1 function and, thereby, affects drug bioavailability.	Acetaldehyde	44-56	solute carrier family 15 member 1	Rattus norvegicus	81-86
18028502-3	2008	OBJECTIVES: This study was designed to determine if pharmacological inhibition of calcium-independent phospholipase A (iPLA(2)) impairs ACE in normal human epidermal keratinocytes.	Acetaldehyde	136-139	phospholipase A and acyltransferase 1	Homo sapiens	102-117
18028502-3	2008	OBJECTIVES: This study was designed to determine if pharmacological inhibition of calcium-independent phospholipase A (iPLA(2)) impairs ACE in normal human epidermal keratinocytes.	Acetaldehyde	136-139	phospholipase A2 group VI	Homo sapiens	119-126
19122804-3	2008	AcH can be formed in the brain tissues through the peroxidatic activity of catalase and by oxidation via other oxidizing enzymes such as cytochrome P-4502E1.	Acetaldehyde	0-3	catalase	Homo sapiens	75-83
19122804-6	2008	Modulation of aldehyde dehydrogenase (ALDH) and brain catalase activity can change EtOH-related addictive behaviors presumably by changing AcH levels.	Acetaldehyde	139-142	catalase	Homo sapiens	54-62
17943953-5	2008	Treatment of BMVEC with EtOH or acetaldehyde (AA) for 2-48 h increased MMP-1, -2 and -9 activities or decreased the levels of tissue inhibitors of MMPs (TIMP-1, -2) in a PTK-dependent manner without affecting protein tyrosine phosphatase activity.	Acetaldehyde	32-44	matrix metallopeptidase 1	Homo sapiens	71-87
17943953-5	2008	Treatment of BMVEC with EtOH or acetaldehyde (AA) for 2-48 h increased MMP-1, -2 and -9 activities or decreased the levels of tissue inhibitors of MMPs (TIMP-1, -2) in a PTK-dependent manner without affecting protein tyrosine phosphatase activity.	Acetaldehyde	32-44	TIMP metallopeptidase inhibitor 1	Homo sapiens	153-159
17943953-5	2008	Treatment of BMVEC with EtOH or acetaldehyde (AA) for 2-48 h increased MMP-1, -2 and -9 activities or decreased the levels of tissue inhibitors of MMPs (TIMP-1, -2) in a PTK-dependent manner without affecting protein tyrosine phosphatase activity.	Acetaldehyde	32-44	EPH receptor A8	Homo sapiens	170-173
17980998-2	2007	Acetaldehyde, an intermediate metabolite of ethanol, is metabolized very slowly in people with ALDH2*2 because the mutant ALDH2 protein lacks the activity of acetaldehyde metabolism.	Acetaldehyde	0-12	aldehyde dehydrogenase 2 family member	Homo sapiens	95-100
20016718-7	2008	However, acetaldehyde was observed to reduce the dehydrogenase activity of FDH in a dose- and time-dependent manner with an apparent IC(50) of 4 mM, while the hydrolase activity of FDH was not affected by acetaldehyde in vitro.	Acetaldehyde	9-21	aldehyde dehydrogenase 1 family, member L1	Rattus norvegicus	75-78
20016718-7	2008	However, acetaldehyde was observed to reduce the dehydrogenase activity of FDH in a dose- and time-dependent manner with an apparent IC(50) of 4 mM, while the hydrolase activity of FDH was not affected by acetaldehyde in vitro.	Acetaldehyde	205-217	aldehyde dehydrogenase 1 family, member L1	Rattus norvegicus	75-78
17698255-0	2008	Ethanol and acetaldehyde alter NTPDase and 5"-nucleotidase from zebrafish brain membranes.	Acetaldehyde	12-24	5'-nucleotidase, ecto (CD73)	Danio rerio	43-58
20016718-0	2008	In vitro inhibition of 10-formyltetrahydrofolate dehydrogenase activity by acetaldehyde.	Acetaldehyde	75-87	aldehyde dehydrogenase 1 family, member L1	Rattus norvegicus	23-62
17949463-0	2007	Acetaldehyde increases endogenous adiponectin and fibrogenesis in hepatic stellate cells but exogenous adiponectin inhibits fibrogenesis.	Acetaldehyde	0-12	adiponectin, C1Q and collagen domain containing	Mus musculus	34-45
17949463-3	2007	The aim of this study was to determine the expression of adiponectin in activated stellate cells obtained from wt and ob/ob mice and to determine the effects of acetaldehyde on adiponectin in relation to the expression of type I collagen.	Acetaldehyde	161-173	adiponectin, C1Q and collagen domain containing	Mus musculus	177-188
17980998-2	2007	Acetaldehyde, an intermediate metabolite of ethanol, is metabolized very slowly in people with ALDH2*2 because the mutant ALDH2 protein lacks the activity of acetaldehyde metabolism.	Acetaldehyde	0-12	aldehyde dehydrogenase 2 family member	Homo sapiens	122-127
17949463-9	2007	Acetaldehyde (200 microM) increased adiponectin both in wt and in ob/ob stellate cells (p &lt; 0.05), but increased AdipoR2 immunoprotein only in ob/ob stellate cells (p &lt; 0.01).	Acetaldehyde	0-12	adiponectin, C1Q and collagen domain containing	Mus musculus	36-47
17980998-2	2007	Acetaldehyde, an intermediate metabolite of ethanol, is metabolized very slowly in people with ALDH2*2 because the mutant ALDH2 protein lacks the activity of acetaldehyde metabolism.	Acetaldehyde	158-170	aldehyde dehydrogenase 2 family member	Homo sapiens	95-100
17980998-2	2007	Acetaldehyde, an intermediate metabolite of ethanol, is metabolized very slowly in people with ALDH2*2 because the mutant ALDH2 protein lacks the activity of acetaldehyde metabolism.	Acetaldehyde	158-170	aldehyde dehydrogenase 2 family member	Homo sapiens	122-127
17989515-4	2007	The results of such studies are, however, difficult to interpret because cyanamide is an inhibitor of the enzymes catalase and aldehyde dehydrogenase, two enzymes with opposite effects on brain acetaldehyde concentrations.	Acetaldehyde	194-206	catalase	Mus musculus	114-149
17949463-9	2007	Acetaldehyde (200 microM) increased adiponectin both in wt and in ob/ob stellate cells (p &lt; 0.05), but increased AdipoR2 immunoprotein only in ob/ob stellate cells (p &lt; 0.01).	Acetaldehyde	0-12	adiponectin receptor 2	Mus musculus	116-123
17949463-10	2007	However, in the presence of leptin, acetaldehyde decreased adiponectin in ob/ob stellate cells (p &lt; 0.01).	Acetaldehyde	36-48	adiponectin, C1Q and collagen domain containing	Mus musculus	59-70
17949463-13	2007	Adiponectin inhibited alpha(1)(I) collagen mRNA in the basal state in wt stellate cells or when enhanced by acetaldehyde.	Acetaldehyde	108-120	adiponectin, C1Q and collagen domain containing	Mus musculus	0-11
17949463-15	2007	Adiponectin has a negative regulatory role on the enhancing effect of acetaldehyde on fibrogenesis in alcoholic liver disease.	Acetaldehyde	70-82	adiponectin, C1Q and collagen domain containing	Mus musculus	0-11
17980789-4	2007	A significant amount of acetaldehyde is derived from ethanol metabolism via the catalase system.	Acetaldehyde	24-36	catalase	Rattus norvegicus	80-88
18056434-7	2007	In addition, FANCD2-deficient DT40 cells are hypersensitive to acetaldehyde, but not to acrolein, crotonaldehyde, glyoxal, and methylglyoxal.	Acetaldehyde	63-75	Fanconi anemia complementation group D2	Gallus gallus	13-19
17268812-2	2007	Individuals differ in their ability to metabolize alcohol through genetic differences in alcohol dehydrogenase (ADH), the enzyme that catalyzes the oxidation of approximately 80% of ethanol to acetaldehyde, a known carcinogen.	Acetaldehyde	193-205	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	112-115
17436086-6	2007	The stabilization times measured for Factor XIIIa activity appear to be the most sensitive to acetaldehyde compared to acetaldehyde effects on thrombin, Factor Xa, and fibrinogen studied earlier in this laboratory, as well as Factors II, VII, and X.	Acetaldehyde	94-106	coagulation factor XIII A chain	Homo sapiens	37-49
17436086-6	2007	The stabilization times measured for Factor XIIIa activity appear to be the most sensitive to acetaldehyde compared to acetaldehyde effects on thrombin, Factor Xa, and fibrinogen studied earlier in this laboratory, as well as Factors II, VII, and X.	Acetaldehyde	119-131	coagulation factor II, thrombin	Homo sapiens	143-151
17436086-6	2007	The stabilization times measured for Factor XIIIa activity appear to be the most sensitive to acetaldehyde compared to acetaldehyde effects on thrombin, Factor Xa, and fibrinogen studied earlier in this laboratory, as well as Factors II, VII, and X.	Acetaldehyde	119-131	coagulation factor X	Homo sapiens	153-162
17643407-0	2007	Histone H3 phosphorylation at serine 10 and serine 28 is mediated by p38 MAPK in rat hepatocytes exposed to ethanol and acetaldehyde.	Acetaldehyde	120-132	mitogen activated protein kinase 14	Rattus norvegicus	69-72
17643407-8	2007	In the nuclear fraction, the phosphorylation of p38 MAPK and its protein level increased with peak activation at 24 h by ethanol and at 30 min by acetaldehyde.	Acetaldehyde	146-158	mitogen activated protein kinase 14	Rattus norvegicus	48-51
17643407-14	2007	These studies demonstrate for the first time that ethanol and acetaldehyde stimulated phosphorylation of histone H3 at serine 10 and serine 28 are downstream nuclear response mediated by p38 MAPK in hepatocytes.	Acetaldehyde	62-74	mitogen activated protein kinase 14	Rattus norvegicus	187-190
17952709-1	2007	BACKGROUND: Aldehyde dehydrogenase-2 (ALDH2) degrades acetaldehyde metabolized from ethanol.	Acetaldehyde	54-66	aldehyde dehydrogenase 2 family member	Homo sapiens	12-36
17600310-7	2007	4-hydroxy-2-nonenal (30-100 microM), an endogenous alpha,beta-unsaturated aldehyde that is abundant in lungs of patients with COPD, stimulated the release of IL-8 from U937 cells, whereas the saturated aldehyde, acetaldehyde, was ineffective.	Acetaldehyde	212-224	C-X-C motif chemokine ligand 8	Homo sapiens	158-162
17952709-1	2007	BACKGROUND: Aldehyde dehydrogenase-2 (ALDH2) degrades acetaldehyde metabolized from ethanol.	Acetaldehyde	54-66	aldehyde dehydrogenase 2 family member	Homo sapiens	38-43
17665311-2	2007	Alcohol dehydrogenase catalyzes the oxidation of approximately 80% of ethanol to acetaldehyde, a carcinogen.	Acetaldehyde	81-93	aldo-keto reductase family 1 member A1	Homo sapiens	0-21
17665311-3	2007	The alcohol dehydrogenase gene has several polymorphisms which may lead to faster conversion of ethanol to acetaldehyde, which may increase cancer risk.	Acetaldehyde	107-119	aldo-keto reductase family 1 member A1	Homo sapiens	4-25
17970723-3	2007	Here we show that human and mouse TRPA1 are activated by acetaldehyde, an intermediate substance of ethanol metabolism, in the HEK293T cell heterologous expression system and in cultured mouse trigeminal neurons.	Acetaldehyde	57-69	transient receptor potential cation channel, subfamily A, member 1	Mus musculus	34-39
17970723-5	2007	TRPA1 antagonists camphor and gadolinium, and a general TRP blocker ruthenium red inhibited TRPA1 activation by acetaldehyde.	Acetaldehyde	112-124	transient receptor potential cation channel, subfamily A, member 1	Mus musculus	0-5
17970723-5	2007	TRPA1 antagonists camphor and gadolinium, and a general TRP blocker ruthenium red inhibited TRPA1 activation by acetaldehyde.	Acetaldehyde	112-124	transient receptor potential cation channel, subfamily A, member 1	Mus musculus	92-97
17970723-7	2007	Intradermal co-application of prostaglandin E2 and acetaldehyde greatly potentiated the acetaldehyde-induced nociceptive responses, and this effect was reversed by treatment with the TRPA1 antagonist camphor.	Acetaldehyde	51-63	transient receptor potential cation channel, subfamily A, member 1	Mus musculus	183-188
17970723-7	2007	Intradermal co-application of prostaglandin E2 and acetaldehyde greatly potentiated the acetaldehyde-induced nociceptive responses, and this effect was reversed by treatment with the TRPA1 antagonist camphor.	Acetaldehyde	88-100	transient receptor potential cation channel, subfamily A, member 1	Mus musculus	183-188
17970723-8	2007	These results suggest that acetaldehyde causes nociception via TRPA1 activation.	Acetaldehyde	27-39	transient receptor potential cation channel, subfamily A, member 1	Mus musculus	63-68
17631643-7	2007	In summary, our results suggested that the ALDH2 Ex1+82 G allele may be functionally deficient in eliminating acetaldehyde and discourage alcohol drinking.	Acetaldehyde	110-122	aldehyde dehydrogenase 2 family member	Homo sapiens	43-48
17992629-0	2007	The dual substrate specificity of aldehyde oxidase 1 for retinal and acetaldehyde and its role in ABCA1 mediated efflux.	Acetaldehyde	69-81	aldehyde oxidase 1	Homo sapiens	34-52
17992631-2	2007	AOX1 is well-described as xenobiotic metabolizing enzyme, which upon oxidation of acetaldehyde and retinaldehyde to acetic acid and retinoic acid generates reactive oxygen species.	Acetaldehyde	82-94	aldehyde oxidase 1	Homo sapiens	0-4
17655273-10	2007	Aliphatic aldehydes such as glyoxal, acetaldehyde, and propanal are relatively weak inactivators of PTP1B under the conditions employed here.	Acetaldehyde	37-49	protein tyrosine phosphatase non-receptor type 1	Homo sapiens	100-105
17975074-1	2007	Alcohol dehydrogenase 1 (Adh1)p catalyses the conversion of acetaldehyde to ethanol, regenerating NAD+.	Acetaldehyde	60-72	alcohol dehydrogenase ADH1	Saccharomyces cerevisiae S288C	25-29
17597213-0	2007	Catalase mediates acetaldehyde formation in the striatum of free-moving rats.	Acetaldehyde	18-30	catalase	Rattus norvegicus	0-8
17597213-6	2007	The catalase or ADH inhibitor in combination with CY lowered considerably the AcH concentration in the brain.	Acetaldehyde	78-81	catalase	Rattus norvegicus	4-12
17597213-9	2007	The findings strongly support the assumption that the enzyme catalase plays a significant role in AcH formation directly in the rat brain.	Acetaldehyde	98-101	catalase	Rattus norvegicus	61-69
17953569-9	2007	When yeast fermenting the diluted fermentation was exposed to exogenous acetaldehyde, the transient spike in acetaldehyde increased the expression of ALD3 but this response alone was not sufficient to cause an increase in acetic acid.	Acetaldehyde	72-84	aldehyde dehydrogenase (NAD(+)) ALD3	Saccharomyces cerevisiae S288C	150-154
17953569-9	2007	When yeast fermenting the diluted fermentation was exposed to exogenous acetaldehyde, the transient spike in acetaldehyde increased the expression of ALD3 but this response alone was not sufficient to cause an increase in acetic acid.	Acetaldehyde	109-121	aldehyde dehydrogenase (NAD(+)) ALD3	Saccharomyces cerevisiae S288C	150-154
17953569-13	2007	Acetaldehyde at a concentration produced during Icewine fermentation stimulates the expression of ALD3, but has no impact on the expression of ALD2, -4, -5 and -6.	Acetaldehyde	0-12	aldehyde dehydrogenase (NAD(+)) ALD3	Saccharomyces cerevisiae S288C	98-102
17471563-0	2007	Contribution of the alcohol dehydrogenase-1B genotype and oral microorganisms to high salivary acetaldehyde concentrations in Japanese alcoholic men.	Acetaldehyde	95-107	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	20-44
17471563-4	2007	The ethanol levels in blood and saliva were similar, but the acetaldehyde levels in saliva were strikingly higher than in the blood, and were higher in ADH1B*1/*1 carriers than in ADH1B*2 allele carriers [47.4 muM (22.2-87.6) vs. 1.60 (&lt;DL-26.3) in the saliva, p = 0.009].	Acetaldehyde	61-73	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	152-157
17471563-4	2007	The ethanol levels in blood and saliva were similar, but the acetaldehyde levels in saliva were strikingly higher than in the blood, and were higher in ADH1B*1/*1 carriers than in ADH1B*2 allele carriers [47.4 muM (22.2-87.6) vs. 1.60 (&lt;DL-26.3) in the saliva, p = 0.009].	Acetaldehyde	61-73	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	180-185
17471563-9	2007	In conclusion, the high salivary acetaldehyde levels in the alcoholics were partly attributable to prolonged ethanol exposure because of the less-active ADH1B and increased salivary acetaldehyde production as a result of oral microorganism overgrowth, and may explain their high risk for UADTC.	Acetaldehyde	33-45	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	153-158
17287824-10	2007	Acetaldehyde potentiated nicotine-induced c-fos in CeA and SC, and activation of PVN c-fos expression/plasma corticosterone release; however, this drug interaction was only observed in behaviorally tested animals, not those that were minimally stressed.	Acetaldehyde	0-12	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	42-47
17287824-10	2007	Acetaldehyde potentiated nicotine-induced c-fos in CeA and SC, and activation of PVN c-fos expression/plasma corticosterone release; however, this drug interaction was only observed in behaviorally tested animals, not those that were minimally stressed.	Acetaldehyde	0-12	carcinoembryonic antigen gene family 4	Rattus norvegicus	51-54
17543481-0	2007	Acetaldehyde induces matrix metalloproteinase-9 gene expression via nuclear factor-kappaB and activator protein 1 signaling pathways in human hepatocellular carcinoma cells: Association with the invasive potential.	Acetaldehyde	0-12	matrix metallopeptidase 9	Homo sapiens	21-47
17673211-1	2007	Aldehyde dehydrogenase (ALDH) isozymes are critically important in the metabolism of acetaldehyde, thus preventing its accumulation after ethanol-exposure.	Acetaldehyde	85-97	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	0-22
17673211-1	2007	Aldehyde dehydrogenase (ALDH) isozymes are critically important in the metabolism of acetaldehyde, thus preventing its accumulation after ethanol-exposure.	Acetaldehyde	85-97	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	24-28
17673211-3	2007	This study was aimed at investigating whether cytosolic ALDH1, with a relatively-low-Km value (11-18 microM) for acetaldehyde, could be also inhibited in ethanol-exposed rats.	Acetaldehyde	113-125	aldehyde dehydrogenase 2 family member	Rattus norvegicus	56-61
17673211-6	2007	Therefore inactivation of ALDH1 via S-nitrosylation can result in accumulation of acetaldehyde upon ethanol-exposure.	Acetaldehyde	82-94	aldehyde dehydrogenase 2 family member	Rattus norvegicus	26-31
17543481-7	2007	Acetaldehyde also induced AP-1 activity via the phosphorylation of p38 kinase.	Acetaldehyde	0-12	Jun proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	26-30
17690585-2	2007	Under normal conditions, alcohol is hepatically cleared via alcohol dehydrogenase to acetaldehyde, and subsequently by acetaldehyde dehydrogenase (ACD) to acetic acid.	Acetaldehyde	85-97	aldo-keto reductase family 1 member A1	Homo sapiens	60-81
17764883-8	2007	These include prominent roles for the second messengers calcium and nitric oxide, regulatory kinases including PKG and PKA, alcohol- and acetaldehyde-metabolizing enzymes such as aldehyde dehydrogenase 2.	Acetaldehyde	137-149	aldehyde dehydrogenase 2 family member	Homo sapiens	179-203
17650227-1	2007	OBJECTIVE: To investigate the effects of PD98059 on the cell cycle, cell proliferation, the secretion of type I collagen and expression of transforming growth factor-beta-1 mRNA in rat hepatic stellate cells stimulated by acetaldehyde.	Acetaldehyde	222-234	transforming growth factor, beta 1	Rattus norvegicus	139-172
17650227-8	2007	The secretion of type I collagen and transforming growth factor-beta-1 mRNA expression of acetaldehyde-induced hepatic stellate cells were markedly inhibited by 50 and 100 micromol/L PD98059, respectively.	Acetaldehyde	90-102	transforming growth factor, beta 1	Rattus norvegicus	37-70
17650227-9	2007	CONCLUSION: Extracellular signal-regulated kinase signal transduction pathway could regulate cell proliferation, the secretion of type I collagen and transforming growth factor-beta-1 mRNA expression of rat hepatic stellate cells stimulated by acetaldehyde.	Acetaldehyde	244-256	transforming growth factor, beta 1	Rattus norvegicus	150-183
17543481-7	2007	Acetaldehyde also induced AP-1 activity via the phosphorylation of p38 kinase.	Acetaldehyde	0-12	mitogen-activated protein kinase 14	Homo sapiens	67-70
17543481-0	2007	Acetaldehyde induces matrix metalloproteinase-9 gene expression via nuclear factor-kappaB and activator protein 1 signaling pathways in human hepatocellular carcinoma cells: Association with the invasive potential.	Acetaldehyde	0-12	Jun proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	94-113
17543481-8	2007	In conclusion, our findings demonstrated for the first time that acetaldehyde activated NF-kappaB and AP-1 activities via IkappaB, JNK/beta-TrCP, and p38 signaling pathways, resulting in MMP-9 gene expression and hepatocarcinoma cells invasion.	Acetaldehyde	65-77	Jun proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	102-106
17543481-4	2007	Herein we demonstrated that acetaldehyde, the primary metabolite of ethanol, increased matrix metalloproteinase-9 (MMP-9) gelatinolytic activity and promoted cell invasion through the up-regulation of MMP-9 gene transcription in HepG2 cells.	Acetaldehyde	28-40	matrix metallopeptidase 9	Homo sapiens	87-113
17543481-8	2007	In conclusion, our findings demonstrated for the first time that acetaldehyde activated NF-kappaB and AP-1 activities via IkappaB, JNK/beta-TrCP, and p38 signaling pathways, resulting in MMP-9 gene expression and hepatocarcinoma cells invasion.	Acetaldehyde	65-77	mitogen-activated protein kinase 8	Homo sapiens	131-134
17543481-4	2007	Herein we demonstrated that acetaldehyde, the primary metabolite of ethanol, increased matrix metalloproteinase-9 (MMP-9) gelatinolytic activity and promoted cell invasion through the up-regulation of MMP-9 gene transcription in HepG2 cells.	Acetaldehyde	28-40	matrix metallopeptidase 9	Homo sapiens	115-120
17543481-8	2007	In conclusion, our findings demonstrated for the first time that acetaldehyde activated NF-kappaB and AP-1 activities via IkappaB, JNK/beta-TrCP, and p38 signaling pathways, resulting in MMP-9 gene expression and hepatocarcinoma cells invasion.	Acetaldehyde	65-77	beta-transducin repeat containing E3 ubiquitin protein ligase	Homo sapiens	135-144
17543481-8	2007	In conclusion, our findings demonstrated for the first time that acetaldehyde activated NF-kappaB and AP-1 activities via IkappaB, JNK/beta-TrCP, and p38 signaling pathways, resulting in MMP-9 gene expression and hepatocarcinoma cells invasion.	Acetaldehyde	65-77	mitogen-activated protein kinase 14	Homo sapiens	150-153
17543481-4	2007	Herein we demonstrated that acetaldehyde, the primary metabolite of ethanol, increased matrix metalloproteinase-9 (MMP-9) gelatinolytic activity and promoted cell invasion through the up-regulation of MMP-9 gene transcription in HepG2 cells.	Acetaldehyde	28-40	matrix metallopeptidase 9	Homo sapiens	201-206
17543481-8	2007	In conclusion, our findings demonstrated for the first time that acetaldehyde activated NF-kappaB and AP-1 activities via IkappaB, JNK/beta-TrCP, and p38 signaling pathways, resulting in MMP-9 gene expression and hepatocarcinoma cells invasion.	Acetaldehyde	65-77	matrix metallopeptidase 9	Homo sapiens	187-192
17543481-5	2007	The transcription of MMP-9 gene was regulated by 10 microM acetaldehyde via inductions of nuclear factor-kappaB (NF-kappaB) and activator protein 1 (AP-1) activities.	Acetaldehyde	59-71	matrix metallopeptidase 9	Homo sapiens	21-26
17543481-5	2007	The transcription of MMP-9 gene was regulated by 10 microM acetaldehyde via inductions of nuclear factor-kappaB (NF-kappaB) and activator protein 1 (AP-1) activities.	Acetaldehyde	59-71	Jun proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	128-147
17543481-5	2007	The transcription of MMP-9 gene was regulated by 10 microM acetaldehyde via inductions of nuclear factor-kappaB (NF-kappaB) and activator protein 1 (AP-1) activities.	Acetaldehyde	59-71	Jun proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	149-153
17543481-6	2007	Acetaldehyde stimulated the translocation of NF-kappaB into nucleus through inhibitory kappaB-alpha (IkappaB-alpha) and c-Jun N-terminal kinase (JNK)/beta-transducin repeat-containing protein (beta-TrCP) signaling pathways.	Acetaldehyde	0-12	NFKB inhibitor alpha	Homo sapiens	101-114
17543481-6	2007	Acetaldehyde stimulated the translocation of NF-kappaB into nucleus through inhibitory kappaB-alpha (IkappaB-alpha) and c-Jun N-terminal kinase (JNK)/beta-transducin repeat-containing protein (beta-TrCP) signaling pathways.	Acetaldehyde	0-12	mitogen-activated protein kinase 8	Homo sapiens	120-143
17543481-6	2007	Acetaldehyde stimulated the translocation of NF-kappaB into nucleus through inhibitory kappaB-alpha (IkappaB-alpha) and c-Jun N-terminal kinase (JNK)/beta-transducin repeat-containing protein (beta-TrCP) signaling pathways.	Acetaldehyde	0-12	mitogen-activated protein kinase 8	Homo sapiens	145-148
17543481-6	2007	Acetaldehyde stimulated the translocation of NF-kappaB into nucleus through inhibitory kappaB-alpha (IkappaB-alpha) and c-Jun N-terminal kinase (JNK)/beta-transducin repeat-containing protein (beta-TrCP) signaling pathways.	Acetaldehyde	0-12	beta-transducin repeat containing E3 ubiquitin protein ligase	Homo sapiens	193-202
17221190-8	2007	Additionally, the NADH-producing pathway from acetaldehyde to acetate was analysed by overexpressing the stress-induced gene ALD3.	Acetaldehyde	46-58	aldehyde dehydrogenase (NAD(+)) ALD3	Saccharomyces cerevisiae S288C	125-129
17465424-0	2007	Comparative studies of the interaction between ferulic acid and bovine serum albumin by ACE and surface plasmon resonance.	Acetaldehyde	88-91	albumin	Homo sapiens	71-84
17567472-6	2007	Major interest in CYP2E1 reflects the ability of this enzyme to oxidize ethanol, to generate reactive products from ethanol oxidation (e.g. acetaldehyde and 1-hydroxyethyl radical), to activate various agents including CCl(4) and acetaminophen into reactive products, and to generate reactive oxygen species.	Acetaldehyde	140-152	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	18-24
17421009-1	2007	Seven ADH genes, identified until now, located in the long arm of human chromosome 4, produce seven different isozymes involved in the metabolism of ethanol to acetaldehyde.	Acetaldehyde	160-172	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	6-9
17443870-1	2007	The HCN-tetramer, a "classic" of the prebiotic chemistry of HCN, is shown to undergo a remarkable reaction with acetaldehyde in slightly basic or neutral aqueous solution at room temperature.	Acetaldehyde	112-124	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	4-7
18364675-4	2007	Catalase and cytochrome P450 2E1 are distributed throughout the brain and these systems can oxidize ethanol to acetaldehyde.	Acetaldehyde	111-123	catalase	Homo sapiens	0-8
18364675-4	2007	Catalase and cytochrome P450 2E1 are distributed throughout the brain and these systems can oxidize ethanol to acetaldehyde.	Acetaldehyde	111-123	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	13-32
17443870-1	2007	The HCN-tetramer, a "classic" of the prebiotic chemistry of HCN, is shown to undergo a remarkable reaction with acetaldehyde in slightly basic or neutral aqueous solution at room temperature.	Acetaldehyde	112-124	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	60-63
17443871-1	2007	Encouraged by observations made on the course of reactions the HCN-tetramer can undergo with acetaldehyde, I delineate a constitutional and potentially generational relationship between HCN and those constituents of the reductive citric acid cycle that are direct precursors of amino acids in contemporary metabolism.	Acetaldehyde	93-105	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	63-66
17443871-1	2007	Encouraged by observations made on the course of reactions the HCN-tetramer can undergo with acetaldehyde, I delineate a constitutional and potentially generational relationship between HCN and those constituents of the reductive citric acid cycle that are direct precursors of amino acids in contemporary metabolism.	Acetaldehyde	93-105	metastasis associated lung adenocarcinoma transcript 1	Homo sapiens	186-189
16759795-6	2007	The risk for cancer multiplicity was associated with inactive heterozygous ALDH2 alone (OR=4.22) among the risk factors investigated, which also included smoking, less-active alcohol dehydrogenase-1B, and macrocytosis, enhancing the validity of the link between acetaldehyde exposure and cancer multiplicity.	Acetaldehyde	262-274	aldehyde dehydrogenase 2 family member	Homo sapiens	75-80
16860297-7	2007	Exposure to the photochemically generated products of BD (primarily acrolein, acetaldehyde, formaldehyde, furan and ozone) induced significant increases in cytotoxicity, IL-8, and IL-6 gene expression compared to a synthetic mixture of primary products that was created by injecting the correct concentrations of the detected products from the irradiation experiments.	Acetaldehyde	78-90	C-X-C motif chemokine ligand 8	Homo sapiens	170-174
16860297-7	2007	Exposure to the photochemically generated products of BD (primarily acrolein, acetaldehyde, formaldehyde, furan and ozone) induced significant increases in cytotoxicity, IL-8, and IL-6 gene expression compared to a synthetic mixture of primary products that was created by injecting the correct concentrations of the detected products from the irradiation experiments.	Acetaldehyde	78-90	interleukin 6	Homo sapiens	180-184
17273965-1	2007	The alcohol dehydrogenase (ADH) family of enzymes catalyzes the reversible oxidation of alcohol to acetaldehyde.	Acetaldehyde	99-111	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	27-30
17295732-1	2007	BACKGROUND: In vitro, human isoenzymes encoded by genes homozygous for the ADH1C*1 or ADH1B*2 alleles metabolize ethanol to acetaldehyde at a faster rate than those homozygous for the ADH1C*2 or ADH1B*1 allele.	Acetaldehyde	124-136	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	75-80
17295732-1	2007	BACKGROUND: In vitro, human isoenzymes encoded by genes homozygous for the ADH1C*1 or ADH1B*2 alleles metabolize ethanol to acetaldehyde at a faster rate than those homozygous for the ADH1C*2 or ADH1B*1 allele.	Acetaldehyde	124-136	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	86-91
17295732-1	2007	BACKGROUND: In vitro, human isoenzymes encoded by genes homozygous for the ADH1C*1 or ADH1B*2 alleles metabolize ethanol to acetaldehyde at a faster rate than those homozygous for the ADH1C*2 or ADH1B*1 allele.	Acetaldehyde	124-136	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	184-189
17295732-1	2007	BACKGROUND: In vitro, human isoenzymes encoded by genes homozygous for the ADH1C*1 or ADH1B*2 alleles metabolize ethanol to acetaldehyde at a faster rate than those homozygous for the ADH1C*2 or ADH1B*1 allele.	Acetaldehyde	124-136	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	195-200
17087658-0	2007	Acetaldehyde dissociates the PTP1B-E-cadherin-beta-catenin complex in Caco-2 cell monolayers by a phosphorylation-dependent mechanism.	Acetaldehyde	0-12	protein tyrosine phosphatase non-receptor type 1	Homo sapiens	29-34
17087658-0	2007	Acetaldehyde dissociates the PTP1B-E-cadherin-beta-catenin complex in Caco-2 cell monolayers by a phosphorylation-dependent mechanism.	Acetaldehyde	0-12	cadherin 1	Homo sapiens	35-45
17087658-0	2007	Acetaldehyde dissociates the PTP1B-E-cadherin-beta-catenin complex in Caco-2 cell monolayers by a phosphorylation-dependent mechanism.	Acetaldehyde	0-12	catenin beta 1	Homo sapiens	46-58
17087658-3	2007	Treatment of cell monolayers with acetaldehyde induced redistribution of E-cadherin and beta-catenin from the intercellular junctions by a tyrosine phosphorylation-dependent mechanism.	Acetaldehyde	34-46	cadherin 1	Homo sapiens	73-83
17087658-3	2007	Treatment of cell monolayers with acetaldehyde induced redistribution of E-cadherin and beta-catenin from the intercellular junctions by a tyrosine phosphorylation-dependent mechanism.	Acetaldehyde	34-46	catenin beta 1	Homo sapiens	88-100
17087658-4	2007	The PTPase activity associated with E-cadherin and beta-catenin was significantly reduced and the interaction of PTP1B with E-cadherin and beta-catenin was attenuated by acetaldehyde.	Acetaldehyde	170-182	cadherin 1	Homo sapiens	36-46
17087658-4	2007	The PTPase activity associated with E-cadherin and beta-catenin was significantly reduced and the interaction of PTP1B with E-cadherin and beta-catenin was attenuated by acetaldehyde.	Acetaldehyde	170-182	protein tyrosine phosphatase non-receptor type 1	Homo sapiens	113-118
17087658-4	2007	The PTPase activity associated with E-cadherin and beta-catenin was significantly reduced and the interaction of PTP1B with E-cadherin and beta-catenin was attenuated by acetaldehyde.	Acetaldehyde	170-182	cadherin 1	Homo sapiens	124-134
17087658-4	2007	The PTPase activity associated with E-cadherin and beta-catenin was significantly reduced and the interaction of PTP1B with E-cadherin and beta-catenin was attenuated by acetaldehyde.	Acetaldehyde	170-182	catenin beta 1	Homo sapiens	139-151
17087658-5	2007	Acetaldehyde treatment resulted in phosphorylation of beta-catenin on tyrosine residues, and abolished the interaction of beta-catenin with E-cadherin by a tyrosine kinase-dependent mechanism.	Acetaldehyde	0-12	catenin beta 1	Homo sapiens	54-66
17087658-5	2007	Acetaldehyde treatment resulted in phosphorylation of beta-catenin on tyrosine residues, and abolished the interaction of beta-catenin with E-cadherin by a tyrosine kinase-dependent mechanism.	Acetaldehyde	0-12	catenin beta 1	Homo sapiens	122-134
17087658-5	2007	Acetaldehyde treatment resulted in phosphorylation of beta-catenin on tyrosine residues, and abolished the interaction of beta-catenin with E-cadherin by a tyrosine kinase-dependent mechanism.	Acetaldehyde	0-12	cadherin 1	Homo sapiens	140-150
17087658-6	2007	Protein binding studies showed that the treatment of cells with acetaldehyde reduced the binding of beta-catenin to the C-terminal region of E-cadherin.	Acetaldehyde	64-76	catenin beta 1	Homo sapiens	100-112
17087658-6	2007	Protein binding studies showed that the treatment of cells with acetaldehyde reduced the binding of beta-catenin to the C-terminal region of E-cadherin.	Acetaldehyde	64-76	cadherin 1	Homo sapiens	141-151
17087658-8	2007	Treatment of cells with acetaldehyde also reduced the binding of E-cadherin to GST (glutathione S-transferase)-PTP1B.	Acetaldehyde	24-36	cadherin 1	Homo sapiens	65-75
17087658-8	2007	Treatment of cells with acetaldehyde also reduced the binding of E-cadherin to GST (glutathione S-transferase)-PTP1B.	Acetaldehyde	24-36	glutathione S-transferase kappa 1	Homo sapiens	79-82
17087658-8	2007	Treatment of cells with acetaldehyde also reduced the binding of E-cadherin to GST (glutathione S-transferase)-PTP1B.	Acetaldehyde	24-36	glutathione S-transferase kappa 1	Homo sapiens	84-109
17087658-8	2007	Treatment of cells with acetaldehyde also reduced the binding of E-cadherin to GST (glutathione S-transferase)-PTP1B.	Acetaldehyde	24-36	protein tyrosine phosphatase non-receptor type 1	Homo sapiens	111-116
17087658-10	2007	Acetaldehyde increased the phosphorylation of beta-catenin on Tyr-331, Tyr-333, Tyr-654 and Tyr-670.	Acetaldehyde	0-12	catenin beta 1	Homo sapiens	46-58
17087658-11	2007	These results show that acetaldehyde induces disruption of interactions between E-cadherin, beta-catenin and PTP1B by a phosphorylation-dependent mechanism.	Acetaldehyde	24-36	cadherin 1	Homo sapiens	80-90
17087658-11	2007	These results show that acetaldehyde induces disruption of interactions between E-cadherin, beta-catenin and PTP1B by a phosphorylation-dependent mechanism.	Acetaldehyde	24-36	catenin beta 1	Homo sapiens	92-104
17087658-11	2007	These results show that acetaldehyde induces disruption of interactions between E-cadherin, beta-catenin and PTP1B by a phosphorylation-dependent mechanism.	Acetaldehyde	24-36	protein tyrosine phosphatase non-receptor type 1	Homo sapiens	109-114
17273805-6	2007	Incubation with ACE resulted in a significant reduction in IL-1beta and IFN-gamma-induced NO production, a finding that correlated well with reduced levels of the iNOS mRNA and protein.	Acetaldehyde	16-19	interleukin 1 beta	Rattus norvegicus	59-67
17236798-9	2007	This delayed expression of Aldh9 mRNA by ethanol may enhance acetaldehyde concentration in the embryo and induce teratogenesis during development.	Acetaldehyde	61-73	4-trimethylaminobutyraldehyde dehydrogenase	Oryzias latipes	27-32
17273805-6	2007	Incubation with ACE resulted in a significant reduction in IL-1beta and IFN-gamma-induced NO production, a finding that correlated well with reduced levels of the iNOS mRNA and protein.	Acetaldehyde	16-19	interferon gamma	Rattus norvegicus	72-81
17273805-6	2007	Incubation with ACE resulted in a significant reduction in IL-1beta and IFN-gamma-induced NO production, a finding that correlated well with reduced levels of the iNOS mRNA and protein.	Acetaldehyde	16-19	nitric oxide synthase 2	Rattus norvegicus	163-167
17452299-2	2007	Acetaldehyde, an intermediate metabolite of ethanol, is metabolized very slowly in people who have ALDH2*2, as the mutated ALDH2 lacks acetaldehyde metabolizing activity.	Acetaldehyde	0-12	aldehyde dehydrogenase 2 family member	Homo sapiens	99-104
17452299-2	2007	Acetaldehyde, an intermediate metabolite of ethanol, is metabolized very slowly in people who have ALDH2*2, as the mutated ALDH2 lacks acetaldehyde metabolizing activity.	Acetaldehyde	0-12	aldehyde dehydrogenase 2 family member	Homo sapiens	123-128
17452299-2	2007	Acetaldehyde, an intermediate metabolite of ethanol, is metabolized very slowly in people who have ALDH2*2, as the mutated ALDH2 lacks acetaldehyde metabolizing activity.	Acetaldehyde	135-147	aldehyde dehydrogenase 2 family member	Homo sapiens	99-104
17452299-2	2007	Acetaldehyde, an intermediate metabolite of ethanol, is metabolized very slowly in people who have ALDH2*2, as the mutated ALDH2 lacks acetaldehyde metabolizing activity.	Acetaldehyde	135-147	aldehyde dehydrogenase 2 family member	Homo sapiens	123-128
17127431-0	2007	Susceptibility to inhalation toxicity of acetaldehyde in Aldh2 knockout mice.	Acetaldehyde	41-53	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	57-62
17211707-3	2007	The one of them was ethanol, that is oxidized by alcohol dehydrogenase (ADH) to high concentration of acetaldehyde, a toxic and carcinogenic compound.	Acetaldehyde	102-114	aldo-keto reductase family 1 member A1	Homo sapiens	49-70
17211707-3	2007	The one of them was ethanol, that is oxidized by alcohol dehydrogenase (ADH) to high concentration of acetaldehyde, a toxic and carcinogenic compound.	Acetaldehyde	102-114	aldo-keto reductase family 1 member A1	Homo sapiens	72-75
17211707-13	2007	The increased ADH IV activity may be 1 of the factors intensifying carcinogenesis by the increased ability to acetaldehyde formation from ethanol.	Acetaldehyde	110-122	aldo-keto reductase family 1 member A1	Homo sapiens	14-17
17127373-5	2007	The expression of the death receptor ligand CD95 is also up-regulated by acetaldehyde metabolism.	Acetaldehyde	73-85	Fas cell surface death receptor	Homo sapiens	44-48
17127373-6	2007	Consequently, a dual mechanism, NADH-driven MMPT and CD95-mediated apoptosis, involving in both cases acetaldehyde metabolism and ROS production, operates in ethanol-induced apoptosis.	Acetaldehyde	102-114	Fas cell surface death receptor	Homo sapiens	53-57
17718394-5	2007	For example, certain ADH1B and ADH1C alleles encode particularly active ADH enzymes, resulting in more rapid conversion of alcohol (i.e., ethanol) to acetaldehyde; these alleles have a protective effect on the risk of alcoholism.	Acetaldehyde	150-162	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	21-26
17718394-5	2007	For example, certain ADH1B and ADH1C alleles encode particularly active ADH enzymes, resulting in more rapid conversion of alcohol (i.e., ethanol) to acetaldehyde; these alleles have a protective effect on the risk of alcoholism.	Acetaldehyde	150-162	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	31-36
17718394-5	2007	For example, certain ADH1B and ADH1C alleles encode particularly active ADH enzymes, resulting in more rapid conversion of alcohol (i.e., ethanol) to acetaldehyde; these alleles have a protective effect on the risk of alcoholism.	Acetaldehyde	150-162	aldo-keto reductase family 1 member A1	Homo sapiens	21-24
17718394-6	2007	A variant of the ALDH2 gene encodes an essentially inactive ALDH enzyme, resulting in acetaldehyde accumulation and a protective effect.	Acetaldehyde	86-98	aldehyde dehydrogenase 2 family member	Homo sapiens	17-22
16962100-0	2007	Acetaldehyde promotes rapamycin-dependent activation of p70(S6K) and glucose uptake despite inhibition of Akt and mTOR in dopaminergic SH-SY5Y human neuroblastoma cells.	Acetaldehyde	0-12	ribosomal protein S6 kinase B1	Homo sapiens	56-59
16962100-0	2007	Acetaldehyde promotes rapamycin-dependent activation of p70(S6K) and glucose uptake despite inhibition of Akt and mTOR in dopaminergic SH-SY5Y human neuroblastoma cells.	Acetaldehyde	0-12	AKT serine/threonine kinase 1	Homo sapiens	106-109
16962100-2	2007	Acetaldehyde, the major ethanol metabolite which is far more reactive than ethanol, has been postulated to participate in alcohol-induced tissue injury although its direct impact on insulin signaling is unclear.	Acetaldehyde	0-12	insulin	Homo sapiens	182-189
16962100-6	2007	Short-term exposure (12 h) of acetaldehyde (150 muM) facilitated glucose uptake in a rapamycin-dependent manner without affecting apoptosis, IRS-2 expression and insulin-stimulated glucose uptake in SH-SY5Y cells.	Acetaldehyde	30-42	latexin	Homo sapiens	48-51
16962100-6	2007	Short-term exposure (12 h) of acetaldehyde (150 muM) facilitated glucose uptake in a rapamycin-dependent manner without affecting apoptosis, IRS-2 expression and insulin-stimulated glucose uptake in SH-SY5Y cells.	Acetaldehyde	30-42	insulin receptor substrate 2	Homo sapiens	141-146
16962100-7	2007	Acetaldehyde suppressed basal and insulin-stimulated Akt phosphorylation without affecting total Akt expression.	Acetaldehyde	0-12	insulin	Homo sapiens	34-41
16962100-7	2007	Acetaldehyde suppressed basal and insulin-stimulated Akt phosphorylation without affecting total Akt expression.	Acetaldehyde	0-12	AKT serine/threonine kinase 1	Homo sapiens	53-56
16962100-8	2007	Acetaldehyde inhibited mTOR phosphorylation without affecting total mTOR and insulin-elicited response on mTOR phosphorylation.	Acetaldehyde	0-12	mechanistic target of rapamycin kinase	Homo sapiens	23-27
16962100-10	2007	Interestingly, acetaldehyde enhanced p70(S6K) activation and depressed 4E-BP1 phosphorylation, the effect of which was blunted and exaggerated, respectively, by rapamycin.	Acetaldehyde	15-27	ribosomal protein S6 kinase B1	Homo sapiens	37-40
16962100-10	2007	Interestingly, acetaldehyde enhanced p70(S6K) activation and depressed 4E-BP1 phosphorylation, the effect of which was blunted and exaggerated, respectively, by rapamycin.	Acetaldehyde	15-27	eukaryotic translation initiation factor 4E binding protein 1	Homo sapiens	71-77
16962100-11	2007	Collectively, these data suggested that acetaldehyde did not adversely affect glucose uptake despite inhibition of insulin signaling cascade at the levels of Akt and mTOR, possibly due to presence of certain mechanism(s) responsible for enhanced p70(S6K) phosphorylation.	Acetaldehyde	40-52	insulin	Homo sapiens	115-122
17127431-1	2007	In this study, we evaluated the inhalation toxicity of acetaldehyde in Aldh2 KO (Aldh -/-) mice, using pathological method.	Acetaldehyde	55-67	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	71-76
17127431-1	2007	In this study, we evaluated the inhalation toxicity of acetaldehyde in Aldh2 KO (Aldh -/-) mice, using pathological method.	Acetaldehyde	55-67	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	71-75
17127431-3	2007	Although the average blood acetaldehyde concentration of Aldh -/- mice was higher than that of Aldh2 +/+ mice in the acetaldehyde exposure group, observable effects by the acetaldehyde exposure on the lung and liver were not different between wild type and ALDH2 null mice.	Acetaldehyde	27-39	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	57-61
17127431-4	2007	In Aldh2 -/- mice, the levels of 1) erosion of respiratory epithelium and the subepithelial hemorrhage in nose, 2) hemorrhage in nasal cavity, 3) degeneration of respiratory epithelium in larynx, pharynx and trachea, and 4) degeneration of dorsal skin were higher compared with Aldh2 +/+ mice, indicating that Aldh2 -/- mice are more acetaldehyde-sensitive than Aldh2 +/+ mice.	Acetaldehyde	334-346	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	3-8
17127431-5	2007	This is the first example for studying pathological effects of Aldh2 deficiency using Aldh -/- mice exposed to a low level of acetaldehyde.	Acetaldehyde	126-138	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	63-68
17127431-5	2007	This is the first example for studying pathological effects of Aldh2 deficiency using Aldh -/- mice exposed to a low level of acetaldehyde.	Acetaldehyde	126-138	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	63-67
17590984-0	2007	Acetaldehyde generating enzyme systems: roles of alcohol dehydrogenase, CYP2E1 and catalase, and speculations on the role of other enzymes and processes.	Acetaldehyde	0-12	aldo-keto reductase family 1 member A1	Homo sapiens	49-70
17590984-0	2007	Acetaldehyde generating enzyme systems: roles of alcohol dehydrogenase, CYP2E1 and catalase, and speculations on the role of other enzymes and processes.	Acetaldehyde	0-12	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	72-78
17590997-3	2007	Acetaldehyde caused temporal activation of p42/44 MAPK followed by JNK, but the activation of the p42/44 MAPK was not a prerequisite for the JNK activation.	Acetaldehyde	0-12	cyclin dependent kinase 20	Homo sapiens	43-46
17590997-3	2007	Acetaldehyde caused temporal activation of p42/44 MAPK followed by JNK, but the activation of the p42/44 MAPK was not a prerequisite for the JNK activation.	Acetaldehyde	0-12	mitogen-activated protein kinase 8	Homo sapiens	67-70
17590984-0	2007	Acetaldehyde generating enzyme systems: roles of alcohol dehydrogenase, CYP2E1 and catalase, and speculations on the role of other enzymes and processes.	Acetaldehyde	0-12	catalase	Homo sapiens	83-91
17590997-5	2007	Ethanol and acetaldehyde activatedJNK have opposing roles; ethanol-induced JNK activation increased apoptosis whereas that by acetaldehyde decreased apoptosis.	Acetaldehyde	12-24	mitogen-activated protein kinase 8	Homo sapiens	34-37
17590997-5	2007	Ethanol and acetaldehyde activatedJNK have opposing roles; ethanol-induced JNK activation increased apoptosis whereas that by acetaldehyde decreased apoptosis.	Acetaldehyde	126-138	mitogen-activated protein kinase 8	Homo sapiens	34-37
17590997-6	2007	Acetaldehyde also caused histone H3 acetylation at Lys9 and phosphorylation of histone H3 at Serl0 and 28, the latter being dependent on p38 MAP kinase.	Acetaldehyde	0-12	mitogen-activated protein kinase 14	Homo sapiens	137-140
17590984-1	2007	Most acetaldehyde is generated in the liver by alcohol dehydrogenase (ADH) during ethanol metabolism.	Acetaldehyde	5-17	aldo-keto reductase family 1 member A1	Homo sapiens	47-68
17590984-1	2007	Most acetaldehyde is generated in the liver by alcohol dehydrogenase (ADH) during ethanol metabolism.	Acetaldehyde	5-17	aldo-keto reductase family 1 member A1	Homo sapiens	70-73
17590984-3	2007	Two additional pathways of acetaldehyde generation are by the cytochrome P450 2E1 (CYP2E1) and catalase.	Acetaldehyde	27-39	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	62-81
17590984-3	2007	Two additional pathways of acetaldehyde generation are by the cytochrome P450 2E1 (CYP2E1) and catalase.	Acetaldehyde	27-39	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	83-89
17590984-3	2007	Two additional pathways of acetaldehyde generation are by the cytochrome P450 2E1 (CYP2E1) and catalase.	Acetaldehyde	27-39	catalase	Homo sapiens	95-103
17590984-5	2007	Additional sources of acetaldehyde include other minor enzymes (nitric oxide synthase, other cytochrome P450s, P450 reductase, xanthine oxidoreductase) as well as non-enzymatic pathways (formation of hydroxyethyl radicals from the reaction of ethanol with hydroxyl radical, and its subsequent decomposition to acetaldehyde).	Acetaldehyde	22-34	xanthine dehydrogenase	Homo sapiens	127-150
17590985-7	2007	The best known ALDH genetic polymorphism is in ALDH2 gene, which encodes a mitochondrial enzyme primarily responsible for the oxidation of the ethanol-derived acetaldehyde.	Acetaldehyde	159-171	aldehyde dehydrogenase 2 family member	Homo sapiens	47-52
17590985-17	2007	There are a few other enzymes such as aldehyde oxidase, xanthine oxidase, cytochrome P450 oxidase and glyceraldehyde-3-phosphate dehydrogenase that are capable of oxidizing acetaldehyde.	Acetaldehyde	173-185	aldehyde oxidase 1	Homo sapiens	38-54
17590987-0	2007	Acetaldehyde and alcoholic cardiomyopathy: lessons from the ADH and ALDH2 transgenic models.	Acetaldehyde	0-12	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	68-73
17590991-1	2007	Breath acetaldehyde has been used to investigate the production of acetaldehyde after ethanol ingestion in ALDH2-deficient individuals, to compare ethanol and acetaldehyde metabolism, to study the toxicological outcome of metabolic inhibitors of ALDH2, and as a biomarker of exposure to ethanol vapours.	Acetaldehyde	7-19	aldehyde dehydrogenase 2 family member	Homo sapiens	107-112
17590991-1	2007	Breath acetaldehyde has been used to investigate the production of acetaldehyde after ethanol ingestion in ALDH2-deficient individuals, to compare ethanol and acetaldehyde metabolism, to study the toxicological outcome of metabolic inhibitors of ALDH2, and as a biomarker of exposure to ethanol vapours.	Acetaldehyde	67-79	aldehyde dehydrogenase 2 family member	Homo sapiens	107-112
17590991-1	2007	Breath acetaldehyde has been used to investigate the production of acetaldehyde after ethanol ingestion in ALDH2-deficient individuals, to compare ethanol and acetaldehyde metabolism, to study the toxicological outcome of metabolic inhibitors of ALDH2, and as a biomarker of exposure to ethanol vapours.	Acetaldehyde	67-79	aldehyde dehydrogenase 2 family member	Homo sapiens	107-112
17590991-4	2007	The interpretation of breath acetaldehyde is compounded by several factors; smoking, ALDH2 polymorphism and alcohol drinking habits are associated with higher breath/blood levels.	Acetaldehyde	29-41	aldehyde dehydrogenase 2 family member	Homo sapiens	85-90
17590992-10	2007	The study suggested that catalase made a significant contribution to acetaldehyde formation in the rat brain, and that EtOH and acetaldehyde decreased ChAT expression at 40 and 240 min after EtOH dosing.	Acetaldehyde	69-81	catalase	Rattus norvegicus	25-33
17590996-8	2007	In PSCs, additional signalling molecules identified as important to the process of ethanol and acetaldehyde-induced PSC activation include protein kinase C (PKC), phosphatidylinositol-3-kinase (PI3K) and peroxisome proliferator-activated receptor gamma (PPARgamma).	Acetaldehyde	95-107	phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit gamma	Homo sapiens	163-192
17590996-8	2007	In PSCs, additional signalling molecules identified as important to the process of ethanol and acetaldehyde-induced PSC activation include protein kinase C (PKC), phosphatidylinositol-3-kinase (PI3K) and peroxisome proliferator-activated receptor gamma (PPARgamma).	Acetaldehyde	95-107	peroxisome proliferator activated receptor gamma	Homo sapiens	204-252
17590996-8	2007	In PSCs, additional signalling molecules identified as important to the process of ethanol and acetaldehyde-induced PSC activation include protein kinase C (PKC), phosphatidylinositol-3-kinase (PI3K) and peroxisome proliferator-activated receptor gamma (PPARgamma).	Acetaldehyde	95-107	peroxisome proliferator activated receptor gamma	Homo sapiens	254-263
17176845-5	2006	Acetoaldehyde has been suggested to be involved in the mechanism of exacerbation of ARDS by inducing lung remodeling through stimulation of fibronectin expression following nicotinic acetylcholine receptor stimulation and CREB activation in chronic alcohol abuse.	Acetaldehyde	0-13	fibronectin 1	Homo sapiens	140-151
17084997-0	2006	Ethanol oxidation into acetaldehyde by 16 recombinant human cytochrome P450 isoforms: role of CYP2C isoforms in human liver microsomes.	Acetaldehyde	23-35	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	60-75
17084997-3	2006	All of the tested CYPs, except CYP2A6 and CYP2C18, metabolized ethanol into significant amounts of acetaldehyde and displayed K(m) values around 10mM.	Acetaldehyde	99-111	cytochrome P450 family 2 subfamily A member 6	Homo sapiens	31-37
17084997-3	2006	All of the tested CYPs, except CYP2A6 and CYP2C18, metabolized ethanol into significant amounts of acetaldehyde and displayed K(m) values around 10mM.	Acetaldehyde	99-111	cytochrome P450 family 2 subfamily C member 18	Homo sapiens	42-49
17040107-2	2006	Although many studies suggest that acetaldehyde, a major metabolite of orally ingested alcohol, plays a crucial role in cancer initiation, the link between the aldehyde dehydrogenase-2 (ALDH2) genotype and acetaldehyde-derived DNA damage has not yet been explored.	Acetaldehyde	35-47	aldehyde dehydrogenase 2 family member	Homo sapiens	186-191
17040107-2	2006	Although many studies suggest that acetaldehyde, a major metabolite of orally ingested alcohol, plays a crucial role in cancer initiation, the link between the aldehyde dehydrogenase-2 (ALDH2) genotype and acetaldehyde-derived DNA damage has not yet been explored.	Acetaldehyde	206-218	aldehyde dehydrogenase 2 family member	Homo sapiens	160-184
17040107-2	2006	Although many studies suggest that acetaldehyde, a major metabolite of orally ingested alcohol, plays a crucial role in cancer initiation, the link between the aldehyde dehydrogenase-2 (ALDH2) genotype and acetaldehyde-derived DNA damage has not yet been explored.	Acetaldehyde	206-218	aldehyde dehydrogenase 2 family member	Homo sapiens	186-191
17040107-5	2006	The levels of three acetaldehyde-derived DNA adducts, N(2)-Et-dG, alpha-S-Me-gamma-OH-PdG, and alpha-R-Me-gamma-OH-PdG, were significantly higher in alcoholics with the ALDH2 1/2 2 genotype compared to those with the ALDH2 1/2 1 genotype.	Acetaldehyde	20-32	aldehyde dehydrogenase 2 family member	Homo sapiens	169-174
17040107-5	2006	The levels of three acetaldehyde-derived DNA adducts, N(2)-Et-dG, alpha-S-Me-gamma-OH-PdG, and alpha-R-Me-gamma-OH-PdG, were significantly higher in alcoholics with the ALDH2 1/2 2 genotype compared to those with the ALDH2 1/2 1 genotype.	Acetaldehyde	20-32	aldehyde dehydrogenase 2 family member	Homo sapiens	217-222
17040107-7	2006	These results provide molecular evidence that the ALDH2 genotype affects the genotoxic damage caused by acetaldehyde.	Acetaldehyde	104-116	aldehyde dehydrogenase 2 family member	Homo sapiens	50-55
17030193-0	2006	Acetaldehyde inhibits PPARgamma via H2O2-mediated c-Abl activation in human hepatic stellate cells.	Acetaldehyde	0-12	peroxisome proliferator activated receptor gamma	Homo sapiens	22-31
17030193-0	2006	Acetaldehyde inhibits PPARgamma via H2O2-mediated c-Abl activation in human hepatic stellate cells.	Acetaldehyde	0-12	ABL proto-oncogene 1, non-receptor tyrosine kinase	Homo sapiens	50-55
16829625-7	2006	Although ethanol clearance was increased, acetaldehyde elimination was reduced when RXRalpha was not expressed in the liver.	Acetaldehyde	42-54	retinoid X receptor alpha	Mus musculus	84-92
16829625-11	2006	Thus, RXRalpha differentially affects ADH and ALDH activity, leading to an increase in alcohol clearance, but a reduction in acetaldehyde elimination.	Acetaldehyde	125-137	retinoid X receptor alpha	Mus musculus	6-14
16829625-11	2006	Thus, RXRalpha differentially affects ADH and ALDH activity, leading to an increase in alcohol clearance, but a reduction in acetaldehyde elimination.	Acetaldehyde	125-137	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	46-50
17050345-7	2006	Significant inductions of IL-1beta, TNF-alpha, and Cox-1 and Cox-2 mRNA were observed following exposure to &gt; or =50 ppm acetaldehyde for 4 h. IL-6 and MCP-1 were also induced following a 4-h exposure to 500 ppm acetaldehyde.	Acetaldehyde	124-136	interleukin 1 beta	Homo sapiens	26-34
17050345-7	2006	Significant inductions of IL-1beta, TNF-alpha, and Cox-1 and Cox-2 mRNA were observed following exposure to &gt; or =50 ppm acetaldehyde for 4 h. IL-6 and MCP-1 were also induced following a 4-h exposure to 500 ppm acetaldehyde.	Acetaldehyde	124-136	tumor necrosis factor	Homo sapiens	36-45
17050345-7	2006	Significant inductions of IL-1beta, TNF-alpha, and Cox-1 and Cox-2 mRNA were observed following exposure to &gt; or =50 ppm acetaldehyde for 4 h. IL-6 and MCP-1 were also induced following a 4-h exposure to 500 ppm acetaldehyde.	Acetaldehyde	124-136	mitochondrially encoded cytochrome c oxidase I	Homo sapiens	51-56
17050345-7	2006	Significant inductions of IL-1beta, TNF-alpha, and Cox-1 and Cox-2 mRNA were observed following exposure to &gt; or =50 ppm acetaldehyde for 4 h. IL-6 and MCP-1 were also induced following a 4-h exposure to 500 ppm acetaldehyde.	Acetaldehyde	124-136	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	61-66
17050345-7	2006	Significant inductions of IL-1beta, TNF-alpha, and Cox-1 and Cox-2 mRNA were observed following exposure to &gt; or =50 ppm acetaldehyde for 4 h. IL-6 and MCP-1 were also induced following a 4-h exposure to 500 ppm acetaldehyde.	Acetaldehyde	124-136	interleukin 6	Homo sapiens	146-150
17050345-7	2006	Significant inductions of IL-1beta, TNF-alpha, and Cox-1 and Cox-2 mRNA were observed following exposure to &gt; or =50 ppm acetaldehyde for 4 h. IL-6 and MCP-1 were also induced following a 4-h exposure to 500 ppm acetaldehyde.	Acetaldehyde	124-136	C-C motif chemokine ligand 2	Homo sapiens	155-160
17050345-7	2006	Significant inductions of IL-1beta, TNF-alpha, and Cox-1 and Cox-2 mRNA were observed following exposure to &gt; or =50 ppm acetaldehyde for 4 h. IL-6 and MCP-1 were also induced following a 4-h exposure to 500 ppm acetaldehyde.	Acetaldehyde	215-227	interleukin 1 beta	Homo sapiens	26-34
17050345-7	2006	Significant inductions of IL-1beta, TNF-alpha, and Cox-1 and Cox-2 mRNA were observed following exposure to &gt; or =50 ppm acetaldehyde for 4 h. IL-6 and MCP-1 were also induced following a 4-h exposure to 500 ppm acetaldehyde.	Acetaldehyde	215-227	mitochondrially encoded cytochrome c oxidase I	Homo sapiens	51-56
17050345-7	2006	Significant inductions of IL-1beta, TNF-alpha, and Cox-1 and Cox-2 mRNA were observed following exposure to &gt; or =50 ppm acetaldehyde for 4 h. IL-6 and MCP-1 were also induced following a 4-h exposure to 500 ppm acetaldehyde.	Acetaldehyde	215-227	mitochondrially encoded cytochrome c oxidase II	Homo sapiens	61-66
17050345-7	2006	Significant inductions of IL-1beta, TNF-alpha, and Cox-1 and Cox-2 mRNA were observed following exposure to &gt; or =50 ppm acetaldehyde for 4 h. IL-6 and MCP-1 were also induced following a 4-h exposure to 500 ppm acetaldehyde.	Acetaldehyde	215-227	interleukin 6	Homo sapiens	146-150
17050345-7	2006	Significant inductions of IL-1beta, TNF-alpha, and Cox-1 and Cox-2 mRNA were observed following exposure to &gt; or =50 ppm acetaldehyde for 4 h. IL-6 and MCP-1 were also induced following a 4-h exposure to 500 ppm acetaldehyde.	Acetaldehyde	215-227	C-C motif chemokine ligand 2	Homo sapiens	155-160
16971503-5	2006	Acetaldehyde also induced RANKL expression.	Acetaldehyde	0-12	TNF superfamily member 11	Rattus norvegicus	26-31
17010132-1	2006	BACKGROUND: It is widely accepted that, in addition to removing acetaldehyde produced during the metabolism of ethanol, mitochondrial aldehyde dehydrogenase (ALDH2) functions in the pathway by which aldehyde metabolites of the monoamines dopamine (DA) and serotonin (5-HT) are converted to their acidic metabolites.	Acetaldehyde	64-76	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	158-163
17010133-5	2006	However, significantly higher expression of mRNA for aldehyde dehydrogenase 2 (ALDH2), an isoform mainly responsible for the catabolism of acetaldehyde, was observed in whole brains of DBA/2 mice with both platforms.	Acetaldehyde	139-151	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	53-77
17010133-5	2006	However, significantly higher expression of mRNA for aldehyde dehydrogenase 2 (ALDH2), an isoform mainly responsible for the catabolism of acetaldehyde, was observed in whole brains of DBA/2 mice with both platforms.	Acetaldehyde	139-151	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	79-84
17176845-5	2006	Acetoaldehyde has been suggested to be involved in the mechanism of exacerbation of ARDS by inducing lung remodeling through stimulation of fibronectin expression following nicotinic acetylcholine receptor stimulation and CREB activation in chronic alcohol abuse.	Acetaldehyde	0-13	cAMP responsive element binding protein 1	Homo sapiens	222-226
16939272-3	2006	While the crotylations of acetaldehyde and propionaldehyde mainly result in the syn product for E-configurated silane and in the anti product for Z-configurated silane, the syn product is found as main product for the crotylation of pivaldehyde regardless of substrate double bond geometry.	Acetaldehyde	26-38	synemin	Homo sapiens	80-83
16939272-3	2006	While the crotylations of acetaldehyde and propionaldehyde mainly result in the syn product for E-configurated silane and in the anti product for Z-configurated silane, the syn product is found as main product for the crotylation of pivaldehyde regardless of substrate double bond geometry.	Acetaldehyde	26-38	synemin	Homo sapiens	173-176
16713055-6	2006	These observations suggest that NOS2 can behave similarly to cytochrome P-450 in the catalysis of acetaldehyde formation from ethanol via the generation of alpha-hydroxyethyl radical when L-arginine is present.	Acetaldehyde	98-110	nitric oxide synthase 2	Homo sapiens	32-36
16930209-3	2006	Variations in the ADH1B and ADH1C genes may influence the LR to alcohol by increasing levels of acetaldehyde during alcohol metabolism, although most data on this question come from Asian populations.	Acetaldehyde	96-108	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	18-23
16930209-3	2006	Variations in the ADH1B and ADH1C genes may influence the LR to alcohol by increasing levels of acetaldehyde during alcohol metabolism, although most data on this question come from Asian populations.	Acetaldehyde	96-108	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	28-33
16878979-6	2006	Consistent with the rate-limiting step for ALDH1 being changed from coenzyme dissociation to deacylation was finding that chloroacetaldehyde was oxidized more rapidly than acetaldehyde.	Acetaldehyde	128-140	aldehyde dehydrogenase 1 family member A1	Homo sapiens	43-48
16675441-2	2006	Class I ADH is the major enzyme that catalyzes alcohol to acetaldehyde in the liver.	Acetaldehyde	58-70	alcohol dehydrogenase 7 (class IV), mu or sigma polypeptide	Homo sapiens	8-11
16818871-1	2006	CONTEXT: The ALDH2*2 allele has been shown to be a protective factor against alcoholism in a normal population owing in part to the elevated blood level of acetaldehyde and its accompanying physiological discomforts after drinking alcohol.	Acetaldehyde	156-168	aldehyde dehydrogenase 2 family member	Homo sapiens	13-18
16784954-0	2006	Alcohol alters skeletal muscle heat shock protein gene expression in rats: these effects are moderated by sex, raised endogenous acetaldehyde, and starvation.	Acetaldehyde	129-141	selenoprotein K	Rattus norvegicus	31-49
16930212-9	2006	Ethanol-derived AC accumulation in brain homogenates of acatalasemic mice was 47% of the control value, 91% in CYP2E1-null mice, and 24% in double mutants (with deficiency of both catalase and CYP2E1).	Acetaldehyde	16-18	cytochrome P450, family 2, subfamily e, polypeptide 1	Mus musculus	111-117
16814256-0	2006	Adiponectin protects human neuroblastoma SH-SY5Y cells against acetaldehyde-induced cytotoxicity.	Acetaldehyde	63-75	adiponectin, C1Q and collagen domain containing	Homo sapiens	0-11
16814256-3	2006	In this study, we investigated the protective effects of adiponectin on acetaldehyde-induced apoptosis in human neuroblastoma SH-SY5Y cells and attempted to examine its mechanism.	Acetaldehyde	72-84	adiponectin, C1Q and collagen domain containing	Homo sapiens	57-68
16814256-4	2006	Acetaldehyde-induced apoptosis was moderately reversed by adiponectin treatment.	Acetaldehyde	0-12	adiponectin, C1Q and collagen domain containing	Homo sapiens	58-69
16814256-5	2006	Our results suggest that the protective effects of adiponectin on acetaldehyde-induced apoptosis may be ascribed to ability to induce the expression of anti-oxidant enzymes and to regulate Bcl-2 and Bax expression.	Acetaldehyde	66-78	adiponectin, C1Q and collagen domain containing	Homo sapiens	51-62
16814256-5	2006	Our results suggest that the protective effects of adiponectin on acetaldehyde-induced apoptosis may be ascribed to ability to induce the expression of anti-oxidant enzymes and to regulate Bcl-2 and Bax expression.	Acetaldehyde	66-78	BCL2 apoptosis regulator	Homo sapiens	189-194
16814256-5	2006	Our results suggest that the protective effects of adiponectin on acetaldehyde-induced apoptosis may be ascribed to ability to induce the expression of anti-oxidant enzymes and to regulate Bcl-2 and Bax expression.	Acetaldehyde	66-78	BCL2 associated X, apoptosis regulator	Homo sapiens	199-202
16881685-6	2006	The concentration of methionine, adenine, and sulfite in a synthetic grape must influences the progress of fermentation and at the transcriptional level the expression of genes involved in sulfur (MET16), adenine (ADE4), and acetaldehyde (ALD6) metabolism.	Acetaldehyde	225-237	aldehyde dehydrogenase (NADP(+)) ALD6	Saccharomyces cerevisiae S288C	239-243
16713055-6	2006	These observations suggest that NOS2 can behave similarly to cytochrome P-450 in the catalysis of acetaldehyde formation from ethanol via the generation of alpha-hydroxyethyl radical when L-arginine is present.	Acetaldehyde	98-110	cytochrome P450 family 4 subfamily F member 3	Homo sapiens	61-77
16554376-4	2006	RESULTS: Rosiglitazone caused an upregulation of mitochondrial ALD2, thus significantly detoxifying acetaldehyde.	Acetaldehyde	100-112	aldehyde dehydrogenase 1 family, member A1	Rattus norvegicus	63-67
16637693-6	2006	In parallel with the activity of LOX, C6 compound [hexanal, hex-1-enol, (E)-hex-2-enal] concentrations reached a peak at 11.7% of weight loss, whereas ethanol and acetaldehyde increased with the increase of ADH and successively decrease and ethyl acetate increased.	Acetaldehyde	163-175	lipoxygenase	Vitis vinifera	33-36
16344274-2	2006	Individuals differ in their ability to metabolize alcohol through genetic differences in alcohol dehydrogenase (ADH), the enzyme that catalyzes the oxidation of approximately 80% of ethanol to acetaldehyde, a known carcinogen.	Acetaldehyde	193-205	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	112-115
16123765-4	2006	The locomotor effects of intranigral ethanol (1.4 micromol) were reduced by coadministration of 10 mg/kg sodium azide, a catalase inhibitor that acts to reduce the metabolism of ethanol into acetaldehyde in the brain.	Acetaldehyde	191-203	catalase	Homo sapiens	121-129
16732922-0	2006	[Effects of ERK deactivation on functions of rat cultured hepatic stellate cells stimulated by acetaldehyde].	Acetaldehyde	95-107	Eph receptor B1	Rattus norvegicus	12-15
16287084-2	2006	Increased acetaldehyde production via alcohol dehydrogenase (ADH) has been implicated in the pathogenesis.	Acetaldehyde	10-22	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	61-64
16287084-3	2006	The allele ADH1C*1 of ADH1C encodes for an enzyme with a high capacity to generate acetaldehyde.	Acetaldehyde	83-95	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	11-16
16287084-3	2006	The allele ADH1C*1 of ADH1C encodes for an enzyme with a high capacity to generate acetaldehyde.	Acetaldehyde	83-95	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	22-27
16566845-1	2006	The enzyme aldehyde dehydrogenase (ALDH) is essential for ethanol metabolism in mammals, converting the highly toxic intermediate acetaldehyde to acetate.	Acetaldehyde	130-142	Aldehyde dehydrogenase	Drosophila melanogaster	35-39
16566845-2	2006	The role of ALDH in Drosophila has been debated, with some authors arguing that, at least in larvae, acetaldehyde detoxification is carried out mainly by alcohol dehydrogenase (ADH), the enzyme responsible for converting ethanol to acetaldehyde.	Acetaldehyde	101-113	Aldehyde dehydrogenase	Drosophila melanogaster	12-16
16566845-1	2006	The enzyme aldehyde dehydrogenase (ALDH) is essential for ethanol metabolism in mammals, converting the highly toxic intermediate acetaldehyde to acetate.	Acetaldehyde	130-142	Aldehyde dehydrogenase	Drosophila melanogaster	11-33
16566845-2	2006	The role of ALDH in Drosophila has been debated, with some authors arguing that, at least in larvae, acetaldehyde detoxification is carried out mainly by alcohol dehydrogenase (ADH), the enzyme responsible for converting ethanol to acetaldehyde.	Acetaldehyde	101-113	Alcohol dehydrogenase	Drosophila melanogaster	154-175
16566845-2	2006	The role of ALDH in Drosophila has been debated, with some authors arguing that, at least in larvae, acetaldehyde detoxification is carried out mainly by alcohol dehydrogenase (ADH), the enzyme responsible for converting ethanol to acetaldehyde.	Acetaldehyde	101-113	Alcohol dehydrogenase	Drosophila melanogaster	177-180
16566845-2	2006	The role of ALDH in Drosophila has been debated, with some authors arguing that, at least in larvae, acetaldehyde detoxification is carried out mainly by alcohol dehydrogenase (ADH), the enzyme responsible for converting ethanol to acetaldehyde.	Acetaldehyde	232-244	Alcohol dehydrogenase	Drosophila melanogaster	154-175
16502397-3	2006	Acetaldehyde, the first metabolite of ethanol, can upregulate transcription of collagen I directly as well as indirectly by upregulating the synthesis of transforming growth factor-beta 1 (TGF-beta1).	Acetaldehyde	0-12	transforming growth factor beta 1	Homo sapiens	154-187
16566845-2	2006	The role of ALDH in Drosophila has been debated, with some authors arguing that, at least in larvae, acetaldehyde detoxification is carried out mainly by alcohol dehydrogenase (ADH), the enzyme responsible for converting ethanol to acetaldehyde.	Acetaldehyde	232-244	Alcohol dehydrogenase	Drosophila melanogaster	177-180
16502397-3	2006	Acetaldehyde, the first metabolite of ethanol, can upregulate transcription of collagen I directly as well as indirectly by upregulating the synthesis of transforming growth factor-beta 1 (TGF-beta1).	Acetaldehyde	0-12	transforming growth factor beta 1	Homo sapiens	189-198
16502397-11	2006	The inactive aldehyde dehydrogenase (ALDH2) and the super-active alcohol dehydrogenase (ADH2) alleles may promote hepatic fibrosis through increased accumulation of acetaldehyde in the liver.	Acetaldehyde	165-177	aldehyde dehydrogenase 2 family member	Homo sapiens	37-42
16502397-11	2006	The inactive aldehyde dehydrogenase (ALDH2) and the super-active alcohol dehydrogenase (ADH2) alleles may promote hepatic fibrosis through increased accumulation of acetaldehyde in the liver.	Acetaldehyde	165-177	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	88-92
16499490-1	2006	BACKGROUND: Aldehyde dehydrogenase-2 (ALDH2) is the key enzyme for elimination of acetaldehyde, an established animal carcinogen produced after drinking.	Acetaldehyde	82-94	aldehyde dehydrogenase 2 family member	Homo sapiens	12-36
16734278-1	2006	The deficiency in activity of aldehyde dehydrogenase-2 (ALDH2), commonly found in Asians, is due to a mutation at position 487 in exon 12, encoded by the ALDH2*2 allele, which is a crucial factor for deficient ability to acetaldehyde (AcH) oxidation.	Acetaldehyde	221-233	aldehyde dehydrogenase 2 family member	Homo sapiens	30-54
16734278-1	2006	The deficiency in activity of aldehyde dehydrogenase-2 (ALDH2), commonly found in Asians, is due to a mutation at position 487 in exon 12, encoded by the ALDH2*2 allele, which is a crucial factor for deficient ability to acetaldehyde (AcH) oxidation.	Acetaldehyde	221-233	aldehyde dehydrogenase 2 family member	Homo sapiens	56-61
16734278-1	2006	The deficiency in activity of aldehyde dehydrogenase-2 (ALDH2), commonly found in Asians, is due to a mutation at position 487 in exon 12, encoded by the ALDH2*2 allele, which is a crucial factor for deficient ability to acetaldehyde (AcH) oxidation.	Acetaldehyde	221-233	aldehyde dehydrogenase 2 family member	Homo sapiens	154-159
16734278-1	2006	The deficiency in activity of aldehyde dehydrogenase-2 (ALDH2), commonly found in Asians, is due to a mutation at position 487 in exon 12, encoded by the ALDH2*2 allele, which is a crucial factor for deficient ability to acetaldehyde (AcH) oxidation.	Acetaldehyde	235-238	aldehyde dehydrogenase 2 family member	Homo sapiens	30-54
16734278-1	2006	The deficiency in activity of aldehyde dehydrogenase-2 (ALDH2), commonly found in Asians, is due to a mutation at position 487 in exon 12, encoded by the ALDH2*2 allele, which is a crucial factor for deficient ability to acetaldehyde (AcH) oxidation.	Acetaldehyde	235-238	aldehyde dehydrogenase 2 family member	Homo sapiens	56-61
16734278-1	2006	The deficiency in activity of aldehyde dehydrogenase-2 (ALDH2), commonly found in Asians, is due to a mutation at position 487 in exon 12, encoded by the ALDH2*2 allele, which is a crucial factor for deficient ability to acetaldehyde (AcH) oxidation.	Acetaldehyde	235-238	aldehyde dehydrogenase 2 family member	Homo sapiens	154-159
16553429-0	2006	Theoretical study of the mechanism of acetaldehyde hydroxylation by compound I of CYP2E1.	Acetaldehyde	38-50	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	82-88
16553429-1	2006	Recent experimental studies revealed that cytochrome P450 2E1 (CYP2E1) could metabolize not only ethanol but also its primary product, acetaldehyde, accompanying the well-known acetaldehyde dehydrogenases (ALDH) in the metabolism of acetaldehyde.	Acetaldehyde	135-147	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	42-61
16553429-1	2006	Recent experimental studies revealed that cytochrome P450 2E1 (CYP2E1) could metabolize not only ethanol but also its primary product, acetaldehyde, accompanying the well-known acetaldehyde dehydrogenases (ALDH) in the metabolism of acetaldehyde.	Acetaldehyde	135-147	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	63-69
16553429-1	2006	Recent experimental studies revealed that cytochrome P450 2E1 (CYP2E1) could metabolize not only ethanol but also its primary product, acetaldehyde, accompanying the well-known acetaldehyde dehydrogenases (ALDH) in the metabolism of acetaldehyde.	Acetaldehyde	177-189	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	42-61
16553429-1	2006	Recent experimental studies revealed that cytochrome P450 2E1 (CYP2E1) could metabolize not only ethanol but also its primary product, acetaldehyde, accompanying the well-known acetaldehyde dehydrogenases (ALDH) in the metabolism of acetaldehyde.	Acetaldehyde	177-189	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	63-69
16553429-2	2006	Mechanistic aspects of acetaldehyde hydroxylation by Compound I model active species of CYP2E1 were investigated by means of B3LYP DFT calculations in the present paper.	Acetaldehyde	23-35	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	88-94
16553429-3	2006	Our study results demonstrate that acetaldehyde hydroxylation by CYP2E1 is in accord with the effectively concerted mechanisms both on the high quartet spin state (HS) and on the low doublet spin state (LS).	Acetaldehyde	35-47	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	65-71
16499490-2	2006	In persons with inactive ALDH2, the body fails to metabolize acetaldehyde rapidly, leading to excessive accumulation of acetaldehyde.	Acetaldehyde	120-132	aldehyde dehydrogenase 2 family member	Homo sapiens	25-30
16499490-1	2006	BACKGROUND: Aldehyde dehydrogenase-2 (ALDH2) is the key enzyme for elimination of acetaldehyde, an established animal carcinogen produced after drinking.	Acetaldehyde	82-94	aldehyde dehydrogenase 2 family member	Homo sapiens	38-43
16499490-2	2006	In persons with inactive ALDH2, the body fails to metabolize acetaldehyde rapidly, leading to excessive accumulation of acetaldehyde.	Acetaldehyde	61-73	aldehyde dehydrogenase 2 family member	Homo sapiens	25-30
16603817-4	2006	All divalent cations tested inhibited the oxidation of acetaldehyde and retinal by ALDH1A1.	Acetaldehyde	55-67	aldehyde dehydrogenase 1 family member A1 L homeolog	Xenopus laevis	83-90
16603817-2	2006	ALDH1A1, also known as ALDH class 1 (ALDH1) or retinaldehyde dehydrogenase (RALDH1), prefers retinal to acetaldehyde as a substrate.	Acetaldehyde	104-116	aldehyde dehydrogenase 1 family member A1 L homeolog	Xenopus laevis	0-7
16603817-6	2006	Kinetic studies of ALDH1A1 dehydrogenase activity in the presence or absence of each cation revealed that the inhibition mode by cations was uncompetitive against acetaldehyde, retinal, and NAD+, and that their inhibitory potencies were greater against acetaldehyde than retinal.	Acetaldehyde	163-175	aldehyde dehydrogenase 1 family member A1 L homeolog	Xenopus laevis	19-26
16603817-2	2006	ALDH1A1, also known as ALDH class 1 (ALDH1) or retinaldehyde dehydrogenase (RALDH1), prefers retinal to acetaldehyde as a substrate.	Acetaldehyde	104-116	aldehyde dehydrogenase 1 family member A1 L homeolog	Xenopus laevis	23-35
16603817-6	2006	Kinetic studies of ALDH1A1 dehydrogenase activity in the presence or absence of each cation revealed that the inhibition mode by cations was uncompetitive against acetaldehyde, retinal, and NAD+, and that their inhibitory potencies were greater against acetaldehyde than retinal.	Acetaldehyde	253-265	aldehyde dehydrogenase 1 family member A1 L homeolog	Xenopus laevis	19-26
16603817-2	2006	ALDH1A1, also known as ALDH class 1 (ALDH1) or retinaldehyde dehydrogenase (RALDH1), prefers retinal to acetaldehyde as a substrate.	Acetaldehyde	104-116	aldehyde dehydrogenase 1 family member A1 L homeolog	Xenopus laevis	0-5
16603817-2	2006	ALDH1A1, also known as ALDH class 1 (ALDH1) or retinaldehyde dehydrogenase (RALDH1), prefers retinal to acetaldehyde as a substrate.	Acetaldehyde	104-116	aldehyde dehydrogenase 1 family member A1 L homeolog	Xenopus laevis	76-82
16126235-1	2006	Ethanol is converted to acetaldehyde by alcohol dehydrogenase (ADH), cytochrome p4502E1 (CYP2E1) and catalase.	Acetaldehyde	24-36	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	89-95
16603817-3	2006	To investigate the effects of divalent cations on the dehydrogenase activity of Xenopus laevis ALDH1A1, the formation of acetate and retinoic acid from acetaldehyde and retinal, respectively, was investigated in the presence of Ca2+, Mg2+, Mn2+ or Zn2+.	Acetaldehyde	152-164	aldehyde dehydrogenase 1 family member A1 L homeolog	Xenopus laevis	95-102
16387289-2	2006	This study aims at the search for direct in vitro effects of different concentrations of acetaldehyde (30, 100 and 300microM) on the activities of glutathione reductase (GR), glutathione peroxidase (GPx) from liver supernatants, and the thiol-peroxidase activity of ebselen.	Acetaldehyde	89-101	glutathione reductase	Mus musculus	147-168
16387289-2	2006	This study aims at the search for direct in vitro effects of different concentrations of acetaldehyde (30, 100 and 300microM) on the activities of glutathione reductase (GR), glutathione peroxidase (GPx) from liver supernatants, and the thiol-peroxidase activity of ebselen.	Acetaldehyde	89-101	glutathione reductase	Mus musculus	170-172
16387289-5	2006	In addition, acetaldehyde (up to 300microM) significantly oxidized GSH when incubated in the presence of commercially available gamma-glutamyltranspeptidase (GGT), but not in the presence of glutathione-S-transferase.	Acetaldehyde	13-25	gamma-glutamyltransferase 1	Mus musculus	128-156
16387289-5	2006	In addition, acetaldehyde (up to 300microM) significantly oxidized GSH when incubated in the presence of commercially available gamma-glutamyltranspeptidase (GGT), but not in the presence of glutathione-S-transferase.	Acetaldehyde	13-25	gamma-glutamyltransferase 1	Mus musculus	158-161
16387289-8	2006	Overall, the acetaldehyde oxidation of hepatic low-molecular thiols depends on mouse liver constituents and GGT is proposed as an important enzyme involved in this phenomenon.	Acetaldehyde	13-25	gamma-glutamyltransferase 1	Mus musculus	108-111
16126235-2	2006	This metabolite is then detoxified by aldehyde dehydrogenase 2 (ALDH2), a key enzyme in the elimination of acetaldehyde, via further oxidation to acetic acid.	Acetaldehyde	107-119	aldehyde dehydrogenase 2 family member	Homo sapiens	38-62
16126235-2	2006	This metabolite is then detoxified by aldehyde dehydrogenase 2 (ALDH2), a key enzyme in the elimination of acetaldehyde, via further oxidation to acetic acid.	Acetaldehyde	107-119	aldehyde dehydrogenase 2 family member	Homo sapiens	64-69
16144726-8	2006	Using a transgenic MEF feeder spheroid, engineered for gaseous acetaldehyde-inducible interferon-beta (ifn-beta) production by cotransduction of retro-/ lenti-viral particles, a short 6-h ifn-beta induction was sufficient to rescue the integrity of DRG:MEF spheroids and enable long-term cultivation of these microtissues.	Acetaldehyde	63-75	interferon beta 1, fibroblast	Mus musculus	86-101
16403513-0	2006	Attenuation of acetaldehyde-induced cell injury by overexpression of aldehyde dehydrogenase-2 (ALDH2) transgene in human cardiac myocytes: role of MAP kinase signaling.	Acetaldehyde	15-27	aldehyde dehydrogenase 2 family member	Homo sapiens	69-93
16403513-0	2006	Attenuation of acetaldehyde-induced cell injury by overexpression of aldehyde dehydrogenase-2 (ALDH2) transgene in human cardiac myocytes: role of MAP kinase signaling.	Acetaldehyde	15-27	aldehyde dehydrogenase 2 family member	Homo sapiens	95-100
16403513-2	2006	This study was designed to examine the impact of facilitated acetaldehyde metabolism using transfection of human aldehyde dehydrogenase-2 (ALDH2) transgene on acetaldehyde- and ethanol-induced cell injury.	Acetaldehyde	61-73	aldehyde dehydrogenase 2 family member	Homo sapiens	113-137
16403513-2	2006	This study was designed to examine the impact of facilitated acetaldehyde metabolism using transfection of human aldehyde dehydrogenase-2 (ALDH2) transgene on acetaldehyde- and ethanol-induced cell injury.	Acetaldehyde	61-73	aldehyde dehydrogenase 2 family member	Homo sapiens	139-144
16403513-2	2006	This study was designed to examine the impact of facilitated acetaldehyde metabolism using transfection of human aldehyde dehydrogenase-2 (ALDH2) transgene on acetaldehyde- and ethanol-induced cell injury.	Acetaldehyde	159-171	aldehyde dehydrogenase 2 family member	Homo sapiens	113-137
16403513-2	2006	This study was designed to examine the impact of facilitated acetaldehyde metabolism using transfection of human aldehyde dehydrogenase-2 (ALDH2) transgene on acetaldehyde- and ethanol-induced cell injury.	Acetaldehyde	159-171	aldehyde dehydrogenase 2 family member	Homo sapiens	139-144
16403513-7	2006	Immunostaining revealed activation of the MAP kinase cascades ERK1/2, SAPK/JNK and p38 MAP kinase in acetaldehyde-treated myocytes.	Acetaldehyde	101-113	mitogen-activated protein kinase 3	Homo sapiens	62-68
16403513-7	2006	Immunostaining revealed activation of the MAP kinase cascades ERK1/2, SAPK/JNK and p38 MAP kinase in acetaldehyde-treated myocytes.	Acetaldehyde	101-113	mitogen-activated protein kinase 9	Homo sapiens	70-74
16403513-7	2006	Immunostaining revealed activation of the MAP kinase cascades ERK1/2, SAPK/JNK and p38 MAP kinase in acetaldehyde-treated myocytes.	Acetaldehyde	101-113	mitogen-activated protein kinase 8	Homo sapiens	75-78
16403513-7	2006	Immunostaining revealed activation of the MAP kinase cascades ERK1/2, SAPK/JNK and p38 MAP kinase in acetaldehyde-treated myocytes.	Acetaldehyde	101-113	mitogen-activated protein kinase 1	Homo sapiens	83-86
16403513-8	2006	Interestingly, ALDH2 transgene significantly attenuated acetaldehyde-induced ROS generation, apoptosis and phosphorylation of ERK1/2 and SAPK/JNK.	Acetaldehyde	56-68	aldehyde dehydrogenase 2 family member	Homo sapiens	15-20
16403513-8	2006	Interestingly, ALDH2 transgene significantly attenuated acetaldehyde-induced ROS generation, apoptosis and phosphorylation of ERK1/2 and SAPK/JNK.	Acetaldehyde	56-68	mitogen-activated protein kinase 3	Homo sapiens	126-132
16403513-8	2006	Interestingly, ALDH2 transgene significantly attenuated acetaldehyde-induced ROS generation, apoptosis and phosphorylation of ERK1/2 and SAPK/JNK.	Acetaldehyde	56-68	mitogen-activated protein kinase 9	Homo sapiens	137-141
16403513-8	2006	Interestingly, ALDH2 transgene significantly attenuated acetaldehyde-induced ROS generation, apoptosis and phosphorylation of ERK1/2 and SAPK/JNK.	Acetaldehyde	56-68	mitogen-activated protein kinase 8	Homo sapiens	142-145
16360119-5	2006	Our results suggest that the protective effects of rosiglitazone on acetaldehyde-induced apoptosis may be ascribed to ability to induce the expression of anti-oxidant enzymes and to regulate Bcl-2 and Bax expression.	Acetaldehyde	68-80	BCL2 apoptosis regulator	Homo sapiens	191-196
16360119-5	2006	Our results suggest that the protective effects of rosiglitazone on acetaldehyde-induced apoptosis may be ascribed to ability to induce the expression of anti-oxidant enzymes and to regulate Bcl-2 and Bax expression.	Acetaldehyde	68-80	BCL2 associated X, apoptosis regulator	Homo sapiens	201-204
16403513-11	2006	Our results suggested that ALDH2 transgene overexpression may effectively alleviate acetaldehyde-elicited cell injury through an ERK1/2 and SPAK/JNK-dependent mechanism.	Acetaldehyde	84-96	aldehyde dehydrogenase 2 family member	Homo sapiens	27-32
16403513-11	2006	Our results suggested that ALDH2 transgene overexpression may effectively alleviate acetaldehyde-elicited cell injury through an ERK1/2 and SPAK/JNK-dependent mechanism.	Acetaldehyde	84-96	mitogen-activated protein kinase 3	Homo sapiens	129-135
16403513-11	2006	Our results suggested that ALDH2 transgene overexpression may effectively alleviate acetaldehyde-elicited cell injury through an ERK1/2 and SPAK/JNK-dependent mechanism.	Acetaldehyde	84-96	serine/threonine kinase 39	Homo sapiens	140-144
16403513-11	2006	Our results suggested that ALDH2 transgene overexpression may effectively alleviate acetaldehyde-elicited cell injury through an ERK1/2 and SPAK/JNK-dependent mechanism.	Acetaldehyde	84-96	mitogen-activated protein kinase 8	Homo sapiens	145-148
16144726-8	2006	Using a transgenic MEF feeder spheroid, engineered for gaseous acetaldehyde-inducible interferon-beta (ifn-beta) production by cotransduction of retro-/ lenti-viral particles, a short 6-h ifn-beta induction was sufficient to rescue the integrity of DRG:MEF spheroids and enable long-term cultivation of these microtissues.	Acetaldehyde	63-75	interferon beta 1, fibroblast	Mus musculus	103-111
16144726-8	2006	Using a transgenic MEF feeder spheroid, engineered for gaseous acetaldehyde-inducible interferon-beta (ifn-beta) production by cotransduction of retro-/ lenti-viral particles, a short 6-h ifn-beta induction was sufficient to rescue the integrity of DRG:MEF spheroids and enable long-term cultivation of these microtissues.	Acetaldehyde	63-75	interferon beta 1, fibroblast	Mus musculus	188-196
16203750-11	2006	CONCLUSIONS: We conclude that CETP from alcohol abusers may have a glycosylation defect due to defective sialylation caused posttranslationally by alcohol itself or its metabolite acetaldehyde.	Acetaldehyde	180-192	cholesteryl ester transfer protein	Homo sapiens	30-34
16610557-1	2006	To clarify the carcinogenicity of acetaldehyde when associated with ALDH (aldehyde dehydrogenase) 2 polymorphism, Aldh2 knock-out (Aldh2-/-) mice and their wild type (Aldh2+/+) mice were exposed to two different concentrations of acetaldehyde (125 ppm and 500 ppm) for two weeks.	Acetaldehyde	34-46	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	68-72
17718404-7	2006	Studies manipulating the activity of the enzyme catalase, which promotes acetaldehyde production in the brain, suggest that acetaldehyde contributes to many behavioral effects of alcohol, especially its stimulant properties.	Acetaldehyde	73-85	catalase	Homo sapiens	48-56
17718404-7	2006	Studies manipulating the activity of the enzyme catalase, which promotes acetaldehyde production in the brain, suggest that acetaldehyde contributes to many behavioral effects of alcohol, especially its stimulant properties.	Acetaldehyde	124-136	catalase	Homo sapiens	48-56
16610557-4	2006	At 125 ppm acetaldehyde exposure for 12 d, urinary 8-OHdG levels in Aldh2+/+ mice did not increase.	Acetaldehyde	11-23	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	68-73
16610557-9	2006	In conclusion, it is suspected that DNA was damaged by acetaldehyde inhalation, and that susceptibility to acetaldehyde varies according to Aldh2 genotype.	Acetaldehyde	107-119	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	140-145
16679777-5	2006	We also genotyped a polymorphism, G1510A, in the acetaldehyde dehydrogenase 2 gene (ALDH2), in which the A allele causes poor metabolism of acetaldehyde, a major metabolite of alcohol.	Acetaldehyde	49-61	aldehyde dehydrogenase 2 family member	Homo sapiens	84-89
16365683-1	2006	Deficiencies in mitochondrial low-Km aldehyde dehydrogenase (ALDH2) activity, and consequently high blood acetaldehyde levels, have been suggested to relate to various diseases in Japanese, including esophageal cancer.	Acetaldehyde	106-118	aldehyde dehydrogenase 2 family member	Homo sapiens	61-66
16365683-2	2006	In the present study, 200 men aged 35-59 years randomly selected from an occupational population were analyzed for the association of ALDH2 genotypes and cytochrome P450-2E1 (CYP2E1) genotypes with the urinary excretion of acetaldehyde (which is bound to some chemicals in the urine) and with common alcohol-related health consequences.	Acetaldehyde	223-235	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	154-173
15950440-4	2005	The aim of the present study was to characterize the anxiolytic effects of acetaldehyde in two strains of mice, C57BL/6J and CD1 mice with the elevated plus-maze procedure.	Acetaldehyde	75-87	CD1 antigen complex	Mus musculus	125-128
16344722-2	2006	Ethanol is metabolized to acetaldehyde mainly by the alcohol dehydrogenase pathway (ADHs) and, to a lesser extent, by microsomal oxidization (CYP2E1) and the catalase-H2O2 system.	Acetaldehyde	26-38	catalase	Mus musculus	158-166
16344722-8	2006	The Cyp2e1(-/-) animals produced lower whole blood levels of acetaldehyde than wild-type controls; however, this difference was seen only at higher doses of ethanol.	Acetaldehyde	61-73	cytochrome P450, family 2, subfamily e, polypeptide 1	Mus musculus	4-10
16344722-9	2006	The amount of acetaldehyde produced following the incubation of ethanol with liver and brain microsomes was greater in tissues derived from 129/sv than in those from Cyp2e1(-/-) mice.	Acetaldehyde	14-26	cytochrome P450, family 2, subfamily e, polypeptide 1	Mus musculus	166-172
16385179-4	2005	ALDH inactive form resulting from ALDH2*2, which slows the elimination of acetaldehyde and the more active isozymes produced by ADH1B*2, could generate higher acetaldehyde levels and thus deter heavy drinking ().	Acetaldehyde	74-86	aldehyde dehydrogenase 2 family member	Homo sapiens	34-39
16385179-4	2005	ALDH inactive form resulting from ALDH2*2, which slows the elimination of acetaldehyde and the more active isozymes produced by ADH1B*2, could generate higher acetaldehyde levels and thus deter heavy drinking ().	Acetaldehyde	159-171	aldehyde dehydrogenase 2 family member	Homo sapiens	34-39
16385179-4	2005	ALDH inactive form resulting from ALDH2*2, which slows the elimination of acetaldehyde and the more active isozymes produced by ADH1B*2, could generate higher acetaldehyde levels and thus deter heavy drinking ().	Acetaldehyde	159-171	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	128-133
16373280-9	2006	An ALDH isoform(s) is responsible for this process and physiological concentration of acetaldehyde hampers the process, probably in a competitive manner.	Acetaldehyde	86-98	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	3-7
16326430-9	2005	The levels of p53, bcl-2, and 8-OHdG were concomitantly changed by alcohol and acetaldehyde treatment in midbrain cells.	Acetaldehyde	79-91	tumor protein p53	Homo sapiens	14-17
16326430-9	2005	The levels of p53, bcl-2, and 8-OHdG were concomitantly changed by alcohol and acetaldehyde treatment in midbrain cells.	Acetaldehyde	79-91	BCL2 apoptosis regulator	Homo sapiens	19-24
16109828-6	2005	ADH or ADH-CAT myocytes had higher acetaldehyde-producing ability.	Acetaldehyde	35-47	catalase	Mus musculus	11-14
16340452-0	2005	Aldehyde dehydrogenase 2 gene targeting mouse lacking enzyme activity shows high acetaldehyde level in blood, brain, and liver after ethanol gavages.	Acetaldehyde	81-93	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	0-22
16404140-0	2005	Aldehyde dehydrogenase 2 activity affects symptoms produced by an intraperitoneal acetaldehyde injection, but not acetaldehyde lethality.	Acetaldehyde	82-94	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	0-24
16404140-1	2005	Aldehyde dehydrogenase 2 (ALDH2) is an important enzyme that oxidizes acetaldehyde.	Acetaldehyde	70-82	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	0-24
16404140-1	2005	Aldehyde dehydrogenase 2 (ALDH2) is an important enzyme that oxidizes acetaldehyde.	Acetaldehyde	70-82	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	26-31
16404140-11	2005	This might be attributable to the absence of a significant difference in the blood acetaldehyde concentrations in both mice during the first 0-15 min following administration; however, acetaldehyde elimination delay was observed in the Aldh2-/- mice as compared with the Aldh2+/+ mice.	Acetaldehyde	185-197	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	236-241
16404141-0	2005	Paired acute inhalation test reveals that acetaldehyde toxicity is higher in aldehyde dehydrogenase 2 knockout mice than in wild-type mice.	Acetaldehyde	42-54	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	77-101
16404141-1	2005	Aldehyde dehydrogenase 2 (ALDH2) is an important enzyme that oxidizes acetaldehyde.	Acetaldehyde	70-82	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	0-24
16404141-1	2005	Aldehyde dehydrogenase 2 (ALDH2) is an important enzyme that oxidizes acetaldehyde.	Acetaldehyde	70-82	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	26-31
16404141-12	2005	The blood acetaldehyde level in the Aldh2-/- mice was approximately twice that in the Aldh2+/+ mice 4 hr after inhalation.	Acetaldehyde	10-22	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	36-41
16404141-12	2005	The blood acetaldehyde level in the Aldh2-/- mice was approximately twice that in the Aldh2+/+ mice 4 hr after inhalation.	Acetaldehyde	10-22	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	86-91
16404141-13	2005	The Aldh2-/- mice evidently showed more severe toxicity as compared with the Aldh2+/+ mice due to acute inhalation of acetaldehyde at a concentration of 5000 ppm.	Acetaldehyde	118-130	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	4-9
16404141-15	2005	Based on this study, acetaldehyde inhalations were inferred to pose a higher risk to ALDH2-inactive human individuals.	Acetaldehyde	21-33	aldehyde dehydrogenase 2 family member	Homo sapiens	85-90
16404797-5	2005	The hypothesized mechanism underlying the associations of the ADH1B and ALDH2 polymorphisms with alcohol dependence is that the isoenzymes encoded by these alleles lead to an accumulation of acetaldehyde during alcohol metabolism.	Acetaldehyde	191-203	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	62-67
16404797-5	2005	The hypothesized mechanism underlying the associations of the ADH1B and ALDH2 polymorphisms with alcohol dependence is that the isoenzymes encoded by these alleles lead to an accumulation of acetaldehyde during alcohol metabolism.	Acetaldehyde	191-203	aldehyde dehydrogenase 2 family member	Homo sapiens	72-77
16404797-6	2005	Based on their kinetic properties, ALDH2 *2 theoretically should lead to a slower removal of acetaldehyde than ALDH2*1, whereas ADH1B*2 and ADH1B*3 should lead to a more rapid production of acetaldehyde than ADHIB*I.	Acetaldehyde	93-105	aldehyde dehydrogenase 2 family member	Homo sapiens	35-40
16404797-6	2005	Based on their kinetic properties, ALDH2 *2 theoretically should lead to a slower removal of acetaldehyde than ALDH2*1, whereas ADH1B*2 and ADH1B*3 should lead to a more rapid production of acetaldehyde than ADHIB*I.	Acetaldehyde	93-105	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	128-133
16404797-6	2005	Based on their kinetic properties, ALDH2 *2 theoretically should lead to a slower removal of acetaldehyde than ALDH2*1, whereas ADH1B*2 and ADH1B*3 should lead to a more rapid production of acetaldehyde than ADHIB*I.	Acetaldehyde	93-105	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	140-145
16404797-6	2005	Based on their kinetic properties, ALDH2 *2 theoretically should lead to a slower removal of acetaldehyde than ALDH2*1, whereas ADH1B*2 and ADH1B*3 should lead to a more rapid production of acetaldehyde than ADHIB*I.	Acetaldehyde	190-202	aldehyde dehydrogenase 2 family member	Homo sapiens	35-40
16404797-6	2005	Based on their kinetic properties, ALDH2 *2 theoretically should lead to a slower removal of acetaldehyde than ALDH2*1, whereas ADH1B*2 and ADH1B*3 should lead to a more rapid production of acetaldehyde than ADHIB*I.	Acetaldehyde	190-202	aldehyde dehydrogenase 2 family member	Homo sapiens	111-116
16404797-6	2005	Based on their kinetic properties, ALDH2 *2 theoretically should lead to a slower removal of acetaldehyde than ALDH2*1, whereas ADH1B*2 and ADH1B*3 should lead to a more rapid production of acetaldehyde than ADHIB*I.	Acetaldehyde	190-202	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	128-133
16404797-6	2005	Based on their kinetic properties, ALDH2 *2 theoretically should lead to a slower removal of acetaldehyde than ALDH2*1, whereas ADH1B*2 and ADH1B*3 should lead to a more rapid production of acetaldehyde than ADHIB*I.	Acetaldehyde	190-202	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	140-145
16404797-8	2005	Data are consistent with the hypothesis that elevations in acetaldehyde, increased sensitivity to alcohol, and lower levels of drinking reflect the mechanism by which the ALDH2*2 allele reduces risk for alcohol dependence.	Acetaldehyde	59-71	aldehyde dehydrogenase 2 family member	Homo sapiens	171-176
16242127-1	2005	Mitochondrial aldehyde dehydrogenase (ALDH2) is responsible for the metabolism of acetaldehyde and other toxic lipid aldehydes.	Acetaldehyde	82-94	aldehyde dehydrogenase 2 family member	Rattus norvegicus	0-36
16242127-1	2005	Mitochondrial aldehyde dehydrogenase (ALDH2) is responsible for the metabolism of acetaldehyde and other toxic lipid aldehydes.	Acetaldehyde	82-94	aldehyde dehydrogenase 2 family member	Rattus norvegicus	38-43
16340452-6	2005	RESULTS: Significantly higher blood acetaldehyde concentrations were found in the Aldh2-/- mice than in the Aldh2+/+ mice 1 hr after the administration of ethanol gavages at doses of 0.5, 1.0, 2.0, and 5.0 g/kg.	Acetaldehyde	36-48	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	82-87
16340452-6	2005	RESULTS: Significantly higher blood acetaldehyde concentrations were found in the Aldh2-/- mice than in the Aldh2+/+ mice 1 hr after the administration of ethanol gavages at doses of 0.5, 1.0, 2.0, and 5.0 g/kg.	Acetaldehyde	36-48	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	108-113
16340452-9	2005	The aldehyde dehydrogenase 2 enzyme metabolized 94% of the acetaldehyde produced from the ethanol as calculated from the area under the curve (AUC) of acetaldehyde when ethanol was administered at a dose of 5.0 g/kg.	Acetaldehyde	59-71	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	4-26
16340452-9	2005	The aldehyde dehydrogenase 2 enzyme metabolized 94% of the acetaldehyde produced from the ethanol as calculated from the area under the curve (AUC) of acetaldehyde when ethanol was administered at a dose of 5.0 g/kg.	Acetaldehyde	151-163	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	4-26
16340452-10	2005	CONCLUSIONS: These data indicate that mouse ALDH2 is a major enzyme for acetaldehyde metabolism, and the Aldh2-/- mice have significantly high acetaldehyde levels after ethanol gavages.	Acetaldehyde	72-84	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	44-49
16340452-10	2005	CONCLUSIONS: These data indicate that mouse ALDH2 is a major enzyme for acetaldehyde metabolism, and the Aldh2-/- mice have significantly high acetaldehyde levels after ethanol gavages.	Acetaldehyde	72-84	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	105-110
16340452-10	2005	CONCLUSIONS: These data indicate that mouse ALDH2 is a major enzyme for acetaldehyde metabolism, and the Aldh2-/- mice have significantly high acetaldehyde levels after ethanol gavages.	Acetaldehyde	143-155	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	105-110
16132116-0	2005	Acetaldehyde-induced interleukin-1beta and tumor necrosis factor-alpha production is inhibited by berberine through nuclear factor-kappaB signaling pathway in HepG2 cells.	Acetaldehyde	0-12	interleukin 1 beta	Homo sapiens	21-38
16241166-6	2005	One-electron oxidation of 3 leads to oxidative degradation of the fifth EtO ligand to liberate acetaldehyde even at 203 K. The iron(III)-phenoxyl radical shows high reactivity for alcoxide on iron(III) but exhibits virtually no reactivity for alcohols including even benzyl alcohol without a base to remove an alcohol proton.	Acetaldehyde	95-107	RUNX1 partner transcriptional co-repressor 1	Homo sapiens	72-75
16218611-2	2005	Keys for success were (1) stereoselective intermolecular aldol reaction at the C-4 position with acetaldehyde, (2) stereoelective Claisen rearrangement to introduce an allyl group to the most sterically crowded position at C-6, (3) ring-closing metathesis to construct the B-ring, and (4) Wacker-type oxidative C-ring formation.	Acetaldehyde	97-109	complement C4A (Rodgers blood group)	Homo sapiens	79-82
16132116-0	2005	Acetaldehyde-induced interleukin-1beta and tumor necrosis factor-alpha production is inhibited by berberine through nuclear factor-kappaB signaling pathway in HepG2 cells.	Acetaldehyde	0-12	tumor necrosis factor	Homo sapiens	43-70
16132116-0	2005	Acetaldehyde-induced interleukin-1beta and tumor necrosis factor-alpha production is inhibited by berberine through nuclear factor-kappaB signaling pathway in HepG2 cells.	Acetaldehyde	0-12	nuclear factor kappa B subunit 1	Homo sapiens	116-137
16132116-4	2005	In this study, we demonstrated that acetaldehyde, the metabolic product of ethanol, was able to induce IL-1beta and TNF-alpha production in HepG2 cells.	Acetaldehyde	36-48	interleukin 1 beta	Homo sapiens	103-111
16132116-4	2005	In this study, we demonstrated that acetaldehyde, the metabolic product of ethanol, was able to induce IL-1beta and TNF-alpha production in HepG2 cells.	Acetaldehyde	36-48	tumor necrosis factor	Homo sapiens	116-125
16132116-5	2005	Nuclear factor-kappaB (NF-kappaB), the transcription factor involved in the regulation of cytokine production, was also activated by acetaldehyde through inhibitory kappaB-alpha (IkappaB-alpha) phosphorylation and degradation.	Acetaldehyde	133-145	nuclear factor kappa B subunit 1	Homo sapiens	0-21
16132116-5	2005	Nuclear factor-kappaB (NF-kappaB), the transcription factor involved in the regulation of cytokine production, was also activated by acetaldehyde through inhibitory kappaB-alpha (IkappaB-alpha) phosphorylation and degradation.	Acetaldehyde	133-145	nuclear factor kappa B subunit 1	Homo sapiens	23-32
16132116-5	2005	Nuclear factor-kappaB (NF-kappaB), the transcription factor involved in the regulation of cytokine production, was also activated by acetaldehyde through inhibitory kappaB-alpha (IkappaB-alpha) phosphorylation and degradation.	Acetaldehyde	133-145	NFKB inhibitor alpha	Homo sapiens	179-192
16132116-6	2005	However, the NF-kappaB inhibitors, such as aspirin, cyclosporin A and dexamethasone, inhibited both the acetaldehyde-induced NF-kappaB activity and the induced cytokine production.	Acetaldehyde	104-116	nuclear factor kappa B subunit 1	Homo sapiens	13-22
16132116-6	2005	However, the NF-kappaB inhibitors, such as aspirin, cyclosporin A and dexamethasone, inhibited both the acetaldehyde-induced NF-kappaB activity and the induced cytokine production.	Acetaldehyde	104-116	nuclear factor kappa B subunit 1	Homo sapiens	125-134
16132116-7	2005	Therefore, these data suggested that acetaldehyde stimulated IL-1beta and TNF-alpha production via the regulation of NF-kappaB signaling pathway.	Acetaldehyde	37-49	interleukin 1 beta	Homo sapiens	61-69
16132116-7	2005	Therefore, these data suggested that acetaldehyde stimulated IL-1beta and TNF-alpha production via the regulation of NF-kappaB signaling pathway.	Acetaldehyde	37-49	tumor necrosis factor	Homo sapiens	74-83
16132116-7	2005	Therefore, these data suggested that acetaldehyde stimulated IL-1beta and TNF-alpha production via the regulation of NF-kappaB signaling pathway.	Acetaldehyde	37-49	nuclear factor kappa B subunit 1	Homo sapiens	117-126
16132116-8	2005	By screening 297 controlled Chinese medicinal herbs supervised by Committee on Chinese Medicine and Pharmacy at Taiwan, we found that Coptis chinensis (Huang-Lien) and Phellodendron amurense (Huang-Po) were capable of inhibiting acetaldehyde-induced NF-kappaB activity.	Acetaldehyde	229-241	nuclear factor kappa B subunit 1	Homo sapiens	250-259
16132116-9	2005	Berberine, the major ingredient of these herbs, abolished acetaldehyde-induced NF-kappaB activity and cytokine production in a dose-dependent manner.	Acetaldehyde	58-70	nuclear factor kappa B subunit 1	Homo sapiens	79-88
16132116-11	2005	In conclusion, we first linked the acetaldehyde-induced NF-kappaB activity to the induced proinflammatory cytokine production in HepG2 cells.	Acetaldehyde	35-47	nuclear factor kappa B subunit 1	Homo sapiens	56-65
15718285-0	2005	Acetaldehyde disrupts tight junctions and adherens junctions in human colonic mucosa: protection by EGF and L-glutamine.	Acetaldehyde	0-12	epidermal growth factor	Homo sapiens	100-103
15982967-9	2005	Furthermore, an acetaldehyde-adducted protein, i.e. bovine serum albumin (BSA) is less degraded than a native BSA by purified proteasome.	Acetaldehyde	16-28	albumin	Rattus norvegicus	59-72
15970497-2	2005	Acetaldehyde, a highly toxic intermediate produced from ethanol, is converted to acetic acid mainly by aldehyde dehydrogenase 2 (ALDH2) in the metabolic pathway of ethanol.	Acetaldehyde	0-12	aldehyde dehydrogenase 2 family member	Homo sapiens	103-127
15970497-2	2005	Acetaldehyde, a highly toxic intermediate produced from ethanol, is converted to acetic acid mainly by aldehyde dehydrogenase 2 (ALDH2) in the metabolic pathway of ethanol.	Acetaldehyde	0-12	aldehyde dehydrogenase 2 family member	Homo sapiens	129-134
15718285-4	2005	Acetaldehyde reduced the protein tyrosine phosphatase activity, thereby increasing the tyrosine phosphorylation of occludin, E-cadherin, and beta-catenin.	Acetaldehyde	0-12	occludin	Homo sapiens	115-123
15718285-4	2005	Acetaldehyde reduced the protein tyrosine phosphatase activity, thereby increasing the tyrosine phosphorylation of occludin, E-cadherin, and beta-catenin.	Acetaldehyde	0-12	cadherin 1	Homo sapiens	125-135
15718285-4	2005	Acetaldehyde reduced the protein tyrosine phosphatase activity, thereby increasing the tyrosine phosphorylation of occludin, E-cadherin, and beta-catenin.	Acetaldehyde	0-12	catenin beta 1	Homo sapiens	141-153
15718285-5	2005	The levels of occludin, zonula occludens-1, E-cadherin, and beta-catenin in detergent-insoluble fractions were reduced by acetaldehyde, while it increased their levels in detergent-soluble fractions.	Acetaldehyde	122-134	occludin	Homo sapiens	14-22
15718285-5	2005	The levels of occludin, zonula occludens-1, E-cadherin, and beta-catenin in detergent-insoluble fractions were reduced by acetaldehyde, while it increased their levels in detergent-soluble fractions.	Acetaldehyde	122-134	cadherin 1	Homo sapiens	44-54
15718285-5	2005	The levels of occludin, zonula occludens-1, E-cadherin, and beta-catenin in detergent-insoluble fractions were reduced by acetaldehyde, while it increased their levels in detergent-soluble fractions.	Acetaldehyde	122-134	catenin beta 1	Homo sapiens	60-72
15718285-6	2005	Pretreatment with EGF or L-glutamine prevented acetaldehyde-induced protein tyrosine phosphorylation, redistribution from intercellular junctions, and reduction in the levels of detergent-insoluble fractions of occludin, zonula occludens-1, E-cadherin, and beta-catenin.	Acetaldehyde	47-59	epidermal growth factor	Homo sapiens	18-21
15718285-6	2005	Pretreatment with EGF or L-glutamine prevented acetaldehyde-induced protein tyrosine phosphorylation, redistribution from intercellular junctions, and reduction in the levels of detergent-insoluble fractions of occludin, zonula occludens-1, E-cadherin, and beta-catenin.	Acetaldehyde	47-59	occludin	Homo sapiens	211-219
15718285-6	2005	Pretreatment with EGF or L-glutamine prevented acetaldehyde-induced protein tyrosine phosphorylation, redistribution from intercellular junctions, and reduction in the levels of detergent-insoluble fractions of occludin, zonula occludens-1, E-cadherin, and beta-catenin.	Acetaldehyde	47-59	cadherin 1	Homo sapiens	241-251
15718285-6	2005	Pretreatment with EGF or L-glutamine prevented acetaldehyde-induced protein tyrosine phosphorylation, redistribution from intercellular junctions, and reduction in the levels of detergent-insoluble fractions of occludin, zonula occludens-1, E-cadherin, and beta-catenin.	Acetaldehyde	47-59	catenin beta 1	Homo sapiens	257-269
15718285-7	2005	These results demonstrate that acetaldehyde induces tyrosine phosphorylation and disrupts tight junction and adherens junction in human colonic mucosa, which can be prevented by EGF and glutamine.	Acetaldehyde	31-43	epidermal growth factor	Homo sapiens	178-181
16103445-4	2005	The ability to metabolize acetaldehyde is encoded by the ALDH2 gene, which is polymorphic in some populations.	Acetaldehyde	26-38	aldehyde dehydrogenase 2 family member	Homo sapiens	57-62
16025520-9	2005	In conclusion, acetaldehyde-dependent mechanisms involved in COL1A2 upregulation are similar, but not identical, to those of TGF-beta1.	Acetaldehyde	15-27	collagen type I alpha 2 chain	Homo sapiens	61-67
16131845-1	2005	BACKGROUND: Individuals carrying the Glu487Lys coding mutation in the gene for mitochondrial aldehyde dehydrogenase (ALDH2) have a diminished capacity to metabolize acetaldehyde.	Acetaldehyde	165-177	aldehyde dehydrogenase 2 family member	Homo sapiens	117-122
16131845-3	2005	In the present studies, we aimed to mimic the high-acetaldehyde low-ALDH2 activity phenotype in a rat hepatoma cell line by inhibiting Aldh2 gene expression by an Aldh2 antisense-coding gene carried by an adenoviral vector.	Acetaldehyde	51-63	aldehyde dehydrogenase 2 family member	Rattus norvegicus	135-140
16131845-3	2005	In the present studies, we aimed to mimic the high-acetaldehyde low-ALDH2 activity phenotype in a rat hepatoma cell line by inhibiting Aldh2 gene expression by an Aldh2 antisense-coding gene carried by an adenoviral vector.	Acetaldehyde	51-63	aldehyde dehydrogenase 2 family member	Rattus norvegicus	163-168
16131845-6	2005	RESULTS: Studies showed that 1) the antisense gene is actively transcribed in the cells and high levels of antisense mRNA are attained, 2) the antisense gene reduced ALDH2 activity by 65%, and 3) when incubated with 10 mM ethanol, acetaldehyde accumulation by cells increased 8-fold to levels (80-90 microM) known to be aversive to animals and humans.	Acetaldehyde	231-243	aldehyde dehydrogenase 2 family member	Homo sapiens	166-171
16131845-7	2005	CONCLUSIONS: Data presented show that antialcohol drugs that inhibit Aldh2 gene expression can be generated endogenously in liver cells infected by an adenoviral vector carrying an antisense-coding gene, thus mimicking the high-acetaldehyde phenotype that exists in humans carrying the Glu487Lys mutation who are protected against alcoholism.	Acetaldehyde	228-240	aldehyde dehydrogenase 2 family member	Homo sapiens	69-74
16025520-0	2005	Early response of alpha2(I) collagen to acetaldehyde in human hepatic stellate cells is TGF-beta independent.	Acetaldehyde	40-52	collagen type I alpha 2 chain	Homo sapiens	18-36
16025520-0	2005	Early response of alpha2(I) collagen to acetaldehyde in human hepatic stellate cells is TGF-beta independent.	Acetaldehyde	40-52	transforming growth factor beta 1	Homo sapiens	88-96
16025520-10	2005	We suggest that early acetaldehyde-dependent events induce the late expression of TGF-beta1 and create an H(2)O(2)-dependent autocrine loop that may sustain and amplify the fibrogenic response of this alcohol metabolite.	Acetaldehyde	22-34	transforming growth factor beta 1	Homo sapiens	82-91
15864308-2	2005	Pyruvate loses carbon dioxide to produce acetaldehyde, which is reduced by alcohol dehydrogenase 1 (Adh1) to ethanol, which accumulates.	Acetaldehyde	41-53	alcohol dehydrogenase ADH1	Saccharomyces cerevisiae S288C	75-98
16025520-3	2005	We localized to the -378 to -183 region of the alpha2(I) collagen (COL1A2) promoter an acetaldehyde-responsive element (AcRE) functional in human hepatic stellate cells (HHSCs) and investigated molecular mechanisms whereby acetaldehyde stimulates and modulates its transcriptional activity.	Acetaldehyde	87-99	collagen type I alpha 2 chain	Homo sapiens	47-65
16025520-3	2005	We localized to the -378 to -183 region of the alpha2(I) collagen (COL1A2) promoter an acetaldehyde-responsive element (AcRE) functional in human hepatic stellate cells (HHSCs) and investigated molecular mechanisms whereby acetaldehyde stimulates and modulates its transcriptional activity.	Acetaldehyde	87-99	collagen type I alpha 2 chain	Homo sapiens	67-73
16025520-3	2005	We localized to the -378 to -183 region of the alpha2(I) collagen (COL1A2) promoter an acetaldehyde-responsive element (AcRE) functional in human hepatic stellate cells (HHSCs) and investigated molecular mechanisms whereby acetaldehyde stimulates and modulates its transcriptional activity.	Acetaldehyde	223-235	collagen type I alpha 2 chain	Homo sapiens	47-65
16025520-3	2005	We localized to the -378 to -183 region of the alpha2(I) collagen (COL1A2) promoter an acetaldehyde-responsive element (AcRE) functional in human hepatic stellate cells (HHSCs) and investigated molecular mechanisms whereby acetaldehyde stimulates and modulates its transcriptional activity.	Acetaldehyde	223-235	collagen type I alpha 2 chain	Homo sapiens	67-73
16025520-5	2005	Here we show that acetaldehyde-induced COL1A2 upregulation in HHSCs recognizes two distinct but overlapping early and late stages that last from 1 to 6 hours and from 6 to 24 hours, respectively.	Acetaldehyde	18-30	collagen type I alpha 2 chain	Homo sapiens	39-45
15948243-7	2005	Ethanol and acetaldehyde at clinically relevant concentrations decreased basal activation of JAK2 and STAT3.	Acetaldehyde	12-24	Janus kinase 2	Rattus norvegicus	93-97
16046871-11	2005	CONCLUSIONS: Inactive heterozygous ALDH2, alcohol flushing, and increased MCV were positively associated with hangover susceptibility in Japanese workers, suggesting that acetaldehyde is etiologically linked to the development of hangover.	Acetaldehyde	171-183	aldehyde dehydrogenase 2 family member	Homo sapiens	35-40
15948243-7	2005	Ethanol and acetaldehyde at clinically relevant concentrations decreased basal activation of JAK2 and STAT3.	Acetaldehyde	12-24	signal transducer and activator of transcription 3	Rattus norvegicus	102-107
15864308-2	2005	Pyruvate loses carbon dioxide to produce acetaldehyde, which is reduced by alcohol dehydrogenase 1 (Adh1) to ethanol, which accumulates.	Acetaldehyde	41-53	alcohol dehydrogenase ADH1	Saccharomyces cerevisiae S288C	100-104
15900217-0	2005	Polymorphisms in the mitochondrial aldehyde dehydrogenase gene (Aldh2) determine peak blood acetaldehyde levels and voluntary ethanol consumption in rats.	Acetaldehyde	92-104	aldehyde dehydrogenase 2 family member	Rattus norvegicus	21-57
15900217-7	2005	A major phenotypic difference was a five-fold higher (P&lt;0.0025) peak blood acetaldehyde level following ethanol administration in the lower drinker F2 Aldh2(2)/Aldh2(2) compared to the higher drinker F2 Aldh2(1)/Aldh2(1) animals, despite the existence of identical steady-state levels of blood acetaldehyde in animals of both genotypes.	Acetaldehyde	78-90	aldehyde dehydrogenase 2 family member	Rattus norvegicus	154-159
15900217-0	2005	Polymorphisms in the mitochondrial aldehyde dehydrogenase gene (Aldh2) determine peak blood acetaldehyde levels and voluntary ethanol consumption in rats.	Acetaldehyde	92-104	aldehyde dehydrogenase 2 family member	Rattus norvegicus	64-69
15900217-7	2005	A major phenotypic difference was a five-fold higher (P&lt;0.0025) peak blood acetaldehyde level following ethanol administration in the lower drinker F2 Aldh2(2)/Aldh2(2) compared to the higher drinker F2 Aldh2(1)/Aldh2(1) animals, despite the existence of identical steady-state levels of blood acetaldehyde in animals of both genotypes.	Acetaldehyde	78-90	aldehyde dehydrogenase 2 family member	Rattus norvegicus	163-168
16257351-2	2005	Previously, we have shown that malondialdehyde, an inflammation product of lipid peroxidation, and acetaldehyde, a component of both ethanol metabolism and cigarette smoke, form protein adducts that stimulate protein kinase C (PKC) activation in bronchial epithelial cells.	Acetaldehyde	99-111	protein kinase C alpha	Homo sapiens	227-230
15900217-7	2005	A major phenotypic difference was a five-fold higher (P&lt;0.0025) peak blood acetaldehyde level following ethanol administration in the lower drinker F2 Aldh2(2)/Aldh2(2) compared to the higher drinker F2 Aldh2(1)/Aldh2(1) animals, despite the existence of identical steady-state levels of blood acetaldehyde in animals of both genotypes.	Acetaldehyde	78-90	aldehyde dehydrogenase 2 family member	Rattus norvegicus	163-168
15900217-7	2005	A major phenotypic difference was a five-fold higher (P&lt;0.0025) peak blood acetaldehyde level following ethanol administration in the lower drinker F2 Aldh2(2)/Aldh2(2) compared to the higher drinker F2 Aldh2(1)/Aldh2(1) animals, despite the existence of identical steady-state levels of blood acetaldehyde in animals of both genotypes.	Acetaldehyde	78-90	aldehyde dehydrogenase 2 family member	Rattus norvegicus	163-168
15900217-8	2005	Polymorphisms in Aldh2 play an important role in: (i) determining peak blood acetaldehyde levels and (ii) modulating voluntary ethanol consumption.	Acetaldehyde	77-89	aldehyde dehydrogenase 2 family member	Rattus norvegicus	17-22
15900217-9	2005	We postulate that the markedly higher peak of blood acetaldehyde generated in Aldh2(2)/Aldh2(2)(2) animals is aversive, leading to a reduced alcohol intake in Aldh2(2)/Aldh2(2) versus that in Aldh2(1)/Aldh2(1) animals.	Acetaldehyde	52-64	aldehyde dehydrogenase 2 family member	Rattus norvegicus	78-83
15900217-9	2005	We postulate that the markedly higher peak of blood acetaldehyde generated in Aldh2(2)/Aldh2(2)(2) animals is aversive, leading to a reduced alcohol intake in Aldh2(2)/Aldh2(2) versus that in Aldh2(1)/Aldh2(1) animals.	Acetaldehyde	52-64	aldehyde dehydrogenase 2 family member	Rattus norvegicus	87-92
15900217-9	2005	We postulate that the markedly higher peak of blood acetaldehyde generated in Aldh2(2)/Aldh2(2)(2) animals is aversive, leading to a reduced alcohol intake in Aldh2(2)/Aldh2(2) versus that in Aldh2(1)/Aldh2(1) animals.	Acetaldehyde	52-64	aldehyde dehydrogenase 2 family member	Rattus norvegicus	87-92
15900217-9	2005	We postulate that the markedly higher peak of blood acetaldehyde generated in Aldh2(2)/Aldh2(2)(2) animals is aversive, leading to a reduced alcohol intake in Aldh2(2)/Aldh2(2) versus that in Aldh2(1)/Aldh2(1) animals.	Acetaldehyde	52-64	aldehyde dehydrogenase 2 family member	Rattus norvegicus	87-92
15900217-9	2005	We postulate that the markedly higher peak of blood acetaldehyde generated in Aldh2(2)/Aldh2(2)(2) animals is aversive, leading to a reduced alcohol intake in Aldh2(2)/Aldh2(2) versus that in Aldh2(1)/Aldh2(1) animals.	Acetaldehyde	52-64	aldehyde dehydrogenase 2 family member	Rattus norvegicus	87-92
15900217-9	2005	We postulate that the markedly higher peak of blood acetaldehyde generated in Aldh2(2)/Aldh2(2)(2) animals is aversive, leading to a reduced alcohol intake in Aldh2(2)/Aldh2(2) versus that in Aldh2(1)/Aldh2(1) animals.	Acetaldehyde	52-64	aldehyde dehydrogenase 2 family member	Rattus norvegicus	87-92
15840430-0	2005	Association of ALDH2 polymorphism with sensitivity to acetaldehyde-induced micronuclei and facial flushing after alcohol intake.	Acetaldehyde	54-66	aldehyde dehydrogenase 2 family member	Homo sapiens	15-20
15767272-7	2005	In presence of ethanol, the concomitant induction of catalase (i.e. by glucose oxidase) and inhibition of aldehyde dehydrogenase (i.e. by methylene blue) led to acetaldehyde accumulation within cells.	Acetaldehyde	161-173	catalase	Rattus norvegicus	53-61
15840430-5	2005	The frequency of micronuclei induced by acetaldehyde increased in a dose-dependent manner with the largest increase seen in subjects that were homozygous for the ALDH2(2) allele.	Acetaldehyde	40-52	aldehyde dehydrogenase 2 family member	Homo sapiens	162-167
15840430-10	2005	The results suggest that the ALDH2 genotype is significantly associated with acetaldehyde-induced micronuclei and alcohol-induced facial flushing.	Acetaldehyde	77-89	aldehyde dehydrogenase 2 family member	Homo sapiens	29-34
15897724-3	2005	Recent studies from Japan revealed that macrocytosis is related to ALDH-2/2 genotype, leading to increased acetaldehyde accumulation.	Acetaldehyde	107-119	aldehyde dehydrogenase 2 family member	Homo sapiens	67-75
16257351-11	2005	Scavenger receptor-mediated activation of PKC alpha may function to reduce wound healing under conditions of alcohol and cigarette smoke exposure where malondialdehyde-acetaldehyde adducts may be present.	Acetaldehyde	168-180	protein kinase C alpha	Homo sapiens	42-51
15885616-8	2005	Gaseous acetaldehyde-inducible IFN-beta production management was fully reversible while maintaining cell viability at over 95% during the entire process.	Acetaldehyde	8-20	interferon beta 1	Homo sapiens	31-39
15653713-8	2005	The ethanol-induced fibronectin response was dependent on ethanol metabolism since 4-methylpyrazole, an inhibitor of alcohol dehydrogenase, abolished the effect and acetaldehyde induced it.	Acetaldehyde	165-177	fibronectin 1	Mus musculus	20-31
15703303-2	2005	Acetaldehyde, which is responsible for some of the deleterious effects of ethanol, is further oxidized to acetic acid by aldehyde dehydrogenases (ALDHs), of which mitochondrial ALDH2 is the most efficient.	Acetaldehyde	0-12	aldehyde dehydrogenase 2 family member, tandem duplicate 1	Danio rerio	177-182
15703303-6	2005	We found that zebrafish ALDH2 is catalytically active and efficiently oxidizes acetaldehyde (K(m) = 11.5 microM) and propionaldehyde (K(m) = 6.1 microM).	Acetaldehyde	79-91	aldehyde dehydrogenase 2 family member, tandem duplicate 1	Danio rerio	24-29
15714130-1	2005	OBJECTIVES: Most of the acetaldehyde, a recognized animal carcinogen, generated during alcohol metabolism is eliminated by liver mitochondrial aldehyde dehydrogenase 2 (ALDH2).	Acetaldehyde	24-36	aldehyde dehydrogenase 2 family member	Homo sapiens	169-174
16054981-4	2005	Ethanol metabolism by alcohol dehydrogenase leads to the generation of acetaldehyde and free radicals that bind rapidly to numerous cellular targets, including components of cell signaling pathways and DNA.	Acetaldehyde	71-83	aldo-keto reductase family 1 member A1	Homo sapiens	22-43
16054981-6	2005	Chronic ethanol abuse leads to induction of hepatocyte microsomal cytochrome P450 2E1, an enzyme that metabolizes ethanol to acetaldehyde and, in doing so, causes further free radical production and aberrant cell function.	Acetaldehyde	125-137	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	66-85
15694276-7	2005	According to these data we propose a model in which ethanol oxidation via catalase could produce acetaldehyde into the ARC and to promote a release of beta-endorphins that would activate opioid receptors to produce locomotion and other ethanol-induced neurobehavioural changes.	Acetaldehyde	97-109	catalase	Rattus norvegicus	74-82
15550448-0	2005	Effects of acetaldehyde and TNF alpha on the inhibitory kappa B-alpha protein and nuclear factor kappa B activation in hepatic stellate cells.	Acetaldehyde	11-23	nuclear factor kappa B subunit 1	Homo sapiens	82-104
15550448-3	2005	NF-kappaB, an inhibitor of the type I collagen promoters, is increased by both acetaldehyde and TNFalpha.	Acetaldehyde	79-91	nuclear factor kappa B subunit 1	Homo sapiens	0-9
15550448-6	2005	RESULTS: Acetaldehyde increased IkappaB-alpha kinase activity and decreased IkappaB-alpha after 10 min of exposure, with recovery towards control levels at 20 min.	Acetaldehyde	9-21	NFKB inhibitor alpha	Homo sapiens	32-45
15550448-6	2005	RESULTS: Acetaldehyde increased IkappaB-alpha kinase activity and decreased IkappaB-alpha after 10 min of exposure, with recovery towards control levels at 20 min.	Acetaldehyde	9-21	NFKB inhibitor alpha	Homo sapiens	76-89
15550448-8	2005	Both acetaldehyde and TNFalpha enhanced nuclear NF-kappaB (p65), but acetaldehyde alone also increased NF-kappaB (p50).	Acetaldehyde	5-17	nuclear factor kappa B subunit 1	Homo sapiens	48-57
15550448-8	2005	Both acetaldehyde and TNFalpha enhanced nuclear NF-kappaB (p65), but acetaldehyde alone also increased NF-kappaB (p50).	Acetaldehyde	5-17	RELA proto-oncogene, NF-kB subunit	Homo sapiens	59-62
15550448-8	2005	Both acetaldehyde and TNFalpha enhanced nuclear NF-kappaB (p65), but acetaldehyde alone also increased NF-kappaB (p50).	Acetaldehyde	69-81	nuclear factor kappa B subunit 1	Homo sapiens	103-112
15550448-8	2005	Both acetaldehyde and TNFalpha enhanced nuclear NF-kappaB (p65), but acetaldehyde alone also increased NF-kappaB (p50).	Acetaldehyde	69-81	nuclear factor kappa B subunit 1	Homo sapiens	114-117
15550448-9	2005	CONCLUSIONS: TNFalpha and acetaldehyde independently activate NF-kappaB by rapid enhancement of IkappaB-alpha kinase activity and degradation of IkB-alpha protein.	Acetaldehyde	26-38	nuclear factor kappa B subunit 1	Homo sapiens	62-71
15550448-9	2005	CONCLUSIONS: TNFalpha and acetaldehyde independently activate NF-kappaB by rapid enhancement of IkappaB-alpha kinase activity and degradation of IkB-alpha protein.	Acetaldehyde	26-38	NFKB inhibitor alpha	Homo sapiens	96-109
15550448-9	2005	CONCLUSIONS: TNFalpha and acetaldehyde independently activate NF-kappaB by rapid enhancement of IkappaB-alpha kinase activity and degradation of IkB-alpha protein.	Acetaldehyde	26-38	NFKB inhibitor alpha	Homo sapiens	145-154
15550448-12	2005	In contrast, the effect of acetaldehyde in activating NF-kappaB is associated with increases in both liver injury and fibrogenesis, indicating that the effects of acetaldehyde on fibrogenesis are mediated by cytokines and by trans-acting factors other than NF-kappaB.	Acetaldehyde	27-39	nuclear factor kappa B subunit 1	Homo sapiens	54-63
15550448-12	2005	In contrast, the effect of acetaldehyde in activating NF-kappaB is associated with increases in both liver injury and fibrogenesis, indicating that the effects of acetaldehyde on fibrogenesis are mediated by cytokines and by trans-acting factors other than NF-kappaB.	Acetaldehyde	27-39	nuclear factor kappa B subunit 1	Homo sapiens	257-266
15550448-12	2005	In contrast, the effect of acetaldehyde in activating NF-kappaB is associated with increases in both liver injury and fibrogenesis, indicating that the effects of acetaldehyde on fibrogenesis are mediated by cytokines and by trans-acting factors other than NF-kappaB.	Acetaldehyde	163-175	nuclear factor kappa B subunit 1	Homo sapiens	54-63
15550448-12	2005	In contrast, the effect of acetaldehyde in activating NF-kappaB is associated with increases in both liver injury and fibrogenesis, indicating that the effects of acetaldehyde on fibrogenesis are mediated by cytokines and by trans-acting factors other than NF-kappaB.	Acetaldehyde	163-175	nuclear factor kappa B subunit 1	Homo sapiens	257-266
15626611-6	2005	The ethanol and acetaldehyde concentrations in expired air from ALDH2 [-] (aldehyde dehydrogenase type 2 negative) subjects were higher than that of the ALDH2 [+] (positive) subjects.	Acetaldehyde	16-28	aldehyde dehydrogenase 2 family member	Homo sapiens	64-69
15626611-7	2005	The results indicated that the lower activity of ALDH2 induced an adverse effect on ethanol metabolism, leading to ethanol and acetaldehyde remaining in the human body, even human expired air.	Acetaldehyde	127-139	aldehyde dehydrogenase 2 family member	Homo sapiens	49-54
15698409-0	2005	Differential modulation of interleukin 8 by interleukin 4 and interleukin 10 in HepG2 cells treated with acetaldehyde.	Acetaldehyde	105-117	C-X-C motif chemokine ligand 8	Homo sapiens	27-40
15698409-0	2005	Differential modulation of interleukin 8 by interleukin 4 and interleukin 10 in HepG2 cells treated with acetaldehyde.	Acetaldehyde	105-117	interleukin 10	Homo sapiens	62-76
15698409-2	2005	The purpose of this work was to study the regulation of IL-8 by IL-10 and IL-4 in HepG2 cells treated with acetaldehyde (Ac).	Acetaldehyde	107-119	C-X-C motif chemokine ligand 8	Homo sapiens	56-60
15698409-2	2005	The purpose of this work was to study the regulation of IL-8 by IL-10 and IL-4 in HepG2 cells treated with acetaldehyde (Ac).	Acetaldehyde	107-119	interleukin 10	Homo sapiens	64-69
15698409-2	2005	The purpose of this work was to study the regulation of IL-8 by IL-10 and IL-4 in HepG2 cells treated with acetaldehyde (Ac).	Acetaldehyde	107-119	interleukin 4	Homo sapiens	74-78
15698409-2	2005	The purpose of this work was to study the regulation of IL-8 by IL-10 and IL-4 in HepG2 cells treated with acetaldehyde (Ac).	Acetaldehyde	121-123	C-X-C motif chemokine ligand 8	Homo sapiens	56-60
15698409-2	2005	The purpose of this work was to study the regulation of IL-8 by IL-10 and IL-4 in HepG2 cells treated with acetaldehyde (Ac).	Acetaldehyde	121-123	interleukin 10	Homo sapiens	64-69
15698409-2	2005	The purpose of this work was to study the regulation of IL-8 by IL-10 and IL-4 in HepG2 cells treated with acetaldehyde (Ac).	Acetaldehyde	121-123	interleukin 4	Homo sapiens	74-78
15698409-4	2005	RESULTS: Ac treatment produced an increment in IL-8 induction and secretion that was prevented by IL-4 pretreatment, while IL-10 pretreatment failed to decrease Ac-induced IL-8 production.	Acetaldehyde	9-11	C-X-C motif chemokine ligand 8	Homo sapiens	47-51
15698409-4	2005	RESULTS: Ac treatment produced an increment in IL-8 induction and secretion that was prevented by IL-4 pretreatment, while IL-10 pretreatment failed to decrease Ac-induced IL-8 production.	Acetaldehyde	9-11	interleukin 4	Homo sapiens	98-102
15569633-1	2005	In alcohol metabolism, acetaldehyde, a highly reactive intermediate that may cause cellular and DNA damages, is converted to acetate by mitochondrial aldehyde dehydrogenase ALDH2.	Acetaldehyde	23-35	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	173-178
15680252-5	2005	In fact, SP600125 potentiated acetaldehyde-induced apoptosis, suggesting that JNK activation is anti-apoptotic.	Acetaldehyde	30-42	mitogen-activated protein kinase 8	Rattus norvegicus	78-81
15680252-6	2005	Inhibition of p42/44 MAPK by MAPK kinase (MKK1) inhibitor, 1,4-diamino-2,3-dicyano-1,4-bis(2-aminophenylthio)butadiene (U0126), potentiated apoptosis by acetaldehyde or ethanol, suggesting anti-apoptotic role of p42/44 MAPK.	Acetaldehyde	153-165	mitogen activated protein kinase 3	Rattus norvegicus	14-25
15680252-6	2005	Inhibition of p42/44 MAPK by MAPK kinase (MKK1) inhibitor, 1,4-diamino-2,3-dicyano-1,4-bis(2-aminophenylthio)butadiene (U0126), potentiated apoptosis by acetaldehyde or ethanol, suggesting anti-apoptotic role of p42/44 MAPK.	Acetaldehyde	153-165	mitogen activated protein kinase 3	Rattus norvegicus	21-25
15680252-9	2005	In summary, transient activation of JNK by acetaldehyde is anti-apoptotic, whereas sustained activation of JNK by ethanol is pro-apoptotic.	Acetaldehyde	43-55	mitogen-activated protein kinase 8	Rattus norvegicus	36-39
15680252-10	2005	The activation of p42/44 MAPK appears to be anti-apoptotic for both ethanol and acetaldehyde.	Acetaldehyde	80-92	mitogen activated protein kinase 3	Rattus norvegicus	18-29
15922132-10	2005	The model"s transient output correlates strongly with the experimentally observed results for healthy individuals and for those with reduced ALDH activity caused by a genetic deficiency of the primary acetaldehyde-metabolizing enzyme ALDH2.	Acetaldehyde	201-213	aldehyde dehydrogenase 2 family member	Homo sapiens	234-239
15922138-5	2005	In addition, liquid chromatographic-electrospray ionization mass spectrometric analysis of GSTs that were affinity purified with glutathione showed the formation of acetaldehyde adducts to the rGSTA3 subunit.	Acetaldehyde	165-177	glutathione S-transferase alpha 3	Rattus norvegicus	193-199
15922138-6	2005	Given the abundant expression of rGSTA3 subunit and acetaldehyde adduct formation, results of the current study support the suggestion that modification of rGSTA3 subunit, and thus its impaired function, in alcohol-exposed rats may contribute to the progression of alcohol-induced liver damage.	Acetaldehyde	52-64	glutathione S-transferase alpha 3	Rattus norvegicus	156-162
15680252-0	2005	Pro- and anti-apoptotic roles of c-Jun N-terminal kinase (JNK) in ethanol and acetaldehyde exposed rat hepatocytes.	Acetaldehyde	78-90	mitogen-activated protein kinase 8	Rattus norvegicus	33-56
15680252-0	2005	Pro- and anti-apoptotic roles of c-Jun N-terminal kinase (JNK) in ethanol and acetaldehyde exposed rat hepatocytes.	Acetaldehyde	78-90	mitogen-activated protein kinase 8	Rattus norvegicus	58-61
15680252-2	2005	Acetaldehyde induced rapid and transient (15 min) activation of p42/44 MAPK followed by activation of JNK, which remained above control up to 1 h. Ethanol activated JNK for up to 4 h. Both ethanol and acetaldehyde caused apoptosis as determined by DNA fragmentation, caspase-3 activation and 2"[4-ethoxyphenyl]-5-[4-methyl-piperazinyl]-2,5"-bi-1H-benzimidazole (Hoechst 33342) staining.	Acetaldehyde	0-12	mitogen activated protein kinase 1	Rattus norvegicus	64-75
15680252-2	2005	Acetaldehyde induced rapid and transient (15 min) activation of p42/44 MAPK followed by activation of JNK, which remained above control up to 1 h. Ethanol activated JNK for up to 4 h. Both ethanol and acetaldehyde caused apoptosis as determined by DNA fragmentation, caspase-3 activation and 2"[4-ethoxyphenyl]-5-[4-methyl-piperazinyl]-2,5"-bi-1H-benzimidazole (Hoechst 33342) staining.	Acetaldehyde	0-12	mitogen-activated protein kinase 8	Rattus norvegicus	102-105
15680252-2	2005	Acetaldehyde induced rapid and transient (15 min) activation of p42/44 MAPK followed by activation of JNK, which remained above control up to 1 h. Ethanol activated JNK for up to 4 h. Both ethanol and acetaldehyde caused apoptosis as determined by DNA fragmentation, caspase-3 activation and 2"[4-ethoxyphenyl]-5-[4-methyl-piperazinyl]-2,5"-bi-1H-benzimidazole (Hoechst 33342) staining.	Acetaldehyde	0-12	mitogen-activated protein kinase 8	Rattus norvegicus	165-168
15680252-2	2005	Acetaldehyde induced rapid and transient (15 min) activation of p42/44 MAPK followed by activation of JNK, which remained above control up to 1 h. Ethanol activated JNK for up to 4 h. Both ethanol and acetaldehyde caused apoptosis as determined by DNA fragmentation, caspase-3 activation and 2"[4-ethoxyphenyl]-5-[4-methyl-piperazinyl]-2,5"-bi-1H-benzimidazole (Hoechst 33342) staining.	Acetaldehyde	0-12	caspase 3	Rattus norvegicus	267-276
15680252-2	2005	Acetaldehyde induced rapid and transient (15 min) activation of p42/44 MAPK followed by activation of JNK, which remained above control up to 1 h. Ethanol activated JNK for up to 4 h. Both ethanol and acetaldehyde caused apoptosis as determined by DNA fragmentation, caspase-3 activation and 2"[4-ethoxyphenyl]-5-[4-methyl-piperazinyl]-2,5"-bi-1H-benzimidazole (Hoechst 33342) staining.	Acetaldehyde	201-213	mitogen activated protein kinase 1	Rattus norvegicus	64-75
15680252-2	2005	Acetaldehyde induced rapid and transient (15 min) activation of p42/44 MAPK followed by activation of JNK, which remained above control up to 1 h. Ethanol activated JNK for up to 4 h. Both ethanol and acetaldehyde caused apoptosis as determined by DNA fragmentation, caspase-3 activation and 2"[4-ethoxyphenyl]-5-[4-methyl-piperazinyl]-2,5"-bi-1H-benzimidazole (Hoechst 33342) staining.	Acetaldehyde	201-213	mitogen-activated protein kinase 8	Rattus norvegicus	102-105
15680252-2	2005	Acetaldehyde induced rapid and transient (15 min) activation of p42/44 MAPK followed by activation of JNK, which remained above control up to 1 h. Ethanol activated JNK for up to 4 h. Both ethanol and acetaldehyde caused apoptosis as determined by DNA fragmentation, caspase-3 activation and 2"[4-ethoxyphenyl]-5-[4-methyl-piperazinyl]-2,5"-bi-1H-benzimidazole (Hoechst 33342) staining.	Acetaldehyde	201-213	mitogen-activated protein kinase 8	Rattus norvegicus	165-168
15680252-2	2005	Acetaldehyde induced rapid and transient (15 min) activation of p42/44 MAPK followed by activation of JNK, which remained above control up to 1 h. Ethanol activated JNK for up to 4 h. Both ethanol and acetaldehyde caused apoptosis as determined by DNA fragmentation, caspase-3 activation and 2"[4-ethoxyphenyl]-5-[4-methyl-piperazinyl]-2,5"-bi-1H-benzimidazole (Hoechst 33342) staining.	Acetaldehyde	201-213	caspase 3	Rattus norvegicus	267-276
15452360-0	2005	Modulation of urokinase-type plasminogen activator by transforming growth factor beta1 in acetaldehyde-activated hepatic stellate cells.	Acetaldehyde	90-102	plasminogen activator, urokinase	Homo sapiens	14-50
15623784-4	2005	In addition, the endotoxin-induced expression of the inducible nitric oxide synthase (iNOS) and cyclooxygenase (COX)-2 proteins was investigated in a mouse macrophage cell line (RAW 264.7) treated with ACE in vitro, to clarify the anti-inflammatory effect.	Acetaldehyde	202-205	nitric oxide synthase 2, inducible	Mus musculus	53-84
15623784-4	2005	In addition, the endotoxin-induced expression of the inducible nitric oxide synthase (iNOS) and cyclooxygenase (COX)-2 proteins was investigated in a mouse macrophage cell line (RAW 264.7) treated with ACE in vitro, to clarify the anti-inflammatory effect.	Acetaldehyde	202-205	nitric oxide synthase 2, inducible	Mus musculus	86-90
15623784-4	2005	In addition, the endotoxin-induced expression of the inducible nitric oxide synthase (iNOS) and cyclooxygenase (COX)-2 proteins was investigated in a mouse macrophage cell line (RAW 264.7) treated with ACE in vitro, to clarify the anti-inflammatory effect.	Acetaldehyde	202-205	cytochrome c oxidase II, mitochondrial	Mus musculus	96-118
15623784-11	2005	RESULTS: The number of inflammatory cells, the protein concentrations, and the levels of NO, PGE2, and TNF-alpha in the aqueous humor in the groups treated with ACE were significantly decreased in a dose-dependent manner.	Acetaldehyde	161-164	tumor necrosis factor	Rattus norvegicus	103-112
15808017-3	2005	Alcohol dehydrogenase (ADH) oxidizes ethanol to acetaldehyde using the coenzyme nicotinamide adenine dinucleotide (NAD), which is concurrently reduced to form NADH.	Acetaldehyde	48-60	aldo-keto reductase family 1 member A1	Homo sapiens	0-21
15808017-3	2005	Alcohol dehydrogenase (ADH) oxidizes ethanol to acetaldehyde using the coenzyme nicotinamide adenine dinucleotide (NAD), which is concurrently reduced to form NADH.	Acetaldehyde	48-60	aldo-keto reductase family 1 member A1	Homo sapiens	23-26
15452360-5	2005	TGF-beta1 had a modest stimulatory action on the release of uPA into the conditioned medium, but reduced acetaldehyde-induced release, as demonstrated by Western blot analysis.	Acetaldehyde	105-117	transforming growth factor beta 1	Homo sapiens	0-9
15452360-6	2005	In accord, whereas TGF-beta1 produces no effect on uPA activity in the conditioned media from quiescent cells, it significantly reduces the stimulatory action of acetaldehyde.	Acetaldehyde	162-174	transforming growth factor beta 1	Homo sapiens	19-28
15452360-7	2005	These results show that the activity and gene expression of uPA are regulated by both acetaldehyde and TGF-beta1 and that the proteolytic activity in the extracellular space is reduced by the influence of TGF-beta1.	Acetaldehyde	86-98	plasminogen activator, urokinase	Homo sapiens	60-63
15452360-8	2005	Further studies on the molecular mechanisms responsible for the regulation of the plasminogen system by TGF-beta1 and other molecules in the presence of acetaldehyde will contribute to a better understanding of the processes involved in fibrogenesis.	Acetaldehyde	153-165	transforming growth factor beta 1	Homo sapiens	104-113
15597079-1	2004	BACKGROUND: Cytosolic aldehyde dehydrogenase (ALDH1A1) is an important enzyme in the metabolism of acetaldehyde and the synthesis of retinoic acid.	Acetaldehyde	99-111	aldehyde dehydrogenase 1 family member A1	Homo sapiens	46-53
15499379-0	2004	Suicide gene therapy: conversion of ethanol to acetaldehyde mediated by human beta 2 alcohol dehydrogenase.	Acetaldehyde	47-59	aldo-keto reductase family 1 member A1	Homo sapiens	85-106
15499379-2	2004	The antitumour activity of a suicide gene system using adenovirus delivered alcohol dehydrogenase (ADH) to convert ethanol to acetaldehyde inside cancer cells has been investigated in vitro and in vivo.	Acetaldehyde	126-138	aldo-keto reductase family 1 member A1	Homo sapiens	76-97
15499379-2	2004	The antitumour activity of a suicide gene system using adenovirus delivered alcohol dehydrogenase (ADH) to convert ethanol to acetaldehyde inside cancer cells has been investigated in vitro and in vivo.	Acetaldehyde	126-138	aldo-keto reductase family 1 member A1	Homo sapiens	99-102
15868480-12	2004	In contrast, the inhibition of catalase, which suppresses acetaldehyde synthesis, led to no reduced viability in the same exposure conditions.	Acetaldehyde	58-70	catalase	Homo sapiens	31-39
15502819-5	2004	AIR-controlled interferon-beta production in transgenic CHO-K1-derived serum-free suspension cultures could be modulated by fine-tuning inflow and outflow of acetaldehyde-containing gas during standard bioreactor operation.	Acetaldehyde	158-170	interferon beta 1	Homo sapiens	15-30
15542751-1	2004	Alcohol dehydrogenase (ADH) and aldehyde dehydrogenase-2 (ALDH2) play central roles in the metabolism of ethanol and its metabolite, acetaldehyde, in the liver.	Acetaldehyde	133-145	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	23-26
15542751-1	2004	Alcohol dehydrogenase (ADH) and aldehyde dehydrogenase-2 (ALDH2) play central roles in the metabolism of ethanol and its metabolite, acetaldehyde, in the liver.	Acetaldehyde	133-145	aldehyde dehydrogenase 2 family member	Homo sapiens	32-56
15542751-1	2004	Alcohol dehydrogenase (ADH) and aldehyde dehydrogenase-2 (ALDH2) play central roles in the metabolism of ethanol and its metabolite, acetaldehyde, in the liver.	Acetaldehyde	133-145	aldehyde dehydrogenase 2 family member	Homo sapiens	58-63
15536764-9	2004	Recently, however, it has been established that ethanol is metabolized to acetaldehyde (primarily by catalase) and then to acetate (by aldehyde dehydrogenase) in the brain.	Acetaldehyde	74-86	catalase	Homo sapiens	101-109
15535104-7	2004	Ethanol inducible cytochrome P450 2EI isoenzyme oxidise ethanol and acetaldehyde and numerous potentially toxic xenobiotic and produce toxic oxygen free radicals, which are implicated in the pathogenesis of alcoholic liver diseases.	Acetaldehyde	68-80	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	18-37
15375565-2	2004	Since acetaldehyde is a carcinogenic factor associated with chronic alcohol consumption, individuals with the alcohol dehydrogenase 1C*1 allele (ADH1C*1 allele) seem to be at particular risk, since this allele encodes for a rapidly ethanol metabolizing enzyme leading to increased acetaldehyde levels.	Acetaldehyde	6-18	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	145-150
15375565-2	2004	Since acetaldehyde is a carcinogenic factor associated with chronic alcohol consumption, individuals with the alcohol dehydrogenase 1C*1 allele (ADH1C*1 allele) seem to be at particular risk, since this allele encodes for a rapidly ethanol metabolizing enzyme leading to increased acetaldehyde levels.	Acetaldehyde	281-293	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	145-150
15380331-1	2004	People who have a Glu487Lys mutation (single nucleotide polymorphism) in the aldehyde dehydrogenase-2 (ALDH2) gene are slow to metabolize the alcohol breakdown product acetaldehyde.	Acetaldehyde	168-180	aldehyde dehydrogenase 2 family member	Homo sapiens	77-101
15380331-1	2004	People who have a Glu487Lys mutation (single nucleotide polymorphism) in the aldehyde dehydrogenase-2 (ALDH2) gene are slow to metabolize the alcohol breakdown product acetaldehyde.	Acetaldehyde	168-180	aldehyde dehydrogenase 2 family member	Homo sapiens	103-108
15380331-3	2004	This suggests that acetaldehyde accumulation due to hypoactive ALDH2 is associated with a prolongation of the central sensory conduction time between pons and primary sensory cortex.	Acetaldehyde	19-31	aldehyde dehydrogenase 2 family member	Homo sapiens	63-68
15331350-4	2004	L-Glutamine reduced the acetaldehyde-induced redistribution of occludin, zonula occludens-1 (ZO-1), E-cadherin, and beta-catenin from the intercellular junctions.	Acetaldehyde	24-36	occludin	Homo sapiens	63-71
15331350-4	2004	L-Glutamine reduced the acetaldehyde-induced redistribution of occludin, zonula occludens-1 (ZO-1), E-cadherin, and beta-catenin from the intercellular junctions.	Acetaldehyde	24-36	tight junction protein 1	Homo sapiens	73-91
15331350-4	2004	L-Glutamine reduced the acetaldehyde-induced redistribution of occludin, zonula occludens-1 (ZO-1), E-cadherin, and beta-catenin from the intercellular junctions.	Acetaldehyde	24-36	tight junction protein 1	Homo sapiens	93-97
15331350-4	2004	L-Glutamine reduced the acetaldehyde-induced redistribution of occludin, zonula occludens-1 (ZO-1), E-cadherin, and beta-catenin from the intercellular junctions.	Acetaldehyde	24-36	cadherin 1	Homo sapiens	100-110
15331350-4	2004	L-Glutamine reduced the acetaldehyde-induced redistribution of occludin, zonula occludens-1 (ZO-1), E-cadherin, and beta-catenin from the intercellular junctions.	Acetaldehyde	24-36	catenin beta 1	Homo sapiens	116-128
15331350-5	2004	Acetaldehyde dissociates occludin, ZO-1, E-cadherin, and beta-catenin from the actin cytoskeleton, and this effect was reduced by L-glutamine.	Acetaldehyde	0-12	occludin	Homo sapiens	25-33
15331350-5	2004	Acetaldehyde dissociates occludin, ZO-1, E-cadherin, and beta-catenin from the actin cytoskeleton, and this effect was reduced by L-glutamine.	Acetaldehyde	0-12	tight junction protein 1	Homo sapiens	35-39
15331350-5	2004	Acetaldehyde dissociates occludin, ZO-1, E-cadherin, and beta-catenin from the actin cytoskeleton, and this effect was reduced by L-glutamine.	Acetaldehyde	0-12	cadherin 1	Homo sapiens	41-51
15331350-5	2004	Acetaldehyde dissociates occludin, ZO-1, E-cadherin, and beta-catenin from the actin cytoskeleton, and this effect was reduced by L-glutamine.	Acetaldehyde	0-12	catenin beta 1	Homo sapiens	57-69
15333745-6	2004	In addition, in Japanese studies, consumers of alcohol possessing the ALDH2*2 allele, who have very elevated levels of acetaldehyde, are at high risk for colorectal cancer.	Acetaldehyde	119-131	aldehyde dehydrogenase 2 family member	Homo sapiens	70-75
15536764-13	2004	Stimulation of catalase should lead to increased levels of acetaldehyde in the brain, but this has not been directly demonstrated.	Acetaldehyde	59-71	catalase	Homo sapiens	15-23
15536764-14	2004	Inhibition of catalase should lead to decreased acetaldehyde concentrations in vivo, but, again, this has not been directly demonstrated.	Acetaldehyde	48-60	catalase	Homo sapiens	14-22
15234196-7	2004	The levels of triglyceride, total-cholesterol and leptin in blood serum were significantly decreased in HFD + ACE group compared to those of sham group.	Acetaldehyde	110-113	leptin	Rattus norvegicus	50-56
15670660-1	2004	Liver disease in the alcoholic is due not only to malnutrition but also to ethanol"s hepatotoxicity linked to its metabolism by means of the alcohol dehydrogenase and cytochrome P450 2E1 (CYP2E1) pathways and the resulting production of toxic acetaldehyde.	Acetaldehyde	243-255	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	167-186
15138216-0	2004	Increased cancer risk in heavy drinkers with the alcohol dehydrogenase 1C*1 allele, possibly due to salivary acetaldehyde.	Acetaldehyde	109-121	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	49-73
15182962-1	2004	Persons who have the Glu-487--&gt;Lys mutation (single nucleotide polymorphism) of the aldehyde dehydrogenase-2 (ALDH2) gene have less ability to metabolize the alcohol breakdown product acetaldehyde.	Acetaldehyde	187-199	aldehyde dehydrogenase 2 family member	Homo sapiens	87-111
15182962-1	2004	Persons who have the Glu-487--&gt;Lys mutation (single nucleotide polymorphism) of the aldehyde dehydrogenase-2 (ALDH2) gene have less ability to metabolize the alcohol breakdown product acetaldehyde.	Acetaldehyde	187-199	aldehyde dehydrogenase 2 family member	Homo sapiens	113-118
15182962-3	2004	Alcoholics with ALDH2*2 heterozygotes showed significantly lower sensory nerve action potential amplitudes of the sural and median nerves than those with ALDH2*1 homozygotes, suggesting that the accumulation of acetaldehyde due to ALDH2 inactivity is associated with alcoholic polyneuropathy.	Acetaldehyde	211-223	aldehyde dehydrogenase 2 family member	Homo sapiens	16-21
15182962-3	2004	Alcoholics with ALDH2*2 heterozygotes showed significantly lower sensory nerve action potential amplitudes of the sural and median nerves than those with ALDH2*1 homozygotes, suggesting that the accumulation of acetaldehyde due to ALDH2 inactivity is associated with alcoholic polyneuropathy.	Acetaldehyde	211-223	aldehyde dehydrogenase 2 family member	Homo sapiens	154-159
15182962-3	2004	Alcoholics with ALDH2*2 heterozygotes showed significantly lower sensory nerve action potential amplitudes of the sural and median nerves than those with ALDH2*1 homozygotes, suggesting that the accumulation of acetaldehyde due to ALDH2 inactivity is associated with alcoholic polyneuropathy.	Acetaldehyde	211-223	aldehyde dehydrogenase 2 family member	Homo sapiens	154-159
15178893-9	2004	A histamine (H1 receptor) antagonist completely inhibited acetaldehyde-induced bronchial smooth muscle contraction.	Acetaldehyde	58-70	histamine receptor H1	Homo sapiens	2-24
15130784-6	2004	Acetaldehyde increased free cell TGF beta1 and secretion of total and free TGF beta 1 in wild-type, but not in ob/ob cells.	Acetaldehyde	0-12	transforming growth factor, beta 1	Mus musculus	33-42
15130784-6	2004	Acetaldehyde increased free cell TGF beta1 and secretion of total and free TGF beta 1 in wild-type, but not in ob/ob cells.	Acetaldehyde	0-12	transforming growth factor, beta 1	Mus musculus	75-85
15138216-2	2004	As acetaldehyde seems to be a carcinogenic factor associated with chronic alcohol consumption, alcoholics with the alcohol dehydrogenase (ADH) 1C*1 allele seem to be particularly at risk as this allele encodes for a rapidly ethanol metabolising enzyme leading to increased acetaldehyde levels.	Acetaldehyde	3-15	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	115-145
15138216-2	2004	As acetaldehyde seems to be a carcinogenic factor associated with chronic alcohol consumption, alcoholics with the alcohol dehydrogenase (ADH) 1C*1 allele seem to be particularly at risk as this allele encodes for a rapidly ethanol metabolising enzyme leading to increased acetaldehyde levels.	Acetaldehyde	273-285	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	115-145
15138216-10	2004	Healthy volunteers homozygous for the ADH1C*1 allele had higher salivary acetaldehyde concentrations following alcohol ingestion than volunteers heterozygous for ADH1C (p = 0.056) or homozygous for ADH1C*2 (p = 0.011).	Acetaldehyde	73-85	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	38-43
15138216-11	2004	CONCLUSIONS: These data demonstrate that heavy drinkers homozygous for the ADH1C*1 allele have a predisposition to develop upper aerodigestive tract cancer, possibly due to elevated salivary acetaldehyde levels following alcohol consumption.	Acetaldehyde	191-203	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	75-80
15164086-5	2004	Whereas alcohol dehydrogenase metabolizes the bulk of ethanol within the liver, other enzymes, such as cytochrome P4502E1 and catalase, also contributes to the production of acetaldehyde from ethanol oxidation.	Acetaldehyde	174-186	aldo-keto reductase family 1 member A1	Homo sapiens	8-29
15164086-5	2004	Whereas alcohol dehydrogenase metabolizes the bulk of ethanol within the liver, other enzymes, such as cytochrome P4502E1 and catalase, also contributes to the production of acetaldehyde from ethanol oxidation.	Acetaldehyde	174-186	catalase	Homo sapiens	114-134
15215505-4	2004	Consistent with this, gek1 shows enhanced sensitivity to acetaldehyde in the medium.	Acetaldehyde	57-69	D-aminoacyl-tRNA deacylase	Arabidopsis thaliana	22-26
15215505-6	2004	These results indicate that the ethanol hypersensitivity of gek1 is due to an enhanced sensitivity to acetaldehyde toxicity, instead of abnormally elevated accumulation of toxic acetaldehyde, which has been thought to be the major cause of ethanol toxicity in mammal cells.	Acetaldehyde	102-114	D-aminoacyl-tRNA deacylase	Arabidopsis thaliana	60-64
15215500-5	2004	Transgenic Arabidopsis plants overexpressing GEK1 displayed an enhanced tolerance to ethanol and acetaldehyde, suggesting that GEK1 is directly involved in the tolerance to those chemicals.	Acetaldehyde	97-109	D-aminoacyl-tRNA deacylase	Arabidopsis thaliana	45-49
15215500-5	2004	Transgenic Arabidopsis plants overexpressing GEK1 displayed an enhanced tolerance to ethanol and acetaldehyde, suggesting that GEK1 is directly involved in the tolerance to those chemicals.	Acetaldehyde	97-109	D-aminoacyl-tRNA deacylase	Arabidopsis thaliana	127-131
15215505-6	2004	These results indicate that the ethanol hypersensitivity of gek1 is due to an enhanced sensitivity to acetaldehyde toxicity, instead of abnormally elevated accumulation of toxic acetaldehyde, which has been thought to be the major cause of ethanol toxicity in mammal cells.	Acetaldehyde	178-190	D-aminoacyl-tRNA deacylase	Arabidopsis thaliana	60-64
15166657-0	2004	Epidermal growth factor prevents acetaldehyde-induced paracellular permeability in Caco-2 cell monolayer.	Acetaldehyde	33-45	epidermal growth factor	Homo sapiens	0-23
15166657-9	2004	Acetaldehyde treatment induced a reorganization of actin cytoskeletal network and reduced the levels of occludin, ZO-1, E-cadherin, and beta-catenin associated with the actin cytoskeleton.	Acetaldehyde	0-12	cadherin 1	Homo sapiens	120-130
15166657-9	2004	Acetaldehyde treatment induced a reorganization of actin cytoskeletal network and reduced the levels of occludin, ZO-1, E-cadherin, and beta-catenin associated with the actin cytoskeleton.	Acetaldehyde	0-12	catenin beta 1	Homo sapiens	136-148
15166657-3	2004	In the present study, the role of epidermal growth factor (EGF) in protection of epithelial barrier function from acetaldehyde was evaluated in Caco-2 intestinal epithelial cell monolayer.	Acetaldehyde	114-126	epidermal growth factor	Homo sapiens	34-57
15166657-10	2004	EGF effectively prevented acetaldehyde-induced reorganization of actin cytoskeleton and the interaction of occludin, ZO-1, E-cadherin, and beta-catenin with the actin cytoskeleton.	Acetaldehyde	26-38	epidermal growth factor	Homo sapiens	0-3
15166657-3	2004	In the present study, the role of epidermal growth factor (EGF) in protection of epithelial barrier function from acetaldehyde was evaluated in Caco-2 intestinal epithelial cell monolayer.	Acetaldehyde	114-126	epidermal growth factor	Homo sapiens	59-62
15166657-10	2004	EGF effectively prevented acetaldehyde-induced reorganization of actin cytoskeleton and the interaction of occludin, ZO-1, E-cadherin, and beta-catenin with the actin cytoskeleton.	Acetaldehyde	26-38	occludin	Homo sapiens	107-115
15166657-7	2004	RESULTS: Acetaldehyde increased paracellular permeability to inulin and lipopolysaccharide, and EGF significantly reduced these effects of acetaldehyde in a time- and dose-dependent manner.	Acetaldehyde	139-151	epidermal growth factor	Homo sapiens	96-99
15166657-10	2004	EGF effectively prevented acetaldehyde-induced reorganization of actin cytoskeleton and the interaction of occludin, ZO-1, E-cadherin, and beta-catenin with the actin cytoskeleton.	Acetaldehyde	26-38	tight junction protein 1	Homo sapiens	117-121
15166657-10	2004	EGF effectively prevented acetaldehyde-induced reorganization of actin cytoskeleton and the interaction of occludin, ZO-1, E-cadherin, and beta-catenin with the actin cytoskeleton.	Acetaldehyde	26-38	cadherin 1	Homo sapiens	123-133
15166657-8	2004	EGF prevented acetaldehyde-induced reorganization of occludin, ZO-1, E-cadherin, and beta-catenin from the cellular junctions to the intracellular compartments.	Acetaldehyde	14-26	epidermal growth factor	Homo sapiens	0-3
15166657-10	2004	EGF effectively prevented acetaldehyde-induced reorganization of actin cytoskeleton and the interaction of occludin, ZO-1, E-cadherin, and beta-catenin with the actin cytoskeleton.	Acetaldehyde	26-38	catenin beta 1	Homo sapiens	139-151
15166657-8	2004	EGF prevented acetaldehyde-induced reorganization of occludin, ZO-1, E-cadherin, and beta-catenin from the cellular junctions to the intracellular compartments.	Acetaldehyde	14-26	occludin	Homo sapiens	53-61
15166657-11	2004	CONCLUSION: These results indicate that EGF attenuates acetaldehyde-induced disruption of tight junctions and adherens junctions and prevents acetaldehyde-induced reorganization of actin cytoskeleton and its interaction with occludin, ZO-1, E-cadherin, and beta-catenin.	Acetaldehyde	55-67	epidermal growth factor	Homo sapiens	40-43
15166657-11	2004	CONCLUSION: These results indicate that EGF attenuates acetaldehyde-induced disruption of tight junctions and adherens junctions and prevents acetaldehyde-induced reorganization of actin cytoskeleton and its interaction with occludin, ZO-1, E-cadherin, and beta-catenin.	Acetaldehyde	142-154	epidermal growth factor	Homo sapiens	40-43
15166657-11	2004	CONCLUSION: These results indicate that EGF attenuates acetaldehyde-induced disruption of tight junctions and adherens junctions and prevents acetaldehyde-induced reorganization of actin cytoskeleton and its interaction with occludin, ZO-1, E-cadherin, and beta-catenin.	Acetaldehyde	142-154	occludin	Homo sapiens	225-233
15166657-11	2004	CONCLUSION: These results indicate that EGF attenuates acetaldehyde-induced disruption of tight junctions and adherens junctions and prevents acetaldehyde-induced reorganization of actin cytoskeleton and its interaction with occludin, ZO-1, E-cadherin, and beta-catenin.	Acetaldehyde	142-154	tight junction protein 1	Homo sapiens	235-239
15166657-11	2004	CONCLUSION: These results indicate that EGF attenuates acetaldehyde-induced disruption of tight junctions and adherens junctions and prevents acetaldehyde-induced reorganization of actin cytoskeleton and its interaction with occludin, ZO-1, E-cadherin, and beta-catenin.	Acetaldehyde	142-154	cadherin 1	Homo sapiens	241-251
15166657-11	2004	CONCLUSION: These results indicate that EGF attenuates acetaldehyde-induced disruption of tight junctions and adherens junctions and prevents acetaldehyde-induced reorganization of actin cytoskeleton and its interaction with occludin, ZO-1, E-cadherin, and beta-catenin.	Acetaldehyde	142-154	catenin beta 1	Homo sapiens	257-269
15166657-8	2004	EGF prevented acetaldehyde-induced reorganization of occludin, ZO-1, E-cadherin, and beta-catenin from the cellular junctions to the intracellular compartments.	Acetaldehyde	14-26	tight junction protein 1	Homo sapiens	63-67
15166657-8	2004	EGF prevented acetaldehyde-induced reorganization of occludin, ZO-1, E-cadherin, and beta-catenin from the cellular junctions to the intracellular compartments.	Acetaldehyde	14-26	cadherin 1	Homo sapiens	69-79
15166657-8	2004	EGF prevented acetaldehyde-induced reorganization of occludin, ZO-1, E-cadherin, and beta-catenin from the cellular junctions to the intracellular compartments.	Acetaldehyde	14-26	catenin beta 1	Homo sapiens	85-97
15166657-9	2004	Acetaldehyde treatment induced a reorganization of actin cytoskeletal network and reduced the levels of occludin, ZO-1, E-cadherin, and beta-catenin associated with the actin cytoskeleton.	Acetaldehyde	0-12	occludin	Homo sapiens	104-112
15166657-9	2004	Acetaldehyde treatment induced a reorganization of actin cytoskeletal network and reduced the levels of occludin, ZO-1, E-cadherin, and beta-catenin associated with the actin cytoskeleton.	Acetaldehyde	0-12	tight junction protein 1	Homo sapiens	114-118
15282111-5	2004	Acetaldehyde-elicited cardiac dysfunction may be mediated through cytochrome P450 oxidase, xanthine oxidase, and the stress-signaling cascade.	Acetaldehyde	0-12	xanthine dehydrogenase	Mus musculus	91-107
14722113-7	2004	Acetaldehyde increased IkappaB-alpha kinase activity and phosphorylated IkappaB-alpha, NF-kappaB nuclear protein, and its binding to the promoter.	Acetaldehyde	0-12	nuclear factor of kappa light polypeptide gene enhancer in B cells inhibitor, alpha	Mus musculus	23-36
14722113-7	2004	Acetaldehyde increased IkappaB-alpha kinase activity and phosphorylated IkappaB-alpha, NF-kappaB nuclear protein, and its binding to the promoter.	Acetaldehyde	0-12	nuclear factor of kappa light polypeptide gene enhancer in B cells inhibitor, alpha	Mus musculus	72-85
14722113-7	2004	Acetaldehyde increased IkappaB-alpha kinase activity and phosphorylated IkappaB-alpha, NF-kappaB nuclear protein, and its binding to the promoter.	Acetaldehyde	0-12	nuclear factor of kappa light polypeptide gene enhancer in B cells 1, p105	Mus musculus	87-96
14722113-9	2004	In conclusion, although acetaldehyde increases the binding of NF-kappaB to the murine alpha(2)(I) collagen promoter, this binding does not mediate the activating effect of acetaldehyde on promoter activity.	Acetaldehyde	24-36	nuclear factor of kappa light polypeptide gene enhancer in B cells 1, p105	Mus musculus	62-71
14722113-9	2004	In conclusion, although acetaldehyde increases the binding of NF-kappaB to the murine alpha(2)(I) collagen promoter, this binding does not mediate the activating effect of acetaldehyde on promoter activity.	Acetaldehyde	24-36	collagen type I alpha 2 chain	Homo sapiens	86-106
14722113-10	2004	The effects of acetaldehyde in increasing the translocation of NF-kappaB to the nucleus with increased DNA binding activity may be important in mediating the effects of acetaldehyde on other genes.	Acetaldehyde	15-27	nuclear factor of kappa light polypeptide gene enhancer in B cells 1, p105	Mus musculus	63-72
14722113-10	2004	The effects of acetaldehyde in increasing the translocation of NF-kappaB to the nucleus with increased DNA binding activity may be important in mediating the effects of acetaldehyde on other genes.	Acetaldehyde	169-181	nuclear factor of kappa light polypeptide gene enhancer in B cells 1, p105	Mus musculus	63-72
15075218-1	2004	We studied whether acetaldehyde, which is produced by alcohol consumption, impacts ryanodine receptor (RyR) activity and muscle force.	Acetaldehyde	19-31	LOC100009439	Oryctolagus cuniculus	83-101
15075218-1	2004	We studied whether acetaldehyde, which is produced by alcohol consumption, impacts ryanodine receptor (RyR) activity and muscle force.	Acetaldehyde	19-31	LOC100009439	Oryctolagus cuniculus	103-106
15075218-2	2004	Exposure to approximately 50-200 microM acetaldehyde enhanced channel activity of frog RyR and rabbit RyR1 incorporated into lipid bilayers.	Acetaldehyde	40-52	LOC100009439	Oryctolagus cuniculus	87-90
15075218-2	2004	Exposure to approximately 50-200 microM acetaldehyde enhanced channel activity of frog RyR and rabbit RyR1 incorporated into lipid bilayers.	Acetaldehyde	40-52	ryanodine receptor 1	Oryctolagus cuniculus	102-106
15075218-8	2004	These results suggest that moderate concentrations of acetaldehyde can elicit Ca(2+) release from the SR by increasing the open probability of the RyR channel, resulting in increased tension.	Acetaldehyde	54-66	LOC100009439	Oryctolagus cuniculus	147-150
14722101-0	2004	Overexpression of aldehyde dehydrogenase-2 (ALDH2) transgene prevents acetaldehyde-induced cell injury in human umbilical vein endothelial cells: role of ERK and p38 mitogen-activated protein kinase.	Acetaldehyde	70-82	aldehyde dehydrogenase 2 family member	Homo sapiens	18-42
15066780-0	2004	Exposure of Saccharomyces cerevisiae to acetaldehyde induces sulfur amino acid metabolism and polyamine transporter genes, which depend on Met4p and Haa1p transcription factors, respectively.	Acetaldehyde	40-52	Met4p	Saccharomyces cerevisiae S288C	139-144
15066780-7	2004	Moreover, the deletion of MET4 leads to increased acetaldehyde sensitivity.	Acetaldehyde	50-62	Met4p	Saccharomyces cerevisiae S288C	26-30
14722101-7	2004	Acetaldehyde (0-200 microm) elicited ROS generation and apoptosis in HUVECs in a time- and concentration-dependent manner, associated with activation of the stress signal molecules ERK1/2 and p38 mitogen-activated protein (MAP) kinase.	Acetaldehyde	0-12	mitogen-activated protein kinase 3	Homo sapiens	181-187
14722101-7	2004	Acetaldehyde (0-200 microm) elicited ROS generation and apoptosis in HUVECs in a time- and concentration-dependent manner, associated with activation of the stress signal molecules ERK1/2 and p38 mitogen-activated protein (MAP) kinase.	Acetaldehyde	0-12	mitogen-activated protein kinase 1	Homo sapiens	192-195
14722101-0	2004	Overexpression of aldehyde dehydrogenase-2 (ALDH2) transgene prevents acetaldehyde-induced cell injury in human umbilical vein endothelial cells: role of ERK and p38 mitogen-activated protein kinase.	Acetaldehyde	70-82	aldehyde dehydrogenase 2 family member	Homo sapiens	44-49
14722101-9	2004	Interestingly, the acetaldehyde-induced ROS generation, apoptosis, activation of ERK1/2, and p38 MAP kinase were prevented by the ALDH2 transgene or antioxidant alpha-tocopherol.	Acetaldehyde	19-31	mitogen-activated protein kinase 3	Homo sapiens	81-87
14722101-3	2004	Transgene-encoding human aldehyde dehydrogenase-2 (ALDH2), which converts acetaldehyde into acetate, was constructed under chicken beta-actin promoter and transfected into human umbilical vein endothelial cells (HUVECs).	Acetaldehyde	74-86	aldehyde dehydrogenase 2 family member	Homo sapiens	25-49
14722101-9	2004	Interestingly, the acetaldehyde-induced ROS generation, apoptosis, activation of ERK1/2, and p38 MAP kinase were prevented by the ALDH2 transgene or antioxidant alpha-tocopherol.	Acetaldehyde	19-31	mitogen-activated protein kinase 1	Homo sapiens	93-96
14722101-9	2004	Interestingly, the acetaldehyde-induced ROS generation, apoptosis, activation of ERK1/2, and p38 MAP kinase were prevented by the ALDH2 transgene or antioxidant alpha-tocopherol.	Acetaldehyde	19-31	aldehyde dehydrogenase 2 family member	Homo sapiens	130-135
14722101-10	2004	The involvement of ERK1/2 and p38 MAP kinase in acetaldehyde-induced apoptosis was confirmed by selective kinase inhibitors U0126, SB203580, and SB202190.	Acetaldehyde	48-60	mitogen-activated protein kinase 3	Homo sapiens	19-25
14722101-3	2004	Transgene-encoding human aldehyde dehydrogenase-2 (ALDH2), which converts acetaldehyde into acetate, was constructed under chicken beta-actin promoter and transfected into human umbilical vein endothelial cells (HUVECs).	Acetaldehyde	74-86	aldehyde dehydrogenase 2 family member	Homo sapiens	51-56
14741743-13	2004	Therefore, the protective effect of UDCA or TUDCA in alcohol- or acetaldehyde-treated SK-Hep-1 cells remains dubious.	Acetaldehyde	65-77	DNL-type zinc finger	Homo sapiens	89-94
14722101-10	2004	The involvement of ERK1/2 and p38 MAP kinase in acetaldehyde-induced apoptosis was confirmed by selective kinase inhibitors U0126, SB203580, and SB202190.	Acetaldehyde	48-60	mitogen-activated protein kinase 1	Homo sapiens	30-33
14722101-11	2004	Collectively, our data revealed that facilitation of acetaldehyde metabolism by ALDH2 transgene overexpression may prevent acetaldehyde-induced cell injury and activation of stress signals.	Acetaldehyde	53-65	aldehyde dehydrogenase 2 family member	Homo sapiens	80-85
14722101-11	2004	Collectively, our data revealed that facilitation of acetaldehyde metabolism by ALDH2 transgene overexpression may prevent acetaldehyde-induced cell injury and activation of stress signals.	Acetaldehyde	123-135	aldehyde dehydrogenase 2 family member	Homo sapiens	80-85
14722101-12	2004	These results indicated therapeutic potential of ALDH2 enzyme in the prevention and detoxification of acetaldehyde or alcohol-induced cell injury.	Acetaldehyde	102-114	aldehyde dehydrogenase 2 family member	Homo sapiens	49-54
15042439-2	2004	Catalase is an enzyme that oxidizes ethanol to acetaldehyde.	Acetaldehyde	47-59	catalase	Rattus norvegicus	0-8
15639999-1	2004	An atypical allele (ALDH2*2) in low K(m) aldehyde dehydrogenase (ALDH2), which is highly prevalent in Asians, may influence drinking behavior because of higher production of acetaldehyde in the liver.	Acetaldehyde	174-186	aldehyde dehydrogenase 2 family member	Homo sapiens	20-25
15639999-1	2004	An atypical allele (ALDH2*2) in low K(m) aldehyde dehydrogenase (ALDH2), which is highly prevalent in Asians, may influence drinking behavior because of higher production of acetaldehyde in the liver.	Acetaldehyde	174-186	aldehyde dehydrogenase 2 family member	Homo sapiens	65-70
14752838-2	2004	In this study, we characterized peripheral blood mononuclear cell (PBMC) T-cell and antibody responses to human serum albumin (HAS) adducted with acetaldehyde under reducing conditions (AcA-HSA) or with malondialdehyde (MDA-HSA) in patients with advanced ALD (AALD, n = 28), heavy drinkers with no liver disease (NALD, n = 14), and mild/moderate drinking controls (n = 22).	Acetaldehyde	146-158	albumin	Homo sapiens	112-125
14664838-4	2004	Acetaldehyde decomposition was used as a probe reaction to evaluate the photocatalysis of these MOx-ZnO powders.	Acetaldehyde	0-12	monooxygenase DBH like 1	Homo sapiens	96-99
15099407-6	2004	The pathophysiological effects of these variants may be mediated by accumulation of acetaldehyde; high-activity ADH variants are predicted to increase the rate of acetaldehyde generation, while the low-activity ALDH2 variant is associated with an inability to metabolize this compound.	Acetaldehyde	84-96	aldo-keto reductase family 1 member A1	Homo sapiens	112-115
15099407-6	2004	The pathophysiological effects of these variants may be mediated by accumulation of acetaldehyde; high-activity ADH variants are predicted to increase the rate of acetaldehyde generation, while the low-activity ALDH2 variant is associated with an inability to metabolize this compound.	Acetaldehyde	84-96	aldehyde dehydrogenase 2 family member	Homo sapiens	211-216
15099407-6	2004	The pathophysiological effects of these variants may be mediated by accumulation of acetaldehyde; high-activity ADH variants are predicted to increase the rate of acetaldehyde generation, while the low-activity ALDH2 variant is associated with an inability to metabolize this compound.	Acetaldehyde	163-175	aldo-keto reductase family 1 member A1	Homo sapiens	112-115
15099407-6	2004	The pathophysiological effects of these variants may be mediated by accumulation of acetaldehyde; high-activity ADH variants are predicted to increase the rate of acetaldehyde generation, while the low-activity ALDH2 variant is associated with an inability to metabolize this compound.	Acetaldehyde	163-175	aldehyde dehydrogenase 2 family member	Homo sapiens	211-216
14737322-2	2004	The fragment ion of m/z 210 from TNT undergoes [4(+)+ 2] cycloaddition with EVE to form an oxo-iminium ion of m/z 282, which dissociates by acetaldehyde loss after a [1,5-H] shift to form a quinolynium ion of m/z 238.	Acetaldehyde	140-152	chromosome 16 open reading frame 82	Homo sapiens	33-36
14690875-0	2003	Brain mitochondrial aldehyde dehydrogenase: relation to acetaldehyde aversion in low-alcohol-drinking (UChA) and high-alcohol-drinking (UChB) rats.	Acetaldehyde	56-68	aldehyde dehydrogenase 2 family member	Rattus norvegicus	6-42
15069620-0	2004	Acetaldehyde accumulation suppresses Kupffer cell release of TNF-Alpha and modifies acute hepatic inflammation in rats.	Acetaldehyde	0-12	tumor necrosis factor	Rattus norvegicus	61-70
15069620-1	2004	BACKGROUND: Alcohol-related diseases have multiple and varied associations with acetaldehyde, a highly toxic product of ethanol oxidation that accumulates in the absence of active aldehyde dehydrogenase (ALDH).	Acetaldehyde	80-92	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	180-202
15069620-1	2004	BACKGROUND: Alcohol-related diseases have multiple and varied associations with acetaldehyde, a highly toxic product of ethanol oxidation that accumulates in the absence of active aldehyde dehydrogenase (ALDH).	Acetaldehyde	80-92	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	204-208
15069620-2	2004	This study was designed to clarify the role of acetaldehyde in liver injury, specifically in vivo and in vitro effects on Kupffer cell release of the inflammatory cytokine tumor necrosis factor-alpha (TNF-Alpha).	Acetaldehyde	47-59	tumor necrosis factor	Rattus norvegicus	172-199
15069620-2	2004	This study was designed to clarify the role of acetaldehyde in liver injury, specifically in vivo and in vitro effects on Kupffer cell release of the inflammatory cytokine tumor necrosis factor-alpha (TNF-Alpha).	Acetaldehyde	47-59	tumor necrosis factor	Rattus norvegicus	201-210
15069620-8	2004	Acetaldehyde significantly suppressed Kupffer cell TNF-Alpha release ( P &lt; 0.05), but acetate treatment did not.	Acetaldehyde	0-12	tumor necrosis factor	Rattus norvegicus	51-60
15069620-9	2004	CONCLUSIONS: Acetaldehyde accumulation suppresses macrophage function, at least suppressing TNF-Alpha release, which plays a role in modifying acute hepatic inflammation in rats.	Acetaldehyde	13-25	tumor necrosis factor	Rattus norvegicus	92-101
14690875-9	2003	The finding that blocking the brain ALDH2 (52%) by cyanamide can make a non-aversive dose of AcH (25 mg/kg) aversive to UChA and UChB rats at blood AcH levels comparable to those induced by a non-aversive dose of AcH (100 mg/kg) in control UChB rats indicates that the line difference in AcH aversion is associated more with brain ALDH2 activity than with liver ALDH2 activity.	Acetaldehyde	93-96	aldehyde dehydrogenase 2 family member	Rattus norvegicus	36-41
14690875-9	2003	The finding that blocking the brain ALDH2 (52%) by cyanamide can make a non-aversive dose of AcH (25 mg/kg) aversive to UChA and UChB rats at blood AcH levels comparable to those induced by a non-aversive dose of AcH (100 mg/kg) in control UChB rats indicates that the line difference in AcH aversion is associated more with brain ALDH2 activity than with liver ALDH2 activity.	Acetaldehyde	148-151	aldehyde dehydrogenase 2 family member	Rattus norvegicus	36-41
14690875-9	2003	The finding that blocking the brain ALDH2 (52%) by cyanamide can make a non-aversive dose of AcH (25 mg/kg) aversive to UChA and UChB rats at blood AcH levels comparable to those induced by a non-aversive dose of AcH (100 mg/kg) in control UChB rats indicates that the line difference in AcH aversion is associated more with brain ALDH2 activity than with liver ALDH2 activity.	Acetaldehyde	148-151	aldehyde dehydrogenase 2 family member	Rattus norvegicus	36-41
14690875-9	2003	The finding that blocking the brain ALDH2 (52%) by cyanamide can make a non-aversive dose of AcH (25 mg/kg) aversive to UChA and UChB rats at blood AcH levels comparable to those induced by a non-aversive dose of AcH (100 mg/kg) in control UChB rats indicates that the line difference in AcH aversion is associated more with brain ALDH2 activity than with liver ALDH2 activity.	Acetaldehyde	148-151	aldehyde dehydrogenase 2 family member	Rattus norvegicus	36-41
15456641-6	2004	In the present study, we provide evidence of the ability of different natural polyphenols and of folic acid derivatives to inhibit the biotransformation of alcohol to acetaldehyde by rat breast cytosolic XOR.	Acetaldehyde	167-179	xanthine dehydrogenase	Rattus norvegicus	204-207
14682707-3	2003	Ring splitting of the radical anion 1*- occurs with cleavage of O-C2 and C3-C4 bonds, leading to products (acetaldehyde and p-cyanostilbene) different from the reagents used in the Paterno-Buchi synthesis of 1.	Acetaldehyde	107-119	one cut homeobox 2	Homo sapiens	64-68
12943535-7	2003	Short-chain aliphatic aldehydes, such as acetaldehyde, propionaldehyde and malondialdehyde, were found to be very poor substrates for human ALDH3A1.	Acetaldehyde	41-53	aldehyde dehydrogenase 3 family member A1	Homo sapiens	140-147
14690875-7	2003	In experiment 2, the possibility that the inhibition of the brain ALDH2 would lower the AcH aversion threshold in both lines was studied by determining the effect of cyanamide (10 mg/kg i.p.)	Acetaldehyde	88-91	aldehyde dehydrogenase 2 family member	Rattus norvegicus	66-71
12876071-10	2003	The increases in c-myc may well represent a preapoptotic effect, or even a nonspecific cellular stress response to alcohol and/or acetaldehyde.	Acetaldehyde	130-142	MYC proto-oncogene, bHLH transcription factor	Rattus norvegicus	17-22
12876071-5	2003	We hypothesized that 1) increases in c-myc mRNA levels also occur in muscle exposed chronically to alcohol, 2) muscle of female rats is more sensitive than that from male rats, 3) raising acetaldehyde will also increase c-myc, 4) prior starvation will cause further increases in c-myc mRNA expression in response to ethanol, and 5) other genes involved in apoptosis (i.e., p53 and Bcl-2) would also be affected by alcohol.	Acetaldehyde	188-200	MYC proto-oncogene, bHLH transcription factor	Rattus norvegicus	37-42
12876071-5	2003	We hypothesized that 1) increases in c-myc mRNA levels also occur in muscle exposed chronically to alcohol, 2) muscle of female rats is more sensitive than that from male rats, 3) raising acetaldehyde will also increase c-myc, 4) prior starvation will cause further increases in c-myc mRNA expression in response to ethanol, and 5) other genes involved in apoptosis (i.e., p53 and Bcl-2) would also be affected by alcohol.	Acetaldehyde	188-200	MYC proto-oncogene, bHLH transcription factor	Rattus norvegicus	220-225
12876071-5	2003	We hypothesized that 1) increases in c-myc mRNA levels also occur in muscle exposed chronically to alcohol, 2) muscle of female rats is more sensitive than that from male rats, 3) raising acetaldehyde will also increase c-myc, 4) prior starvation will cause further increases in c-myc mRNA expression in response to ethanol, and 5) other genes involved in apoptosis (i.e., p53 and Bcl-2) would also be affected by alcohol.	Acetaldehyde	188-200	MYC proto-oncogene, bHLH transcription factor	Rattus norvegicus	220-225
15143530-2	2003	In this connection, we studied the effect of chronic acetaldehyde intoxication on the activities of alcohol dehydrogenase (ADH), aldehyde dehydrogenase (ALDH), the microsomal ethanol oxidizing system (MEOS) and liver and brain catalase as well as ethanol and acetaldehyde levels in the blood.	Acetaldehyde	53-65	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	129-151
12876071-5	2003	We hypothesized that 1) increases in c-myc mRNA levels also occur in muscle exposed chronically to alcohol, 2) muscle of female rats is more sensitive than that from male rats, 3) raising acetaldehyde will also increase c-myc, 4) prior starvation will cause further increases in c-myc mRNA expression in response to ethanol, and 5) other genes involved in apoptosis (i.e., p53 and Bcl-2) would also be affected by alcohol.	Acetaldehyde	188-200	Wistar clone pR53P1 p53 pseudogene	Rattus norvegicus	373-376
12876071-5	2003	We hypothesized that 1) increases in c-myc mRNA levels also occur in muscle exposed chronically to alcohol, 2) muscle of female rats is more sensitive than that from male rats, 3) raising acetaldehyde will also increase c-myc, 4) prior starvation will cause further increases in c-myc mRNA expression in response to ethanol, and 5) other genes involved in apoptosis (i.e., p53 and Bcl-2) would also be affected by alcohol.	Acetaldehyde	188-200	BCL2, apoptosis regulator	Rattus norvegicus	381-386
15143530-4	2003	In parallel with this, the systemic acetaldehyde administration led to shortened time of ethanol narcosis and activation of catalase in the cerebellum and left hemisphere, which may indicate involvement of this enzyme into metabolic tolerance development.	Acetaldehyde	36-48	catalase	Rattus norvegicus	124-132
14636436-0	2003	[Effects of Erk signal transduction on the cell cycle of rat hepatic stellate cells stimulated by acetaldehyde].	Acetaldehyde	98-110	Eph receptor B1	Rattus norvegicus	12-15
15143530-2	2003	In this connection, we studied the effect of chronic acetaldehyde intoxication on the activities of alcohol dehydrogenase (ADH), aldehyde dehydrogenase (ALDH), the microsomal ethanol oxidizing system (MEOS) and liver and brain catalase as well as ethanol and acetaldehyde levels in the blood.	Acetaldehyde	53-65	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	153-157
14636436-8	2003	CONCLUSION: The Erk signal transduction pathway plays an important role in regulating the proliferation and cell cycle of rat hepatic stellate cells stimulated by acetaldehyde, which may be partly related to its regulative effect on the expression of cyclin D1 gene and CDK4 gene	Acetaldehyde	163-175	Eph receptor B1	Rattus norvegicus	16-19
12963492-3	2003	The discovery that alcohol metabolite derived aldehydes can modify proteins prompted a study to determine if malondialdehyde-acetaldehyde-modified albumin (MAA-Alb) would be degraded similar to that reported for f-Alb, and whether ethanol-fed rats would demonstrate an impaired RME with respect to this ligand which occurs as a consequence of chronic ethanol consumption.	Acetaldehyde	125-137	albumin	Rattus norvegicus	160-163
14636436-8	2003	CONCLUSION: The Erk signal transduction pathway plays an important role in regulating the proliferation and cell cycle of rat hepatic stellate cells stimulated by acetaldehyde, which may be partly related to its regulative effect on the expression of cyclin D1 gene and CDK4 gene	Acetaldehyde	163-175	cyclin D1	Rattus norvegicus	251-260
14636436-8	2003	CONCLUSION: The Erk signal transduction pathway plays an important role in regulating the proliferation and cell cycle of rat hepatic stellate cells stimulated by acetaldehyde, which may be partly related to its regulative effect on the expression of cyclin D1 gene and CDK4 gene	Acetaldehyde	163-175	cyclin-dependent kinase 4	Rattus norvegicus	270-274
13129829-11	2003	Results show that acute tolerance to motor impairment, as well as ethanol consumption induced by ethanol, appears to be the consequence of acetaldehyde formed centrally during ethanol oxidation via the catalase system, because pretreatment of rats with the catalase inhibitor attenuated the increase in acute tolerance development and the increase in voluntary ethanol consumption in UChB rats that received the acute i.p.	Acetaldehyde	139-151	catalase	Rattus norvegicus	202-210
13129829-11	2003	Results show that acute tolerance to motor impairment, as well as ethanol consumption induced by ethanol, appears to be the consequence of acetaldehyde formed centrally during ethanol oxidation via the catalase system, because pretreatment of rats with the catalase inhibitor attenuated the increase in acute tolerance development and the increase in voluntary ethanol consumption in UChB rats that received the acute i.p.	Acetaldehyde	139-151	catalase	Rattus norvegicus	257-265
13129829-4	2003	In the present paper we investigated the involvement of acetaldehyde produced centrally during ethanol oxidation by brain catalase and its oxidation by mitochondrial aldehyde dehydrogenase, on acute tolerance development and on voluntary ethanol consumption by rats.	Acetaldehyde	56-68	catalase	Rattus norvegicus	122-130
13129829-15	2003	injection of ethanol to UChB rats induces an increase in ethanol consumption is the development of acute tolerance, where acetaldehyde formed during brain ethanol metabolism via catalase and its subsequent oxidation via aldehyde dehydrogenase have an important role.	Acetaldehyde	122-134	catalase	Rattus norvegicus	178-186
14506399-3	2003	Inactive ALDH2 dramatically increases blood acetaldehyde levels after alcohol intake.	Acetaldehyde	44-56	aldehyde dehydrogenase 2 family member	Homo sapiens	9-14
12883264-3	2003	Cultured PSCs become activated when exposed to ethanol or its metabolite acetaldehyde (as indicated by increased alpha-smooth muscle actin [alpha-SMA] expression and increased collagen synthesis).	Acetaldehyde	73-85	actin gamma 2, smooth muscle	Rattus norvegicus	113-138
14615007-1	2003	The high-affinity (K(M)&lt;1 microM) mitochondrial class 2 aldehyde dehydrogenase (ALDH2) metabolizes most of the acetaldehyde generated in the hepatic oxidation of ethanol.	Acetaldehyde	114-126	aldehyde dehydrogenase 2 family member	Rattus norvegicus	83-88
14615007-4	2003	To determine only the high-affinity ALDH2 activity it is necessary to keep constant low concentrations of acetaldehyde in the cells to minimize its metabolism by high-K(M) aldehyde dehydrogenases.	Acetaldehyde	106-118	aldehyde dehydrogenase 2 family member	Rattus norvegicus	36-41
14615012-10	2003	These results, together with the finding that after administration of a 50-mg/kg dose of acetaldehyde cerebral venous blood acetaldehyde levels in UChA rats were consistently higher than levels in UChB rats, support the suggestion that differential acetaldehyde levels, differential brain ALDH2 activity, or both were responsible for the different effects of acetaldehyde in the two rat lines.	Acetaldehyde	89-101	aldehyde dehydrogenase 2 family member	Rattus norvegicus	289-294
14619338-0	2003	Acetaldehyde induces granulocyte macrophage colony-stimulating factor production in human bronchi through activation of nuclear factor-kappa B.	Acetaldehyde	0-12	colony stimulating factor 2	Homo sapiens	21-69
14619338-7	2003	Acetaldehyde significantly increased GM-CSF production from human bronchi and nuclear translocation of NF-kappa Bp65 in airway epithelium but had no effects on other cytokines.	Acetaldehyde	0-12	colony stimulating factor 2	Homo sapiens	37-43
14619338-7	2003	Acetaldehyde significantly increased GM-CSF production from human bronchi and nuclear translocation of NF-kappa Bp65 in airway epithelium but had no effects on other cytokines.	Acetaldehyde	0-12	RELA proto-oncogene, NF-kB subunit	Homo sapiens	103-116
14619338-8	2003	Our findings suggest that acetaldehyde potentially causes airway inflammation via increased GM-CSF production through nuclear translocation of NF-kappa B.	Acetaldehyde	26-38	colony stimulating factor 2	Homo sapiens	92-98
14619338-8	2003	Our findings suggest that acetaldehyde potentially causes airway inflammation via increased GM-CSF production through nuclear translocation of NF-kappa B.	Acetaldehyde	26-38	nuclear factor kappa B subunit 1	Homo sapiens	143-153
12884000-3	2003	Specifically, ADH1B*47His (previously ADH2-2) and ALDH2-2 have been shown to confer protection against alcoholism, presumably through accumulation of acetaldehyde in the blood and a resultant "flushing response" to alcohol consumption.	Acetaldehyde	150-162	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	14-19
12884000-3	2003	Specifically, ADH1B*47His (previously ADH2-2) and ALDH2-2 have been shown to confer protection against alcoholism, presumably through accumulation of acetaldehyde in the blood and a resultant "flushing response" to alcohol consumption.	Acetaldehyde	150-162	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	38-44
12884000-3	2003	Specifically, ADH1B*47His (previously ADH2-2) and ALDH2-2 have been shown to confer protection against alcoholism, presumably through accumulation of acetaldehyde in the blood and a resultant "flushing response" to alcohol consumption.	Acetaldehyde	150-162	aldehyde dehydrogenase 2 family member	Homo sapiens	50-57
12883264-11	2003	RESULTS: Ethanol and acetaldehyde increased the activation of all 3 subfamilies (ERK 1/2, JNK and p38 kinase) of the MAPK pathway in PSCs.	Acetaldehyde	21-33	mitogen activated protein kinase 3	Rattus norvegicus	81-88
12883264-11	2003	RESULTS: Ethanol and acetaldehyde increased the activation of all 3 subfamilies (ERK 1/2, JNK and p38 kinase) of the MAPK pathway in PSCs.	Acetaldehyde	21-33	mitogen-activated protein kinase 8	Rattus norvegicus	90-93
12883264-3	2003	Cultured PSCs become activated when exposed to ethanol or its metabolite acetaldehyde (as indicated by increased alpha-smooth muscle actin [alpha-SMA] expression and increased collagen synthesis).	Acetaldehyde	73-85	actin gamma 2, smooth muscle	Rattus norvegicus	140-149
12883264-11	2003	RESULTS: Ethanol and acetaldehyde increased the activation of all 3 subfamilies (ERK 1/2, JNK and p38 kinase) of the MAPK pathway in PSCs.	Acetaldehyde	21-33	mitogen activated protein kinase 14	Rattus norvegicus	98-101
12883264-11	2003	RESULTS: Ethanol and acetaldehyde increased the activation of all 3 subfamilies (ERK 1/2, JNK and p38 kinase) of the MAPK pathway in PSCs.	Acetaldehyde	21-33	mitogen activated protein kinase 3	Rattus norvegicus	117-121
12883264-6	2003	AIMS: To examine the effects of ethanol and acetaldehyde on the MAPK pathway (by assessing the activities of the 3 major subfamilies (extracellular-regulated kinases 1 and 2 [ERK 1/2], JNK and p38 kinase) in PSCs and to examine the role of p38 kinase in mediating the ethanol- and acetaldehyde-induced increase in alpha-SMA expression in activated rat PSCs.	Acetaldehyde	44-56	mitogen activated protein kinase 3	Rattus norvegicus	64-68
12883264-12	2003	Treatment of PSCs with SB203580 abolished the ethanol- and acetaldehyde-induced increase in p38 MAPK activity and also prevented the induction of alpha-SMA expression in PSCs.	Acetaldehyde	59-71	mitogen activated protein kinase 14	Rattus norvegicus	92-95
12883264-12	2003	Treatment of PSCs with SB203580 abolished the ethanol- and acetaldehyde-induced increase in p38 MAPK activity and also prevented the induction of alpha-SMA expression in PSCs.	Acetaldehyde	59-71	mitogen activated protein kinase 3	Rattus norvegicus	96-100
12940444-3	2003	Cytochrome p450 2E1 (CYP2E1) oxidizes ethanol to form acetaldehyde and aldehyde dehydrogenase 2 (ALDH2) detoxifies acetaldehyde, which is carcinogenic in humans, and both alcohol-metabolizing enzymes show the genetic polymorphisms in a Japanese population.	Acetaldehyde	54-66	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	0-19
12883264-15	2003	(2) The p38 MAPK pathway mediates the activation (as indicated by increased alpha-SMA expression) of PSCs by ethanol or acetaldehyde.	Acetaldehyde	120-132	mitogen activated protein kinase 14	Rattus norvegicus	8-11
12883264-15	2003	(2) The p38 MAPK pathway mediates the activation (as indicated by increased alpha-SMA expression) of PSCs by ethanol or acetaldehyde.	Acetaldehyde	120-132	mitogen activated protein kinase 3	Rattus norvegicus	12-16
12883264-15	2003	(2) The p38 MAPK pathway mediates the activation (as indicated by increased alpha-SMA expression) of PSCs by ethanol or acetaldehyde.	Acetaldehyde	120-132	actin gamma 2, smooth muscle	Rattus norvegicus	76-85
12940444-3	2003	Cytochrome p450 2E1 (CYP2E1) oxidizes ethanol to form acetaldehyde and aldehyde dehydrogenase 2 (ALDH2) detoxifies acetaldehyde, which is carcinogenic in humans, and both alcohol-metabolizing enzymes show the genetic polymorphisms in a Japanese population.	Acetaldehyde	54-66	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	21-27
12940444-3	2003	Cytochrome p450 2E1 (CYP2E1) oxidizes ethanol to form acetaldehyde and aldehyde dehydrogenase 2 (ALDH2) detoxifies acetaldehyde, which is carcinogenic in humans, and both alcohol-metabolizing enzymes show the genetic polymorphisms in a Japanese population.	Acetaldehyde	115-127	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	0-19
12940444-3	2003	Cytochrome p450 2E1 (CYP2E1) oxidizes ethanol to form acetaldehyde and aldehyde dehydrogenase 2 (ALDH2) detoxifies acetaldehyde, which is carcinogenic in humans, and both alcohol-metabolizing enzymes show the genetic polymorphisms in a Japanese population.	Acetaldehyde	115-127	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	21-27
12940444-3	2003	Cytochrome p450 2E1 (CYP2E1) oxidizes ethanol to form acetaldehyde and aldehyde dehydrogenase 2 (ALDH2) detoxifies acetaldehyde, which is carcinogenic in humans, and both alcohol-metabolizing enzymes show the genetic polymorphisms in a Japanese population.	Acetaldehyde	115-127	aldehyde dehydrogenase 2 family member	Homo sapiens	71-95
12940444-3	2003	Cytochrome p450 2E1 (CYP2E1) oxidizes ethanol to form acetaldehyde and aldehyde dehydrogenase 2 (ALDH2) detoxifies acetaldehyde, which is carcinogenic in humans, and both alcohol-metabolizing enzymes show the genetic polymorphisms in a Japanese population.	Acetaldehyde	115-127	aldehyde dehydrogenase 2 family member	Homo sapiens	97-102
12940444-4	2003	METHODS: Using polymorphism analysis, we studied the frequency of ALDH2 functional deletion due to the G to A single-bp mutation in exon 12 and CYP2E1 polymorphism in the transcriptional region, both associated with higher levels of acetaldehyde, in 135 patients with LC and/or HCC, including 99 with HCC, and 135 non-cancer controls.	Acetaldehyde	233-245	aldehyde dehydrogenase 2 family member	Homo sapiens	66-71
12672787-2	2003	Ethanol is oxidized to acetaldehyde and then to acetate by alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH), both of which have genetic polymorphisms.	Acetaldehyde	23-35	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	82-85
12878915-12	2003	CONCLUSION: These data suggest that increased cardiac acetaldehyde exposure due to ADH transgene may play an important role in cardiac contractile dysfunctions associated with lipid and protein damage after alcohol intake.	Acetaldehyde	54-66	aldo-keto reductase family 1, member A1 (aldehyde reductase)	Mus musculus	83-86
12826984-10	2003	Aldehyde oxidase is unrelated to the similarly named enzyme aldehyde dehydrogenase, which is predominantly responsible for the oxidation of acetaldehyde during ethanol metabolism.	Acetaldehyde	140-152	aldehyde oxidase 1	Homo sapiens	0-16
12805625-9	2003	None of the three genes is induced by anoxia but ALDH2B7 reacts strongly to ABA application and dehydration, suggesting that ALDH may play a role in aerobic detoxification of acetaldehyde.	Acetaldehyde	175-187	aldehyde dehydrogenase 2B7	Arabidopsis thaliana	49-55
12750236-1	2003	Alcohol is a probable risk factor with regard to colorectal neoplasm and is metabolized to the carcinogen acetaldehyde by the genetically polymorphic alcohol dehydrogenase 3 (ADH3) enzyme.	Acetaldehyde	106-118	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	150-173
12750236-1	2003	Alcohol is a probable risk factor with regard to colorectal neoplasm and is metabolized to the carcinogen acetaldehyde by the genetically polymorphic alcohol dehydrogenase 3 (ADH3) enzyme.	Acetaldehyde	106-118	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	175-179
12711919-4	2003	This study was designed to examine the role of cytochrome P450 oxidase 2E1 (CYP 2E1), xanthine oxidase, and lipid peroxidation in the short-term ACA exposure-induced mechanical defects in adult rat ventricular myocytes.	Acetaldehyde	145-148	cytochrome P450, family 2, subfamily e, polypeptide 1	Rattus norvegicus	47-74
12711919-4	2003	This study was designed to examine the role of cytochrome P450 oxidase 2E1 (CYP 2E1), xanthine oxidase, and lipid peroxidation in the short-term ACA exposure-induced mechanical defects in adult rat ventricular myocytes.	Acetaldehyde	145-148	cytochrome P450, family 2, subfamily e, polypeptide 1	Rattus norvegicus	76-83
12711919-8	2003	It is interesting to note that the ACA-induced effects on myocyte mechanical properties were abolished with co-treatment of the lipid peroxidation inhibitor butylated hydroxytoluene (20 microM), the CYP 2E1 inhibitor diallyl sulfide (100 microM), and the xanthine oxidase inhibitor allopurinol (100 microM).	Acetaldehyde	35-38	cytochrome P450, family 2, subfamily e, polypeptide 1	Rattus norvegicus	199-206
12676688-5	2003	The S. cerevisiae GLY1 gene encodes threonine aldolase (EC 4.1.2.5), which catalyzes the cleavage of threonine to glycine and acetaldehyde.	Acetaldehyde	126-138	threonine aldolase GLY1	Saccharomyces cerevisiae S288C	18-22
12676688-6	2003	Overexpression of GLY1 enabled a Pdc(-) strain to grow under conditions of carbon limitation in chemostat cultures on glucose as the sole carbon source, indicating that acetaldehyde formed by threonine aldolase served as a precursor for the synthesis of cytosolic acetyl-CoA.	Acetaldehyde	169-181	threonine aldolase GLY1	Saccharomyces cerevisiae S288C	18-22
12603834-1	2003	Mitochondrial aldehyde dehydrogenase 2 (ALDH2) plays a major role in acetaldehyde detoxification.	Acetaldehyde	69-81	aldehyde dehydrogenase 2 family member	Rattus norvegicus	0-36
12603834-1	2003	Mitochondrial aldehyde dehydrogenase 2 (ALDH2) plays a major role in acetaldehyde detoxification.	Acetaldehyde	69-81	aldehyde dehydrogenase 2 family member	Rattus norvegicus	40-45
12878915-2	2003	This study was designed to examine the impact of enhanced acetaldehyde exposure on cardiac function via cardiac-specific overexpression of alcohol dehydrogenase (ADH) after alcohol intake.	Acetaldehyde	58-70	aldo-keto reductase family 1, member A1 (aldehyde reductase)	Mus musculus	139-160
12878915-2	2003	This study was designed to examine the impact of enhanced acetaldehyde exposure on cardiac function via cardiac-specific overexpression of alcohol dehydrogenase (ADH) after alcohol intake.	Acetaldehyde	58-70	aldo-keto reductase family 1, member A1 (aldehyde reductase)	Mus musculus	162-165
12878915-6	2003	RESULTS: FVB and ADH mice consuming ethanol exhibited elevated blood ethanol/acetaldehyde, cardiac acetaldehyde, and cardiac hypertrophy compared with non-ethanol-consuming mice.	Acetaldehyde	77-89	aldo-keto reductase family 1, member A1 (aldehyde reductase)	Mus musculus	17-20
12878915-6	2003	RESULTS: FVB and ADH mice consuming ethanol exhibited elevated blood ethanol/acetaldehyde, cardiac acetaldehyde, and cardiac hypertrophy compared with non-ethanol-consuming mice.	Acetaldehyde	99-111	aldo-keto reductase family 1, member A1 (aldehyde reductase)	Mus musculus	17-20
12878915-7	2003	However, the levels of cardiac acetaldehyde and hypertrophy were significantly greater in ADH ethanol-fed mice than FVB ethanol-fed mice.	Acetaldehyde	31-43	aldo-keto reductase family 1, member A1 (aldehyde reductase)	Mus musculus	90-93
12809941-0	2003	Interleukin 8 response and oxidative stress in HepG2 cells treated with ethanol, acetaldehyde or lipopolysaccharide.	Acetaldehyde	81-93	C-X-C motif chemokine ligand 8	Homo sapiens	0-13
12809941-1	2003	The aim of this work was to study the induction and secretion of interleukin 8 (IL-8) and some oxidative stress parameters after ethanol (EtOH), acetaldehyde (Ac) or lipopolysaccharide (LPS) treatment on HepG2 cells.	Acetaldehyde	145-157	C-X-C motif chemokine ligand 8	Homo sapiens	65-78
12809941-1	2003	The aim of this work was to study the induction and secretion of interleukin 8 (IL-8) and some oxidative stress parameters after ethanol (EtOH), acetaldehyde (Ac) or lipopolysaccharide (LPS) treatment on HepG2 cells.	Acetaldehyde	145-157	C-X-C motif chemokine ligand 8	Homo sapiens	80-84
12809941-1	2003	The aim of this work was to study the induction and secretion of interleukin 8 (IL-8) and some oxidative stress parameters after ethanol (EtOH), acetaldehyde (Ac) or lipopolysaccharide (LPS) treatment on HepG2 cells.	Acetaldehyde	159-161	C-X-C motif chemokine ligand 8	Homo sapiens	65-78
12809941-1	2003	The aim of this work was to study the induction and secretion of interleukin 8 (IL-8) and some oxidative stress parameters after ethanol (EtOH), acetaldehyde (Ac) or lipopolysaccharide (LPS) treatment on HepG2 cells.	Acetaldehyde	159-161	C-X-C motif chemokine ligand 8	Homo sapiens	80-84
12794936-10	2003	Finally, analyses indicate that the Msn2/4p and Hsf1p transcription factors are necessary for HSP26, ALD2/3 and ALD4 gene expression under acetaldehyde stress, while PKA represses the expression of these genes.	Acetaldehyde	139-151	stress-responsive transcriptional activator MSN2	Saccharomyces cerevisiae S288C	36-43
12794936-10	2003	Finally, analyses indicate that the Msn2/4p and Hsf1p transcription factors are necessary for HSP26, ALD2/3 and ALD4 gene expression under acetaldehyde stress, while PKA represses the expression of these genes.	Acetaldehyde	139-151	stress-responsive transcription factor HSF1	Saccharomyces cerevisiae S288C	48-53
12794936-10	2003	Finally, analyses indicate that the Msn2/4p and Hsf1p transcription factors are necessary for HSP26, ALD2/3 and ALD4 gene expression under acetaldehyde stress, while PKA represses the expression of these genes.	Acetaldehyde	139-151	chaperone protein HSP26	Saccharomyces cerevisiae S288C	94-99
12794936-10	2003	Finally, analyses indicate that the Msn2/4p and Hsf1p transcription factors are necessary for HSP26, ALD2/3 and ALD4 gene expression under acetaldehyde stress, while PKA represses the expression of these genes.	Acetaldehyde	139-151	aldehyde dehydrogenase (NAD(+)) ALD2	Saccharomyces cerevisiae S288C	101-107
12794936-10	2003	Finally, analyses indicate that the Msn2/4p and Hsf1p transcription factors are necessary for HSP26, ALD2/3 and ALD4 gene expression under acetaldehyde stress, while PKA represses the expression of these genes.	Acetaldehyde	139-151	aldehyde dehydrogenase (NADP(+)) ALD4	Saccharomyces cerevisiae S288C	112-116
12681527-2	2003	Brain acetaldehyde is believed to originate mainly from local brain metabolism of ethanol by the enzyme catalase.	Acetaldehyde	6-18	catalase	Homo sapiens	104-112
12681527-3	2003	Therefore, the inhibition of catalase by 3-amino-1,2,4-triazole (aminotriazole) may help to clarify the involvement of acetaldehyde in ethanol"s hedonic effects.	Acetaldehyde	119-131	catalase	Homo sapiens	29-37
12612910-10	2003	The acetaldehyde-stimulated mitochondrial cholesterol content was preceded by increased levels of endoplasmic reticulum (ER)-responsive gene GADD153 and transcription factor sterol regulatory element-binding protein 1 and mimicked by the ER stress-inducing agents tunicamycin and homocysteine.	Acetaldehyde	4-16	DNA damage inducible transcript 3	Homo sapiens	141-148
12612910-10	2003	The acetaldehyde-stimulated mitochondrial cholesterol content was preceded by increased levels of endoplasmic reticulum (ER)-responsive gene GADD153 and transcription factor sterol regulatory element-binding protein 1 and mimicked by the ER stress-inducing agents tunicamycin and homocysteine.	Acetaldehyde	4-16	sterol regulatory element binding transcription factor 1	Homo sapiens	174-217
12612910-11	2003	Finally, the mGSH depletion induced by acetaldehyde sensitized HepG2 cells to tumor necrosis factor (TNF)-alpha-induced apoptosis that was prevented by cyclosporin A, GSH ethyl ester, and lovastatin.	Acetaldehyde	39-51	tumor necrosis factor	Homo sapiens	78-111
12612910-12	2003	CONCLUSIONS: Acetaldehyde sensitizes HepG2 cells to TNF-alpha by impairing mGSH transport through an ER stress-mediated increase in cholesterol.	Acetaldehyde	13-25	tumor necrosis factor	Homo sapiens	52-61
12672787-6	2003	ALDH2-associated cancer susceptibility fits into a scenario in which acetaldehyde plays a critical role in the development of human cancer.	Acetaldehyde	69-81	aldehyde dehydrogenase 2 family member	Homo sapiens	0-5
12524413-11	2003	The effect of ethanol and acetaldehyde on MMP2 and TIMP2 secretion was also assessed by this method.	Acetaldehyde	26-38	matrix metallopeptidase 2	Rattus norvegicus	42-46
12604200-12	2003	Antiquitin had much lower affinity towards acetaldehyde; the Km value being approximately 220-fold higher than that of ALDH-2.	Acetaldehyde	43-55	aldehyde dehydrogenase 2 family member	Homo sapiens	119-125
12524413-11	2003	The effect of ethanol and acetaldehyde on MMP2 and TIMP2 secretion was also assessed by this method.	Acetaldehyde	26-38	TIMP metallopeptidase inhibitor 2	Rattus norvegicus	51-56
12524413-15	2003	Ethanol and acetaldehyde induced secretion of both MMP2 and TIMP2 by PSCs.	Acetaldehyde	12-24	matrix metallopeptidase 2	Rattus norvegicus	51-55
12524413-15	2003	Ethanol and acetaldehyde induced secretion of both MMP2 and TIMP2 by PSCs.	Acetaldehyde	12-24	TIMP metallopeptidase inhibitor 2	Rattus norvegicus	60-65
12524413-18	2003	Both ethanol and its metabolite acetaldehyde increase MMP2 as well as TIMP2 secretion by PSCs.	Acetaldehyde	32-44	matrix metallopeptidase 2	Rattus norvegicus	54-58
12524413-18	2003	Both ethanol and its metabolite acetaldehyde increase MMP2 as well as TIMP2 secretion by PSCs.	Acetaldehyde	32-44	TIMP metallopeptidase inhibitor 2	Rattus norvegicus	70-75
12734561-7	2003	The ACA-induced cardiac contractile depression may be reconciled with inhibitors of Cytochrome P-450 oxidase, xanthine oxidase and lipid peroxidation Unfortunately, the common methods to investigate the toxicity of ACA have been hampered by the fact that direct intake of ACA is toxic and unsuitable for chronic study, which is unable to provide direct evidence of direct cardiac toxicity for ACA.	Acetaldehyde	4-7	xanthine dehydrogenase	Mus musculus	110-126
12223099-6	2002	In addition, EGCG markedly suppressed the activation of cultured HSC as demonstrated by blocking transforming growth factor-beta signal transduction and by inhibiting the expression of alpha1(I) collagen, fibronectin and alpha-smooth muscle actin genes induced by acetaldehyde, the most active metabolite of ethanol.	Acetaldehyde	264-276	fibronectin 1	Homo sapiens	205-216
12905081-1	2003	Mitochondrial aldehyde dehydrogenase 2 (ALDH2) plays a major role in acetaldehyde detoxification.	Acetaldehyde	69-81	aldehyde dehydrogenase 2 family member	Homo sapiens	40-45
12486230-6	2002	AlkB, ABH2, and ABH3 can also repair 1-ethyladenine residues in DNA with the release of acetaldehyde.	Acetaldehyde	88-100	alkB homolog 1, histone H2A dioxygenase	Homo sapiens	0-4
12486230-6	2002	AlkB, ABH2, and ABH3 can also repair 1-ethyladenine residues in DNA with the release of acetaldehyde.	Acetaldehyde	88-100	alkB homolog 2, alpha-ketoglutarate dependent dioxygenase	Homo sapiens	6-10
12486230-6	2002	AlkB, ABH2, and ABH3 can also repair 1-ethyladenine residues in DNA with the release of acetaldehyde.	Acetaldehyde	88-100	alkB homolog 3, alpha-ketoglutarate dependent dioxygenase	Homo sapiens	16-20
12223100-6	2002	It was hypothesized that acetaldehyde activated TGF-beta signalling by inducing the expression of elements in the TGF-beta signal transduction pathway, which might contribute to alpha1(I) collagen gene expression in cultured HSC.	Acetaldehyde	25-37	transforming growth factor, beta 1	Rattus norvegicus	48-56
12223100-6	2002	It was hypothesized that acetaldehyde activated TGF-beta signalling by inducing the expression of elements in the TGF-beta signal transduction pathway, which might contribute to alpha1(I) collagen gene expression in cultured HSC.	Acetaldehyde	25-37	transforming growth factor, beta 1	Rattus norvegicus	114-122
12223100-7	2002	Initial results revealed that acetaldehyde activated TGF-beta signalling in cultured HSC.	Acetaldehyde	30-42	transforming growth factor, beta 1	Rattus norvegicus	53-61
12223100-8	2002	Additional studies demonstrated that acetaldehyde stimulated the secretion and activation of latent TGF-beta1, and induced the expression of the type II TGF-beta receptor (Tbeta-RII).	Acetaldehyde	37-49	transforming growth factor, beta 1	Rattus norvegicus	100-109
12223100-0	2002	Acetaldehyde stimulates the activation of latent transforming growth factor-beta1 and induces expression of the type II receptor of the cytokine in rat cultured hepatic stellate cells.	Acetaldehyde	0-12	transforming growth factor, beta 1	Rattus norvegicus	49-81
12223100-5	2002	The aims of this study were to determine the effect of acetaldehyde on TGF-beta signalling, to elucidate the underlying mechanisms as well as to evaluate its role in expression of alpha1(I) collagen gene in cultured HSC.	Acetaldehyde	55-67	transforming growth factor, beta 1	Rattus norvegicus	71-79
12473414-4	2002	Allelic variants in ALDH2 cause decreased ability to clear acetaldehyde and other aldehyde substrates, with homozygous variants (ALDH2*2/2) having no activity and heterozygotes (ALDH2*1/2) having intermediate activity relative to the predominant wild type (ALDH2*1/1).	Acetaldehyde	59-71	aldehyde dehydrogenase 2 family member	Homo sapiens	20-25
12223100-8	2002	Additional studies demonstrated that acetaldehyde stimulated the secretion and activation of latent TGF-beta1, and induced the expression of the type II TGF-beta receptor (Tbeta-RII).	Acetaldehyde	37-49	transforming growth factor, beta 1	Rattus norvegicus	100-108
12223100-8	2002	Additional studies demonstrated that acetaldehyde stimulated the secretion and activation of latent TGF-beta1, and induced the expression of the type II TGF-beta receptor (Tbeta-RII).	Acetaldehyde	37-49	transforming growth factor, beta receptor 2	Rattus norvegicus	172-181
12223100-9	2002	Further experiments found cis - and trans -activating elements responsible for Tbeta-RII gene expression induced by acetaldehyde.	Acetaldehyde	116-128	transforming growth factor, beta receptor 2	Rattus norvegicus	79-88
12223100-10	2002	Activation of TGF-beta signalling by acetaldehyde contributed to alpha1(I) collagen gene expression in cultured HSC.	Acetaldehyde	37-49	transforming growth factor, beta 1	Rattus norvegicus	14-22
12223100-11	2002	In summary, this report demonstrated that acetaldehyde stimulated TGF-beta signalling by increasing the secretion and activation of latent TGF-beta1 as well as by inducing the expression of Tbeta-RII in cultured HSC.	Acetaldehyde	42-54	transforming growth factor, beta 1	Rattus norvegicus	66-74
12223100-11	2002	In summary, this report demonstrated that acetaldehyde stimulated TGF-beta signalling by increasing the secretion and activation of latent TGF-beta1 as well as by inducing the expression of Tbeta-RII in cultured HSC.	Acetaldehyde	42-54	transforming growth factor, beta 1	Rattus norvegicus	139-148
12223100-11	2002	In summary, this report demonstrated that acetaldehyde stimulated TGF-beta signalling by increasing the secretion and activation of latent TGF-beta1 as well as by inducing the expression of Tbeta-RII in cultured HSC.	Acetaldehyde	42-54	transforming growth factor, beta receptor 2	Rattus norvegicus	190-199
12445823-2	2002	Here we show that DLPC also decreases TNF-alpha induction by acetaldehyde, a toxic metabolite released by ethanol oxidation.	Acetaldehyde	61-73	tumor necrosis factor	Rattus norvegicus	38-47
12445823-3	2002	Acetaldehyde induces TNF-alpha generation with a maximal effect at 200 microM and activates p38 and ERK1/2; the latter in turn activates NF-kappaB.	Acetaldehyde	0-12	tumor necrosis factor	Rattus norvegicus	21-30
12445823-3	2002	Acetaldehyde induces TNF-alpha generation with a maximal effect at 200 microM and activates p38 and ERK1/2; the latter in turn activates NF-kappaB.	Acetaldehyde	0-12	mitogen activated protein kinase 14	Rattus norvegicus	92-95
12445823-3	2002	Acetaldehyde induces TNF-alpha generation with a maximal effect at 200 microM and activates p38 and ERK1/2; the latter in turn activates NF-kappaB.	Acetaldehyde	0-12	mitogen activated protein kinase 3	Rattus norvegicus	100-106
12445823-0	2002	Dilinoleoylphosphatidylcholine decreases acetaldehyde-induced TNF-alpha generation in Kupffer cells of ethanol-fed rats.	Acetaldehyde	41-53	tumor necrosis factor	Rattus norvegicus	62-71
12474118-2	2002	This role seems to be related to the ability of cerebral catalase to metabolise ethanol to acetaldehyde using H(2)O(2)as a co-substrate.	Acetaldehyde	91-103	catalase	Mus musculus	57-65
12419648-0	2002	Pentoxifylline diminished acetaldehyde-induced collagen production in hepatic stellate cells by decreasing interleukin-6 expression.	Acetaldehyde	26-38	interleukin 6	Rattus norvegicus	107-120
12517056-10	2002	CONCLUSION: Individuals heterozygous for ALDH2*2 exhibit strong alcohol hypersensitivity caused by persistent accumulation of large amounts of acetaldehyde, but homozygosity for ADH2*2 is not dependent upon this pathway against alcoholism.	Acetaldehyde	143-155	aldehyde dehydrogenase 2 family member	Homo sapiens	41-46
12367788-8	2002	In conclusion, subjects with the ADH3*1 allele showed higher ADH activity and acetaldehyde-DNA adducts in lung than other subjects; thus, the ADH3*1 allele could be considered a risk factor for lung cancer.	Acetaldehyde	78-90	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	33-37
12439222-6	2002	After free-choice ethanol and water drinking, brain and liver acetaldehyde concentrations of Aldh2-/- mice were almost equal to those of wild-type (Aldh2+/+) mice although the Aldh2-/- mice drank less ethanol than the Aldh2+/+ mice.	Acetaldehyde	62-74	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	93-98
12439222-7	2002	This result indicates that a direct effect of the Aldh2 genotype plays an important role on alcohol preference and acetaldehyde concentration in the brain is correlated with alcohol avoidance.	Acetaldehyde	115-127	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	50-55
12376487-13	2002	After alcohol ingestion, acetaldehyde in the breath was elevated to a significantly higher level in all patients with the ALDH2-2 allele than in those without it.	Acetaldehyde	25-37	aldehyde dehydrogenase 2 family member	Homo sapiens	122-127
12376487-14	2002	The high levels of breath acetaldehyde were significantly modified by the slow-metabolizing ADH3-2 allele.	Acetaldehyde	26-38	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	92-96
12419648-7	2002	However, PTX induced a decrease of 32% in IL-6 mRNA in acetaldehyde-treated cells.	Acetaldehyde	55-67	interleukin 6	Rattus norvegicus	42-46
12419648-9	2002	These results show that PTX inhibits the expression of alpha(1)(I) collagen via the inhibition of IL-6 in acetaldehyde treated cells.	Acetaldehyde	106-118	interleukin 6	Rattus norvegicus	98-102
12419648-10	2002	The effect herein reported on IL-6 and alpha(1)(I) collagen mRNA adds to the previously described effect of PTX, which could be useful in the fibrogenic process induced by acetaldehyde.	Acetaldehyde	172-184	interleukin 6	Rattus norvegicus	30-34
12387818-5	2002	Purified wild-type ALDH2 and mutant ALDH2(2) had a K(m) for acetaldehyde of 0.65 and 25.73 microM, respectively.	Acetaldehyde	60-72	aldehyde dehydrogenase 2 family member	Homo sapiens	19-24
12387818-5	2002	Purified wild-type ALDH2 and mutant ALDH2(2) had a K(m) for acetaldehyde of 0.65 and 25.73 microM, respectively.	Acetaldehyde	60-72	aldehyde dehydrogenase 2 family member	Homo sapiens	36-41
12387818-6	2002	Co-expression of ALDH2 with ALDH2(2) in the presence of E. coli chaperonins produced a soluble enzyme with a K(m) for acetaldehyde of 8.79 microM, suggesting that the product was a heteromer.	Acetaldehyde	118-130	aldehyde dehydrogenase 2 family member	Homo sapiens	17-22
12387818-6	2002	Co-expression of ALDH2 with ALDH2(2) in the presence of E. coli chaperonins produced a soluble enzyme with a K(m) for acetaldehyde of 8.79 microM, suggesting that the product was a heteromer.	Acetaldehyde	118-130	aldehyde dehydrogenase 2 family member	Homo sapiens	28-33
12367788-8	2002	In conclusion, subjects with the ADH3*1 allele showed higher ADH activity and acetaldehyde-DNA adducts in lung than other subjects; thus, the ADH3*1 allele could be considered a risk factor for lung cancer.	Acetaldehyde	78-90	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	142-146
12237745-15	2002	These data demonstrate that inhibition of MAO-A, but not MAO-B, reduces the volitional consumption of ethanol probably by preventing the formation of both biogenic aldehydes and acetaldehyde so that rewarding alkaloidal products cannot be formed.	Acetaldehyde	178-190	monoamine oxidase A	Rattus norvegicus	42-47
12217933-0	2002	Effects of acetaldehyde on c-fos mRNA induction in the paraventricular nucleus following ethanol administration.	Acetaldehyde	11-23	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	27-32
12217933-1	2002	AIMS: The effect of acetaldehyde on c-fos mRNA expression in the paraventricular nucleus (PVN) of the rat was examined using in situ hybridization histochemistry.	Acetaldehyde	20-32	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	36-41
12217933-8	2002	CONCLUSIONS: These data suggest that acetaldehyde accumulation in blood has an important stimulatory effect on c-fos expression in the PVN at low ethanol concentrations.	Acetaldehyde	37-49	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	111-116
12223435-1	2002	Aldehyde dehydrogenase-2 (ALDH2) is a key enzyme for the elimination of acetaldehyde, an established animal carcinogen generated by alcohol metabolism.	Acetaldehyde	72-84	aldehyde dehydrogenase 2 family member	Homo sapiens	0-24
12223435-1	2002	Aldehyde dehydrogenase-2 (ALDH2) is a key enzyme for the elimination of acetaldehyde, an established animal carcinogen generated by alcohol metabolism.	Acetaldehyde	72-84	aldehyde dehydrogenase 2 family member	Homo sapiens	26-31
12223435-2	2002	In the presence of ALDH2*2, a mutant allele that is prevalent in East Asians, this enzyme is inactive, leading to excessive accumulation of acetaldehyde.	Acetaldehyde	140-152	aldehyde dehydrogenase 2 family member	Homo sapiens	19-24
12122204-10	2002	Livers from ethanol-fed animals showed increased centrilobular CYP2E1 and protein adducts with acetaldehyde and MDA.	Acetaldehyde	95-107	cytochrome P450 family 2 subfamily E member 1	Sus scrofa	63-69
12198372-0	2002	Acetaldehyde-induced growth retardation and micro-heterogeneity of the sugar chain in transferrin synthesized by HepG2 cells.	Acetaldehyde	0-12	transferrin	Homo sapiens	86-97
12034373-3	2002	We have obtained in vitro, by the reaction of dopa-enkephalin (dopa-Gly-Gly-Phe-Leu) with acetaldehyde in the presence of rameic ions, a TIQ derivative of Leu-enkephalin.	Acetaldehyde	90-102	prodynorphin	Homo sapiens	155-169
12065697-6	2002	Ethanol and acetaldehyde activated activator protein-1 but not nuclear factor-kappaB.	Acetaldehyde	12-24	Jun proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	35-54
12065697-8	2002	Ethanol- and acetaldehyde-induced activation of activator protein-1 and MAP kinases was blocked by the antioxidant N-acetyl-cysteine, suggesting a role of oxidative stress in the signal transduction.	Acetaldehyde	13-25	Jun proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	48-67
12065697-10	2002	The acetaldehyde-induced increase of alpha1(I) procollagen gene expression was inhibited by the p38 MAP kinase inhibitor 4-(4-fluorophenyl)-2-(4-methylsulfinylphenyl)-5-(4-pyridyl)imidazole (SB203580) but not by the MAP kinase inhibitor 2"-amino-3"-methoxyflavone (PD98059).	Acetaldehyde	4-16	mitogen activated protein kinase 14	Rattus norvegicus	96-99
12068249-2	2002	Acetaldehyde can be produced by the enzyme catalase within the brain after ethanol administration.	Acetaldehyde	0-12	catalase	Rattus norvegicus	43-51
12068249-3	2002	The catalase inhibitor 3-amino-1,2,4-triazole (AT) reduces the production of acetaldehyde, and AT administration can reduce a number of ethanol-induced behavioral effects; this suggests the involvement of acetaldehyde in these behaviors.	Acetaldehyde	77-89	catalase	Rattus norvegicus	4-12
12068249-3	2002	The catalase inhibitor 3-amino-1,2,4-triazole (AT) reduces the production of acetaldehyde, and AT administration can reduce a number of ethanol-induced behavioral effects; this suggests the involvement of acetaldehyde in these behaviors.	Acetaldehyde	205-217	catalase	Rattus norvegicus	4-12
12023518-3	2002	Acetaldehyde caused peak activation of p42/44 MAPK at 10 min followed by JNK activation at 1 h. These responses were acetaldehyde dose-dependent (0.2-5 mM).	Acetaldehyde	0-12	mitogen-activated protein kinase 8	Rattus norvegicus	73-76
12023518-3	2002	Acetaldehyde caused peak activation of p42/44 MAPK at 10 min followed by JNK activation at 1 h. These responses were acetaldehyde dose-dependent (0.2-5 mM).	Acetaldehyde	117-129	mitogen-activated protein kinase 8	Rattus norvegicus	73-76
12023518-8	2002	Thus, ethanol-activated JNK may be both acetaldehyde-dependent and -independent.	Acetaldehyde	40-52	mitogen-activated protein kinase 8	Rattus norvegicus	24-27
12023518-9	2002	The activation of JNK by ethanol or acetaldehyde was insensitive to the treatment of hepatocytes with genistein (tyrosine kinase inhibitor) and 2-[1-(3-dimethylaminopropyl)-1H-indol-3-yl]-3-(1H-indol-3-yl)maleimide (GF109203X) (protein kinase C inhibitor).	Acetaldehyde	36-48	mitogen-activated protein kinase 8	Rattus norvegicus	18-21
12243086-3	2002	on the blood concentrations of endogenous acetaldehyde and ethanol and the activities of enzymes producing and oxidizing acetaldehyde in the liver of normal rats and rats with liver injury provoked by chronic carbon tetrachloride (CCl4) treatment (0.2 ml i.p.	Acetaldehyde	121-133	C-C motif chemokine ligand 4	Rattus norvegicus	231-235
12128098-10	2002	The absence of enzymes to convert ethanol to acetaldehyde, coupled with oocyte expression of the acetaldehyde-degrading enzyme, Ahd-5, may be protective for the early embryo.	Acetaldehyde	97-109	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	128-133
12243086-7	2002	The CCl4 treatment resulted in decreased liver alcohol dehydrogenase and aldehyde dehydrogenase activities and a significant elevation of liver endogenous ehtanol and a clear tendency to enhance blood acetaldehyde levels.	Acetaldehyde	201-213	C-C motif chemokine ligand 4	Rattus norvegicus	4-8
12243086-8	2002	Pyruvate increased blood endogenous acetaldehyde in CCl4-treated animals and endogenous ethanol--in the control group of animals.	Acetaldehyde	36-48	C-C motif chemokine ligand 4	Rattus norvegicus	52-56
12243086-12	2002	Thus, the CCl4 effect on blood endogenous acetaldehyde and ethanol may be mediated through decreased liver ALDH and ADH activities.	Acetaldehyde	42-54	C-C motif chemokine ligand 4	Rattus norvegicus	10-14
11825850-1	2002	A significant difference in blood-acetaldehyde concentration was observed between high alcohol-preference (HAP) rats and low alcohol-preference (LAP) rats, newly developed different alcohol preference lines.	Acetaldehyde	34-46	acid phosphatase 2, lysosomal	Rattus norvegicus	121-143
11893554-2	2002	This study examined the impact of cardiac overexpression of alcohol dehydrogenase (ADH), which oxidizes ethanol into acetaldehyde (ACA), on ethanol-induced cardiac contractile defect.	Acetaldehyde	117-129	aldo-keto reductase family 1, member A1 (aldehyde reductase)	Mus musculus	60-81
11893554-2	2002	This study examined the impact of cardiac overexpression of alcohol dehydrogenase (ADH), which oxidizes ethanol into acetaldehyde (ACA), on ethanol-induced cardiac contractile defect.	Acetaldehyde	117-129	aldo-keto reductase family 1, member A1 (aldehyde reductase)	Mus musculus	83-86
11893554-2	2002	This study examined the impact of cardiac overexpression of alcohol dehydrogenase (ADH), which oxidizes ethanol into acetaldehyde (ACA), on ethanol-induced cardiac contractile defect.	Acetaldehyde	131-134	aldo-keto reductase family 1, member A1 (aldehyde reductase)	Mus musculus	60-81
11893554-2	2002	This study examined the impact of cardiac overexpression of alcohol dehydrogenase (ADH), which oxidizes ethanol into acetaldehyde (ACA), on ethanol-induced cardiac contractile defect.	Acetaldehyde	131-134	aldo-keto reductase family 1, member A1 (aldehyde reductase)	Mus musculus	83-86
11978551-0	2002	Acetaldehyde activates Jun/AP-1 expression and DNA binding activity in human oral keratinocytes.	Acetaldehyde	0-12	Jun proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	27-31
11978551-4	2002	We hypothesize that acetaldehyde, the first metabolite of ethanol, may activate the expression and/or activity of Jun/AP-1 in oral keratinocytes analogous to the phorbol ester TPA and other tumor promoters in epidermal keratinocytes.	Acetaldehyde	20-32	Jun proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	118-122
11978551-6	2002	Our results indicated that c-Jun mRNA and protein levels increased in the acetaldehyde treated cells compared to untreated control cells.	Acetaldehyde	74-86	Jun proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	27-32
11978551-7	2002	Moreover, Jun/AP-1 DNA binding activity was rapidly activated by acetaldehyde in a dose-dependent fashion.	Acetaldehyde	65-77	Jun proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	14-18
12026193-2	2002	Pretreatment with ACE (dose, 70mg/kg body weight and 700 mg/kg body weight) inhibited increases in the levels of proliferating nuclear cell antigen and ornithine decarboxylase at the promotion stage.	Acetaldehyde	18-21	ornithine decarboxylase, structural 1	Mus musculus	152-175
11981126-9	2002	Heavy alcohol consumption seems to alter the effect of apoE polymorphism on apoB levels, and further investigations are needed to clarify the mechanisms involved in this phenomenon: a defect in sialylation of apoE, formation of acetaldehyde adducts on apoB, or both.	Acetaldehyde	228-240	apolipoprotein E	Homo sapiens	55-59
11981126-9	2002	Heavy alcohol consumption seems to alter the effect of apoE polymorphism on apoB levels, and further investigations are needed to clarify the mechanisms involved in this phenomenon: a defect in sialylation of apoE, formation of acetaldehyde adducts on apoB, or both.	Acetaldehyde	228-240	apolipoprotein B	Homo sapiens	76-80
11889484-5	2002	Moreover, gene expression analysis revealed induction of the heat shock protein (HSP) genes HSP12, HSP82, and especially HSP26 and HSP104, under acetaldehyde stress in most of the strains.	Acetaldehyde	145-157	lipid-binding protein HSP12	Saccharomyces cerevisiae S288C	92-97
11889484-5	2002	Moreover, gene expression analysis revealed induction of the heat shock protein (HSP) genes HSP12, HSP82, and especially HSP26 and HSP104, under acetaldehyde stress in most of the strains.	Acetaldehyde	145-157	Hsp90 family chaperone HSP82	Saccharomyces cerevisiae S288C	99-104
11889484-5	2002	Moreover, gene expression analysis revealed induction of the heat shock protein (HSP) genes HSP12, HSP82, and especially HSP26 and HSP104, under acetaldehyde stress in most of the strains.	Acetaldehyde	145-157	chaperone protein HSP26	Saccharomyces cerevisiae S288C	121-126
11889484-5	2002	Moreover, gene expression analysis revealed induction of the heat shock protein (HSP) genes HSP12, HSP82, and especially HSP26 and HSP104, under acetaldehyde stress in most of the strains.	Acetaldehyde	145-157	chaperone ATPase HSP104	Saccharomyces cerevisiae S288C	131-137
11919660-2	2002	Diethyldithiocarbamate (DDTC), an ALDH inhibitor, elevates blood acetaldehyde levels in the presence of ethanol.	Acetaldehyde	65-77	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	34-38
11919660-12	2002	This role of the enzyme ALDH in some of the psychopharmacological effects of ethanol may be a result of its ability to regulate levels of acetaldehyde in brain.	Acetaldehyde	138-150	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	24-28
11841919-1	2002	Malondialdehyde and acetaldehyde react together with proteins in a synergistic manner and form hybrid protein adducts, designated as MAA adducts.	Acetaldehyde	20-32	MAA	Homo sapiens	133-136
11853706-0	2002	Effect of malondialdehyde-acetaldehyde-protein adducts on the protein kinase C-dependent secretion of urokinase-type plasminogen activator in hepatic stellate cells.	Acetaldehyde	26-38	plasminogen activator, urokinase	Rattus norvegicus	102-138
11825850-2	2002	This difference of acetaldehyde accumulation may be due to cytosolic aldehyde dehydrogenase (ALDH1) polymorphism, which has been reported previously.	Acetaldehyde	19-31	aldehyde dehydrogenase 1 family, member A1	Rattus norvegicus	93-98
11798074-1	2001	The genotypes of liver mitochondrial high-affinity aldehyde dehydrogenase-2 (ALDH2) are strongly associated with the drinking behavior and the alcohol liver diseases, since the individuals with atypical ALDH2(2) allele have higher levels of acetaldehyde in their plasma.	Acetaldehyde	241-253	aldehyde dehydrogenase 2 family member	Homo sapiens	51-75
11782879-12	2002	(5) Cathepsin D activities were reduced in muscle homogenates upon addition of alcohol and acetaldehyde in vitro.	Acetaldehyde	91-103	cathepsin D	Rattus norvegicus	4-15
11798074-1	2001	The genotypes of liver mitochondrial high-affinity aldehyde dehydrogenase-2 (ALDH2) are strongly associated with the drinking behavior and the alcohol liver diseases, since the individuals with atypical ALDH2(2) allele have higher levels of acetaldehyde in their plasma.	Acetaldehyde	241-253	aldehyde dehydrogenase 2 family member	Homo sapiens	77-82
11798074-1	2001	The genotypes of liver mitochondrial high-affinity aldehyde dehydrogenase-2 (ALDH2) are strongly associated with the drinking behavior and the alcohol liver diseases, since the individuals with atypical ALDH2(2) allele have higher levels of acetaldehyde in their plasma.	Acetaldehyde	241-253	aldehyde dehydrogenase 2 family member	Homo sapiens	203-208
11748356-1	2001	Alcohol is oxidized to acetaldehyde by alcohol dehydrogenase (ADH) and cytochrome P-4502E1 (CYP2E1), and then to acetate by aldehyde dehydrogenase (ALDH).	Acetaldehyde	23-35	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	62-65
11748356-1	2001	Alcohol is oxidized to acetaldehyde by alcohol dehydrogenase (ADH) and cytochrome P-4502E1 (CYP2E1), and then to acetate by aldehyde dehydrogenase (ALDH).	Acetaldehyde	23-35	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	92-98
11698345-0	2001	Mutational spectrum induced by acetaldehyde in the HPRT gene of human T lymphocytes resembles that in the p53 gene of esophageal cancers.	Acetaldehyde	31-43	hypoxanthine phosphoribosyltransferase 1	Homo sapiens	51-55
11828713-3	2001	The inactive form of aldehyde dehydrogenase-2 (ALDH2), encoded by the gene ALDH2*1/2*2, which is prevalent in Asians, exposes them to higher levels of acetaldehyde after drinking and was a strong risk factor for these cancers among Japanese heavy drinkers.	Acetaldehyde	151-163	aldehyde dehydrogenase 2 family member	Homo sapiens	21-45
11828713-3	2001	The inactive form of aldehyde dehydrogenase-2 (ALDH2), encoded by the gene ALDH2*1/2*2, which is prevalent in Asians, exposes them to higher levels of acetaldehyde after drinking and was a strong risk factor for these cancers among Japanese heavy drinkers.	Acetaldehyde	151-163	aldehyde dehydrogenase 2 family member	Homo sapiens	47-52
11828713-3	2001	The inactive form of aldehyde dehydrogenase-2 (ALDH2), encoded by the gene ALDH2*1/2*2, which is prevalent in Asians, exposes them to higher levels of acetaldehyde after drinking and was a strong risk factor for these cancers among Japanese heavy drinkers.	Acetaldehyde	151-163	aldehyde dehydrogenase 2 family member	Homo sapiens	75-80
11839459-0	2001	Malondialdehyde-acetaldehyde-adducted bovine serum albumin activates protein kinase C and stimulates interleukin-8 release in bovine bronchial epithelial cells.	Acetaldehyde	16-28	albumin	Bos taurus	45-58
11839459-0	2001	Malondialdehyde-acetaldehyde-adducted bovine serum albumin activates protein kinase C and stimulates interleukin-8 release in bovine bronchial epithelial cells.	Acetaldehyde	16-28	C-X-C motif chemokine ligand 8	Bos taurus	101-114
11839459-1	2001	Previous study results have demonstrated that cigarette smoke or acetaldehyde rapidly stimulates protein kinase C (PKC)-mediated release of interleukin-8 (IL-8) in bovine bronchial epithelial cells (BECs).	Acetaldehyde	65-77	protein kinase C alpha	Bos taurus	115-118
11839459-1	2001	Previous study results have demonstrated that cigarette smoke or acetaldehyde rapidly stimulates protein kinase C (PKC)-mediated release of interleukin-8 (IL-8) in bovine bronchial epithelial cells (BECs).	Acetaldehyde	65-77	C-X-C motif chemokine ligand 8	Bos taurus	140-153
11839459-1	2001	Previous study results have demonstrated that cigarette smoke or acetaldehyde rapidly stimulates protein kinase C (PKC)-mediated release of interleukin-8 (IL-8) in bovine bronchial epithelial cells (BECs).	Acetaldehyde	65-77	C-X-C motif chemokine ligand 8	Bos taurus	155-159
11839459-2	2001	Low concentrations of acetaldehyde combine synergistically with malondialdehyde to increase significantly maximal BEC PKC activity at 48 to 96 h stimulation.	Acetaldehyde	22-34	protein kinase C alpha	Bos taurus	118-121
11839459-3	2001	Because more than 95% of alcoholics are cigarette smokers, we hypothesized that malondialdehyde, an inflammation product of lipid peroxidation, and acetaldehyde, both a product of ethanol metabolism and a component of cigarette smoke, might stimulate PKC-mediated IL-8 release in BECs by malondialdehyde-acetaldehyde (MAA) adduct formation, rather than as free aldehydes.	Acetaldehyde	148-160	protein kinase C alpha	Bos taurus	251-254
11839459-3	2001	Because more than 95% of alcoholics are cigarette smokers, we hypothesized that malondialdehyde, an inflammation product of lipid peroxidation, and acetaldehyde, both a product of ethanol metabolism and a component of cigarette smoke, might stimulate PKC-mediated IL-8 release in BECs by malondialdehyde-acetaldehyde (MAA) adduct formation, rather than as free aldehydes.	Acetaldehyde	148-160	C-X-C motif chemokine ligand 8	Bos taurus	264-268
11839459-8	2001	Results of these studies indicate that metabolites derived from ethanol and cigarette smoke, such as acetaldehyde and malondialdehyde, form adducts that stimulate airway epithelial cell PKC alpha-mediated release of promigratory cytokines.	Acetaldehyde	101-113	protein kinase C alpha	Bos taurus	186-195
11700261-2	2001	Alcohol dehydrogenase 3 (ADH3) converts ethanol to acetaldehyde, which is a suspected oral carcinogen.	Acetaldehyde	51-63	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	0-23
11700261-2	2001	Alcohol dehydrogenase 3 (ADH3) converts ethanol to acetaldehyde, which is a suspected oral carcinogen.	Acetaldehyde	51-63	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	25-29
11700261-3	2001	The ADH3*1 allele is associated with increased conversion of ethanol to acetaldehyde, but whether the risk of OSCC is increased among ADH3*1 carriers, or whether the risk of OSCC attributable to alcohol consumption is modified by ADH3 genotype is unclear from previous studies.	Acetaldehyde	72-84	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	4-8
11698345-0	2001	Mutational spectrum induced by acetaldehyde in the HPRT gene of human T lymphocytes resembles that in the p53 gene of esophageal cancers.	Acetaldehyde	31-43	tumor protein p53	Homo sapiens	106-109
11668012-3	2001	The purpose of this work was to examine the effect of acetaldehyde on PDH in vitro.	Acetaldehyde	54-66	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	70-73
11641261-3	2001	Acute ethanol or acetaldehyde exposure potentiates HBX or HCV core protein activation of NF-kappaB in primary mouse hepatocytes.	Acetaldehyde	17-29	nuclear factor of kappa light polypeptide gene enhancer in B cells 1, p105	Mus musculus	89-98
11641261-5	2001	Moreover, pertussis toxin attenuates NF-kappaB activation induced by acetaldehyde but not by HBX or HCV core protein, whereas HBX or HCV core protein-mediated activation of NF-kappaB is abolished completely in tumor necrosis factor a receptor 1 (TNFR1) (-/-) hepatocytes.	Acetaldehyde	69-81	nuclear factor kappa B subunit 1	Homo sapiens	37-46
11692094-1	2001	BACKGROUND: We have previously reported that alcohol-induced asthma in Japanese patients is caused by increased blood acetaldehyde concentration resulting from abnormalities of acetaldehyde dehydrogenase 2 (ALDH2) enzyme activity on the basis of ALDH2 genotype differences.	Acetaldehyde	118-130	aldehyde dehydrogenase 2 family member	Homo sapiens	177-205
11692094-1	2001	BACKGROUND: We have previously reported that alcohol-induced asthma in Japanese patients is caused by increased blood acetaldehyde concentration resulting from abnormalities of acetaldehyde dehydrogenase 2 (ALDH2) enzyme activity on the basis of ALDH2 genotype differences.	Acetaldehyde	118-130	aldehyde dehydrogenase 2 family member	Homo sapiens	207-212
11692094-1	2001	BACKGROUND: We have previously reported that alcohol-induced asthma in Japanese patients is caused by increased blood acetaldehyde concentration resulting from abnormalities of acetaldehyde dehydrogenase 2 (ALDH2) enzyme activity on the basis of ALDH2 genotype differences.	Acetaldehyde	118-130	aldehyde dehydrogenase 2 family member	Homo sapiens	246-251
11903746-12	2001	Interleukin-6 production increased to 288 +/- 48, 1195 +/- 86 and 247 +/- 35 pg/mL per 10(6) cells after ethanol, acetaldehyde and LPS exposure, and increased further with LPS pretreatment in ethanol-exposed cells (680 +/- 23 pg/mL 10(6) cells).	Acetaldehyde	114-126	interleukin 6	Homo sapiens	0-13
11762132-2	2001	Most ethanol elimination occurs by oxidation to acetaldehyde and acetate, catalyzed principally by alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH).	Acetaldehyde	48-60	aldo-keto reductase family 1 member A1	Homo sapiens	99-120
11762132-2	2001	Most ethanol elimination occurs by oxidation to acetaldehyde and acetate, catalyzed principally by alcohol dehydrogenase (ADH) and aldehyde dehydrogenase (ALDH).	Acetaldehyde	48-60	aldo-keto reductase family 1 member A1	Homo sapiens	122-125
11535626-1	2001	A mutation in the gene encoding for the liver mitochondrial aldehyde dehydrogenase (ALDH2-2), present in some Asian populations, lowers or abolishes the activity of this enzyme and results in elevations in blood acetaldehyde upon ethanol consumption, a phenotype that greatly protects against alcohol abuse and alcoholism.	Acetaldehyde	212-224	aldehyde dehydrogenase 2 family member	Rattus norvegicus	46-82
11535626-1	2001	A mutation in the gene encoding for the liver mitochondrial aldehyde dehydrogenase (ALDH2-2), present in some Asian populations, lowers or abolishes the activity of this enzyme and results in elevations in blood acetaldehyde upon ethanol consumption, a phenotype that greatly protects against alcohol abuse and alcoholism.	Acetaldehyde	212-224	aldehyde dehydrogenase 2 family member	Rattus norvegicus	84-91
11752857-1	2001	OBJECTIVES: The polymorphic enzyme alcohol dehydrogenase (ADH) catalyses the conversion of ethanol into the carcinogenic metabolite acetaldehyde which is partly excreted into the urine.	Acetaldehyde	132-144	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	58-61
11712874-6	2001	In hepatic stellate cells, metadoxine prevents the increase in collagen and attenuated TNF- alpha secretion caused by acetaldehyde.	Acetaldehyde	118-130	tumor necrosis factor	Homo sapiens	87-97
11527411-1	2001	Alcohol dehydrogenase (ADH) is the primary enzyme responsible for metabolism of ethanol to acetaldehyde.	Acetaldehyde	91-103	alcohol dehydrogenase 5	Danio rerio	23-26
11668012-8	2001	Because PDH levels are low throughout development and that the competition between pyruvate and acetaldehyde may be enhanced due to ethanol-induced lowering of ambient pyruvate concentrations, we conclude that impairment of PDH may have a significant effect on the developing fetus.	Acetaldehyde	96-108	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	224-227
11668012-4	2001	The activity of PDH was measured in the presence of acetaldehyde (10 microM-1 mM) by measuring the formation of the reduced form of nicotinamide-adenine dinucleotide at 340 nm.	Acetaldehyde	52-64	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	16-19
11668012-5	2001	Pyruvate dehydrogenase was separated by using the sodium dodecyl sulfate-polyacrylamide gel electrophoresis technique after incubation with [1,2-(14)C]-acetaldehyde to detect the formation of covalent adducts autoradiographically.	Acetaldehyde	152-164	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	0-22
11668012-7	2001	The results of this study show that acetaldehyde impairs PDH activity by a mixed inhibition type mechanism (Kic=62.4+/-25.7 microM, Kiu=225+/-68 microM), which is not a result of the formation of covalent adducts with PDH, nor of a stimulation of phosphorylation or inactivation of the complex.	Acetaldehyde	36-48	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	57-60
11668012-7	2001	The results of this study show that acetaldehyde impairs PDH activity by a mixed inhibition type mechanism (Kic=62.4+/-25.7 microM, Kiu=225+/-68 microM), which is not a result of the formation of covalent adducts with PDH, nor of a stimulation of phosphorylation or inactivation of the complex.	Acetaldehyde	36-48	pyruvate dehydrogenase phosphatase catalytic subunit 1	Homo sapiens	218-221
11352822-4	2001	Immunofluorescence localization of occludin and ZO-1 showed disruption of the tight junctions in acetaldehyde-treated cell monolayer.	Acetaldehyde	97-109	occludin	Homo sapiens	35-43
11560777-2	2001	Acetaldehyde also activates the promoter, and this effect is mediated by an increase in stellate-cell C/EBPbeta protein and C/EBPbeta binding.	Acetaldehyde	0-12	CCAAT/enhancer binding protein (C/EBP), beta	Mus musculus	102-111
11560777-2	2001	Acetaldehyde also activates the promoter, and this effect is mediated by an increase in stellate-cell C/EBPbeta protein and C/EBPbeta binding.	Acetaldehyde	0-12	CCAAT/enhancer binding protein (C/EBP), beta	Mus musculus	124-133
11439094-10	2001	Acetaldehyde treatment of H4IIE cells led to a time- and dose-dependent increase in GCLC mRNA levels, binding of NF-kappaB and AP-1 to the GCLC promoter, and luciferase activity driven by the GCLC promoter fragment containing these binding sites.	Acetaldehyde	0-12	glutamate-cysteine ligase, catalytic subunit	Rattus norvegicus	84-88
11439094-10	2001	Acetaldehyde treatment of H4IIE cells led to a time- and dose-dependent increase in GCLC mRNA levels, binding of NF-kappaB and AP-1 to the GCLC promoter, and luciferase activity driven by the GCLC promoter fragment containing these binding sites.	Acetaldehyde	0-12	Jun proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	127-131
11439094-10	2001	Acetaldehyde treatment of H4IIE cells led to a time- and dose-dependent increase in GCLC mRNA levels, binding of NF-kappaB and AP-1 to the GCLC promoter, and luciferase activity driven by the GCLC promoter fragment containing these binding sites.	Acetaldehyde	0-12	glutamate-cysteine ligase, catalytic subunit	Rattus norvegicus	139-143
11439094-10	2001	Acetaldehyde treatment of H4IIE cells led to a time- and dose-dependent increase in GCLC mRNA levels, binding of NF-kappaB and AP-1 to the GCLC promoter, and luciferase activity driven by the GCLC promoter fragment containing these binding sites.	Acetaldehyde	0-12	glutamate-cysteine ligase, catalytic subunit	Rattus norvegicus	139-143
11410717-0	2001	4-Methylpyrazole decreases salivary acetaldehyde levels in aldh2-deficient subjects but not in subjects with normal aldh2.	Acetaldehyde	36-48	aldehyde dehydrogenase 2 family member	Homo sapiens	59-64
11410717-2	2001	Acetaldehyde is further oxidized into less harmful acetate mainly by the aldehyde dehydrogenase-2 (ALDH2) enzyme.	Acetaldehyde	0-12	aldehyde dehydrogenase 2 family member	Homo sapiens	73-97
11410717-2	2001	Acetaldehyde is further oxidized into less harmful acetate mainly by the aldehyde dehydrogenase-2 (ALDH2) enzyme.	Acetaldehyde	0-12	aldehyde dehydrogenase 2 family member	Homo sapiens	99-104
11560777-5	2001	Acetaldehyde increases C/EBPbeta binding to all three sites.	Acetaldehyde	0-12	CCAAT/enhancer binding protein (C/EBP), beta	Mus musculus	23-32
11560777-7	2001	Binding of the 20-kDa C/EBPbeta isoform (p20C/EBPbeta), which is eliminated by mutation at the distal site 3 of C/EBP binding, is necessary for the activation by acetaldehyde of the alpha(1)(I) collagen promoter.	Acetaldehyde	162-174	CCAAT/enhancer binding protein (C/EBP), beta	Mus musculus	22-31
11560777-7	2001	Binding of the 20-kDa C/EBPbeta isoform (p20C/EBPbeta), which is eliminated by mutation at the distal site 3 of C/EBP binding, is necessary for the activation by acetaldehyde of the alpha(1)(I) collagen promoter.	Acetaldehyde	162-174	CCAAT/enhancer binding protein (C/EBP), alpha	Mus musculus	22-27
11352822-4	2001	Immunofluorescence localization of occludin and ZO-1 showed disruption of the tight junctions in acetaldehyde-treated cell monolayer.	Acetaldehyde	97-109	tight junction protein 1	Homo sapiens	48-52
11352822-6	2001	Acetaldehyde increased tyrosine phosphorylation of three clusters of proteins with molecular masses of 30-50, 60-90, and 110-150 kDa; three of these proteins were ZO-1, E-cadherin, and beta-catenin.	Acetaldehyde	0-12	tight junction protein 1	Homo sapiens	163-167
11352822-6	2001	Acetaldehyde increased tyrosine phosphorylation of three clusters of proteins with molecular masses of 30-50, 60-90, and 110-150 kDa; three of these proteins were ZO-1, E-cadherin, and beta-catenin.	Acetaldehyde	0-12	cadherin 1	Homo sapiens	169-179
11352822-6	2001	Acetaldehyde increased tyrosine phosphorylation of three clusters of proteins with molecular masses of 30-50, 60-90, and 110-150 kDa; three of these proteins were ZO-1, E-cadherin, and beta-catenin.	Acetaldehyde	0-12	catenin beta 1	Homo sapiens	185-197
11352822-8	2001	Treatment with acetaldehyde resulted in a 97% loss of protein tyrosine phosphatase (PTP)1B activity and a partial reduction of PTP1C and PTP1D activities.	Acetaldehyde	15-27	protein tyrosine phosphatase non-receptor type 1	Homo sapiens	54-90
11352822-8	2001	Treatment with acetaldehyde resulted in a 97% loss of protein tyrosine phosphatase (PTP)1B activity and a partial reduction of PTP1C and PTP1D activities.	Acetaldehyde	15-27	protein tyrosine phosphatase non-receptor type 6	Homo sapiens	127-132
11352822-8	2001	Treatment with acetaldehyde resulted in a 97% loss of protein tyrosine phosphatase (PTP)1B activity and a partial reduction of PTP1C and PTP1D activities.	Acetaldehyde	15-27	protein tyrosine phosphatase non-receptor type 11	Homo sapiens	137-142
11375898-1	2001	Aldehyde dehydrogenase-2 (ALDH2) degrades acetaldehyde metabolized from ethanol.	Acetaldehyde	42-54	aldehyde dehydrogenase 2 family member	Homo sapiens	0-24
11375898-1	2001	Aldehyde dehydrogenase-2 (ALDH2) degrades acetaldehyde metabolized from ethanol.	Acetaldehyde	42-54	aldehyde dehydrogenase 2 family member	Homo sapiens	26-31
11295527-2	2001	The purpose of this study was to examine potential molecular signals that lead to increased alpha(2)(I) collagen gene expression by acetaldehyde, the primary metabolite of alcohol and malondialdehyde (MDA), a lipid peroxidation product known to be associated with chronic liver injury.	Acetaldehyde	132-144	collagen type I alpha 2 chain	Homo sapiens	92-112
11453231-9	2001	CONCLUSIONS: Our experimental findings suggest that volatile fractions of cigarette smoke such as acrolein and acetaldehyde, because their ability to bind and interact with the cytoskeleton, prevent HGF adhesion.	Acetaldehyde	111-123	hepatocyte growth factor	Homo sapiens	199-202
11343241-0	2001	Intracellular signaling pathways involved in acetaldehyde-induced collagen and fibronectin gene expression in human hepatic stellate cells.	Acetaldehyde	45-57	fibronectin 1	Homo sapiens	79-90
11343241-3	2001	In this communication we investigated signal transduction pathways triggered by acetaldehyde leading to upregulation of alpha2(I) collagen and fibronectin gene expression in human HSC.	Acetaldehyde	80-92	collagen type I alpha 2 chain	Homo sapiens	120-138
11343241-3	2001	In this communication we investigated signal transduction pathways triggered by acetaldehyde leading to upregulation of alpha2(I) collagen and fibronectin gene expression in human HSC.	Acetaldehyde	80-92	fibronectin 1	Homo sapiens	143-154
11343241-7	2001	As expected, acetaldehyde-elicited ERK1/2 phosphorylation was inhibited by PD98059, a MEK inhibitor, but not by wortmannin, a PI3K inhibitor.	Acetaldehyde	13-25	mitogen-activated protein kinase 3	Homo sapiens	35-41
11343241-7	2001	As expected, acetaldehyde-elicited ERK1/2 phosphorylation was inhibited by PD98059, a MEK inhibitor, but not by wortmannin, a PI3K inhibitor.	Acetaldehyde	13-25	mitogen-activated protein kinase kinase 7	Homo sapiens	86-89
11343241-8	2001	On the other hand, both of these inhibitors partially inhibited phosphorylation of pp70(S6K) induced by acetaldehyde suggesting that its activation is ERK1/2- and PI3K-dependent.	Acetaldehyde	104-116	mitogen-activated protein kinase 3	Homo sapiens	151-157
11343241-9	2001	Acetaldehyde-elicited fibronectin and alpha2(I) collagen upregulation was inhibited by calphostin C. However, while PD98059, wortmannin and rapamycin (a pp70(S6K) inhibitor) completely abrogated alpha2(I) collagen upregulation, they had no effect on fibronectin expression.	Acetaldehyde	0-12	fibronectin 1	Homo sapiens	22-33
11343241-9	2001	Acetaldehyde-elicited fibronectin and alpha2(I) collagen upregulation was inhibited by calphostin C. However, while PD98059, wortmannin and rapamycin (a pp70(S6K) inhibitor) completely abrogated alpha2(I) collagen upregulation, they had no effect on fibronectin expression.	Acetaldehyde	0-12	collagen type I alpha 2 chain	Homo sapiens	38-56
11343241-9	2001	Acetaldehyde-elicited fibronectin and alpha2(I) collagen upregulation was inhibited by calphostin C. However, while PD98059, wortmannin and rapamycin (a pp70(S6K) inhibitor) completely abrogated alpha2(I) collagen upregulation, they had no effect on fibronectin expression.	Acetaldehyde	0-12	collagen type I alpha 2 chain	Homo sapiens	195-213
11343241-9	2001	Acetaldehyde-elicited fibronectin and alpha2(I) collagen upregulation was inhibited by calphostin C. However, while PD98059, wortmannin and rapamycin (a pp70(S6K) inhibitor) completely abrogated alpha2(I) collagen upregulation, they had no effect on fibronectin expression.	Acetaldehyde	0-12	fibronectin 1	Homo sapiens	250-261
11343241-10	2001	Overall, these data suggest that protein kinase C is an upstream component from which acetaldehyde signals are transduced to other pathways such as PI3K and ERK1/2.	Acetaldehyde	86-98	mitogen-activated protein kinase 3	Homo sapiens	157-163
11343241-11	2001	In addition, differential activation of these pathways is needed for the increase in fibronectin and alpha2(I) collagen gene expression induced by acetaldehyde in human HSC.	Acetaldehyde	147-159	fibronectin 1	Homo sapiens	85-96
11343241-11	2001	In addition, differential activation of these pathways is needed for the increase in fibronectin and alpha2(I) collagen gene expression induced by acetaldehyde in human HSC.	Acetaldehyde	147-159	collagen type I alpha 2 chain	Homo sapiens	101-119
11295527-3	2001	MDA and the combination of MDA and acetaldehyde were employed to determine the effect on alpha(2)(I) collagen gene expression as assessed by transient transfection analysis and reverse transcriptase polymerase chain reaction (RT-PCR).	Acetaldehyde	35-47	collagen type I alpha 2 chain	Homo sapiens	89-109
11295527-7	2001	Acetaldehyde, MDA, or both significantly increased JNK activity when compared to untreated stellate cells.	Acetaldehyde	0-12	mitogen-activated protein kinase 8	Homo sapiens	51-54
11398342-4	2001	The cytochrome P450 2E1 (CYP2E1) gene, which is mapped to chromosome 10q24.3-qter contributes also the conversion of ethanol to acetaldehyde.	Acetaldehyde	128-140	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	4-23
11398342-4	2001	The cytochrome P450 2E1 (CYP2E1) gene, which is mapped to chromosome 10q24.3-qter contributes also the conversion of ethanol to acetaldehyde.	Acetaldehyde	128-140	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	25-31
11398342-10	2001	Mitochondrial ALDH2 is a major enzyme in the oxidation of acetaldehyde derived from ethanol metabolism.	Acetaldehyde	58-70	aldehyde dehydrogenase 2 family member	Homo sapiens	14-19
11398342-11	2001	The catalytic deficiency of ALDH2 isozyme is responsible for flushing and other vasomotor symptoms caused by higher acetaldehyde levels after alcohol intake.	Acetaldehyde	116-128	aldehyde dehydrogenase 2 family member	Homo sapiens	28-33
11246119-5	2001	Incubation of cytosolic fraction with xanthine oxidoreductase (XDh+XO) (XOR) cosubstrates (e.g. NAD+, hypoxanthine, xanthine, caffeine, theobromine, theophylline or 1,7-dimethylxanthine) significantly enhanced the biotransformation of ethanol to acetaldehyde.	Acetaldehyde	246-258	xanthine dehydrogenase	Rattus norvegicus	38-61
11246119-5	2001	Incubation of cytosolic fraction with xanthine oxidoreductase (XDh+XO) (XOR) cosubstrates (e.g. NAD+, hypoxanthine, xanthine, caffeine, theobromine, theophylline or 1,7-dimethylxanthine) significantly enhanced the biotransformation of ethanol to acetaldehyde.	Acetaldehyde	246-258	xanthine dehydrogenase	Rattus norvegicus	63-66
11246119-0	2001	Cytosolic xanthine oxidoreductase mediated bioactivation of ethanol to acetaldehyde and free radicals in rat breast tissue.	Acetaldehyde	71-83	xanthine dehydrogenase	Rattus norvegicus	10-33
11246119-5	2001	Incubation of cytosolic fraction with xanthine oxidoreductase (XDh+XO) (XOR) cosubstrates (e.g. NAD+, hypoxanthine, xanthine, caffeine, theobromine, theophylline or 1,7-dimethylxanthine) significantly enhanced the biotransformation of ethanol to acetaldehyde.	Acetaldehyde	246-258	xanthine dehydrogenase	Rattus norvegicus	72-75
11246119-4	2001	In this work, we explore the possibility that alcohol were activated to acetaldehyde and free radicals in situ by xanthine dehydrogenase (XDh) and xanthine oxidase (XO) and/or aldehyde oxidase (AO).	Acetaldehyde	72-84	xanthine dehydrogenase	Rattus norvegicus	114-136
11325063-0	2001	Microtubules and vimentin associated filaments (VIFs) in cultured human gingival fibroblasts (HGFs) after exposure to acrolein and acetaldehyde.	Acetaldehyde	131-143	vimentin	Homo sapiens	17-25
11246119-4	2001	In this work, we explore the possibility that alcohol were activated to acetaldehyde and free radicals in situ by xanthine dehydrogenase (XDh) and xanthine oxidase (XO) and/or aldehyde oxidase (AO).	Acetaldehyde	72-84	xanthine dehydrogenase	Rattus norvegicus	138-141
11290854-8	2001	ADH activity of the strains that produced more than 100 nmol of acetaldehyde/10(9) colony-forming units/hr (n = 23) varied from 3.9 to 1253 nmol of nicotinamide adenine dinucleotide per minute per milligram of protein, and Km values for ethanol ranged from 0.65 to 116 mM and from 0.5 to 3.1 M (high Km).	Acetaldehyde	64-76	aldo-keto reductase family 1 member A1	Homo sapiens	0-3
11290854-9	2001	There was a statistically significant correlation (r = 0.64, p &lt; 0.001) between ADH activity and acetaldehyde production from ethanol in the tested strains.	Acetaldehyde	100-112	aldo-keto reductase family 1 member A1	Homo sapiens	83-86
11181050-4	2001	Acetaldehyde did not exert any significant effects on any of the parameters studied, although the mean expression of TNF-alpha tended to be lower in the acetaldehyde-treated hearts than in control hearts.	Acetaldehyde	153-165	tumor necrosis factor	Rattus norvegicus	117-126
11344824-9	2001	Acetaldehyde markedly increased TNF-alpha and IL-8 expression, stimulated IL-1 beta and IL-8 secretion, increased lipid peroxidation damage and decreased catalase activity, while LPS exposure induced the expression of TNF-alpha, TGF-beta 1, IL-6 and IL-8, the secretion of TGF-beta 1, IL-1 beta, IL-6 and IL-8, and a decrease in catalase activity.	Acetaldehyde	0-12	tumor necrosis factor	Homo sapiens	32-41
11166817-5	2001	In addition, a preparation exhibiting dye-linked aldehyde dehydrogenase activity for acetaldehyde, most probably originating from molybdohemoprotein aldehyde dehydrogenase (ALDH), which has been described for other Acetic acid bacteria, oxidised glycidaldehyde as well with a preference for the (R)-enantiomer, the selectivity quantified by an enantiomeric ratio (E) value of 7.	Acetaldehyde	85-97	D719_p1008	Acetobacter pasteurianus	49-71
11166817-5	2001	In addition, a preparation exhibiting dye-linked aldehyde dehydrogenase activity for acetaldehyde, most probably originating from molybdohemoprotein aldehyde dehydrogenase (ALDH), which has been described for other Acetic acid bacteria, oxidised glycidaldehyde as well with a preference for the (R)-enantiomer, the selectivity quantified by an enantiomeric ratio (E) value of 7.	Acetaldehyde	85-97	D719_p1008	Acetobacter pasteurianus	149-171
11166817-5	2001	In addition, a preparation exhibiting dye-linked aldehyde dehydrogenase activity for acetaldehyde, most probably originating from molybdohemoprotein aldehyde dehydrogenase (ALDH), which has been described for other Acetic acid bacteria, oxidised glycidaldehyde as well with a preference for the (R)-enantiomer, the selectivity quantified by an enantiomeric ratio (E) value of 7.	Acetaldehyde	85-97	D719_p1008	Acetobacter pasteurianus	173-177
11344824-9	2001	Acetaldehyde markedly increased TNF-alpha and IL-8 expression, stimulated IL-1 beta and IL-8 secretion, increased lipid peroxidation damage and decreased catalase activity, while LPS exposure induced the expression of TNF-alpha, TGF-beta 1, IL-6 and IL-8, the secretion of TGF-beta 1, IL-1 beta, IL-6 and IL-8, and a decrease in catalase activity.	Acetaldehyde	0-12	C-X-C motif chemokine ligand 8	Homo sapiens	46-50
11344824-9	2001	Acetaldehyde markedly increased TNF-alpha and IL-8 expression, stimulated IL-1 beta and IL-8 secretion, increased lipid peroxidation damage and decreased catalase activity, while LPS exposure induced the expression of TNF-alpha, TGF-beta 1, IL-6 and IL-8, the secretion of TGF-beta 1, IL-1 beta, IL-6 and IL-8, and a decrease in catalase activity.	Acetaldehyde	0-12	interleukin 1 beta	Homo sapiens	74-83
11344824-9	2001	Acetaldehyde markedly increased TNF-alpha and IL-8 expression, stimulated IL-1 beta and IL-8 secretion, increased lipid peroxidation damage and decreased catalase activity, while LPS exposure induced the expression of TNF-alpha, TGF-beta 1, IL-6 and IL-8, the secretion of TGF-beta 1, IL-1 beta, IL-6 and IL-8, and a decrease in catalase activity.	Acetaldehyde	0-12	C-X-C motif chemokine ligand 8	Homo sapiens	88-92
11344824-9	2001	Acetaldehyde markedly increased TNF-alpha and IL-8 expression, stimulated IL-1 beta and IL-8 secretion, increased lipid peroxidation damage and decreased catalase activity, while LPS exposure induced the expression of TNF-alpha, TGF-beta 1, IL-6 and IL-8, the secretion of TGF-beta 1, IL-1 beta, IL-6 and IL-8, and a decrease in catalase activity.	Acetaldehyde	0-12	catalase	Homo sapiens	154-162
11344824-9	2001	Acetaldehyde markedly increased TNF-alpha and IL-8 expression, stimulated IL-1 beta and IL-8 secretion, increased lipid peroxidation damage and decreased catalase activity, while LPS exposure induced the expression of TNF-alpha, TGF-beta 1, IL-6 and IL-8, the secretion of TGF-beta 1, IL-1 beta, IL-6 and IL-8, and a decrease in catalase activity.	Acetaldehyde	0-12	tumor necrosis factor	Homo sapiens	218-227
11344824-9	2001	Acetaldehyde markedly increased TNF-alpha and IL-8 expression, stimulated IL-1 beta and IL-8 secretion, increased lipid peroxidation damage and decreased catalase activity, while LPS exposure induced the expression of TNF-alpha, TGF-beta 1, IL-6 and IL-8, the secretion of TGF-beta 1, IL-1 beta, IL-6 and IL-8, and a decrease in catalase activity.	Acetaldehyde	0-12	transforming growth factor beta 1	Homo sapiens	229-239
11344824-9	2001	Acetaldehyde markedly increased TNF-alpha and IL-8 expression, stimulated IL-1 beta and IL-8 secretion, increased lipid peroxidation damage and decreased catalase activity, while LPS exposure induced the expression of TNF-alpha, TGF-beta 1, IL-6 and IL-8, the secretion of TGF-beta 1, IL-1 beta, IL-6 and IL-8, and a decrease in catalase activity.	Acetaldehyde	0-12	interleukin 6	Homo sapiens	241-245
11344824-9	2001	Acetaldehyde markedly increased TNF-alpha and IL-8 expression, stimulated IL-1 beta and IL-8 secretion, increased lipid peroxidation damage and decreased catalase activity, while LPS exposure induced the expression of TNF-alpha, TGF-beta 1, IL-6 and IL-8, the secretion of TGF-beta 1, IL-1 beta, IL-6 and IL-8, and a decrease in catalase activity.	Acetaldehyde	0-12	C-X-C motif chemokine ligand 8	Homo sapiens	88-92
11344824-9	2001	Acetaldehyde markedly increased TNF-alpha and IL-8 expression, stimulated IL-1 beta and IL-8 secretion, increased lipid peroxidation damage and decreased catalase activity, while LPS exposure induced the expression of TNF-alpha, TGF-beta 1, IL-6 and IL-8, the secretion of TGF-beta 1, IL-1 beta, IL-6 and IL-8, and a decrease in catalase activity.	Acetaldehyde	0-12	transforming growth factor beta 1	Homo sapiens	273-283
11344824-9	2001	Acetaldehyde markedly increased TNF-alpha and IL-8 expression, stimulated IL-1 beta and IL-8 secretion, increased lipid peroxidation damage and decreased catalase activity, while LPS exposure induced the expression of TNF-alpha, TGF-beta 1, IL-6 and IL-8, the secretion of TGF-beta 1, IL-1 beta, IL-6 and IL-8, and a decrease in catalase activity.	Acetaldehyde	0-12	interleukin 1 beta	Homo sapiens	285-294
11344824-9	2001	Acetaldehyde markedly increased TNF-alpha and IL-8 expression, stimulated IL-1 beta and IL-8 secretion, increased lipid peroxidation damage and decreased catalase activity, while LPS exposure induced the expression of TNF-alpha, TGF-beta 1, IL-6 and IL-8, the secretion of TGF-beta 1, IL-1 beta, IL-6 and IL-8, and a decrease in catalase activity.	Acetaldehyde	0-12	interleukin 6	Homo sapiens	296-300
11344824-9	2001	Acetaldehyde markedly increased TNF-alpha and IL-8 expression, stimulated IL-1 beta and IL-8 secretion, increased lipid peroxidation damage and decreased catalase activity, while LPS exposure induced the expression of TNF-alpha, TGF-beta 1, IL-6 and IL-8, the secretion of TGF-beta 1, IL-1 beta, IL-6 and IL-8, and a decrease in catalase activity.	Acetaldehyde	0-12	C-X-C motif chemokine ligand 8	Homo sapiens	88-92
11344824-9	2001	Acetaldehyde markedly increased TNF-alpha and IL-8 expression, stimulated IL-1 beta and IL-8 secretion, increased lipid peroxidation damage and decreased catalase activity, while LPS exposure induced the expression of TNF-alpha, TGF-beta 1, IL-6 and IL-8, the secretion of TGF-beta 1, IL-1 beta, IL-6 and IL-8, and a decrease in catalase activity.	Acetaldehyde	0-12	catalase	Homo sapiens	329-337
11022051-7	2001	PPAR alpha/retinoid X receptor extracted from hepatoma cells exposed to ethanol or acetaldehyde bound poorly to an oligonucleotide containing peroxisome proliferator response elements.	Acetaldehyde	83-95	peroxisome proliferator activated receptor alpha	Rattus norvegicus	0-10
11306066-1	2001	Mouse ADH4 (purified, recombinant) has a low catalytic efficiency for ethanol and acetaldehyde, but very high activity with longer chain alcohols and aldehydes, at pH 7.3 and temperature 37 degrees C. The observed turnover numbers and catalytic efficiencies for the oxidation of all-trans-retinol and the reduction of all-trans-retinal and 9-cis-retinal are low relative to other substrates; 9-cis-retinal is more reactive than all-trans-retinal.	Acetaldehyde	82-94	alcohol dehydrogenase 4 (class II), pi polypeptide	Mus musculus	6-10
11022051-9	2001	Furthermore, in vitro translated PPAR alpha exposed to acetaldehyde failed to bind DNA.	Acetaldehyde	55-67	peroxisome proliferator activated receptor alpha	Rattus norvegicus	33-43
11131450-6	2000	The sites of CYP2E1 and CYP2A6 immunoreactivity co-localized with fatty deposits, and with the sites of acetaldehyde and lipid peroxidation-derived protein adducts.	Acetaldehyde	104-116	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	13-19
11860963-4	2001	RESULTS: Changes in c-fos gene expression induced by alcohol and acetaldehyde was time and dose dependent.	Acetaldehyde	65-77	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	20-25
11860963-5	2001	After 1 hr exposure, alcohol and acetaldehyde affected c-fos gene expression in two kinds of neuralglia.	Acetaldehyde	33-45	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	55-60
11860963-7	2001	CONCLUSIONS: Alcohol and acetaldehyde cause abnormal increase of c-fos gene expression in astrocytes and oligodendrocytes.	Acetaldehyde	25-37	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	65-70
11147839-0	2000	Cytochrome P450 2E1 (CYP2E1)-dependent production of a 37-kDa acetaldehyde-protein adduct in the rat liver.	Acetaldehyde	62-74	cytochrome P450, family 2, subfamily e, polypeptide 1	Rattus norvegicus	0-19
11147839-0	2000	Cytochrome P450 2E1 (CYP2E1)-dependent production of a 37-kDa acetaldehyde-protein adduct in the rat liver.	Acetaldehyde	62-74	cytochrome P450, family 2, subfamily e, polypeptide 1	Rattus norvegicus	21-27
11147839-1	2000	Ethanol-inducible cytochrome P450 2E1 (CYP2E1) has been shown to be involved in the metabolism of both ethanol and acetaldehyde.	Acetaldehyde	115-127	cytochrome P450, family 2, subfamily e, polypeptide 1	Rattus norvegicus	18-37
11147839-1	2000	Ethanol-inducible cytochrome P450 2E1 (CYP2E1) has been shown to be involved in the metabolism of both ethanol and acetaldehyde.	Acetaldehyde	115-127	cytochrome P450, family 2, subfamily e, polypeptide 1	Rattus norvegicus	39-45
11147839-3	2000	In this study, we investigated the role of CYP2E1 in the production of a 37-kDa acetaldehyde-protein adduct.	Acetaldehyde	80-92	cytochrome P450, family 2, subfamily e, polypeptide 1	Rattus norvegicus	43-49
11268819-7	2001	Chronic ethanol consumption increases CYP2E1, resulting in increased generation of toxic acetaldehyde and free radicals, tolerance to ethanol and other drugs, and multiple ethanol-drug interactions.	Acetaldehyde	89-101	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	38-44
11131450-6	2000	The sites of CYP2E1 and CYP2A6 immunoreactivity co-localized with fatty deposits, and with the sites of acetaldehyde and lipid peroxidation-derived protein adducts.	Acetaldehyde	104-116	cytochrome P450 family 2 subfamily A member 6	Homo sapiens	24-30
10942105-1	2000	A highly prevalent, atypical genotype in low Km aldehyde dehydrogenase (ALDH2) may influence alcohol-induced liver injury because of higher production of acetaldehyde in the liver.	Acetaldehyde	154-166	aldehyde dehydrogenase 2 family member	Homo sapiens	72-77
11093962-1	2000	Many human gastrointestinal facultative anaerobic and aerobic bacteria possess alcohol dehydrogenase (ADH) activity and are therefore capable of oxidizing ethanol to acetaldehyde.	Acetaldehyde	166-178	aldo-keto reductase family 1 member A1	Homo sapiens	79-100
11093962-1	2000	Many human gastrointestinal facultative anaerobic and aerobic bacteria possess alcohol dehydrogenase (ADH) activity and are therefore capable of oxidizing ethanol to acetaldehyde.	Acetaldehyde	166-178	aldo-keto reductase family 1 member A1	Homo sapiens	102-105
11027709-4	2000	Analysis of sub-cellular localization of ALDH2a protein using green fluorescent protein and an in vitro ALDH assay using protein extracts from Escherichia coli cells that overexpressed ALDH2a indicated that ALDH2a functions in the oxidation of acetaldehyde in mitochondria.	Acetaldehyde	244-256	aldehyde dehydrogenase family 2 member B7, mitochondrial-like	Nicotiana tabacum	185-191
11027709-4	2000	Analysis of sub-cellular localization of ALDH2a protein using green fluorescent protein and an in vitro ALDH assay using protein extracts from Escherichia coli cells that overexpressed ALDH2a indicated that ALDH2a functions in the oxidation of acetaldehyde in mitochondria.	Acetaldehyde	244-256	aldehyde dehydrogenase family 2 member B7, mitochondrial-like	Nicotiana tabacum	185-191
10998257-8	2000	ALDH1 was more efficient at oxidizing acetaldehyde, propionaldehyde, and benzaldehyde and was more sensitive to disulfiram inhibition.	Acetaldehyde	38-50	aldehyde dehydrogenase 1 family, member A1	Rattus norvegicus	0-5
11035637-5	2000	The results show that acrolein and acetaldehyde produced dose dependent inhibition of HGF viability and alteration of cytoplasmic organelles.	Acetaldehyde	35-47	hepatocyte growth factor	Homo sapiens	86-89
11035637-6	2000	The main ultrastructural finding for the HGF cytoplasm was the presence of vacuoles and lysosomal structures which became prominent with increasing concentration of acrolein and acetaldehyde.	Acetaldehyde	178-190	hepatocyte growth factor	Homo sapiens	41-44
10940011-8	2000	However, when both ADH3 and NDI1 were deleted, metabolism became respirofermentative, indicating that the ethanol-acetaldehyde shuttle is essential for respiratory growth of the ndi1 delta mutant.	Acetaldehyde	114-126	alcohol dehydrogenase ADH3	Saccharomyces cerevisiae S288C	19-23
10940011-8	2000	However, when both ADH3 and NDI1 were deleted, metabolism became respirofermentative, indicating that the ethanol-acetaldehyde shuttle is essential for respiratory growth of the ndi1 delta mutant.	Acetaldehyde	114-126	NADH-ubiquinone reductase (H(+)-translocating) NDI1	Saccharomyces cerevisiae S288C	28-32
10971205-4	2000	Polymorphism in ALDH2 is associated with altered acetaldehyde metabolism, decreased risk of alcoholism and increased risk of ethanol-induced cancers.	Acetaldehyde	49-61	aldehyde dehydrogenase 2 family member	Homo sapiens	16-21
10940605-10	2000	Those who possess the ALDH2*2 gene show high concentrations of acetaldehyde (AcH) at even comparatively lower alcohol levels.	Acetaldehyde	63-75	aldehyde dehydrogenase 2 family member	Homo sapiens	22-27
10940605-10	2000	Those who possess the ALDH2*2 gene show high concentrations of acetaldehyde (AcH) at even comparatively lower alcohol levels.	Acetaldehyde	77-80	aldehyde dehydrogenase 2 family member	Homo sapiens	22-27
10896918-11	2000	Accumulation of acetaldehyde due to low ALDH2 activity may play a critical role in cancerous changes throughout the mucosa in the upper aerodigestive tract.	Acetaldehyde	16-28	aldehyde dehydrogenase 2 family member	Homo sapiens	40-45
10905996-0	2000	Role of acetaldehyde in the induction of heart left ventricular atrial natriuretic peptide gene expression in rats.	Acetaldehyde	8-20	natriuretic peptide A	Rattus norvegicus	64-90
10905996-1	2000	We studied the effects of ethanol and acetaldehyde on myocardial gene expression of atrial natriuretic peptide (ANP) and growth of rats.	Acetaldehyde	38-50	natriuretic peptide A	Rattus norvegicus	84-110
10905996-1	2000	We studied the effects of ethanol and acetaldehyde on myocardial gene expression of atrial natriuretic peptide (ANP) and growth of rats.	Acetaldehyde	38-50	natriuretic peptide A	Rattus norvegicus	112-115
10963934-8	2000	All these effects underline the crucial role played by catalase which, on one hand converts hydrogen peroxide to water and, on the other hand, ethanol to acetaldehyde.	Acetaldehyde	154-166	catalase	Homo sapiens	55-63
10871045-7	2000	Acetaldehyde (200 microM) increased C/EBPbeta protein in stellate nuclear extracts, increased its binding to the promoter, and activated the alpha1(I) collagen promoter in transfected stellate cells.	Acetaldehyde	0-12	CCAAT/enhancer binding protein (C/EBP), beta	Mus musculus	36-45
10871045-10	2000	This study shows that C/EBPbeta is the predominant C/EBP isoform found in activated stellate cells and that increased C/EBPbeta protein and C/EBPbeta binding to a proximal C/EBP binding site in the promoter mediates the activating effect of acetaldehyde.	Acetaldehyde	241-253	CCAAT/enhancer binding protein (C/EBP), beta	Mus musculus	22-31
10871045-10	2000	This study shows that C/EBPbeta is the predominant C/EBP isoform found in activated stellate cells and that increased C/EBPbeta protein and C/EBPbeta binding to a proximal C/EBP binding site in the promoter mediates the activating effect of acetaldehyde.	Acetaldehyde	241-253	CCAAT/enhancer binding protein (C/EBP), alpha	Mus musculus	22-27
10871045-10	2000	This study shows that C/EBPbeta is the predominant C/EBP isoform found in activated stellate cells and that increased C/EBPbeta protein and C/EBPbeta binding to a proximal C/EBP binding site in the promoter mediates the activating effect of acetaldehyde.	Acetaldehyde	241-253	CCAAT/enhancer binding protein (C/EBP), beta	Mus musculus	118-127
10871045-10	2000	This study shows that C/EBPbeta is the predominant C/EBP isoform found in activated stellate cells and that increased C/EBPbeta protein and C/EBPbeta binding to a proximal C/EBP binding site in the promoter mediates the activating effect of acetaldehyde.	Acetaldehyde	241-253	CCAAT/enhancer binding protein (C/EBP), beta	Mus musculus	118-127
10871045-10	2000	This study shows that C/EBPbeta is the predominant C/EBP isoform found in activated stellate cells and that increased C/EBPbeta protein and C/EBPbeta binding to a proximal C/EBP binding site in the promoter mediates the activating effect of acetaldehyde.	Acetaldehyde	241-253	CCAAT/enhancer binding protein (C/EBP), alpha	Mus musculus	51-56
11118675-0	2000	Cytochrome P450 reductase-mediated anaerobic biotransformation of ethanol to 1-hydroxyethyl-free radicals and acetaldehyde.	Acetaldehyde	110-122	cytochrome p450 oxidoreductase	Rattus norvegicus	0-25
11118675-1	2000	The ability of cytochrome P450 reductase to metabolize ethanol (EtOH) to acetaldehyde (AC) and 1-hydroxyethyl free radicals (1HEt) in anaerobic media was studied.	Acetaldehyde	73-85	cytochrome p450 oxidoreductase	Rattus norvegicus	15-40
11118675-1	2000	The ability of cytochrome P450 reductase to metabolize ethanol (EtOH) to acetaldehyde (AC) and 1-hydroxyethyl free radicals (1HEt) in anaerobic media was studied.	Acetaldehyde	87-89	cytochrome p450 oxidoreductase	Rattus norvegicus	15-40
10925369-2	2000	Ethanol is oxidized to acetaldehyde (the suspected carcinogenic agent in alcohol) by alcohol dehydrogenases (ADHs) and cytochrome P-4502E1 (CYP2E1), both of which exhibit great inter-individual variability in activity.	Acetaldehyde	23-35	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	119-138
10925369-2	2000	Ethanol is oxidized to acetaldehyde (the suspected carcinogenic agent in alcohol) by alcohol dehydrogenases (ADHs) and cytochrome P-4502E1 (CYP2E1), both of which exhibit great inter-individual variability in activity.	Acetaldehyde	23-35	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	140-146
10940011-8	2000	However, when both ADH3 and NDI1 were deleted, metabolism became respirofermentative, indicating that the ethanol-acetaldehyde shuttle is essential for respiratory growth of the ndi1 delta mutant.	Acetaldehyde	114-126	NADH-ubiquinone reductase (H(+)-translocating) NDI1	Saccharomyces cerevisiae S288C	178-182
10871045-0	2000	CCAAT/enhancer binding protein beta mediates the activation of the murine alpha1(I) collagen promoter by acetaldehyde.	Acetaldehyde	105-117	CCAAT/enhancer binding protein (C/EBP), beta	Mus musculus	0-35
10871045-3	2000	This study investigates the role of C/EBPbeta in mediating the activation of the alpha1(I) collagen promoter by acetaldehyde.	Acetaldehyde	112-124	CCAAT/enhancer binding protein (C/EBP), beta	Mus musculus	36-45
10752532-4	2000	Exposure of HPMC to acetaldehyde, formaldehyde, glyoxal, methylglyoxal, furaldehyde, but not to 5-hydroxymethyl-furfural, resulted in dose-dependent inhibition of cell growth, viability, and interleukin-1beta (IL-1beta)-stimulated IL-6 release; for several GDP, this suppression was significantly greater compared with L929 cells.	Acetaldehyde	20-32	interleukin 1 beta	Mus musculus	191-208
10826103-3	2000	The predicting 95% confidence bounds determined on regression analysis of the data suggested that after venous injection of ethanol, the blood ethanol and acetaldehyde concentrations in a volunteer normal homozygous for ALDH2 (ALDH2*1/1) were lower than in a heterozygous one (ALDH2*1/2).	Acetaldehyde	155-167	aldehyde dehydrogenase 2 family member	Homo sapiens	220-225
10826103-3	2000	The predicting 95% confidence bounds determined on regression analysis of the data suggested that after venous injection of ethanol, the blood ethanol and acetaldehyde concentrations in a volunteer normal homozygous for ALDH2 (ALDH2*1/1) were lower than in a heterozygous one (ALDH2*1/2).	Acetaldehyde	155-167	aldehyde dehydrogenase 2 family member	Homo sapiens	227-232
10826103-3	2000	The predicting 95% confidence bounds determined on regression analysis of the data suggested that after venous injection of ethanol, the blood ethanol and acetaldehyde concentrations in a volunteer normal homozygous for ALDH2 (ALDH2*1/1) were lower than in a heterozygous one (ALDH2*1/2).	Acetaldehyde	155-167	aldehyde dehydrogenase 2 family member	Homo sapiens	227-232
10826103-4	2000	Also, the blood ethanol and acetaldehyde concentrations in a volunteer with the c2 and C alleles of CYP2E1 (c1/c2 and C/D) were lower than in one without the c2 and C alleles (c1/c1 and D/D).	Acetaldehyde	28-40	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	100-106
10826103-4	2000	Also, the blood ethanol and acetaldehyde concentrations in a volunteer with the c2 and C alleles of CYP2E1 (c1/c2 and C/D) were lower than in one without the c2 and C alleles (c1/c1 and D/D).	Acetaldehyde	28-40	heterogeneous nuclear ribonucleoprotein C	Homo sapiens	108-113
10826103-4	2000	Also, the blood ethanol and acetaldehyde concentrations in a volunteer with the c2 and C alleles of CYP2E1 (c1/c2 and C/D) were lower than in one without the c2 and C alleles (c1/c1 and D/D).	Acetaldehyde	28-40	heterogeneous nuclear ribonucleoprotein C	Homo sapiens	176-187
10913661-9	2000	NB in the ALDH 2-deficient group was significantly larger from 15 to 45 minutes after consumption than in the proficient group.Conclusions: It appeared that the consumption of ethanol can increase the blood flow in the human ONH in the acute phase through decreased resistance in blood vessels induced by acetaldehyde, a metabolite of ethanol.	Acetaldehyde	305-317	aldehyde dehydrogenase 2 family member	Homo sapiens	10-16
10803771-14	2000	The data on 24 hr urinary C-peptide level suggested that increased acetaldehyde after light-to-moderate drinking by inactive ALDH2 diabetic patients may increase the HbA1c value by the insulin-resistant condition that resulted in hyperinsulinemia.	Acetaldehyde	67-79	aldehyde dehydrogenase 2 family member	Homo sapiens	125-130
10803776-1	2000	BACKGROUND: Although the mutant low-Km acetaldehyde dehydrogenase (ALDH2) allele (ALDH2(2)) with reduced capacity to metabolize acetaldehyde offers biological protection against alcoholism and subsequent alcohol-induced organ damage in many individuals, a significant proportion of individuals with heterozygote of the normal and mutant ALDH2 gene (ALDH2(1)/2(2)) consume excessive amounts of alcohol.	Acetaldehyde	39-51	aldehyde dehydrogenase 2 family member	Homo sapiens	67-72
10803776-1	2000	BACKGROUND: Although the mutant low-Km acetaldehyde dehydrogenase (ALDH2) allele (ALDH2(2)) with reduced capacity to metabolize acetaldehyde offers biological protection against alcoholism and subsequent alcohol-induced organ damage in many individuals, a significant proportion of individuals with heterozygote of the normal and mutant ALDH2 gene (ALDH2(1)/2(2)) consume excessive amounts of alcohol.	Acetaldehyde	39-51	aldehyde dehydrogenase 2 family member	Homo sapiens	82-87
10803776-1	2000	BACKGROUND: Although the mutant low-Km acetaldehyde dehydrogenase (ALDH2) allele (ALDH2(2)) with reduced capacity to metabolize acetaldehyde offers biological protection against alcoholism and subsequent alcohol-induced organ damage in many individuals, a significant proportion of individuals with heterozygote of the normal and mutant ALDH2 gene (ALDH2(1)/2(2)) consume excessive amounts of alcohol.	Acetaldehyde	39-51	aldehyde dehydrogenase 2 family member	Homo sapiens	82-87
10803776-1	2000	BACKGROUND: Although the mutant low-Km acetaldehyde dehydrogenase (ALDH2) allele (ALDH2(2)) with reduced capacity to metabolize acetaldehyde offers biological protection against alcoholism and subsequent alcohol-induced organ damage in many individuals, a significant proportion of individuals with heterozygote of the normal and mutant ALDH2 gene (ALDH2(1)/2(2)) consume excessive amounts of alcohol.	Acetaldehyde	39-51	aldehyde dehydrogenase 2 family member	Homo sapiens	82-87
10734030-14	2000	This effect of ethanol is most likely mediated by its metabolism (via ADH) to acetaldehyde and the generation of oxidant stress within the cells.	Acetaldehyde	78-90	aldo-keto reductase family 1 member A1	Rattus norvegicus	70-73
10799556-0	2000	Enhanced DNA binding and activation of transcription factors NF-kappa B and AP-1 by acetaldehyde in HEPG2 cells.	Acetaldehyde	84-96	nuclear factor kappa B subunit 1	Homo sapiens	61-71
10799556-0	2000	Enhanced DNA binding and activation of transcription factors NF-kappa B and AP-1 by acetaldehyde in HEPG2 cells.	Acetaldehyde	84-96	Jun proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	76-80
10799556-1	2000	Because transcription factors NF-kappaB and activator protein-1 (AP-1) are known to regulate gene expression, we have analyzed the role of acetaldehyde in the activation of NF-kappaB and AP-1 in HepG2 cells.	Acetaldehyde	139-151	nuclear factor kappa B subunit 1	Homo sapiens	173-182
10799556-1	2000	Because transcription factors NF-kappaB and activator protein-1 (AP-1) are known to regulate gene expression, we have analyzed the role of acetaldehyde in the activation of NF-kappaB and AP-1 in HepG2 cells.	Acetaldehyde	139-151	Jun proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	187-191
10799556-3	2000	Acetaldehyde enhanced the DNA binding of NF-kappaB and AP-1 by 1 and 4 h, respectively, increasing the kappaB- and AP-1-dependent luciferase expression.	Acetaldehyde	0-12	nuclear factor kappa B subunit 1	Homo sapiens	41-50
10799556-3	2000	Acetaldehyde enhanced the DNA binding of NF-kappaB and AP-1 by 1 and 4 h, respectively, increasing the kappaB- and AP-1-dependent luciferase expression.	Acetaldehyde	0-12	Jun proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	55-59
10799556-3	2000	Acetaldehyde enhanced the DNA binding of NF-kappaB and AP-1 by 1 and 4 h, respectively, increasing the kappaB- and AP-1-dependent luciferase expression.	Acetaldehyde	0-12	Jun proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	115-119
10799556-5	2000	The enhanced binding of NF-kappaB to DNA by acetaldehyde in intact cells was accompanied by the proteolytic degradation of IkappaB-alpha.	Acetaldehyde	44-56	nuclear factor kappa B subunit 1	Homo sapiens	24-33
10799556-5	2000	The enhanced binding of NF-kappaB to DNA by acetaldehyde in intact cells was accompanied by the proteolytic degradation of IkappaB-alpha.	Acetaldehyde	44-56	NFKB inhibitor alpha	Homo sapiens	123-136
10799556-6	2000	However, the addition of acetaldehyde to cytostolic extracts from untreated Hep G2 cells did not affect the DNA binding of AP-1 but activated the NF-kappaB heterodimer p65/p50 in the absence of IkappaB-alpha degradation.	Acetaldehyde	25-37	nuclear factor kappa B subunit 1	Homo sapiens	146-155
10799556-6	2000	However, the addition of acetaldehyde to cytostolic extracts from untreated Hep G2 cells did not affect the DNA binding of AP-1 but activated the NF-kappaB heterodimer p65/p50 in the absence of IkappaB-alpha degradation.	Acetaldehyde	25-37	RELA proto-oncogene, NF-kB subunit	Homo sapiens	168-171
10799556-6	2000	However, the addition of acetaldehyde to cytostolic extracts from untreated Hep G2 cells did not affect the DNA binding of AP-1 but activated the NF-kappaB heterodimer p65/p50 in the absence of IkappaB-alpha degradation.	Acetaldehyde	25-37	nuclear factor kappa B subunit 1	Homo sapiens	172-175
10799556-7	2000	Preincubation of HepG2 cells with protein kinase C inhibitors abolished the enhanced DNA binding of NF-kappaB and AP-1 caused by acetaldehyde.	Acetaldehyde	129-141	nuclear factor kappa B subunit 1	Homo sapiens	100-109
10799556-7	2000	Preincubation of HepG2 cells with protein kinase C inhibitors abolished the enhanced DNA binding of NF-kappaB and AP-1 caused by acetaldehyde.	Acetaldehyde	129-141	Jun proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	114-118
10799556-8	2000	Hence, these findings uncover a previously unrecognized role for acetaldehyde in the activation of NF-kappaB and AP-1, which may be of relevance in the alcohol-induced liver disease.	Acetaldehyde	65-77	nuclear factor kappa B subunit 1	Homo sapiens	99-108
10799556-8	2000	Hence, these findings uncover a previously unrecognized role for acetaldehyde in the activation of NF-kappaB and AP-1, which may be of relevance in the alcohol-induced liver disease.	Acetaldehyde	65-77	Jun proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	113-117
10729205-5	2000	The activation of the alpha(2)(I) collagen promoter by acetaldehyde was not decreased significantly by retinoic acid, but was suppressed by the retinoic acid receptor (RAR) selective retinoid SRI-6751-84.	Acetaldehyde	55-67	retinoic acid receptor, beta	Mus musculus	168-171
10729205-7	2000	Acetaldehyde also resulted in a decrease in RAR beta message and RARbeta protein.	Acetaldehyde	0-12	retinoic acid receptor, beta	Mus musculus	44-52
10729205-7	2000	Acetaldehyde also resulted in a decrease in RAR beta message and RARbeta protein.	Acetaldehyde	0-12	retinoic acid receptor, beta	Mus musculus	65-72
10729205-8	2000	This study shows that retinoic acid depresses alpha(2)(I) collagen gene expression but that this effect is less pronounced when the expression of this collagen is enhanced by acetaldehyde, which also decreases RARbeta message and protein.	Acetaldehyde	175-187	retinoic acid receptor, beta	Mus musculus	210-217
10752532-4	2000	Exposure of HPMC to acetaldehyde, formaldehyde, glyoxal, methylglyoxal, furaldehyde, but not to 5-hydroxymethyl-furfural, resulted in dose-dependent inhibition of cell growth, viability, and interleukin-1beta (IL-1beta)-stimulated IL-6 release; for several GDP, this suppression was significantly greater compared with L929 cells.	Acetaldehyde	20-32	interleukin 1 beta	Mus musculus	210-218
10733585-0	2000	The DNA binding protein BTEB mediates acetaldehyde-induced, jun N-terminal kinase-dependent alphaI(I) collagen gene expression in rat hepatic stellate cells.	Acetaldehyde	38-50	Kruppel-like factor 9	Rattus norvegicus	24-28
10733585-10	2000	Inhibition of JNK activation resulted in the reduction of the acetaldehyde-induced BTEB protein abundance and alphaI(I) collagen mRNA levels, indicating that the expression of both genes is JNK dependent in HSC.	Acetaldehyde	62-74	Kruppel-like factor 9	Rattus norvegicus	83-87
10733585-7	2000	The GC box was predominantly bound by the DNA binding transcription factor BTEB (basic transcription element binding protein), expression of which was acetaldehyde and UV inducible.	Acetaldehyde	151-163	Kruppel-like factor 9	Rattus norvegicus	75-79
10733585-10	2000	Inhibition of JNK activation resulted in the reduction of the acetaldehyde-induced BTEB protein abundance and alphaI(I) collagen mRNA levels, indicating that the expression of both genes is JNK dependent in HSC.	Acetaldehyde	62-74	mitogen-activated protein kinase 8	Rattus norvegicus	190-193
10733585-11	2000	Taken together, these studies demonstrate that BTEB mediates acetaldehyde-induced, JNK-dependent alphaI(I) collagen gene expression in HSC.	Acetaldehyde	61-73	Kruppel-like factor 9	Rattus norvegicus	47-51
10733585-11	2000	Taken together, these studies demonstrate that BTEB mediates acetaldehyde-induced, JNK-dependent alphaI(I) collagen gene expression in HSC.	Acetaldehyde	61-73	mitogen-activated protein kinase 8	Rattus norvegicus	83-86
10733585-7	2000	The GC box was predominantly bound by the DNA binding transcription factor BTEB (basic transcription element binding protein), expression of which was acetaldehyde and UV inducible.	Acetaldehyde	151-163	Kruppel-like factor 9	Rattus norvegicus	81-124
10733585-8	2000	Blocking BTEB protein expression significantly reduced the steady-state levels of the acetaldehyde-induced alphaI(I) collagen mRNA, suggesting that BTEB is required for this gene expression.	Acetaldehyde	86-98	Kruppel-like factor 9	Rattus norvegicus	9-13
10733585-8	2000	Blocking BTEB protein expression significantly reduced the steady-state levels of the acetaldehyde-induced alphaI(I) collagen mRNA, suggesting that BTEB is required for this gene expression.	Acetaldehyde	86-98	Kruppel-like factor 9	Rattus norvegicus	148-152
10733585-9	2000	Further studies found that acetaldehyde activated Jun N-terminal kinase (JNK) 1 and 2 and activator protein 1 (AP-1) transactivating activity.	Acetaldehyde	27-39	mitogen-activated protein kinase 8	Rattus norvegicus	73-76
10733585-10	2000	Inhibition of JNK activation resulted in the reduction of the acetaldehyde-induced BTEB protein abundance and alphaI(I) collagen mRNA levels, indicating that the expression of both genes is JNK dependent in HSC.	Acetaldehyde	62-74	mitogen-activated protein kinase 8	Rattus norvegicus	14-17
10776930-7	2000	RESULTS: The results show that acrolein and acetaldehyde produced dose-dependent inhibition of HGF attachment and proliferation.	Acetaldehyde	44-56	hepatocyte growth factor	Homo sapiens	95-98
10716626-2	2000	Threonine aldolase catalyzes the pyridoxal phosphate-dependent, reversible reaction between threonine and acetaldehyde plus glycine.	Acetaldehyde	106-118	serine hydroxymethyltransferase 2	Homo sapiens	0-18
10776930-9	2000	The main ultrastructural finding for the HGF cytoplasm was the presence of vacuoles and lysosomal structures that became prominent with increasing concentration of acrolein and acetaldehyde.	Acetaldehyde	177-189	hepatocyte growth factor	Homo sapiens	41-44
10776930-10	2000	CONCLUSIONS: Our experimental data suggest that acrolein and acetaldehyde, volatile components of tobacco smoke, are detrimental to HGF survival and consequently to the oral connective tissue.	Acetaldehyde	61-73	hepatocyte growth factor	Homo sapiens	132-135
10656185-0	2000	Accumulation of hemoglobin-associated acetaldehyde with habitual alcohol drinking in the atypical ALDH2 genotype.	Acetaldehyde	38-50	aldehyde dehydrogenase 2 family member	Homo sapiens	98-103
10656185-1	2000	BACKGROUND: Those with the atypical genotypes of low Km aldehyde dehydrogenase (ALDH2) have high blood concentrations of free acetaldehyde, an active metabolite of ethanol, after drinking alcohol.	Acetaldehyde	126-138	aldehyde dehydrogenase 2 family member	Homo sapiens	80-85
10525098-3	1999	In this study, we use transgenic overexpression of alcohol dehydrogenase to elevate cardiac exposure to acetaldehyde, the major and most reactive metabolite of alcohol.	Acetaldehyde	104-116	aldo-keto reductase family 1 member A1	Homo sapiens	51-72
10613735-3	2000	In this communication we investigated the molecular mechanisms whereby acetaldehyde induces mouse alpha1(I) procollagen (col1a1) gene expression in cultured hepatic stellate cells.	Acetaldehyde	71-83	collagen, type I, alpha 1	Mus musculus	121-127
10613735-4	2000	Transfection assays using reporter plasmids driven by different segments of the col1a1 promoter localized an acetaldehyde-responsive element (AcRE) between nucleotides -370 and -345.	Acetaldehyde	109-121	collagen, type I, alpha 1	Mus musculus	80-86
10613735-5	2000	We also show that acetaldehyde enhances binding of a CCAAT/enhancer binding protein-beta (C/EBPbeta)-containing complex to this element, and that this effect is due, at least in part, to an increase in the concentration of nuclear p35C/EBPbeta protein.	Acetaldehyde	18-30	CCAAT/enhancer binding protein (C/EBP), beta	Mus musculus	53-88
10613735-6	2000	Although this element overlaps to a previously described transforming growth factor beta1 (TGF-beta1)-responsive element, the stimulatory effect of acetaldehyde is not mediated through this cytokine, because addition of neutralizing anti-TGF-beta1 antibodies does not prevent acetaldehyde-elicited col1a1 up-regulation.	Acetaldehyde	148-160	transforming growth factor, beta 1	Mus musculus	57-89
10613735-6	2000	Although this element overlaps to a previously described transforming growth factor beta1 (TGF-beta1)-responsive element, the stimulatory effect of acetaldehyde is not mediated through this cytokine, because addition of neutralizing anti-TGF-beta1 antibodies does not prevent acetaldehyde-elicited col1a1 up-regulation.	Acetaldehyde	148-160	transforming growth factor, beta 1	Mus musculus	91-100
10613735-6	2000	Although this element overlaps to a previously described transforming growth factor beta1 (TGF-beta1)-responsive element, the stimulatory effect of acetaldehyde is not mediated through this cytokine, because addition of neutralizing anti-TGF-beta1 antibodies does not prevent acetaldehyde-elicited col1a1 up-regulation.	Acetaldehyde	148-160	transforming growth factor, beta 1	Mus musculus	238-247
10613735-6	2000	Although this element overlaps to a previously described transforming growth factor beta1 (TGF-beta1)-responsive element, the stimulatory effect of acetaldehyde is not mediated through this cytokine, because addition of neutralizing anti-TGF-beta1 antibodies does not prevent acetaldehyde-elicited col1a1 up-regulation.	Acetaldehyde	148-160	collagen, type I, alpha 1	Mus musculus	298-304
10613735-6	2000	Although this element overlaps to a previously described transforming growth factor beta1 (TGF-beta1)-responsive element, the stimulatory effect of acetaldehyde is not mediated through this cytokine, because addition of neutralizing anti-TGF-beta1 antibodies does not prevent acetaldehyde-elicited col1a1 up-regulation.	Acetaldehyde	276-288	transforming growth factor, beta 1	Mus musculus	57-89
10613735-6	2000	Although this element overlaps to a previously described transforming growth factor beta1 (TGF-beta1)-responsive element, the stimulatory effect of acetaldehyde is not mediated through this cytokine, because addition of neutralizing anti-TGF-beta1 antibodies does not prevent acetaldehyde-elicited col1a1 up-regulation.	Acetaldehyde	276-288	transforming growth factor, beta 1	Mus musculus	91-100
10613735-9	2000	Thus, these results suggest that acetaldehyde-induced col1a1 up-regulation is mediated, at least in part, through H(2)O(2).	Acetaldehyde	33-45	collagen, type I, alpha 1	Mus musculus	54-60
10613735-11	2000	In addition, we have established a direct connection between oxidative stress and enhanced col1a1 expression induced by acetaldehyde.	Acetaldehyde	120-132	collagen, type I, alpha 1	Mus musculus	91-97
10573527-2	1999	This study compared the effect of ethanol and acetaldehyde in the induction of oxidative stress and activation of transcription factors nuclear factor-kappaB (NF-kappaB) and activating protein 1 (AP-1) in HepG2 cells, which do not express CYP2E1, and HepG2 cells transfected with CYP2E1 (E47 cells).	Acetaldehyde	46-58	JunB proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	196-200
10573527-7	1999	Interestingly, however, despite the inability of acetaldehyde to induce oxidative stress in HepG2, acetaldehyde activated NF-kappaB and AP-1; in contrast, ethanol failed to activate these transcription factors in HepG2.	Acetaldehyde	99-111	JunB proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	136-140
10573527-8	1999	Thus, our findings indicate that activation of NF-kappaB and AP-1 by ethanol and acetaldehyde occurs through distinct mechanisms.	Acetaldehyde	81-93	JunB proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	61-65
10573527-9	1999	CYP2E1 is indispensable in the induction of oxidative stress from ethanol, whereas the activation of NF-kappaB and AP-1 by acetaldehyde is independent of oxidative stress.	Acetaldehyde	123-135	JunB proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	115-119
10513990-1	1999	Liver mitochondrial low-Km aldehyde dehydrogenase (ALDH2, EC 1.2.1.3), the isoform responsible for the conversion of acetaldehyde to acetate, is inhibited by the sulfoxide bioactivation products of Et2NC(O)SMe (from the alcohol aversion drug disulfiram), Pr2NC(O)SEt (the herbicide S-ethyl N,N-dipropylthiocarbamate), and BuNHC(O)SMe (from the fungicide benomyl).	Acetaldehyde	117-129	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	51-56
10620320-1	2000	Cytochrome P4502E (P4502E), the major ethanol-inducible P450 metabolizes ethanol to acetaldehyde and bioactivates procarcinogens to ultimate carcinogens.	Acetaldehyde	84-96	cytochrome P450, family 2, subfamily e, polypeptide 1	Rattus norvegicus	0-6
10825257-3	2000	We demonstrate in this report that MeDTC-SO is a potent irreversible inhibitor of recombinant rat liver mitochondrial aldehyde dehydrogenase (rlmALDH), the enzyme responsible for oxidizing acetaldehyde formed during ethanol metabolism.	Acetaldehyde	189-201	aldehyde dehydrogenase 2 family member	Rattus norvegicus	104-140
10630602-17	1999	Physiological tolerance or innate insensitivity to the accumulation of blood acetaldehyde following alcohol ingestion may be crucial for the development of alcoholism in individuals homozygous for ALDH2*2.	Acetaldehyde	77-89	aldehyde dehydrogenase 2 family member	Homo sapiens	197-202
10573527-0	1999	Differential role of ethanol and acetaldehyde in the induction of oxidative stress in HEP G2 cells: effect on transcription factors AP-1 and NF-kappaB.	Acetaldehyde	33-45	JunB proto-oncogene, AP-1 transcription factor subunit	Homo sapiens	132-136
10487386-15	1999	They also support the notion that acetaldehyde may be produced directly in the brain by catalase and that it may be an important regulator of ethanol"s locomotor effects.	Acetaldehyde	34-46	catalase	Mus musculus	88-96
10513995-0	1999	Acetaldehyde increases the activity and gene expression of urokinase type plasminogen activator in a hepatic stellate cell line.	Acetaldehyde	0-12	plasminogen activator, urokinase	Rattus norvegicus	59-95
10513995-1	1999	The aim of this study was to investigate the effect of acetaldehyde on the activity and expression of urokinase type plasminogen activator gene in a clone of hepatic stellate cells.	Acetaldehyde	55-67	plasminogen activator, urokinase	Rattus norvegicus	102-138
10513995-3	1999	The treatment of the cells with doses of 100 and 175 micromol/l acetaldehyde, produced an increase in the urokinase type plasminogen activator activity not only in the cell extract, but also in conditioned medium.	Acetaldehyde	64-76	plasminogen activator, urokinase	Rattus norvegicus	106-142
10513995-4	1999	However, the use of higher doses of acetaldehyde (250 and 350 micromol/l) produced an inhibitory effect on the urokinase type plasminogen activator activity.	Acetaldehyde	36-48	plasminogen activator, urokinase	Rattus norvegicus	111-147
10513995-6	1999	Our results shown that acetaldehyde induced changes in synthesis, release, and expression of urokinase type plasminogen activator in CFSC-2G cells.	Acetaldehyde	23-35	plasminogen activator, urokinase	Rattus norvegicus	93-129
10513995-7	1999	Those findings suggest that the alterations in the synthesis and expression of the urokinase type plasminogen activator might be another event associated to the activation of hepatic stellate cell after exposure to hepatotoxic agents like-acetaldehyde.	Acetaldehyde	239-251	plasminogen activator, urokinase	Rattus norvegicus	83-119
10446146-0	1999	Kinetics of cytochrome P450 2E1-catalyzed oxidation of ethanol to acetic acid via acetaldehyde.	Acetaldehyde	82-94	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	12-31
10482910-14	1999	The intracerebroventricular dose of acetaldehyde effective in inhibiting LTP induction (0.1 - 0.15 mg brain-1) was approximately 10 fold lower than that of ethanol (1.0 - 1.5 mg <protein-id="192109">brain-1).	Acetaldehyde	36-48	POU class 3 homeobox 3	Rattus norvegicus	102-109
10431222-4	1999	Both of the enzymes required for the production of acetaldehyde and ethanol, pyruvate decarboxylase and alcohol dehydrogenase, are highly abundant in pollen, resulting in fermentation in fully oxygenated cells.	Acetaldehyde	51-63	pyruvate decarboxylase 2	Zea mays	77-99
10780266-7	1999	This low-dose alcohol hypersensitivity, accompanied by a prolonged and large accumulation of acetaldehyde in blood, provides an explanation for the strong protection against heavy drinking and alcoholism in individuals homozygous for the ALDH2*2 gene allele.	Acetaldehyde	93-105	aldehyde dehydrogenase 2 family member	Homo sapiens	238-243
10371398-13	1999	They also provide further support for the notion that acetaldehyde may be produced directly in the brain via catalase and that it may be a factor mediating some of ethanol"s central effects.	Acetaldehyde	54-66	catalase	Mus musculus	109-117
10406936-5	1999	The enzyme is even more efficient in the reverse direction of acetaldehyde reduction (K(m) = 30 microM and k(cat) = 9800 min(-1)), suggesting a physiological function like that seen for the fermentative non-MDR alcohol dehydrogenase.	Acetaldehyde	62-74	Alcohol dehydrogenase	Escherichia coli	211-232
10418820-4	1999	Sustained elevations of acetaldehyde were achieved by daily treatment with two inhibitors of aldehyde dehydrogenase (ALDH): disulfiram and benzcoprine.	Acetaldehyde	24-36	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	93-115
10418820-4	1999	Sustained elevations of acetaldehyde were achieved by daily treatment with two inhibitors of aldehyde dehydrogenase (ALDH): disulfiram and benzcoprine.	Acetaldehyde	24-36	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	117-121
10418820-6	1999	Treatment with the ALDH inhibitors led to increased acetaldehyde in liver and plasma but prevented necrosis and inflammation.	Acetaldehyde	52-64	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	19-23
10552529-5	1999	By contrast, acetaldehyde was a potent inhibitor of PLD.	Acetaldehyde	13-25	phospholipase D alpha 1	Zea mays	52-55
10403637-6	1999	With the same period of treatment, acetaldehyde markedly increased TNF-alpha expression, and stimulated IL-1beta secretion, while LPS exposure induced the expression of TNF-alpha, IL-6, and TGF-beta1, and the secretion of IL-1beta, IL-6, and TGF-beta1.	Acetaldehyde	35-47	tumor necrosis factor	Homo sapiens	67-76
10403637-6	1999	With the same period of treatment, acetaldehyde markedly increased TNF-alpha expression, and stimulated IL-1beta secretion, while LPS exposure induced the expression of TNF-alpha, IL-6, and TGF-beta1, and the secretion of IL-1beta, IL-6, and TGF-beta1.	Acetaldehyde	35-47	interleukin 1 beta	Homo sapiens	104-112
10403637-8	1999	A 72 h acetaldehyde exposure decreased markedly TNF-alpha expression and stimulated a previously absent TGF-beta1 response.	Acetaldehyde	7-19	tumor necrosis factor	Homo sapiens	48-57
10403637-8	1999	A 72 h acetaldehyde exposure decreased markedly TNF-alpha expression and stimulated a previously absent TGF-beta1 response.	Acetaldehyde	7-19	transforming growth factor beta 1	Homo sapiens	104-113
10397278-1	1999	BACKGROUND: Human mitochondrial aldehyde dehydrogenase (ALDH2) is a major enzyme responsible for the oxidation of acetaldehyde derived from ethanol metabolism.	Acetaldehyde	114-126	aldehyde dehydrogenase 2 family member	Homo sapiens	56-61
10397283-12	1999	In addition, metabolism by CYP2E1 results in a significant free radical release and acetaldehyde production which, in turn, diminish reduced glutathione (GSH) and other defense systems against oxidative stress.	Acetaldehyde	84-96	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	27-33
10416267-0	1999	The effect of inhibition of aldehyde dehydrogenase on nasal uptake of inspired acetaldehyde.	Acetaldehyde	79-91	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	28-50
10416267-14	1999	In toto, these results suggest that inspired acetaldehyde is metabolized in situ by ALDH, but at exposure concentrations of 300 ppm or greater, the delivered dosage rate may equal or exceed the capacity of this enzyme.	Acetaldehyde	45-57	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	84-88
10235274-0	1999	Relationship between serum levels of anti-low-density lipoprotein-acetaldehyde-adduct antibody and aldehyde dehydrogenase 2 heterozygotes in patients with alcoholic liver injury.	Acetaldehyde	66-78	aldehyde dehydrogenase 2 family member	Homo sapiens	99-123
10235287-6	1999	ALDH2 may participate in this process, especially in the conversion of acetaldehyde to acetate.	Acetaldehyde	71-83	aldehyde dehydrogenase 2 family member	Homo sapiens	0-5
20575789-3	1999	These results are consistent with previous animal and human studies which suggest that catalase, via its ability to produce acetaldehyde through the metabolism of ethanol, may have a regulatory role in the propensity to drink alcohol.	Acetaldehyde	124-136	catalase	Homo sapiens	87-95
10029200-7	1999	Structural analysis by mass spectrometry of the tryptic digestion fractions of adducted cyt c is consistent with several peptides bearing one-to-three acetaldehyde moieties on Lys residues, and three distinct Tyr/Trp-containing peptides: P[28-53], P[56-73], P[73-91] carrying one-to-two HER.	Acetaldehyde	151-163	cytochrome c, somatic	Homo sapiens	88-93
10064379-5	1999	The student with the inactive form of ALDH2 was flushed and his levels of 2,3-butanediol and acetaldehyde in blood and urine were found to be the highest.	Acetaldehyde	93-105	aldehyde dehydrogenase 2 family member	Homo sapiens	38-43
10069557-0	1999	Acetaldehyde enhances murine alpha2(I) collagen promoter activity by Ca2+-independent protein kinase C activation in cultured rat hepatic stellate cells.	Acetaldehyde	0-12	protein kinase C, gamma	Rattus norvegicus	86-102
10069557-1	1999	Protein kinase C (PKC) inhibitors decrease alpha1(I) collagen mRNA in stellate cells exposed to 200 micromol/liter of acetaldehyde.	Acetaldehyde	118-130	protein kinase C, gamma	Rattus norvegicus	0-16
10069557-1	1999	Protein kinase C (PKC) inhibitors decrease alpha1(I) collagen mRNA in stellate cells exposed to 200 micromol/liter of acetaldehyde.	Acetaldehyde	118-130	protein kinase C, gamma	Rattus norvegicus	18-21
10069557-7	1999	Acetaldehyde exposure enhanced PKC activity translocation to the particulate fraction at 20 min.	Acetaldehyde	0-12	protein kinase C, gamma	Rattus norvegicus	31-34
10069557-10	1999	Calphostin C, a specific PKC inhibitor, which blocks DAG binding, eliminated both activation of the alpha2(I) collagen promoter by acetaldehyde and mRNA production by reverse transcriptase-polymerase chain reaction analysis.	Acetaldehyde	131-143	protein kinase C, gamma	Rattus norvegicus	25-28
10069557-12	1999	This study shows that collagen production by acetaldehyde is mediated by a calcium-independent PKC mechanism.	Acetaldehyde	45-57	protein kinase C, gamma	Rattus norvegicus	95-98
9895226-6	1999	Recently, hepatic XOR and AOX were found to generate ROS in two ways from alcohol metabolism: by acetaldehyde consumption and by the intrinsic NADH oxidase activity of both XOR and AOX.	Acetaldehyde	97-109	xanthine dehydrogenase	Homo sapiens	18-21
9895226-6	1999	Recently, hepatic XOR and AOX were found to generate ROS in two ways from alcohol metabolism: by acetaldehyde consumption and by the intrinsic NADH oxidase activity of both XOR and AOX.	Acetaldehyde	97-109	aldehyde oxidase 1	Homo sapiens	26-29
9895226-7	1999	The data obtained suggests that: (1) expression of ADH and XOR or AOX in breast tissue provides the enzymes that generate ROS; (2) metabolism of alcohol produces acetaldehyde and NADH that can both be substrates for XOR or AOX and thereby result in ROS formation; and (3) ROS generated by XOR or AOX can induce the carcinogenic mutations and DNA damage found in breast cancer.	Acetaldehyde	162-174	aldo-keto reductase family 1 member A1	Homo sapiens	51-54
9895226-7	1999	The data obtained suggests that: (1) expression of ADH and XOR or AOX in breast tissue provides the enzymes that generate ROS; (2) metabolism of alcohol produces acetaldehyde and NADH that can both be substrates for XOR or AOX and thereby result in ROS formation; and (3) ROS generated by XOR or AOX can induce the carcinogenic mutations and DNA damage found in breast cancer.	Acetaldehyde	162-174	xanthine dehydrogenase	Homo sapiens	59-62
9895226-7	1999	The data obtained suggests that: (1) expression of ADH and XOR or AOX in breast tissue provides the enzymes that generate ROS; (2) metabolism of alcohol produces acetaldehyde and NADH that can both be substrates for XOR or AOX and thereby result in ROS formation; and (3) ROS generated by XOR or AOX can induce the carcinogenic mutations and DNA damage found in breast cancer.	Acetaldehyde	162-174	aldehyde oxidase 1	Homo sapiens	66-69
9895226-7	1999	The data obtained suggests that: (1) expression of ADH and XOR or AOX in breast tissue provides the enzymes that generate ROS; (2) metabolism of alcohol produces acetaldehyde and NADH that can both be substrates for XOR or AOX and thereby result in ROS formation; and (3) ROS generated by XOR or AOX can induce the carcinogenic mutations and DNA damage found in breast cancer.	Acetaldehyde	162-174	xanthine dehydrogenase	Homo sapiens	216-219
9895226-7	1999	The data obtained suggests that: (1) expression of ADH and XOR or AOX in breast tissue provides the enzymes that generate ROS; (2) metabolism of alcohol produces acetaldehyde and NADH that can both be substrates for XOR or AOX and thereby result in ROS formation; and (3) ROS generated by XOR or AOX can induce the carcinogenic mutations and DNA damage found in breast cancer.	Acetaldehyde	162-174	aldehyde oxidase 1	Homo sapiens	223-226
9895226-7	1999	The data obtained suggests that: (1) expression of ADH and XOR or AOX in breast tissue provides the enzymes that generate ROS; (2) metabolism of alcohol produces acetaldehyde and NADH that can both be substrates for XOR or AOX and thereby result in ROS formation; and (3) ROS generated by XOR or AOX can induce the carcinogenic mutations and DNA damage found in breast cancer.	Acetaldehyde	162-174	xanthine dehydrogenase	Homo sapiens	216-219
9895226-7	1999	The data obtained suggests that: (1) expression of ADH and XOR or AOX in breast tissue provides the enzymes that generate ROS; (2) metabolism of alcohol produces acetaldehyde and NADH that can both be substrates for XOR or AOX and thereby result in ROS formation; and (3) ROS generated by XOR or AOX can induce the carcinogenic mutations and DNA damage found in breast cancer.	Acetaldehyde	162-174	aldehyde oxidase 1	Homo sapiens	223-226
9895041-1	1999	We report that incubation of acetaldehyde with bovine serum albumin results in the generation of acetate in a reaction that is directly proportional to the levels of albumin and exponentially dependent on the concentration of acetaldehyde.	Acetaldehyde	226-238	albumin	Oryctolagus cuniculus	54-67
9895041-5	1999	Incubation of acetaldehyde (240 mM) with bovine serum albumin was found to generate ethyl-lysine moieties as determined by a specific monoclonal antibody.	Acetaldehyde	14-26	albumin	Oryctolagus cuniculus	48-61
9895041-6	1999	Immunization of rabbits with products of the reaction of bovine serum albumin with acetaldehyde led to the generation of antibodies that reacted to reduced adducts formed in the reaction of acetaldehyde and proteins in the presence of sodium cyanoborohydride.	Acetaldehyde	83-95	albumin	Oryctolagus cuniculus	64-77
9895041-6	1999	Immunization of rabbits with products of the reaction of bovine serum albumin with acetaldehyde led to the generation of antibodies that reacted to reduced adducts formed in the reaction of acetaldehyde and proteins in the presence of sodium cyanoborohydride.	Acetaldehyde	190-202	albumin	Oryctolagus cuniculus	64-77
9895041-10	1999	However, the mechanism by which the bulk of acetate is generated in the reaction of acetaldehyde and bovine serum albumin remains to be elucidated.	Acetaldehyde	84-96	albumin	Oryctolagus cuniculus	108-121
10075087-7	1999	In contrast, acetaldehyde reduced the conversion of t-RAL to t-RA by 25 and 87% at 0.1 and 10 mM respective concentrations.	Acetaldehyde	13-25	RAS like proto-oncogene A	Homo sapiens	54-57
10344773-3	1999	At the periphery, alcohol and acetaldehyde liberate histamine from its store in mast cells and depress histamine elimination by inhibiting diamine oxidase, resulting in elevated histamine levels in tissues.	Acetaldehyde	30-42	amine oxidase copper containing 1	Homo sapiens	139-154
9895041-0	1999	Generation of acetate and production of ethyl-lysine in the reaction of acetaldehyde plus serum albumin.	Acetaldehyde	72-84	albumin	Oryctolagus cuniculus	90-103
9895041-1	1999	We report that incubation of acetaldehyde with bovine serum albumin results in the generation of acetate in a reaction that is directly proportional to the levels of albumin and exponentially dependent on the concentration of acetaldehyde.	Acetaldehyde	29-41	albumin	Oryctolagus cuniculus	54-67
10071484-0	1999	Coagulation protein function: the influence of acetaldehyde-modified heparin on thrombin activity.	Acetaldehyde	47-59	coagulation factor II, thrombin	Homo sapiens	80-88
10071484-1	1999	BACKGROUND: The affect of acetaldehyde-treated heparin on thrombin activity has been investigated using factor II-deficient human plasma.	Acetaldehyde	26-38	coagulation factor II, thrombin	Homo sapiens	58-66
10071484-7	1999	They further indicate that thrombin is targeted by the acetaldehyde-treated heparin.	Acetaldehyde	55-67	coagulation factor II, thrombin	Homo sapiens	27-35
10071484-8	1999	Heparin-acetaldehyde mixtures also reacted with plasma prior to the addition of thrombin to modestly prolong coagulation time.	Acetaldehyde	8-20	coagulation factor II, thrombin	Homo sapiens	80-88
10071484-9	1999	Similarly, but more effectively, thrombin/heparin mixtures increased the clotting time of acetaldehyde-exposed plasma.	Acetaldehyde	90-102	coagulation factor II, thrombin	Homo sapiens	33-41
10071484-10	1999	These data further suggest the possibility that reactions of acetaldehyde and heparin are not restricted to those with thrombin, and that they may extend to other blood factors/proteins.	Acetaldehyde	61-73	coagulation factor II, thrombin	Homo sapiens	119-127
9918814-0	1998	Acetaldehyde inhibits NF-kappaB activation through IkappaBalpha preservation in rat Kupffer cells.	Acetaldehyde	0-12	NFKB inhibitor alpha	Rattus norvegicus	51-63
9918814-3	1998	The present in vitro study was aimed to clarify whether acetaldehyde has an effect on degradation of IkappaBalpha and activation of NF-kappaB in LPS-stimulated rat Kupffer cells.	Acetaldehyde	56-68	NFKB inhibitor alpha	Rattus norvegicus	101-113
9918814-7	1998	RESULTS: In LPS-stimulated rat Kupffer cells, acetaldehyde diminished proteolytic degradation of IkappaBalpha, inhibited nuclear translocation of cytosolic p65 protein, and, accordingly, markedly decreased NF-kappaB activation.	Acetaldehyde	46-58	NFKB inhibitor alpha	Rattus norvegicus	97-109
9918814-7	1998	RESULTS: In LPS-stimulated rat Kupffer cells, acetaldehyde diminished proteolytic degradation of IkappaBalpha, inhibited nuclear translocation of cytosolic p65 protein, and, accordingly, markedly decreased NF-kappaB activation.	Acetaldehyde	46-58	synaptotagmin 1	Rattus norvegicus	156-159
9918814-8	1998	CONCLUSIONS: Acetaldehyde is clearly involved in the stabilization of IkappaBalpha protein and suppression of NF-kappaB activation in rat Kupffer cells.	Acetaldehyde	13-25	NFKB inhibitor alpha	Rattus norvegicus	70-82
9918814-9	1998	Acetaldehyde may form an adduct with IkappaBalpha, thus making the protein less susceptible to degradation.	Acetaldehyde	0-12	NFKB inhibitor alpha	Rattus norvegicus	37-49
9835301-1	1998	The present study examined whether measurement of hemoglobin-acetaldehyde (HbA1-AcH) using an improved methodology may be useful as a biological marker of alcohol abuse.	Acetaldehyde	61-73	hemoglobin subunit alpha 1	Homo sapiens	75-79
9884134-0	1998	Comparison of carbohydrate-deficient transferrin, immunoglobulin A antibodies reactive with acetaldehyde-modified protein and acetaldehyde-modified albumin with conventional markers of alcohol consumption.	Acetaldehyde	92-104	CD79a molecule	Homo sapiens	50-66
9884134-2	1998	Recently plasma immunoglobulin A (IgA) reactivity with acetaldehyde (AcH)-modified proteins, or the modified proteins per se, have been proposed as a markers for high levels of alcohol consumption.	Acetaldehyde	55-67	CD79a molecule	Homo sapiens	16-32
9884134-2	1998	Recently plasma immunoglobulin A (IgA) reactivity with acetaldehyde (AcH)-modified proteins, or the modified proteins per se, have been proposed as a markers for high levels of alcohol consumption.	Acetaldehyde	55-67	CD79a molecule	Homo sapiens	34-37
9884134-2	1998	Recently plasma immunoglobulin A (IgA) reactivity with acetaldehyde (AcH)-modified proteins, or the modified proteins per se, have been proposed as a markers for high levels of alcohol consumption.	Acetaldehyde	69-72	CD79a molecule	Homo sapiens	16-32
9884134-2	1998	Recently plasma immunoglobulin A (IgA) reactivity with acetaldehyde (AcH)-modified proteins, or the modified proteins per se, have been proposed as a markers for high levels of alcohol consumption.	Acetaldehyde	69-72	CD79a molecule	Homo sapiens	34-37
9726283-0	1998	Role of catalase in in vitro acetaldehyde formation by human colonic contents.	Acetaldehyde	29-41	catalase	Homo sapiens	8-16
9855020-7	1998	Acetaldehyde also considerably decreased both sucrase activity and nuclear content of protein kinase A catalytic subunit in Caco-2 cells, which indicate that the differentiation of the cells was disturbed.	Acetaldehyde	0-12	protein kinase cAMP-activated catalytic subunit alpha	Homo sapiens	86-120
9726283-5	1998	In this study we demonstrate acetaldehyde production from ethanol in vitro by colonic contents in a reaction catalyzed by both bacterial ADH and catalase.	Acetaldehyde	29-41	catalase	Homo sapiens	145-153
9726283-7	1998	The catalase inhibitors sodium azide and 3-amino-1,2,4-triazole (3-AT) markedly reduced the amount of acetaldehyde produced from 22 mM ethanol in a concentration dependent manner compared with the control samples (0.1 mM sodium azide to 73% and 10 mM 3-AT to 67% of control).	Acetaldehyde	102-114	catalase	Homo sapiens	4-12
9726283-9	1998	The mean supernatant catalase activity was 0.53+/-0.1 micromol/min/mg protein after the addition of 10 mM H2O2, and there was a significant (p &lt; 0.05) correlation between catalase activity and acetaldehyde production after the addition of the hydrogen peroxide generating system.	Acetaldehyde	196-208	catalase	Homo sapiens	21-29
9726283-9	1998	The mean supernatant catalase activity was 0.53+/-0.1 micromol/min/mg protein after the addition of 10 mM H2O2, and there was a significant (p &lt; 0.05) correlation between catalase activity and acetaldehyde production after the addition of the hydrogen peroxide generating system.	Acetaldehyde	196-208	catalase	Homo sapiens	174-182
9726283-10	1998	Our results demonstrate that colonic contents possess catalase activity, which probably is of bacterial origin, and indicate that in addition to ADH, part of the acetaldehyde produced in the large intestine during ethanol metabolism can be catalase dependent.	Acetaldehyde	162-174	catalase	Homo sapiens	54-62
9726283-10	1998	Our results demonstrate that colonic contents possess catalase activity, which probably is of bacterial origin, and indicate that in addition to ADH, part of the acetaldehyde produced in the large intestine during ethanol metabolism can be catalase dependent.	Acetaldehyde	162-174	catalase	Homo sapiens	240-248
9724163-0	1998	Coagulation protein function V: diminution of antithrombin III function by acetaldehyde.	Acetaldehyde	75-87	serpin family C member 1	Homo sapiens	46-62
9744533-1	1998	Aldehyde dehydrogenase-2 (ALDH2) eliminates most of the acetaldehyde produced during alcohol metabolism.	Acetaldehyde	56-68	aldehyde dehydrogenase 2 family member	Homo sapiens	0-24
9744533-1	1998	Aldehyde dehydrogenase-2 (ALDH2) eliminates most of the acetaldehyde produced during alcohol metabolism.	Acetaldehyde	56-68	aldehyde dehydrogenase 2 family member	Homo sapiens	26-31
9724163-1	1998	The anticoagulant activity of antithrombin III (ATIII), as observed in a plasma-free system consisting of thrombin and fibrinogen, is readily reduced by acetaldehyde (AcH) at concentrations of 447, 89.4, and 17.9 mM.	Acetaldehyde	153-165	serpin family C member 1	Homo sapiens	30-46
9724163-1	1998	The anticoagulant activity of antithrombin III (ATIII), as observed in a plasma-free system consisting of thrombin and fibrinogen, is readily reduced by acetaldehyde (AcH) at concentrations of 447, 89.4, and 17.9 mM.	Acetaldehyde	153-165	serpin family C member 1	Homo sapiens	48-53
9724163-1	1998	The anticoagulant activity of antithrombin III (ATIII), as observed in a plasma-free system consisting of thrombin and fibrinogen, is readily reduced by acetaldehyde (AcH) at concentrations of 447, 89.4, and 17.9 mM.	Acetaldehyde	153-165	coagulation factor II, thrombin	Homo sapiens	34-42
9724163-1	1998	The anticoagulant activity of antithrombin III (ATIII), as observed in a plasma-free system consisting of thrombin and fibrinogen, is readily reduced by acetaldehyde (AcH) at concentrations of 447, 89.4, and 17.9 mM.	Acetaldehyde	153-165	fibrinogen beta chain	Homo sapiens	119-129
9724163-1	1998	The anticoagulant activity of antithrombin III (ATIII), as observed in a plasma-free system consisting of thrombin and fibrinogen, is readily reduced by acetaldehyde (AcH) at concentrations of 447, 89.4, and 17.9 mM.	Acetaldehyde	167-170	serpin family C member 1	Homo sapiens	30-46
9724163-1	1998	The anticoagulant activity of antithrombin III (ATIII), as observed in a plasma-free system consisting of thrombin and fibrinogen, is readily reduced by acetaldehyde (AcH) at concentrations of 447, 89.4, and 17.9 mM.	Acetaldehyde	167-170	serpin family C member 1	Homo sapiens	48-53
9724163-1	1998	The anticoagulant activity of antithrombin III (ATIII), as observed in a plasma-free system consisting of thrombin and fibrinogen, is readily reduced by acetaldehyde (AcH) at concentrations of 447, 89.4, and 17.9 mM.	Acetaldehyde	167-170	coagulation factor II, thrombin	Homo sapiens	34-42
9724163-1	1998	The anticoagulant activity of antithrombin III (ATIII), as observed in a plasma-free system consisting of thrombin and fibrinogen, is readily reduced by acetaldehyde (AcH) at concentrations of 447, 89.4, and 17.9 mM.	Acetaldehyde	167-170	fibrinogen beta chain	Homo sapiens	119-129
9724163-4	1998	Clotting times of 20.9+/-1.0, 32.3+/-1.0, and 45.3+/-1.6 sec were obtained with 447, 89.4, and 17.9 mM AcH-ATIII mixtures, respectively.	Acetaldehyde	103-106	serpin family C member 1	Homo sapiens	107-112
9724163-5	1998	These data suggest that functional groups on ATIII, such as guanidiniums, aminos, and others are susceptible to adduct formation with AcH, thereby altering the shape and charge of the anticoagulant.	Acetaldehyde	134-137	serpin family C member 1	Homo sapiens	45-50
9706843-0	1998	Effect of acetaldehyde and acetylsalicylic acid on HbA1c chromatography in the FPLC method with Mono S cation exchanger.	Acetaldehyde	10-22	hemoglobin subunit alpha 1	Homo sapiens	51-55
9590515-3	1998	The effect of ethanol and its breakdown products, acetate and acetaldehyde, on highly purified rat liver methionine synthase was tested in vitro.	Acetaldehyde	62-74	5-methyltetrahydrofolate-homocysteine methyltransferase	Rattus norvegicus	105-124
26734919-2	1998	In recent studies involving DNA analysis, it was found that a deficiency of the ALDH2 isozyme (ALDH2*2) was responsible for the flushing symptoms as well as other vasomotor symptoms caused by a higher acetaldehyde level after alcohol consumption.	Acetaldehyde	201-213	aldehyde dehydrogenase 2 family member	Homo sapiens	80-85
26734919-2	1998	In recent studies involving DNA analysis, it was found that a deficiency of the ALDH2 isozyme (ALDH2*2) was responsible for the flushing symptoms as well as other vasomotor symptoms caused by a higher acetaldehyde level after alcohol consumption.	Acetaldehyde	201-213	aldehyde dehydrogenase 2 family member	Homo sapiens	95-100
26734919-6	1998	Concerning blood ethanol elimination kinetics, it was reported that the c2 gene of CYP2E1 and the ALDH2*1 gene may have greater effects on ethanol and acetaldehyde elimination than the other genotypes, when the blood ethanol level is below 20 m M.	Acetaldehyde	151-163	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	83-89
26734919-6	1998	Concerning blood ethanol elimination kinetics, it was reported that the c2 gene of CYP2E1 and the ALDH2*1 gene may have greater effects on ethanol and acetaldehyde elimination than the other genotypes, when the blood ethanol level is below 20 m M.	Acetaldehyde	151-163	aldehyde dehydrogenase 2 family member	Homo sapiens	98-103
9590515-5	1998	Acetaldehyde was found to inhibit methionine synthase activity, with an apparent IC50 of 2 mM.	Acetaldehyde	0-12	5-methyltetrahydrofolate-homocysteine methyltransferase	Rattus norvegicus	34-53
9590515-7	1998	Acetaldehyde-induced inhibition of liver methionine synthase activity is thus proposed as the most likely explanation of the reported in vivo effect of ethanol upon methionine synthase.	Acetaldehyde	0-12	5-methyltetrahydrofolate-homocysteine methyltransferase	Rattus norvegicus	41-60
9590515-7	1998	Acetaldehyde-induced inhibition of liver methionine synthase activity is thus proposed as the most likely explanation of the reported in vivo effect of ethanol upon methionine synthase.	Acetaldehyde	0-12	5-methyltetrahydrofolate-homocysteine methyltransferase	Rattus norvegicus	165-184
9635374-9	1998	CONCLUSIONS: These data show that AcH clearly decreases the antichymotryptic activity of serum (consisting of alpha 1-proteinase inhibitor, alpha 1-antichymotrypsin, and alpha 2-macroglobulin).	Acetaldehyde	34-37	alpha-2-macroglobulin	Homo sapiens	170-191
9581663-2	1998	In alcoholics with inactive ALDH2, unidentified factors that overcome the adverse reactions of high blood acetaldehyde concentration after drinking may increase such persons" susceptibility to alcoholism.	Acetaldehyde	106-118	aldehyde dehydrogenase 2 family member	Homo sapiens	28-33
9600491-11	1998	CONCLUSIONS: Alcohol-induced asthma is probably caused by increased blood acetaldehyde concentration resulting from abnormalities of ALDH2 enzyme activity based on ALDH2 genotype differences.	Acetaldehyde	74-86	aldehyde dehydrogenase 2 family member	Homo sapiens	133-138
9600491-11	1998	CONCLUSIONS: Alcohol-induced asthma is probably caused by increased blood acetaldehyde concentration resulting from abnormalities of ALDH2 enzyme activity based on ALDH2 genotype differences.	Acetaldehyde	74-86	aldehyde dehydrogenase 2 family member	Homo sapiens	164-169
9558650-6	1998	Furthermore, an increase in serum GPT activity, which was caused by twice oral administration of acetaldehyde at 1.2 ml/kg at interval of 1 hr, was inhibited by liver hydrolysate.	Acetaldehyde	97-109	glutamic pyruvic transaminase, soluble	Mus musculus	34-37
9548989-9	1998	Drugs causing increases in blood acetaldehyde concentrations when administration was combined with ethanol ingestion also inhibited ALDH activity in vitro.	Acetaldehyde	33-45	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	132-136
9536005-0	1998	The effects of ethanol and acetaldehyde on the metabolism of prostaglandin E2 and leukotriene B4 in isolated rat hepatocytes.	Acetaldehyde	27-39	dihydrolipoamide S-succinyltransferase	Rattus norvegicus	75-96
9478048-5	1998	Likewise, there exists an aldehyde dehydrogenase (ALDH) family containing several members preferring retinal as a substrate over acetaldehyde.	Acetaldehyde	129-141	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	26-48
9478048-5	1998	Likewise, there exists an aldehyde dehydrogenase (ALDH) family containing several members preferring retinal as a substrate over acetaldehyde.	Acetaldehyde	129-141	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	50-54
9425924-0	1998	Cytotoxic effect of 7alpha-hydroxy-4-cholesten-3-one on HepG2 cells: hypothetical role of acetaldehyde-modified delta4-3-ketosteroid-5beta-reductase (the 37-kd-liver protein) in the pathogenesis of alcoholic liver injury in the rat.	Acetaldehyde	90-102	aldo-keto reductase family 1 member D1	Homo sapiens	112-148
9425924-1	1998	We recently identified delta4-3-ketosteroid-5beta-reductase as the 37 kd liver protein which is highly susceptible to acetaldehyde modification in rats continuously fed alcohol.	Acetaldehyde	118-130	aldo-keto reductase family 1, member D1	Rattus norvegicus	23-59
9349259-2	1997	Alternatively, acetaldehyde can be oxidized to acetate by aldehyde dehydrogenase (ALDH) and subsequently converted to acetyl-CoA by acetyl-CoA synthetase (ACS).	Acetaldehyde	15-27	aldehyde dehydrogenase	Nicotiana tabacum	58-80
9463925-3	1997	The model predicts that the addition of MTBE to RFG or oxyfuel will decrease acetaldehyde, benzene, 1,3-butadiene and POM, but increase formaldehyde tailpipe emissions.	Acetaldehyde	77-89	nuclear receptor coactivator 4	Homo sapiens	48-51
9537862-10	1998	CYP2E1 was not expressed in hepatic stellate cells either in basal condition or after ethanol/acetaldehyde exposure.	Acetaldehyde	94-106	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	0-6
9537862-11	1998	CONCLUSIONS: This study shows that human hepatic stellate cells have the capacity to metabolize both ethanol and acetaldehyde through a class I alcohol dehydrogenase- and an aldehyde dehydrogenase-oxidizing pathway.	Acetaldehyde	113-125	aldo-keto reductase family 1 member A1	Homo sapiens	144-165
9390539-2	1997	Alcohol dehydrogenase type 3 (ADH3) metabolizes ethanol to acetaldehyde, a carcinogen.	Acetaldehyde	59-71	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	0-34
9390539-8	1997	CONCLUSIONS: The ADH3(1-1) genotype appears to substantially increase the risk of ethanol-related oral cancer, thus providing further evidence for the carcinogenicity of acetaldehyde.	Acetaldehyde	170-182	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	17-21
9347089-7	1997	The protective allele at each locus (ALDH2*2, ADH2*2, and ADH3*1) encodes a subunit that either metabolizes ethanol to acetaldehyde more rapidly or slows the conversion of acetaldehyde to acetate.	Acetaldehyde	119-131	aldehyde dehydrogenase 2 family member	Homo sapiens	37-42
9347089-7	1997	The protective allele at each locus (ALDH2*2, ADH2*2, and ADH3*1) encodes a subunit that either metabolizes ethanol to acetaldehyde more rapidly or slows the conversion of acetaldehyde to acetate.	Acetaldehyde	119-131	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	46-50
9347089-7	1997	The protective allele at each locus (ALDH2*2, ADH2*2, and ADH3*1) encodes a subunit that either metabolizes ethanol to acetaldehyde more rapidly or slows the conversion of acetaldehyde to acetate.	Acetaldehyde	119-131	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	58-62
9347089-7	1997	The protective allele at each locus (ALDH2*2, ADH2*2, and ADH3*1) encodes a subunit that either metabolizes ethanol to acetaldehyde more rapidly or slows the conversion of acetaldehyde to acetate.	Acetaldehyde	172-184	aldehyde dehydrogenase 2 family member	Homo sapiens	37-42
9347089-7	1997	The protective allele at each locus (ALDH2*2, ADH2*2, and ADH3*1) encodes a subunit that either metabolizes ethanol to acetaldehyde more rapidly or slows the conversion of acetaldehyde to acetate.	Acetaldehyde	172-184	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	46-50
9347089-7	1997	The protective allele at each locus (ALDH2*2, ADH2*2, and ADH3*1) encodes a subunit that either metabolizes ethanol to acetaldehyde more rapidly or slows the conversion of acetaldehyde to acetate.	Acetaldehyde	172-184	alcohol dehydrogenase 1C (class I), gamma polypeptide	Homo sapiens	58-62
9349259-2	1997	Alternatively, acetaldehyde can be oxidized to acetate by aldehyde dehydrogenase (ALDH) and subsequently converted to acetyl-CoA by acetyl-CoA synthetase (ACS).	Acetaldehyde	15-27	aldehyde dehydrogenase	Nicotiana tabacum	82-86
9309300-1	1997	Mitochondrial aldehyde dehydrogenase (ALDH2) is mainly responsible for the oxidation of acetaldehyde generated during alcohol oxidation in vivo.	Acetaldehyde	88-100	aldehyde dehydrogenase 2 family member	Homo sapiens	38-43
9309319-0	1997	Catalase mediates acetaldehyde formation from ethanol in fetal and neonatal rat brain.	Acetaldehyde	18-30	catalase	Rattus norvegicus	0-8
9309300-2	1997	Cytochrome P-4502E1 (CYP2E1), a liver microsomal enzyme, also metabolizes acetaldehyde and ethanol.	Acetaldehyde	74-86	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	21-27
9309874-6	1997	The activities of the ALDH2-active and ALDH2-inactive phenotypes at 200 microM acetaldehyde were determined to be 1.06 +/- 0.13 and 0.71 +/- 0.07 U/g tissue, respectively.	Acetaldehyde	79-91	aldehyde dehydrogenase 2 family member	Homo sapiens	22-27
9273829-10	1997	RESULTS: Participants with ALDH2*2 alleles had significantly higher blood acetaldehyde levels after ingesting alcoholic and placebo beverages than did participants with ALDH2*1 alleles, despite similar blood alcohol concentrations.	Acetaldehyde	74-86	aldehyde dehydrogenase 2 family member	Homo sapiens	27-32
9273829-11	1997	CONCLUSIONS: Blood acetaldehyde levels rather than blood alcohol concentration may mediate enhanced alcohol sensitivity among Asians with ALDH2*2 alleles.	Acetaldehyde	19-31	aldehyde dehydrogenase 2 family member	Homo sapiens	138-143
9328169-4	1997	Previous research has revealed that acetaldehyde can be formed from ethanol via microbial alcohol dehydrogenase.	Acetaldehyde	36-48	aldo-keto reductase family 1 member A1	Homo sapiens	90-111
26735784-2	1997	It is argued that acetaldehyde may be formed in brain through the peroxidatic activity of catalase.	Acetaldehyde	18-30	catalase	Homo sapiens	90-98
26735791-0	1997	The effect of acetaldehyde on human brain transketolase activity.	Acetaldehyde	14-26	transketolase	Homo sapiens	42-55
26735791-3	1997	In the present investigation the direct effect of ACH was studied on the activity of transketolase, a thiaminedependent enzyme, as well as two non-thiamine-dependent enzymes (aspartate aminotransferase and lactate dehydrogenase), isolated from five control human brains.	Acetaldehyde	50-53	transketolase	Homo sapiens	85-98
26735791-4	1997	The concentration of ACH required to inhibit 50% activity of holo- and apo-transketolase was 80 mM and 60 mM, respectively, whereas that for aspartate aminotransferase and lactate dehydrogenase was 14 mM and 10 mM, respectively.	Acetaldehyde	21-24	transketolase	Homo sapiens	75-88
26735791-7	1997	In vitro studies with homogenates pre-treated with ACH in the presence of various concentrations of glutathione showed that the latter had a protective effect against loss of transketolase activity.	Acetaldehyde	51-54	transketolase	Homo sapiens	175-188
9309874-6	1997	The activities of the ALDH2-active and ALDH2-inactive phenotypes at 200 microM acetaldehyde were determined to be 1.06 +/- 0.13 and 0.71 +/- 0.07 U/g tissue, respectively.	Acetaldehyde	79-91	aldehyde dehydrogenase 2 family member	Homo sapiens	39-44
9185762-2	1997	In this study, assays for immunoglobulin (Ig) A, IgG, and IgM antibodies to acetaldehyde-derived adducts were performed on sera of 140 alcohol consumers, 19 patients with nonalcoholic liver disease (NALD), 35 healthy nondrinking controls, and 10 nondrinking patients with IgA or IgG myeloma.	Acetaldehyde	76-88	immunoglobulin heavy variable 4-38-2-like	Homo sapiens	26-47
9234667-8	1997	Acetaldehyde accumulated through the competitive regeneration of NADH via GPDH.	Acetaldehyde	0-12	glycerol-3-phosphate dehydrogenase	Saccharomyces cerevisiae S288C	74-78
9241662-10	1997	We conclude that the alcohol drinking preference between the B6 and D2 inbred mouse strains is independent of the Ah receptor-but is genetically determined, in part, by the level of brain catalase activity which, in turn, regulates brain acetaldehyde concentrations.	Acetaldehyde	238-250	defensin beta 2	Mus musculus	61-70
9154890-6	1997	Two major volatile factors in cigarette smoke, acrolein and acetaldehyde, augmented IL-8 release.	Acetaldehyde	60-72	C-X-C motif chemokine ligand 8	Homo sapiens	84-88
9161608-1	1997	Ethanol and its metabolite acetaldehyde have been shown to stimulate immunoreactive beta-endorphin (IR-beta-EP) secretion from hypothalamic neurons in primary cultures.	Acetaldehyde	27-39	proopiomelanocortin	Homo sapiens	84-98
9161608-1	1997	Ethanol and its metabolite acetaldehyde have been shown to stimulate immunoreactive beta-endorphin (IR-beta-EP) secretion from hypothalamic neurons in primary cultures.	Acetaldehyde	27-39	proopiomelanocortin	Homo sapiens	103-110
9161608-6	1997	Acetaldehyde stimulated IR-beta-EP secretion from this culture for a period of 48 hr, but the IR-beta-EP secretory response to acetaldehyde reduced gradually with time during the first 48-hr period and reached the basal level at 72 hr.	Acetaldehyde	0-12	proopiomelanocortin	Homo sapiens	27-34
9161608-6	1997	Acetaldehyde stimulated IR-beta-EP secretion from this culture for a period of 48 hr, but the IR-beta-EP secretory response to acetaldehyde reduced gradually with time during the first 48-hr period and reached the basal level at 72 hr.	Acetaldehyde	127-139	proopiomelanocortin	Homo sapiens	97-104
9161608-8	1997	However, reduced IR- beta-EP secretory response to acetaldehyde with time was associated with the time-dependent increase in cell death.	Acetaldehyde	51-63	proopiomelanocortin	Homo sapiens	21-28
9161608-11	1997	These results suggest that (i) chronic treatment with ethanol desensitizes beta-EP-secreting neurons due to reduced cellular functions and (ii) chronic acetaldehyde reduces beta-EP neurotransmission due to cell death.	Acetaldehyde	152-164	proopiomelanocortin	Homo sapiens	173-180
9160798-1	1997	Ethanol is metabolized in the brain by catalase/H2O2 to yield acetaldehyde and by an ethanol-inducible form of cytochrome P450 (P450 IIE1) in a reaction that yields oxygen radicals.	Acetaldehyde	62-74	catalase	Rattus norvegicus	39-47
28715099-1	1997	Ethanol and its metabolite acetaldehyde have been shown to stimulate immunoreactive beta-endorphin (IR-beta-EP) secretion from hypothalamic neurons in primary cultures.	Acetaldehyde	27-39	proopiomelanocortin	Homo sapiens	84-98
9113263-5	1997	The addition of the cytochrome P-450 inhibitor, cimetidine, significantly reduced the amount of acetaldehyde accumulating from ethanol when hepatocytes were incubated with either antipyrine or aminopyrine.	Acetaldehyde	96-108	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	20-36
9171333-11	1997	In addition, GPD2 is induced under aerobic conditions by the addition of bisulfite which causes NADH accumulation by inhibiting the final, reductive step in ethanol fermentation and this induction is reversed by addition of acetaldehyde.	Acetaldehyde	224-236	glycerol-3-phosphate dehydrogenase (NAD(+)) GPD2	Saccharomyces cerevisiae S288C	13-17
9113263-9	1997	The results suggest that cytochrome P-450-generated metabolites of antipyrine and aminopyrine cause an inhibition of the low K(m) mitochondrial aldehyde dehydrogenase and thus an accumulation of acetaldehyde from ethanol.	Acetaldehyde	195-207	cytochrome P450, family 2, subfamily g, polypeptide 1	Rattus norvegicus	25-41
9113263-9	1997	The results suggest that cytochrome P-450-generated metabolites of antipyrine and aminopyrine cause an inhibition of the low K(m) mitochondrial aldehyde dehydrogenase and thus an accumulation of acetaldehyde from ethanol.	Acetaldehyde	195-207	aldehyde dehydrogenase 2 family member	Rattus norvegicus	130-166
9463245-4	1997	The correlation of alcohol dehydrogenase activity to that of aldehyde dehydrogenase in the process of formation and development of alcoholism is shifted towards the progressive accumulation of acetaldehyde.	Acetaldehyde	193-205	aldo-keto reductase family 1 member A1	Homo sapiens	19-40
9102206-2	1997	The atypical genotypes of low Km aldehyde dehydrogenase (ALDH2) have higher blood concentrations of free acetaldehyde after drinking alcohol.	Acetaldehyde	105-117	aldehyde dehydrogenase 2 family member	Homo sapiens	57-62
9102206-3	1997	We measured levels of acetaldehyde reversibly bound to hemoglobin (HbAA) after drinking 0.4 ml/kg ethanol using fluorigenic high performance liquid chromatography method in volunteers with the two major ALDH2 genotypes.	Acetaldehyde	22-34	aldehyde dehydrogenase 2 family member	Homo sapiens	203-208
9077581-5	1997	In F2 males, hepatic microsomal high Km ALDH activities correlated negatively with blood acetaldehyde concentrations, indicating that low activity of this isoenzyme in ANA rats could be at least in part responsible for the accumulation of acetaldehyde in their blood.	Acetaldehyde	89-101	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	40-44
9077581-5	1997	In F2 males, hepatic microsomal high Km ALDH activities correlated negatively with blood acetaldehyde concentrations, indicating that low activity of this isoenzyme in ANA rats could be at least in part responsible for the accumulation of acetaldehyde in their blood.	Acetaldehyde	239-251	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	40-44
9077581-6	1997	Finally, F2 rats that possessed the cytosolic ALDH isoenzyme pattern most frequently found in the AA rat line drank significantly more ethanol than the animals with typical ANA pattern, suggesting that this polymorphism might also be relevant in the regulation of voluntary ethanol drinking although it is probably not associated with acetaldehyde metabolism.	Acetaldehyde	335-347	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	46-50
9041238-7	1997	The activities of the ALDH2-inactive phenotypes were significantly lower than that of the ALDH2-active phenotypes at 200 micromol/L acetaldehyde.	Acetaldehyde	132-144	aldehyde dehydrogenase 2 family member	Homo sapiens	22-27
9041238-7	1997	The activities of the ALDH2-inactive phenotypes were significantly lower than that of the ALDH2-active phenotypes at 200 micromol/L acetaldehyde.	Acetaldehyde	132-144	aldehyde dehydrogenase 2 family member	Homo sapiens	90-95
12223614-2	1997	The key point of this technique is the use of a gelatin-acetaldehyde adduct, which is synthesized under 1 mM acetaldehyde and 10 mM NaCNBH3, to pre-coat plate wells to obtain the proper binding parameters for the quantification of APA in seed proteins.	Acetaldehyde	56-68	glutamyl aminopeptidase	Homo sapiens	231-234
9023260-0	1997	Acetaldehyde as well as ethanol is metabolized by human CYP2E1.	Acetaldehyde	0-12	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	56-62
9023260-10	1997	Among the 10 forms of human cytochrome P450 expressed in yeast, CYP2E1 had especially high acetaldehyde oxidation activity.	Acetaldehyde	91-103	cytochrome P450, family 2, subfamily e, polypeptide 1	Rattus norvegicus	64-70
9023260-12	1997	These results indicate that hepatic CYP2E1 mainly contributes to MAOS in rats and humans, the pathway of which may play an alternative role against acetaldehyde in the liver after alcohol consumption together with acetaldehyde dehydrogenase in the metabolism of acetaldehyde.	Acetaldehyde	148-160	cytochrome P450, family 2, subfamily e, polypeptide 1	Rattus norvegicus	36-42
9023260-12	1997	These results indicate that hepatic CYP2E1 mainly contributes to MAOS in rats and humans, the pathway of which may play an alternative role against acetaldehyde in the liver after alcohol consumption together with acetaldehyde dehydrogenase in the metabolism of acetaldehyde.	Acetaldehyde	214-226	cytochrome P450, family 2, subfamily e, polypeptide 1	Rattus norvegicus	36-42
12223614-8	1997	The APA content also increased as viability decreased in five species of seeds, which were aged naturally without exposure to acetaldehyde.	Acetaldehyde	126-138	glutamyl aminopeptidase	Homo sapiens	4-7
9011144-2	1996	The predicting 95% confidence bounds determined on regression analysis of the data suggested that after venous injection of ethanol, the blood ethanol and acetaldehyde concentrations in a volunteer normal homozygous for ALDH2 (ALDH2*1/1) were significantly lower than that heterozygous (ALDH2*1/2).	Acetaldehyde	155-167	aldehyde dehydrogenase 2 family member	Homo sapiens	220-225
11667845-5	1996	Accordingly, addition to alpha-ODPS acetaldehyde 10.2 in the presence of InCl(3) leads to the adduct 10.3 as an inseparable 90:10 mixture of anti and syn diastereomers.	Acetaldehyde	36-48	synemin	Homo sapiens	150-153
8988806-2	1996	The total -SH groups were decreased whereas the specific activities of glutathione-S-transferase [GST] and glutathione peroxidase [GPo] were increased in acetaldehyde treated rats.	Acetaldehyde	154-166	hematopoietic prostaglandin D synthase	Rattus norvegicus	71-96
8988806-2	1996	The total -SH groups were decreased whereas the specific activities of glutathione-S-transferase [GST] and glutathione peroxidase [GPo] were increased in acetaldehyde treated rats.	Acetaldehyde	154-166	hematopoietic prostaglandin D synthase	Rattus norvegicus	98-101
8941476-11	1996	We speculate the trait of acetaldehyde accumulation on ALDH2 inactivity may favor mitochondrial DNA abnormalities, thereby worsening ATP production and impairing insulin secretion.	Acetaldehyde	26-38	aldehyde dehydrogenase 2 family member	Homo sapiens	55-60
8941476-11	1996	We speculate the trait of acetaldehyde accumulation on ALDH2 inactivity may favor mitochondrial DNA abnormalities, thereby worsening ATP production and impairing insulin secretion.	Acetaldehyde	26-38	insulin	Homo sapiens	162-169
26735438-7	1997	In the upper gastrointestinal tract the production of acetaldehyde and free radicals via cytochrome P450 2E1 and via alcohol dehydrogenase may lead to tissue damage and to secondary hyper-regeneration.	Acetaldehyde	54-66	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	89-108
8986205-2	1996	ADH isozyme activities were determined in endoscopic biopsies of the gastric corpus from 24 Japanese and 41 Caucasian men by starch gel electrophoresis and by comparing the reduction of m-nitrobenzaldehyde (a preferred substrate of sigma-ADH) with that of acetaldehyde (a preferred substrate of gamma-ADH) and the glutathione-dependent formaldehyde oxidation (a specific reaction of chi-ADH).	Acetaldehyde	256-268	alcohol dehydrogenase 1A (class I), alpha polypeptide	Homo sapiens	0-3
9011144-2	1996	The predicting 95% confidence bounds determined on regression analysis of the data suggested that after venous injection of ethanol, the blood ethanol and acetaldehyde concentrations in a volunteer normal homozygous for ALDH2 (ALDH2*1/1) were significantly lower than that heterozygous (ALDH2*1/2).	Acetaldehyde	155-167	aldehyde dehydrogenase 2 family member	Homo sapiens	227-232
9011144-2	1996	The predicting 95% confidence bounds determined on regression analysis of the data suggested that after venous injection of ethanol, the blood ethanol and acetaldehyde concentrations in a volunteer normal homozygous for ALDH2 (ALDH2*1/1) were significantly lower than that heterozygous (ALDH2*1/2).	Acetaldehyde	155-167	aldehyde dehydrogenase 2 family member	Homo sapiens	227-232
9011144-3	1996	And the blood ethanol and acetaldehyde concentrations in a volunteer with C2 allele (C1/C2) were significantly lower than that in (C1/1).	Acetaldehyde	26-38	heterogeneous nuclear ribonucleoprotein C	Homo sapiens	85-90
9011144-5	1996	It is possible that the ALDH2*1 and C2 alleles may correspond to the lower blood ethanol and acetaldehyde concentrations after intravenous administrations of 0.2 g /kg of ethanol.	Acetaldehyde	93-105	aldehyde dehydrogenase 2 family member	Homo sapiens	24-29
8949960-2	1996	However, the mechanisms behind the changes in the carbohydrate moiety of transferrin are unclear, although they have been suggested to be mediated by acetaldehyde or liver damage.	Acetaldehyde	150-162	transferrin	Rattus norvegicus	73-84
8949949-0	1996	A hypothesis linking hypoglycemia, hyperuricemia, lactic acidemia, and reduced gluconeogenesis in alcoholics to inactivation of glucose-6-phosphatase activity by acetaldehyde.	Acetaldehyde	162-174	glucose-6-phosphatase catalytic subunit 1	Homo sapiens	128-149
8949949-1	1996	Preliminary data have been obtained indicating that glucose-6-phosphatase is inactivated upon preincubation with 447 and 224 mM acetaldehyde for 30 min at room temperature, resulting in a loss of 67% and 33% of the original activity, respectively.	Acetaldehyde	128-140	glucose-6-phosphatase catalytic subunit 1	Homo sapiens	52-73
8892513-0	1996	In vitro alcohol dehydrogenase-mediated acetaldehyde production by aerobic bacteria representing the normal colonic flora in man.	Acetaldehyde	40-52	aldo-keto reductase family 1 member A1	Homo sapiens	9-30
8892513-9	1996	The alcohol dehydrogenase activity varied from 606 +/- 91 nmol/min/mg protein (Escherichia coli IH 50546) to 1 +/- 0.2 nmol/min/mg protein (E. coli IH 50817), and acetaldehyde formation varied from 1,717 +/- 2 nmol acetaldehyde/10(9) colony-forming units (Klebsiella oxytoca IH 35403) to 5 +/- 2 nmol acetaldehyde/10(9) colony-forming units (Pseudomonas aeruginosa ATCC 27853).	Acetaldehyde	163-175	aldo-keto reductase family 1 member A1	Homo sapiens	4-25
8892513-9	1996	The alcohol dehydrogenase activity varied from 606 +/- 91 nmol/min/mg protein (Escherichia coli IH 50546) to 1 +/- 0.2 nmol/min/mg protein (E. coli IH 50817), and acetaldehyde formation varied from 1,717 +/- 2 nmol acetaldehyde/10(9) colony-forming units (Klebsiella oxytoca IH 35403) to 5 +/- 2 nmol acetaldehyde/10(9) colony-forming units (Pseudomonas aeruginosa ATCC 27853).	Acetaldehyde	215-227	aldo-keto reductase family 1 member A1	Homo sapiens	4-25
8903472-6	1996	The inactive form of ALDH2, encoded by the gene ALDH2*1/2*2 prevalent in Orientals, exposes them to higher blood levels of acetaldehyde, a recognized animal carcinogen, after drinking.	Acetaldehyde	123-135	aldehyde dehydrogenase 2 family member	Homo sapiens	21-26
8903472-6	1996	The inactive form of ALDH2, encoded by the gene ALDH2*1/2*2 prevalent in Orientals, exposes them to higher blood levels of acetaldehyde, a recognized animal carcinogen, after drinking.	Acetaldehyde	123-135	aldehyde dehydrogenase 2 family member	Homo sapiens	48-53
8892513-9	1996	The alcohol dehydrogenase activity varied from 606 +/- 91 nmol/min/mg protein (Escherichia coli IH 50546) to 1 +/- 0.2 nmol/min/mg protein (E. coli IH 50817), and acetaldehyde formation varied from 1,717 +/- 2 nmol acetaldehyde/10(9) colony-forming units (Klebsiella oxytoca IH 35403) to 5 +/- 2 nmol acetaldehyde/10(9) colony-forming units (Pseudomonas aeruginosa ATCC 27853).	Acetaldehyde	215-227	aldo-keto reductase family 1 member A1	Homo sapiens	4-25
8865957-0	1996	Relationship between alcohol intake and immunoglobulin a immunoreactivity with acetaldehyde-modified bovine serum albumin.	Acetaldehyde	79-91	albumin	Homo sapiens	108-121
8892513-10	1996	There was a statistically significant correlation (r = 0.77; p &lt; 0.001) between alcohol dehydrogenase activity and acetaldehyde production from ethanol, strongly suggesting the catalytic role of bacterial alcohol dehydrogenase in this reaction.	Acetaldehyde	118-130	aldo-keto reductase family 1 member A1	Homo sapiens	83-104
8892513-10	1996	There was a statistically significant correlation (r = 0.77; p &lt; 0.001) between alcohol dehydrogenase activity and acetaldehyde production from ethanol, strongly suggesting the catalytic role of bacterial alcohol dehydrogenase in this reaction.	Acetaldehyde	118-130	aldo-keto reductase family 1 member A1	Homo sapiens	208-229
8892520-4	1996	Catalase inhibitors sodium azide (SA) and 3-amino-1,2,4-triazole (3-AT) had little effect on ADH activity but markedly decreased catalase activity and acetaldehyde formation (1 mM of SA to 56 +/- 13% of control, 5 mM of 3-AT to 67 +/- 3% of control; mean +/- SE).	Acetaldehyde	151-163	catalase	Rattus norvegicus	0-8
8797832-0	1996	Structural characterisation of acetaldehyde adducts formed by a synthetic peptide mimicking the N-terminus of the hemoglobin beta-chain under reducing and nonreducing conditions.	Acetaldehyde	31-43	hemoglobin subunit beta	Homo sapiens	114-129
8865957-6	1996	The IgA adduct-specific reactivity (IgA reactivity with acetaldehyde-modified bovine serum albumin-reactivity with native bovine serum albumin) showed a moderate correlation with self-reported alcohol intake, but did not correlate with markers such as plasma transaminase, gamma-glutamyltransferase activity, or mean corpuscular volume.	Acetaldehyde	56-68	albumin	Homo sapiens	85-98
8865957-6	1996	The IgA adduct-specific reactivity (IgA reactivity with acetaldehyde-modified bovine serum albumin-reactivity with native bovine serum albumin) showed a moderate correlation with self-reported alcohol intake, but did not correlate with markers such as plasma transaminase, gamma-glutamyltransferase activity, or mean corpuscular volume.	Acetaldehyde	56-68	albumin	Homo sapiens	129-142
8660697-5	1996	Pretreatment of activated stellate cells with antibodies to TGFbeta1 suppressed the effect of acetaldehyde in increasing the alpha1(I) collagen message, indicating that TGFbeta1 mediates the effect of the acetaldehyde-induced increase in the expression of the alpha1(I) collagen gene which also contains NF-I binding sites.	Acetaldehyde	94-106	transforming growth factor, beta 1	Rattus norvegicus	60-68
8660697-5	1996	Pretreatment of activated stellate cells with antibodies to TGFbeta1 suppressed the effect of acetaldehyde in increasing the alpha1(I) collagen message, indicating that TGFbeta1 mediates the effect of the acetaldehyde-induced increase in the expression of the alpha1(I) collagen gene which also contains NF-I binding sites.	Acetaldehyde	205-217	transforming growth factor, beta 1	Rattus norvegicus	60-68
8660697-5	1996	Pretreatment of activated stellate cells with antibodies to TGFbeta1 suppressed the effect of acetaldehyde in increasing the alpha1(I) collagen message, indicating that TGFbeta1 mediates the effect of the acetaldehyde-induced increase in the expression of the alpha1(I) collagen gene which also contains NF-I binding sites.	Acetaldehyde	205-217	transforming growth factor, beta 1	Rattus norvegicus	169-177
8727253-2	1996	The capacity of colonic mucosa to remove this bacterial acetaldehyde by aldehyde dehydrogenase (ALDH) is, however, poorly known.	Acetaldehyde	56-68	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	72-94
8663198-9	1996	RalDH(II) does not recognize citral, benzaldehyde, acetaldehyde, and propanal efficiently as substrates, but does metabolize octanal and decanal efficiently.	Acetaldehyde	51-63	aldehyde dehydrogenase 1 family, member A2	Rattus norvegicus	0-9
8640660-5	1996	The multiplicity of their esophageal carcinoma and their concurrent UADT cancer was compared with their genotype for aldehyde dehydrogenase-2 (ALDH2), the major determinant of blood acetaldehyde concentration after drinking.	Acetaldehyde	182-194	aldehyde dehydrogenase 2 family member	Homo sapiens	117-141
8640660-5	1996	The multiplicity of their esophageal carcinoma and their concurrent UADT cancer was compared with their genotype for aldehyde dehydrogenase-2 (ALDH2), the major determinant of blood acetaldehyde concentration after drinking.	Acetaldehyde	182-194	aldehyde dehydrogenase 2 family member	Homo sapiens	143-148
8727250-5	1996	Alcohol dehydrogenase (ADH), predominantly a hepatic cytosolic enzyme, may be more important than CYP2E1 in the oxidation of ethanol to acetaldehyde.	Acetaldehyde	136-148	aldo-keto reductase family 1 member A1	Homo sapiens	0-21
8727250-5	1996	Alcohol dehydrogenase (ADH), predominantly a hepatic cytosolic enzyme, may be more important than CYP2E1 in the oxidation of ethanol to acetaldehyde.	Acetaldehyde	136-148	aldo-keto reductase family 1 member A1	Homo sapiens	23-26
8734840-8	1996	The result also suggests that, due to lacking activity of low K(m) ALDH2 and ALDH1, cytotoxic metabolite acetaldehyde may be involved in the etiology of alcohol-related oral injury.	Acetaldehyde	105-117	aldehyde dehydrogenase 2 family member	Homo sapiens	67-72
8727250-5	1996	Alcohol dehydrogenase (ADH), predominantly a hepatic cytosolic enzyme, may be more important than CYP2E1 in the oxidation of ethanol to acetaldehyde.	Acetaldehyde	136-148	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	98-104
8727253-2	1996	The capacity of colonic mucosa to remove this bacterial acetaldehyde by aldehyde dehydrogenase (ALDH) is, however, poorly known.	Acetaldehyde	56-68	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	96-100
8727253-6	1996	Rat colonic mucosa was found to possess detectable amounts of ALDH activity with both micromolar and millimolar acetaldehyde concentrations and in all subcellular fractions.	Acetaldehyde	112-124	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	62-66
8727253-10	1996	ALDH activity of the colonic mucosa should, thus, be sufficient for the removal of acetaldehyde produced by colonic mucosal ADH during ethanol oxidation.	Acetaldehyde	83-95	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	0-4
8605194-4	1996	Thus, for human ALDH-1, the Km value for acetaldehyde is 180 +/- 10 micromolar, whereas those for hamster ALDH-1 and rat ALDH-1 are 12 +/- 3 and 15 +/- 3 micromolar, respectively.	Acetaldehyde	41-53	aldehyde dehydrogenase 1 family member A1	Homo sapiens	16-22
8781384-4	1996	About 50% of Oriental people are deficient in the aldehyde-dehydrogenase 2 isozyme (ALDH2) that can most efficiently detoxify acetaldehyde.	Acetaldehyde	126-138	aldehyde dehydrogenase 2 family member	Homo sapiens	50-74
8781384-4	1996	About 50% of Oriental people are deficient in the aldehyde-dehydrogenase 2 isozyme (ALDH2) that can most efficiently detoxify acetaldehyde.	Acetaldehyde	126-138	aldehyde dehydrogenase 2 family member	Homo sapiens	84-89
8621158-7	1996	Because a negative correlation between Apo A-I and liver fibrosis is amplified in alcoholic patients, we investigated whether the in vitro formation of Apo A-I/acetaldehyde complex (adducts) increased the binding of Apo A-I to the ECM.	Acetaldehyde	160-172	apolipoprotein A1	Homo sapiens	152-159
8621158-7	1996	Because a negative correlation between Apo A-I and liver fibrosis is amplified in alcoholic patients, we investigated whether the in vitro formation of Apo A-I/acetaldehyde complex (adducts) increased the binding of Apo A-I to the ECM.	Acetaldehyde	160-172	apolipoprotein A1	Homo sapiens	152-159
8621158-8	1996	We showed that the amount of Apo A-I that bound to FN was significantly higher with acetaldehyde-modified Apo A-I (OD = 2.18 +/- 0.19, P = .01) than with native Apo A-I.	Acetaldehyde	84-96	apolipoprotein A1	Homo sapiens	29-36
8621158-8	1996	We showed that the amount of Apo A-I that bound to FN was significantly higher with acetaldehyde-modified Apo A-I (OD = 2.18 +/- 0.19, P = .01) than with native Apo A-I.	Acetaldehyde	84-96	fibronectin 1	Homo sapiens	51-53
8621158-8	1996	We showed that the amount of Apo A-I that bound to FN was significantly higher with acetaldehyde-modified Apo A-I (OD = 2.18 +/- 0.19, P = .01) than with native Apo A-I.	Acetaldehyde	84-96	apolipoprotein A1	Homo sapiens	106-113
8621158-8	1996	We showed that the amount of Apo A-I that bound to FN was significantly higher with acetaldehyde-modified Apo A-I (OD = 2.18 +/- 0.19, P = .01) than with native Apo A-I.	Acetaldehyde	84-96	apolipoprotein A1	Homo sapiens	106-113
8605194-10	1996	Apparently, in human liver, only mitochondrial ALDH oxidizes acetaldehyde at physiological concentrations, whereas in hamster or rat liver, both the mitochondrial and cytosolic isozymes will do so.	Acetaldehyde	61-73	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	47-51
8605195-1	1996	Human mitochondrial aldehyde dehydrogenase (ALDH-2) has a Km for acetaldehyde that is 900-fold lower than that for the cytosolic isozyme, ALDH-1.	Acetaldehyde	65-77	aldehyde dehydrogenase 2 family member	Homo sapiens	44-50
8605194-4	1996	Thus, for human ALDH-1, the Km value for acetaldehyde is 180 +/- 10 micromolar, whereas those for hamster ALDH-1 and rat ALDH-1 are 12 +/- 3 and 15 +/- 3 micromolar, respectively.	Acetaldehyde	41-53	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	16-20
8605195-1	1996	Human mitochondrial aldehyde dehydrogenase (ALDH-2) has a Km for acetaldehyde that is 900-fold lower than that for the cytosolic isozyme, ALDH-1.	Acetaldehyde	65-77	aldehyde dehydrogenase 1 family member A1	Homo sapiens	138-144
8605195-6	1996	Addition of one of these tight-binding, slow-turnover substrates to a reaction mixture containing ALDH, NAD+, and a "reference" aldehyde substrate (e.g. acetaldehyde) blocks the principal (reference) enzymatic reaction temporarily and reversibly.	Acetaldehyde	153-165	aldehyde dehydrogenase 1 family member A1	Homo sapiens	98-102
8605195-11	1996	Vitamin A1 aldehydes are specific natural substrates for ALDH-1; at pH 7.5, for all-trans- and 13-cis-retinal, Km = 1.1 and 0.37 micromolar, respectively, and kcat/Km is 50-100 times higher than that for acetaldehyde.	Acetaldehyde	204-216	aldehyde dehydrogenase 1 family member A1	Homo sapiens	57-63
8568140-4	1996	METHODS: An oral ethanol challenge test, a leukocyte histamine release test, and an ELISA for detection of IgE specific to acetaldehyde-human serum albumin conjugate were carried out in 42 adults with bronchial asthma and nine healthy adults.	Acetaldehyde	123-135	immunoglobulin heavy constant epsilon	Homo sapiens	107-110
8730209-10	1996	Thus, the induction of CYP2E1 by ethanol in these cells could cause significant changes in intracellular acetaldehyde concentrations which, together with increased lipid peroxidation, may contribute to the development of alcoholic liver injury.	Acetaldehyde	105-117	cytochrome P450, family 2, subfamily e, polypeptide 1	Rattus norvegicus	23-29
8691480-1	1996	Recent evidence suggests that intraneuronal metabolism of ethanol by catalase/H2O2 and an ethanol-inducible form of cytochrome P450 together generate acetaldehyde and oxygen radicals including the hydroxyl radical (HO.).	Acetaldehyde	150-162	catalase	Homo sapiens	69-77
8737012-9	1996	Our data indicate that catalase-mediated oxidation of ethanol to acetaldehyde takes place mainly in aminergic neurons, which seem to have a limited capacity for the subsequent removal via aldehyde dehydrogenase.	Acetaldehyde	65-77	catalase	Rattus norvegicus	23-31
8850269-2	1996	To help elucidate this problem and develop an implementable preventive strategy, this genetic epidemiological study focused on aldehyde dehydrogenase 2 (ALDH2), the key enzyme for elimination of acetaldehyde generated by alcohol consumption.	Acetaldehyde	195-207	aldehyde dehydrogenase 2 family member	Homo sapiens	127-151
8850269-2	1996	To help elucidate this problem and develop an implementable preventive strategy, this genetic epidemiological study focused on aldehyde dehydrogenase 2 (ALDH2), the key enzyme for elimination of acetaldehyde generated by alcohol consumption.	Acetaldehyde	195-207	aldehyde dehydrogenase 2 family member	Homo sapiens	153-158
8850269-6	1996	The results strongly suggest that because persons who have this mutant ALDH2*2 allele have a high concentration of blood acetaldehyde after drinking alcohol, acetaldehyde (a recognized animal carcinogen) plays a pivotal role in the pathogenesis of alcohol-related esophageal cancer in humans.	Acetaldehyde	121-133	aldehyde dehydrogenase 2 family member	Homo sapiens	71-76
8850269-6	1996	The results strongly suggest that because persons who have this mutant ALDH2*2 allele have a high concentration of blood acetaldehyde after drinking alcohol, acetaldehyde (a recognized animal carcinogen) plays a pivotal role in the pathogenesis of alcohol-related esophageal cancer in humans.	Acetaldehyde	158-170	aldehyde dehydrogenase 2 family member	Homo sapiens	71-76
12893477-4	1996	Pre-treatment of acute ethanol-dosed rats with cyanamide (ALDH inhibitor) was designed to raise acetaldehyde levels.	Acetaldehyde	96-108	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	58-62
8550030-0	1996	Identification of the 37-kd rat liver protein that forms an acetaldehyde adduct in vivo as delta 4-3-ketosteroid 5 beta-reductase.	Acetaldehyde	60-72	aldo-keto reductase family 1, member D1	Rattus norvegicus	91-129
8814645-2	1996	Upon preincubation of the serum with 89.4, 223.5, and 447 mM acetaldehyde at room temperature for 30 min, a reduction in 26.8%, 55.3%, and 75.8% aminopeptidase A activity was observed.	Acetaldehyde	61-73	glutamyl aminopeptidase	Homo sapiens	145-161
8814645-3	1996	Similarly, aminopeptidase M activity was reduced by 26.5% and 53.1% upon preincubation with 223.5 and 447 mM acetaldehyde.	Acetaldehyde	109-121	alanyl aminopeptidase, membrane	Homo sapiens	11-27
8814645-5	1996	Because aminopeptidase A and aminopeptidase M also degrade the pressor substance, angiotensin II, it is suggested that inhibition of aminopeptidase A- and aminopeptidase M-like activity by acetaldehyde, the product of ethanol metabolism, may lead to higher levels of circulating angiotensin II and, consequently, hypertension, in alcoholics.	Acetaldehyde	189-201	glutamyl aminopeptidase	Homo sapiens	8-24
8814645-5	1996	Because aminopeptidase A and aminopeptidase M also degrade the pressor substance, angiotensin II, it is suggested that inhibition of aminopeptidase A- and aminopeptidase M-like activity by acetaldehyde, the product of ethanol metabolism, may lead to higher levels of circulating angiotensin II and, consequently, hypertension, in alcoholics.	Acetaldehyde	189-201	alanyl aminopeptidase, membrane	Homo sapiens	29-45
8814645-5	1996	Because aminopeptidase A and aminopeptidase M also degrade the pressor substance, angiotensin II, it is suggested that inhibition of aminopeptidase A- and aminopeptidase M-like activity by acetaldehyde, the product of ethanol metabolism, may lead to higher levels of circulating angiotensin II and, consequently, hypertension, in alcoholics.	Acetaldehyde	189-201	angiotensinogen	Homo sapiens	82-96
8814645-5	1996	Because aminopeptidase A and aminopeptidase M also degrade the pressor substance, angiotensin II, it is suggested that inhibition of aminopeptidase A- and aminopeptidase M-like activity by acetaldehyde, the product of ethanol metabolism, may lead to higher levels of circulating angiotensin II and, consequently, hypertension, in alcoholics.	Acetaldehyde	189-201	glutamyl aminopeptidase	Homo sapiens	133-149
8814645-5	1996	Because aminopeptidase A and aminopeptidase M also degrade the pressor substance, angiotensin II, it is suggested that inhibition of aminopeptidase A- and aminopeptidase M-like activity by acetaldehyde, the product of ethanol metabolism, may lead to higher levels of circulating angiotensin II and, consequently, hypertension, in alcoholics.	Acetaldehyde	189-201	alanyl aminopeptidase, membrane	Homo sapiens	155-171
8814645-6	1996	The hydrolysis of lysine-p-nitroanilide, an aminopeptidase B substrate, was also inhibited upon addition of acetaldehyde to Moni-Trol ES serum.	Acetaldehyde	108-120	arginyl aminopeptidase	Homo sapiens	44-60
8814648-4	1996	The formation of significant amounts of acetaldehyde the brain in vivo after ethanol ingestion and by what mechanism has not been clearly established, although catalase is a promising candidate.	Acetaldehyde	40-52	catalase	Homo sapiens	160-168
8651460-2	1996	Cytochrome P4502E1 (CYP2E1) catalyzes the oxidation of ethanol, producing acetaldehyde and free radicals capable of reacting with and peroxidizing cell membranes.	Acetaldehyde	74-86	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	0-18
8651460-2	1996	Cytochrome P4502E1 (CYP2E1) catalyzes the oxidation of ethanol, producing acetaldehyde and free radicals capable of reacting with and peroxidizing cell membranes.	Acetaldehyde	74-86	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	20-26
8742318-10	1996	Activities of glutathione S-transferase and glutathione reductase after 3 days of exposure to acrolein, alone or in combination with formaldehyde and acetaldehyde, were depressed whereas the glutathione peroxidase activity was elevated.	Acetaldehyde	150-162	hematopoietic prostaglandin D synthase	Rattus norvegicus	14-39
8742318-10	1996	Activities of glutathione S-transferase and glutathione reductase after 3 days of exposure to acrolein, alone or in combination with formaldehyde and acetaldehyde, were depressed whereas the glutathione peroxidase activity was elevated.	Acetaldehyde	150-162	glutathione-disulfide reductase	Rattus norvegicus	44-65
8632758-12	1996	Because fetal CYP2E1 mediates ethanol metabolism, the enzyme may play a pivotal role in the local production of acetaldehyde and free radicals, both of which have potential deleterious effects on the developing fetus.	Acetaldehyde	112-124	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	14-20
12893455-0	1996	Acetaldehyde metabolism by liver mitochondrial ALDH from UChA and UChB rats: effect of inhibitors.	Acetaldehyde	0-12	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	47-51
12893455-5	1996	AcH metabolism by liver mitochondrial aldehyde dehydrogenase (ALDH) was studied by following AcH disappearance rate and the formation of NADH at 340 nm in the incubation medium.	Acetaldehyde	0-3	aldehyde dehydrogenase 2 family member	Rattus norvegicus	24-60
12893455-5	1996	AcH metabolism by liver mitochondrial aldehyde dehydrogenase (ALDH) was studied by following AcH disappearance rate and the formation of NADH at 340 nm in the incubation medium.	Acetaldehyde	0-3	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	62-66
12893455-5	1996	AcH metabolism by liver mitochondrial aldehyde dehydrogenase (ALDH) was studied by following AcH disappearance rate and the formation of NADH at 340 nm in the incubation medium.	Acetaldehyde	93-96	aldehyde dehydrogenase 2 family member	Rattus norvegicus	24-60
12893455-5	1996	AcH metabolism by liver mitochondrial aldehyde dehydrogenase (ALDH) was studied by following AcH disappearance rate and the formation of NADH at 340 nm in the incubation medium.	Acetaldehyde	93-96	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	62-66
9018378-9	1996	The ALDH1 enzyme had a pI of 7.45 and exhibited a low Km (6.37 microM) for retinal, while the ALDH2 enzyme was found to have very low Km for acetaldehyde (0.98 microM).	Acetaldehyde	141-153	aldehyde dehydrogenase 1 family member A1	Bos taurus	4-9
9018378-9	1996	The ALDH1 enzyme had a pI of 7.45 and exhibited a low Km (6.37 microM) for retinal, while the ALDH2 enzyme was found to have very low Km for acetaldehyde (0.98 microM).	Acetaldehyde	141-153	aldehyde dehydrogenase 2 family member	Bos taurus	94-99
8785998-6	1996	This higher activity of ADH in the rectum could result in increased acetaldehyde levels after alcohol administration and could therefore play a role, at least in part, in the ethanol-associated rectal cocarcinogenesis.	Acetaldehyde	68-80	aldo-keto reductase family 1 member A1	Homo sapiens	24-27
8568140-4	1996	METHODS: An oral ethanol challenge test, a leukocyte histamine release test, and an ELISA for detection of IgE specific to acetaldehyde-human serum albumin conjugate were carried out in 42 adults with bronchial asthma and nine healthy adults.	Acetaldehyde	123-135	albumin	Homo sapiens	142-155
8823990-5	1995	Treatment with recombinant HGF led to enhanced [3H]thymidine incorporation by cells treated with ethanol or acetaldehyde as well as by those left untreated, with no significant differences in the rates of increase among these three cell groups.	Acetaldehyde	108-120	hepatocyte growth factor	Homo sapiens	27-30
8522518-5	1995	Consistent with this hypothesis, the inhibitory effects of acetaldehyde and propionaldehyde on the growth of this polA mutant were demonstrated.	Acetaldehyde	59-71	DNA polymerase I	Salmonella enterica subsp. enterica serovar Typhimurium str. LT2	114-118
8522518-6	1995	A derivative of the polA mutant unable to synthesize glutathione (GSH) was markedly more sensitive to acetaldehyde and propionaldehyde than was the polA mutant proficient in GSH synthesis.	Acetaldehyde	102-114	DNA polymerase I	Salmonella enterica subsp. enterica serovar Typhimurium str. LT2	20-24
8747406-3	1995	Cytochrome P4502E1 (CYP2E1) metabolizes alcohol to acetaldehyde and the hydroxyethyl radical, and is also inducible by alcohol.	Acetaldehyde	51-63	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	20-26
7632171-3	1995	Brain catalase increased significantly after acetaldehyde or chronic ethanol administration although there were no other significant changes in the total brain activity of superoxide dismutase, glutathione peroxidase or glutathione reductase.	Acetaldehyde	45-57	catalase	Rattus norvegicus	6-14
8554727-1	1995	Aldehyde dehydrogenase with a low Michaelis constant (Km), ALDH2, is a major enzyme involved in the conversion of acetaldehyde, a toxic metabolite of ethanol, into acetic acid in the liver.	Acetaldehyde	114-126	aldehyde dehydrogenase 2 family member	Homo sapiens	59-64
7583533-8	1995	The short- and longer-chain saturated aldehydes acetaldehyde and hexanal and the dialdehyde MDA were considerably less effective at inhibiting LCAT than were acrolein and HNE.	Acetaldehyde	48-60	lecithin-cholesterol acyltransferase	Homo sapiens	143-147
7557863-1	1995	Alcohol dehydrogenase (ADH), aldehyde dehydrogenase (ALDH), and P450IIE1 are the primary enzymes that catalyze the conversion of ethanol to acetaldehyde and then to acetate.	Acetaldehyde	140-152	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	23-26
7646056-7	1995	Furthermore, the level of acetaldehyde produced during ethanol oxidation was augmented by cyanamide, an inhibitor of acetaldehyde oxidation, while the ability of these cells to metabolize ethanol was inhibited by pyrazole, an inhibitor of alcohol dehydrogenase.	Acetaldehyde	26-38	aldo-keto reductase family 1 member A1	Homo sapiens	239-260
8690709-5	1995	A decreased activity of the microsomal G-6-Pase was also observed when the microsomes were incubated with aldehydes such as malondialdehyde, n-heptaldehyde, acetaldehyde, and trans-2-nonenal.	Acetaldehyde	157-169	glucose-6-phosphatase catalytic subunit 1	Rattus norvegicus	39-47
7485842-5	1995	The reaction with acetaldehyde in vitro resulted in a significant increase in fast-eluting minor hemoglobin species on cation exchange chromatography concomitant with increased acetaldehyde in the HbA1a+b, HbA1c, and HbA1-AcH fractions.	Acetaldehyde	18-30	hemoglobin subunit alpha 1	Homo sapiens	197-201
7485842-5	1995	The reaction with acetaldehyde in vitro resulted in a significant increase in fast-eluting minor hemoglobin species on cation exchange chromatography concomitant with increased acetaldehyde in the HbA1a+b, HbA1c, and HbA1-AcH fractions.	Acetaldehyde	177-189	hemoglobin subunit alpha 1	Homo sapiens	197-201
7485842-6	1995	We report three new cation exchange chromatographic peaks after reaction with acetaldehyde: HbA1-AcH-3, HbA1c-1, and HbA0-1.	Acetaldehyde	78-90	hemoglobin subunit alpha 1	Homo sapiens	92-96
7473602-8	1995	Acetaldehyde was the weakest inhibitor of LCAT, with 85% enzyme inhibition at 50 mM.	Acetaldehyde	0-12	lecithin-cholesterol acyltransferase	Homo sapiens	42-46
7480358-0	1995	Ethanol and acetaldehyde metabolism in chinese with different aldehyde dehydrogenase-2 genotypes.	Acetaldehyde	12-24	aldehyde dehydrogenase 2 family member	Homo sapiens	62-86
7480358-8	1995	The mutant homozygotes of ALDH2*2/*2 and the heterozygotes exhibited significantly higher peak acetaldehyde concentrations and also greater areas under the blood concentrations-time curve (AUC) than did the normal homozygotes of ALDH2*1/*1, with the mutant homozygotes both being the largest.	Acetaldehyde	95-107	aldehyde dehydrogenase 2 family member	Homo sapiens	26-31
7546332-2	1995	The present study addressed this issue by using an alcohol dehydrogenase (ADH) inhibitor, 4-methylpyrazole (4-MP), that works by blocking the metabolism of alcohol to its primary metabolite acetaldehyde, thereby prolonging the actions of alcohol while minimizing the generation of acetaldehyde.	Acetaldehyde	190-202	aldo-keto reductase family 1 member A1	Rattus norvegicus	51-72
7546332-2	1995	The present study addressed this issue by using an alcohol dehydrogenase (ADH) inhibitor, 4-methylpyrazole (4-MP), that works by blocking the metabolism of alcohol to its primary metabolite acetaldehyde, thereby prolonging the actions of alcohol while minimizing the generation of acetaldehyde.	Acetaldehyde	190-202	aldo-keto reductase family 1 member A1	Rattus norvegicus	74-77
7546332-2	1995	The present study addressed this issue by using an alcohol dehydrogenase (ADH) inhibitor, 4-methylpyrazole (4-MP), that works by blocking the metabolism of alcohol to its primary metabolite acetaldehyde, thereby prolonging the actions of alcohol while minimizing the generation of acetaldehyde.	Acetaldehyde	281-293	aldo-keto reductase family 1 member A1	Rattus norvegicus	51-72
7546332-2	1995	The present study addressed this issue by using an alcohol dehydrogenase (ADH) inhibitor, 4-methylpyrazole (4-MP), that works by blocking the metabolism of alcohol to its primary metabolite acetaldehyde, thereby prolonging the actions of alcohol while minimizing the generation of acetaldehyde.	Acetaldehyde	281-293	aldo-keto reductase family 1 member A1	Rattus norvegicus	74-77
7768510-5	1995	Nuclear proteins extracted from NIH 3T3 cells, or myofibroblastlike cells, 36 hours after the addition of acetaldehyde (200 mumol/L) in serum-free media showed increased binding to the consensus sequence of the NF-I binding site by DNase I protection analysis and by electrophoretic mobility shift assay (EMSA) as compared with control nuclear extracts that were not exposed to acetaldehyde.	Acetaldehyde	106-118	deoxyribonuclease I	Mus musculus	232-239
7768510-5	1995	Nuclear proteins extracted from NIH 3T3 cells, or myofibroblastlike cells, 36 hours after the addition of acetaldehyde (200 mumol/L) in serum-free media showed increased binding to the consensus sequence of the NF-I binding site by DNase I protection analysis and by electrophoretic mobility shift assay (EMSA) as compared with control nuclear extracts that were not exposed to acetaldehyde.	Acetaldehyde	378-390	deoxyribonuclease I	Mus musculus	232-239
7840785-6	1995	Two injections of acetaldehyde (300 mg/kg), given 18 and 2 hr prior to tissue preparation, caused a specific reduction of glutamine synthetase in the striatum and a decrease of GSH levels in both striatum and cerebellum.	Acetaldehyde	18-30	glutamate-ammonia ligase	Rattus norvegicus	122-142
7696266-11	1995	These results, together with the cimetidine inhibition kinetics of acetaldehyde reduction by sigma sigma and beta 2 beta 2, with either varied NADH or varied acetaldehyde, are consistent with cimetidine binding to two enzyme species.	Acetaldehyde	67-79	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	116-122
7887984-10	1995	The substrate (acetaldehyde, 80 microM) and cofactor (NAD, 0.5 mM) together completely protected ALDH from inhibition by MeDTC sulfone; substrate alone partially protected the enzyme.	Acetaldehyde	15-27	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	97-101
7639949-0	1995	Modification of VLDL apoprotein B by acetaldehyde alters apoprotein B metabolism.	Acetaldehyde	37-49	apolipoprotein B	Oryctolagus cuniculus	21-33
7639949-0	1995	Modification of VLDL apoprotein B by acetaldehyde alters apoprotein B metabolism.	Acetaldehyde	37-49	apolipoprotein B	Oryctolagus cuniculus	57-69
7625563-4	1995	In this study, we used FAB/MS to analyze the products of peptide-AAs (pep-AAs) formed by incubating acetaldehyde with Hb peptides.	Acetaldehyde	100-112	FA complementation group B	Homo sapiens	23-26
7625566-0	1995	Effect of ethanol, propanol, butanol, and catalase enzyme blockers on beta-endorphin secretion from primary cultures of hypothalamic neurons: evidence for a mediatory role of acetaldehyde in ethanol stimulation of beta-endorphin release.	Acetaldehyde	175-187	proopiomelanocortin	Homo sapiens	214-228
7625566-1	1995	Previously, we have shown that low doses of ethanol (12.5-100 mM) and acetaldehyde (12.5-50 microM), but not salsolinol, enhanced immunoreactive beta-endorphin (IR-beta-EP) secretion from fetal hypothalamic neurons in primary culture.	Acetaldehyde	70-82	proopiomelanocortin	Homo sapiens	145-159
7625567-0	1995	Acetaldehyde-serum protein adducts inhibit interleukin-2 secretion in concanavalin A-stimulated murine splenocytes: a potential common pathway for ethanol-induced immunomodulation.	Acetaldehyde	0-12	interleukin 2	Mus musculus	43-56
7625567-10	1995	Although cell viability was unchanged, acetaldehyde-treated FBS mixed with native FBS decreased IL-2 secretion in a dose-dependent manner.	Acetaldehyde	39-51	interleukin 2	Mus musculus	96-100
7625567-11	1995	The percentage of cells expressing IL-2R was reduced only at the highest acetaldehyde-FBS dose.	Acetaldehyde	73-85	interleukin 2 receptor, alpha chain	Mus musculus	35-40
7625567-12	1995	Therefore, immunological effects ascribed to ethanol may result in part from the toxic properties of acetaldehyde-protein adducts on IL-2 secretion.	Acetaldehyde	101-113	interleukin 2	Mus musculus	133-137
7726572-3	1995	Some authors have suggested that the oxidation of acetaldehyde by aldehyde oxidase (AO) may be responsible for oxyradical generation during ethanol metabolism.	Acetaldehyde	50-62	aldehyde oxidase 1	Homo sapiens	66-82
7726572-3	1995	Some authors have suggested that the oxidation of acetaldehyde by aldehyde oxidase (AO) may be responsible for oxyradical generation during ethanol metabolism.	Acetaldehyde	50-62	aldehyde oxidase 1	Homo sapiens	84-86
7726572-4	1995	In this study we demonstrated that AO acts not only upon acetaldehyde but also upon NADH, with superoxide anion radical (O2.-) formation.	Acetaldehyde	57-69	aldehyde oxidase 1	Homo sapiens	35-37
7726572-5	1995	The apparent Km of NADH for AO was approximately 28 microM, a much smaller value than the one reported for acetaldehyde (1 mM).	Acetaldehyde	107-119	aldehyde oxidase 1	Homo sapiens	28-30
7772270-0	1995	Acetaldehyde-modified lysozyme function: its potential implication in the promotion of infection in alcoholics.	Acetaldehyde	0-12	lysozyme	Homo sapiens	22-30
7772270-1	1995	Incubation of lysozyme with acetaldehyde (0.44 M) at room temperature for 2 h produces a 62% inhibition of enzymic activity.	Acetaldehyde	28-40	lysozyme	Homo sapiens	14-22
7772270-5	1995	These results suggest the possibility that inactivation of a fraction of the lysozyme activity by acetaldehyde may decrease the effectiveness of the enzyme in chronic alcoholics, thereby leading to an increased potential for susceptibility to bacterial infection.	Acetaldehyde	98-110	lysozyme	Homo sapiens	77-85
7887984-1	1995	Disulfiram inhibits hepatic aldehyde dehydrogenase (ALDH) causing an accumulation of acetaldehyde after ethanol ingestion.	Acetaldehyde	85-97	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	52-56
7887984-5	1995	Therefore, we investigated the effects of MeDTC sulfone on the activity of rat hepatic low Km mitochondrial ALDH, the major enzyme in the metabolism of acetaldehyde.	Acetaldehyde	152-164	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	108-112
24226516-1	1994	The transition state (TS) for loss of CH4 from protonated acetaldehyde has been located at the second-order Moller-Plesset (MP2)/6-31G(d, p) level of theory.	Acetaldehyde	58-70	tryptase pseudogene 1	Homo sapiens	124-127
7748514-6	1995	Cysteine and NAC, upon addition to plasma prior to the addition of AcH, exhibited a prolongation of clotting time compared to that of AcH alone.	Acetaldehyde	67-70	X-linked Kx blood group	Homo sapiens	13-16
7748514-6	1995	Cysteine and NAC, upon addition to plasma prior to the addition of AcH, exhibited a prolongation of clotting time compared to that of AcH alone.	Acetaldehyde	134-137	X-linked Kx blood group	Homo sapiens	13-16
7809835-1	1995	BACKGROUND: With the ex vivo perfused canine pancreas preparation, the infusion of acetaldehyde, the primary metabolite of ethanol oxidation, plus a short period of ischemia to convert xanthine dehydrogenase to xanthine oxidase, results in the physiologic injury response of acute pancreatitis (edema, weight gain, hyperamylasemia).	Acetaldehyde	83-95	xanthine dehydrogenase	Canis lupus familiaris	185-207
7695788-3	1994	Blood acetaldehyde levels scarcely increased in the subjects homozygous for ALDH2*1, regardless of their ADH2 genotypes (ADH2*1/*1, ADH2*1/*2 and ADH2*2/*2).	Acetaldehyde	6-18	aldehyde dehydrogenase 2 family member	Homo sapiens	76-81
7990120-2	1994	N1-Allylchlorpropamide 3 was, as expected, a potent inhibitor of hepatic AlDH in rats, as indicated by the 4-fold increase in the levels of ethanol-derived blood acetaldehyde relative to that elicited by chlorpropamide itself.	Acetaldehyde	162-174	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	73-77
7865150-0	1994	Interaction of acetaldehyde with plasma proteins of the renin-angiotensin system.	Acetaldehyde	15-27	renin	Rattus norvegicus	56-61
7865150-5	1994	Preincubation of NEPEX plasma with 0.2 M acetaldehyde at 4 degrees C for 2 h resulted in a 21% increase in the angiotensin I (A I) formation by the rat plasma renin and 27% increase in the A I formation by the trypsinized rat plasma renin.	Acetaldehyde	41-53	renin	Rattus norvegicus	159-164
7865150-5	1994	Preincubation of NEPEX plasma with 0.2 M acetaldehyde at 4 degrees C for 2 h resulted in a 21% increase in the angiotensin I (A I) formation by the rat plasma renin and 27% increase in the A I formation by the trypsinized rat plasma renin.	Acetaldehyde	41-53	renin	Rattus norvegicus	233-238
7865150-6	1994	When the rat plasma which contains modest quantities of endogenous angiotensinogen in addition to renin was preincubated with 0.2 M acetaldehyde at 4 degrees C for 2 h, the rate of A I formation was increased by 10%.	Acetaldehyde	132-144	renin	Rattus norvegicus	98-103
7704432-0	1994	Comparison of the effects of alcohol and acetaldehyde on proopiomelanocortin mRNA levels and beta-endorphin secretion from hypothalamic neurons in primary cultures.	Acetaldehyde	41-53	proopiomelanocortin	Homo sapiens	57-76
7704432-1	1994	The effects of acute and chronic treatments with ethanol and acute treatments with an ethanol metabolite, acetaldehyde, on proopiomelanocortin (POMC) mRNA expression were compared with those of these agents on the secretion of a POMC gene product, beta-endorphin (beta-EP) peptide.	Acetaldehyde	106-118	proopiomelanocortin	Homo sapiens	123-142
7704432-1	1994	The effects of acute and chronic treatments with ethanol and acute treatments with an ethanol metabolite, acetaldehyde, on proopiomelanocortin (POMC) mRNA expression were compared with those of these agents on the secretion of a POMC gene product, beta-endorphin (beta-EP) peptide.	Acetaldehyde	106-118	proopiomelanocortin	Homo sapiens	144-148
7704432-3	1994	Treatment of hypothalamic cells with 25-, 50-, and 100-mM doses of ethanol or 12.5 and 25 microM acetaldehyde for 3 h increased POMC mRNA levels.	Acetaldehyde	97-109	proopiomelanocortin	Homo sapiens	128-132
7704432-5	1994	Acute treatments with ethanol and acetaldehyde also elevated IR-beta-EP secretion from the cultured neurons for a period of 12 h, and the IR-beta-EP secretory response developed desensitization after 24 h of ethanol incubation.	Acetaldehyde	34-46	proopiomelanocortin	Homo sapiens	64-71
7695788-1	1994	The involvement of genetic polymorphism at the alcohol dehydrogenase 2 (ADH2) and aldehyde dehydrogenase 2 (ALDH2) loci in determining blood acetaldehyde levels and the rate of ethanol elimination after ethanol intake was investigated.	Acetaldehyde	141-153	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	47-70
7695788-1	1994	The involvement of genetic polymorphism at the alcohol dehydrogenase 2 (ADH2) and aldehyde dehydrogenase 2 (ALDH2) loci in determining blood acetaldehyde levels and the rate of ethanol elimination after ethanol intake was investigated.	Acetaldehyde	141-153	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	72-76
7695788-1	1994	The involvement of genetic polymorphism at the alcohol dehydrogenase 2 (ADH2) and aldehyde dehydrogenase 2 (ALDH2) loci in determining blood acetaldehyde levels and the rate of ethanol elimination after ethanol intake was investigated.	Acetaldehyde	141-153	aldehyde dehydrogenase 2 family member	Homo sapiens	82-106
7695788-1	1994	The involvement of genetic polymorphism at the alcohol dehydrogenase 2 (ADH2) and aldehyde dehydrogenase 2 (ALDH2) loci in determining blood acetaldehyde levels and the rate of ethanol elimination after ethanol intake was investigated.	Acetaldehyde	141-153	aldehyde dehydrogenase 2 family member	Homo sapiens	108-113
7865150-8	1994	These results suggest the possibility of a biochemical interaction of acetaldehyde with the renin substrate which may enhance the activity of the RAS cascade, thereby contributing to hypertension in chronic alcoholics.	Acetaldehyde	70-82	renin	Rattus norvegicus	92-97
7695788-4	1994	The acetaldehyde levels in the subjects with the ALDH2*1/*2 heterozygote increased to 23.4 microM on average, and no significant differences were observed between the three ADH2 genotype groups.	Acetaldehyde	4-16	aldehyde dehydrogenase 2 family member	Homo sapiens	49-54
7695788-5	1994	Subjects homozygous for ALDH2*2 showed very high levels of blood acetaldehyde, and the average value was 79.3 microM.	Acetaldehyde	65-77	aldehyde dehydrogenase 2 family member	Homo sapiens	24-29
7695791-2	1994	The development of ALD is genetically controlled and is directly associated with the polymorphisms of the genes of acetaldehyde (Ac-CHO) and ethanol-metabolizing enzymes, aldehyde dehydrogenase-2 (ALDH2) and cytochrome P4502E1.	Acetaldehyde	115-127	aldehyde dehydrogenase 2 family member	Homo sapiens	171-195
7695791-2	1994	The development of ALD is genetically controlled and is directly associated with the polymorphisms of the genes of acetaldehyde (Ac-CHO) and ethanol-metabolizing enzymes, aldehyde dehydrogenase-2 (ALDH2) and cytochrome P4502E1.	Acetaldehyde	115-127	aldehyde dehydrogenase 2 family member	Homo sapiens	197-202
7815709-9	1994	The subjects who belonged to the ALDH2*2/*2 group showed a high blood acetaldehyde level and various psychophysical symptoms.	Acetaldehyde	70-82	aldehyde dehydrogenase 2 family member	Homo sapiens	33-38
7980620-9	1994	In conclusion, the results of the present study support the assumption that line differences in hepatic ADH and ALDH activities may be relevant to the acetaldehyde accumulation and the particularly low ethanol consumption of the ANA rats.	Acetaldehyde	151-163	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	112-116
7821287-0	1994	Mutations induced in the hypoxanthine phosphoribosyl transferase gene by three urban air pollutants: acetaldehyde, benzo[a]pyrene diolepoxide, and ethylene oxide.	Acetaldehyde	101-113	hypoxanthine phosphoribosyltransferase 1	Homo sapiens	25-64
7821287-1	1994	Provisional mutational spectra at the hypoxanthine phosphoribosyl transferase (HPRT) locus in vitro have been worked out for acetaldehyde (AA) and benzo[a]pyrene diolepoxide (BPDE) in human (T)-lymphocytes and for ethylene oxide (EtO) in human diploid fibroblasts using Southern blotting and polymerase chain reaction (PCR)-based DNA sequencing techniques.	Acetaldehyde	125-137	hypoxanthine phosphoribosyltransferase 1	Homo sapiens	38-77
7821287-1	1994	Provisional mutational spectra at the hypoxanthine phosphoribosyl transferase (HPRT) locus in vitro have been worked out for acetaldehyde (AA) and benzo[a]pyrene diolepoxide (BPDE) in human (T)-lymphocytes and for ethylene oxide (EtO) in human diploid fibroblasts using Southern blotting and polymerase chain reaction (PCR)-based DNA sequencing techniques.	Acetaldehyde	125-137	hypoxanthine phosphoribosyltransferase 1	Homo sapiens	79-83
7943667-0	1994	Acetaldehyde exposure causes growth inhibition in a Chinese hamster ovary cell line that expresses alcohol dehydrogenase.	Acetaldehyde	0-12	aldo-keto reductase family 1 member A1	Cricetulus griseus	99-120
7516483-9	1994	Another hprt- mutant, obtained from a T-cell culture treated with acetaldehyde, showed that splice mutation can be caused by a large deletion detectable on Southern blot.	Acetaldehyde	66-78	hypoxanthine phosphoribosyltransferase 1	Homo sapiens	8-12
8066557-8	1994	A correlation was observed between the logarithmic values of PC20-MCh (log PC20-MCh) on the P-S day and the potentiating effect of acetaldehyde on the methacholine responsiveness [(log PC20-MCh on P-A day)-(log PC20-MCh on P-S day)] (rho = 0.82).	Acetaldehyde	131-143	pro-melanin concentrating hormone	Homo sapiens	66-69
8066557-8	1994	A correlation was observed between the logarithmic values of PC20-MCh (log PC20-MCh) on the P-S day and the potentiating effect of acetaldehyde on the methacholine responsiveness [(log PC20-MCh on P-A day)-(log PC20-MCh on P-S day)] (rho = 0.82).	Acetaldehyde	131-143	pro-melanin concentrating hormone	Homo sapiens	80-83
8066557-8	1994	A correlation was observed between the logarithmic values of PC20-MCh (log PC20-MCh) on the P-S day and the potentiating effect of acetaldehyde on the methacholine responsiveness [(log PC20-MCh on P-A day)-(log PC20-MCh on P-S day)] (rho = 0.82).	Acetaldehyde	131-143	pro-melanin concentrating hormone	Homo sapiens	80-83
8066557-8	1994	A correlation was observed between the logarithmic values of PC20-MCh (log PC20-MCh) on the P-S day and the potentiating effect of acetaldehyde on the methacholine responsiveness [(log PC20-MCh on P-A day)-(log PC20-MCh on P-S day)] (rho = 0.82).	Acetaldehyde	131-143	pro-melanin concentrating hormone	Homo sapiens	80-83
7812764-7	1994	By contrast, the condensation products of tryptophan and tryptamine with acetaldehyde scarcely affected TPH activities.	Acetaldehyde	73-85	tryptophan hydroxylase 1	Rattus norvegicus	104-107
7943667-14	1994	Growth inhibition was blocked by the alcohol dehydrogenase inhibitor 4-methylpyrazole, suggesting that acetaldehyde and not ethanol was responsible for growth inhibition in these cells.	Acetaldehyde	103-115	aldo-keto reductase family 1, member A1 (aldehyde reductase)	Mus musculus	37-58
7943668-1	1994	Genetic variation at two polymorphic alcohol dehydrogenase loci, ADH2 and ADH3, and at the polymorphic mitochondrial aldehyde dehydrogenase locus, ALDH2, may influence the risk of developing alcoholism by modulating the rate of elimination of ethanol and the rate of formation and elimination of acetaldehyde.	Acetaldehyde	296-308	aldehyde dehydrogenase 2 family member	Homo sapiens	147-152
8006921-2	1994	About half of the Japanese population have inactive low Km aldehyde dehydrogenase (ALDH2), which metabolizes acetaldehyde to acetic acid at very low concentrations, leading to severe pharmacological effects of aldehyde when drinking alcohol.	Acetaldehyde	109-121	aldehyde dehydrogenase 2 family member	Homo sapiens	83-88
7945571-9	1994	Furthermore, they abolished the stimulatory effect of acetaldehyde on collagen I and fibronectin gene expression by FSCs.	Acetaldehyde	54-66	fibronectin 1	Rattus norvegicus	85-96
7945571-12	1994	We conclude that acetaldehyde increases procollagen I and fibronectin gene transcription in FSCs, possibly through c-fos and c-jun expression, and that PKC may play a regulatory role in this chain of events.	Acetaldehyde	17-29	fibronectin 1	Rattus norvegicus	58-69
7945571-12	1994	We conclude that acetaldehyde increases procollagen I and fibronectin gene transcription in FSCs, possibly through c-fos and c-jun expression, and that PKC may play a regulatory role in this chain of events.	Acetaldehyde	17-29	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	115-120
8060517-0	1994	Acetaldehyde inhibits the anti-elastase activity of alpha 1-antitrypsin.	Acetaldehyde	0-12	serpin family A member 1	Homo sapiens	52-71
8060517-2	1994	The present study was initiated on a biochemical level in order to determine whether acetaldehyde, the major product of ethanol metabolism, is capable of influencing the physiological effect of alpha 1-AT upon elastase, an enzyme which is capable of inducing emphysema.	Acetaldehyde	85-97	serpin family A member 1	Homo sapiens	194-204
8060517-4	1994	Acetaldehyde at 0.3-M and 1.2-M concentrations inhibited the anti-elastase activity of alpha 1-AT.	Acetaldehyde	0-12	serpin family A member 1	Homo sapiens	87-97
8060517-7	1994	These data provide biochemical support for the possibility that heterozygous males with lower than normal alpha 1-AT levels may be at much higher risk to develop liver disease, emphysema, and alpha 1-AT deficiency as a consequence of chronic exposure to ethanol and concomitant circulating acetaldehyde levels.	Acetaldehyde	290-302	serpin family A member 1	Homo sapiens	106-116
7945571-0	1994	Acetaldehyde induces c-fos and c-jun proto-oncogenes in fat-storing cell cultures through protein kinase C activation.	Acetaldehyde	0-12	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	21-26
7945571-2	1994	We previously reported that acetaldehyde stimulates collagen I and fibronectin gene transcription in rat fat-storing cell (FSC) culture.	Acetaldehyde	28-40	fibronectin 1	Rattus norvegicus	67-78
7945571-3	1994	We here evaluated whether acetaldehyde increases Col I and FN gene transcription through the induction of c-fos and c-jun proto-oncogenes and studied the possible role played by protein kinase C (PKC) and c-AMP.	Acetaldehyde	26-38	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	106-111
7945571-5	1994	Acetaldehyde produced a rapid and transient induction of fos mRNA (undetectable at t = 0, peak at t = 45 and still evident at t = 90).	Acetaldehyde	0-12	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	57-60
7945571-8	1994	These inhibitors of PKC activity blocked the stimulatory effect of acetaldehyde on fos and jun mRNA expression.	Acetaldehyde	67-79	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	83-86
8200105-6	1994	Moreover, acetaldehyde significantly decreases the activity of the DNA repair enzyme O6-methylguanine-DNA methyltransferase.	Acetaldehyde	10-22	O-6-methylguanine-DNA methyltransferase	Homo sapiens	85-123
8135774-4	1994	Acetaldehyde inhibited both undulin mRNA and protein expression, whereas it had an opposite (stimulatory) effect on FN synthesis.	Acetaldehyde	0-12	fibronectin 1	Homo sapiens	116-118
8135774-6	1994	Furthermore, TGF-beta 1 antagonized the inhibitory effect of acetaldehyde on undulin production and potentiated the stimulatory effect of acetaldehyde on FN synthesis.	Acetaldehyde	61-73	transforming growth factor beta 1	Homo sapiens	13-23
8135774-6	1994	Furthermore, TGF-beta 1 antagonized the inhibitory effect of acetaldehyde on undulin production and potentiated the stimulatory effect of acetaldehyde on FN synthesis.	Acetaldehyde	138-150	transforming growth factor beta 1	Homo sapiens	13-23
8135774-6	1994	Furthermore, TGF-beta 1 antagonized the inhibitory effect of acetaldehyde on undulin production and potentiated the stimulatory effect of acetaldehyde on FN synthesis.	Acetaldehyde	138-150	fibronectin 1	Homo sapiens	154-156
8294106-5	1994	Acetaldehyde (200 mumol/L) and transforming growth factor-beta 1 (5 ng/ml) activated the wild type promoter.	Acetaldehyde	0-12	transforming growth factor, beta 1	Mus musculus	14-64
7904979-3	1994	The data strongly suggest that genetic variation in both ADH and ALDH may influence drinking behavior and the risk of alcoholism developing through acetaldehyde formation.	Acetaldehyde	148-160	aldo-keto reductase family 1 member A1	Homo sapiens	57-60
8974324-8	1994	Ethanol- and acetaldehyde-oxidizing activities of the liver, lung, and gastrointestinal tract appear to be correlated with their isozyme patterns of ADH and ALDH and with the allozymes.	Acetaldehyde	13-25	aldo-keto reductase family 1 member A1	Homo sapiens	149-152
7549010-0	1994	Inhibitory action of in vitro ethanol and acetaldehyde exposure on LHRH-and phorbol ester-stimulated testosterone secretion by rat testicular interstitial cells.	Acetaldehyde	42-54	gonadotropin releasing hormone 1	Rattus norvegicus	67-71
7549010-5	1994	Acetaldehyde (20 mg %) reduced the amount of testosterone produced by 10(-7) M LHRH and 200 nM PDBu by 59.4 +/- 1.2% and 52.5 +/- 5.4% respectively.	Acetaldehyde	0-12	gonadotropin releasing hormone 1	Rattus norvegicus	79-83
7549010-8	1994	The data presented here suggest that direct ethanol and acetaldehyde exposure results in a reduced ability of the testicular interstitial cells to respond to stimulation of PK-C pathway.	Acetaldehyde	56-68	protein kinase C, gamma	Rattus norvegicus	173-177
8974324-10	1994	These genotyping results support the current notion that genetic variation in ADH and ALDH may influence drinking behavior and susceptibility for alcoholism and possibly alcohol-induced organ injury by modulating the rate of metabolism of ethanol and acetaldehyde.	Acetaldehyde	251-263	aldo-keto reductase family 1 member A1	Homo sapiens	78-81
8974330-10	1994	In addition, the local production of acetaldehyde from ethanol in the oesophagus, where significantly more sigma-ADH is present, may contribute to tissue injury and this may lead to the well known ethanol associated oesophageal cancer development.	Acetaldehyde	37-49	alcohol dehydrogenase 7 (class IV), mu or sigma polypeptide	Homo sapiens	107-116
8974330-11	1994	Various isoenzymes of ADH exist in the colorectum and they are also capable of producing acetaldehyde in amounts sufficient to injure the mucosa.	Acetaldehyde	89-101	alcohol dehydrogenase 7 (class IV), mu or sigma polypeptide	Homo sapiens	22-25
7968224-5	1994	The percentage inhibition of liver ALDH activity generally correlates with the elevation in blood and brain acetaldehyde under these treatment protocols.	Acetaldehyde	108-120	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	35-39
8024462-6	1994	ECL is oxidatively dechlorinated in an NADPH- and O2-dependent reaction, resulting in the formation of acetaldehyde (AC).	Acetaldehyde	103-115	apolipoprotein C4	Rattus norvegicus	0-3
8024462-6	1994	ECL is oxidatively dechlorinated in an NADPH- and O2-dependent reaction, resulting in the formation of acetaldehyde (AC).	Acetaldehyde	117-119	apolipoprotein C4	Rattus norvegicus	0-3
8024462-12	1994	AC was not detected in serum of ECL exposed animals and only slightly enhanced amounts were detected in urine samples from ECL exposed mice, reflecting the high capacities of the AC metabolizing pathways in vivo.	Acetaldehyde	0-2	epistatic circling B C57L/J	Mus musculus	123-126
8024462-12	1994	AC was not detected in serum of ECL exposed animals and only slightly enhanced amounts were detected in urine samples from ECL exposed mice, reflecting the high capacities of the AC metabolizing pathways in vivo.	Acetaldehyde	179-181	epistatic circling B C57L/J	Mus musculus	123-126
8032159-1	1994	Alcohol dehydrogenase (ADH) is best known as the enzyme which catalyzes the reversible oxidation/reduction of ethanol/acetaldehyde.	Acetaldehyde	118-130	aldo-keto reductase family 1 member A1	Homo sapiens	0-21
8032159-1	1994	Alcohol dehydrogenase (ADH) is best known as the enzyme which catalyzes the reversible oxidation/reduction of ethanol/acetaldehyde.	Acetaldehyde	118-130	aldo-keto reductase family 1 member A1	Homo sapiens	23-26
8032149-12	1994	Owing to its high specific activity for ethanol (14 U mg-1) under physiological conditions H. pylori ADH can also effectively produce acetaldehyde at moderate ethanol levels.	Acetaldehyde	134-146	aldo-keto reductase family 1 member A1	Homo sapiens	101-104
8032151-10	1994	Ethanol-inducible cytochrome P450 2E1 (CYP2E1) oxidizes ethanol and acetaldehyde, in addition to over 80 toxicologically important xenobiotics.	Acetaldehyde	68-80	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	18-37
8032151-10	1994	Ethanol-inducible cytochrome P450 2E1 (CYP2E1) oxidizes ethanol and acetaldehyde, in addition to over 80 toxicologically important xenobiotics.	Acetaldehyde	68-80	cytochrome P450 family 2 subfamily E member 1	Homo sapiens	39-45
7934638-0	1994	Acetaldehyde regulates the gene expression of matrix-metalloproteinase-1 and -2 in human fat-storing cells.	Acetaldehyde	0-12	matrix metallopeptidase 1	Homo sapiens	46-79
7934638-2	1994	We studied the effect of acetaldehyde (AcCHO) on gene expression of matrix-metalloproteinase (MMP)-1 (fibroblast type- interstitial collagenase) and MMP-2 (72 kDa gelatinase-type IV collagenase) in comparison with the AcCHO effect on collagen type I and IV synthesis in cultures of fat-storing cells (FSC) isolated from normal human livers.	Acetaldehyde	25-37	matrix metallopeptidase 1	Homo sapiens	68-100
8123215-1	1993	The role of ethanol and its primary metabolite, acetaldehyde, were investigated for their effects upon angiotensin-converting enzyme (ACE) (EC 3.4.15.1), since the enzyme plays a key role in the maintenance of blood pressure homeostasis by transforming angiotensin I into angiotensin II and degrading bradykinin.	Acetaldehyde	48-60	angiotensin I converting enzyme	Bos taurus	134-137
8130882-3	1993	The enzymatic oxidation of ethanol to acetaldehyde by alcohol dehydrogenase was utilized, and the concurrent reduction of NAD+ to NADH was monitored at 340 nm as a measure of the quantity of ethanol injected.	Acetaldehyde	38-50	aldo-keto reductase family 1 member A1	Homo sapiens	54-75
8123215-6	1993	These results suggest that acetaldehyde-mediated ACE inhibition in vivo may play a contributory role in the development of vasodilation and facial flush reaction consequent to ethanol consumption, thereby accounting for localized hypotension.	Acetaldehyde	27-39	angiotensin I converting enzyme	Bos taurus	49-52
8151099-0	1993	Acetaldehyde-protein adducts, but not lactate and pyruvate, stimulate gene transcription of collagen and fibronectin in hepatic fat-storing cells.	Acetaldehyde	0-12	fibronectin 1	Rattus norvegicus	105-116
8151099-2	1993	We previously reported that acetaldehyde, but not ethanol can stimulate type I collagen and fibronectin synthesis in cultures of rat fat-storing cells (FSC) by increasing transcription of the specific genes.	Acetaldehyde	28-40	fibronectin 1	Rattus norvegicus	92-103
8151099-3	1993	The effect of lactate and pyruvate was studied on collagen I, III, fibronectin accumulation by cultured rat FSCs and it was investigated whether acetaldehyde could increase procollagen I and fibronectin gene transcription through the formation of protein adducts.	Acetaldehyde	145-157	fibronectin 1	Rattus norvegicus	191-202
8151099-5	1993	Pyridoxal-phosphate and p-hydroxymecuribenzoate (inhibitors of acetaldehyde-protein adduct formation) blocked the stimulatory effect of acetaldehyde on procollagen I and fibronectin gene transcription.	Acetaldehyde	63-75	fibronectin 1	Rattus norvegicus	170-181
8151099-5	1993	Pyridoxal-phosphate and p-hydroxymecuribenzoate (inhibitors of acetaldehyde-protein adduct formation) blocked the stimulatory effect of acetaldehyde on procollagen I and fibronectin gene transcription.	Acetaldehyde	136-148	fibronectin 1	Rattus norvegicus	170-181
8279674-1	1993	A fast-eluting minor variant of hemoglobin A, designated as HbA1-AcH, appears elevated after the incubation of red blood cell hemolysates with acetaldehyde (AcH) and has been proposed as a diagnostic marker for alcoholism or as an indicator for heavy drinking.	Acetaldehyde	65-68	hemoglobin subunit alpha 1	Homo sapiens	60-64
8279674-1	1993	A fast-eluting minor variant of hemoglobin A, designated as HbA1-AcH, appears elevated after the incubation of red blood cell hemolysates with acetaldehyde (AcH) and has been proposed as a diagnostic marker for alcoholism or as an indicator for heavy drinking.	Acetaldehyde	143-155	hemoglobin subunit alpha 1	Homo sapiens	60-64
8279674-1	1993	A fast-eluting minor variant of hemoglobin A, designated as HbA1-AcH, appears elevated after the incubation of red blood cell hemolysates with acetaldehyde (AcH) and has been proposed as a diagnostic marker for alcoholism or as an indicator for heavy drinking.	Acetaldehyde	157-160	hemoglobin subunit alpha 1	Homo sapiens	60-64
8279674-4	1993	HbA1-AcH and several others, including two peaks in the HbA1a+b cluster, Hb Pre-A1c, and HbA1d3 were significantly increased by AcH incubation, and the changes were only partially reversible with time.	Acetaldehyde	5-8	hemoglobin subunit alpha 1	Homo sapiens	0-4
8279674-4	1993	HbA1-AcH and several others, including two peaks in the HbA1a+b cluster, Hb Pre-A1c, and HbA1d3 were significantly increased by AcH incubation, and the changes were only partially reversible with time.	Acetaldehyde	128-131	hemoglobin subunit alpha 1	Homo sapiens	0-4
8393265-2	1993	After transformation into acetaldehyde, the metabolism of this compound by xanthine oxidase or by aldehyde oxidase also generates oxygen radicals.	Acetaldehyde	26-38	aldehyde oxidase 1	Homo sapiens	98-114
8221058-3	1993	Ibotenic acid lesions of the amygdaloid central nucleus (ACe), but not the lateral and basolateral amygdala, diminished the magnitude of the reduction in renal PBR binding caused by stress.	Acetaldehyde	57-60	translocator protein	Rattus norvegicus	160-163
8160299-6	1993	The apparent values Km and V have been calculated for aldehyde dehydrogenase 1 in people and aldehyde dehydrogenase 2 in rats when using acetaldehyde and NAD as the reaction substrates.	Acetaldehyde	137-149	aldehyde dehydrogenase 2 family member	Homo sapiens	93-117
8371070-10	1993	This suggests that acetaldehyde reacts with apoB prior to its secretion from the liver and that the altered VLDL are partially removed prior to their conversion to LDL.	Acetaldehyde	19-31	apolipoprotein B	Homo sapiens	44-48
8371070-11	1993	In conclusion, alcoholics develop acetaldehyde adducts in apoB-containing lipoproteins, particularly VLDL.	Acetaldehyde	34-46	apolipoprotein B	Homo sapiens	58-62
8290656-1	1993	About half of Chinese individuals lack mitochondrial aldehyde dehydrogenase-2 (ALDH2) activity, which is responsible for the oxidation of acetaldehyde produced during ethanol metabolism.	Acetaldehyde	138-150	aldehyde dehydrogenase 2 family member	Homo sapiens	79-84
8330298-9	1993	Acetaldehyde increased only the cirrhogenous effect of CCl4.	Acetaldehyde	0-12	C-C motif chemokine ligand 4	Rattus norvegicus	55-59
8353517-8	1993	Although larvae and adults use different ALDH activities to detoxify acetaldehyde (from ADH and ALDH enzymes, respectively) both of them are cytosolic.	Acetaldehyde	69-81	Aldehyde dehydrogenase	Drosophila melanogaster	41-45
8353517-8	1993	Although larvae and adults use different ALDH activities to detoxify acetaldehyde (from ADH and ALDH enzymes, respectively) both of them are cytosolic.	Acetaldehyde	69-81	Aldehyde dehydrogenase	Drosophila melanogaster	96-100
8333599-9	1993	We conclude that: (1) Hb-AA has the potential of being a good marker for alcohol abuse, and (2) the site of Hb that is modified by acetaldehyde in vivo is primarily located in a surface-accessible domain near the center of the beta-chain of HbA where several lysine residues are clustered.	Acetaldehyde	131-143	keratin 90, pseudogene	Homo sapiens	241-244
8471082-3	1993	Ethanol is oxidized to acetaldehyde by alcohol dehydrogenase, catalase and the microsomal ethanol oxidizing system (MEOS).	Acetaldehyde	23-35	catalase	Mus musculus	62-70
8003124-1	1993	At least four types of aldehyde dehydrogenase (ALDH) isozymes exist in human liver: acetaldehyde (Ac-CHO) is metabolized mainly by ALDH2.	Acetaldehyde	84-96	aldehyde dehydrogenase 2 family member	Homo sapiens	131-136
8003131-5	1993	CYP1A2 and CYP2E1 had high rates of acetaldehyde formation.	Acetaldehyde	36-48	cytochrome P450, family 1, subfamily a, polypeptide 2	Rattus norvegicus	0-6
8516360-3	1993	In this study, we examined whether this polymorphism of ALDH2 was the underlying cause for the previously reported acetaldehyde accumulation in the alcohol-avoiding ANA rat line and, thus, could be one of the factors explaining the differences in alcohol drinking behavior between the ANA and the alcohol-preferring AA rat lines.	Acetaldehyde	115-127	aldehyde dehydrogenase 2 family member	Rattus norvegicus	56-61
8488982-8	1993	Because the presence of high activity and high Km mu-ADHs as well as low-activity ALDH1 were found in human esophageal mucosa, it is suggested that there may exist an accumulation of intracellular acetaldehyde during alcohol ingestion.	Acetaldehyde	197-209	aldehyde dehydrogenase 1 family member A1	Homo sapiens	82-87
8330019-4	1993	Acetaldehyde formed "in vitro" unstable and stable adducts with Golgi membrane proteins and with purified galactosyltransferase.	Acetaldehyde	0-12	glycoprotein alpha-galactosyltransferase 1	Rattus norvegicus	106-127
8512495-10	1993	All the homozygotes and heterozygotes with the ALDH2*2 allele exhibited facial flushing, and the former showed a marked increase in blood acetaldehyde level and the latter did a mild increase.	Acetaldehyde	138-150	aldehyde dehydrogenase 2 family member	Homo sapiens	47-52
8512495-11	1993	On the other hand, the influence of the ADH2 genotype on blood acetaldehyde level was not significant.	Acetaldehyde	63-75	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	40-44
8003131-5	1993	CYP1A2 and CYP2E1 had high rates of acetaldehyde formation.	Acetaldehyde	36-48	cytochrome P450, family 2, subfamily e, polypeptide 1	Rattus norvegicus	11-17
8141920-5	1993	The spot for transferrin also shifted to the more basic side by treatment with acetaldehyde for 3 hr or by additional treatment for 3 hr following pretreatment with ethanol for 6 hr.	Acetaldehyde	79-91	transferrin	Rattus norvegicus	13-24
8123704-0	1993	Effects of acetaldehyde on glucose-6-phosphate dehydrogenase activity and mRNA levels in primary rat hepatocytes in culture.	Acetaldehyde	11-23	glucose-6-phosphate dehydrogenase	Rattus norvegicus	27-60
1524418-7	1992	Oxidation of 1,2-propanediol to formaldehyde plus acetaldehyde involved interaction with an oxidant derived from H2O2 plus nonheme iron, since production of the two aldehydic products was completely prevented by catalase or glutathione plus glutathione peroxidase and by chelators such as desferrioxamine or EDTA.	Acetaldehyde	50-62	catalase	Rattus norvegicus	212-220
7992014-3	1993	The main role in alcohol metabolism is being payed by cytosolic enzyme, alcohol dehydrogenase, which catalyses metabolism of ethanol to acetaldehyde.	Acetaldehyde	136-148	aldo-keto reductase family 1 member A1	Homo sapiens	72-93
1451979-6	1992	These results indicate that IgA antibodies to a 200-kilodalton acetaldehyde-protein adduct are present in a large proportion of patients with alcoholic liver disease and in a significantly smaller proportion of other individuals.	Acetaldehyde	63-75	immunoglobulin heavy variable 4-38-2-like	Homo sapiens	28-31
1418661-3	1992	Acetaldehyde oxidation was measured by the disappearance rate in presence of the intact or disrupted mitochondria (AlDH activity) by gas chromatography.	Acetaldehyde	0-12	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	115-119
1435747-4	1992	Immunization of mice with acetaldehyde-protein condensates, followed by adoptive transfer of splenocytes, led to the production of IgE anti-acetaldehyde adducts.	Acetaldehyde	26-38	immunoglobulin heavy constant epsilon	Homo sapiens	131-134
1435747-4	1992	Immunization of mice with acetaldehyde-protein condensates, followed by adoptive transfer of splenocytes, led to the production of IgE anti-acetaldehyde adducts.	Acetaldehyde	140-152	immunoglobulin heavy constant epsilon	Homo sapiens	131-134
1524455-3	1992	The present study documented the efficiency of the acetaldehyde-induced hemoglobin fraction, ie, HbA1ach in heavy drinkers, aspartate aminotransferase in alcoholics, and, additionally, mean corpuscular volume and gamma-glutamyltransferase in both groups of alcohol abusers.	Acetaldehyde	51-63	hemoglobin subunit alpha 1	Homo sapiens	97-101
1306115-7	1992	The ALDH2 gene encodes the major liver mitochondrial ALDH2 which has a very low Km for acetaldehyde.	Acetaldehyde	87-99	aldehyde dehydrogenase 2 family member	Homo sapiens	4-9
1306115-7	1992	The ALDH2 gene encodes the major liver mitochondrial ALDH2 which has a very low Km for acetaldehyde.	Acetaldehyde	87-99	aldehyde dehydrogenase 2 family member	Homo sapiens	53-58
1524530-3	1992	The acetaldehyde intake group (AcH) was given a 2% aqueous solution of acetaldehyde for the first time on the first day of pregnancy.	Acetaldehyde	4-16	acyl-CoA thioesterase 12	Rattus norvegicus	31-34
1524530-3	1992	The acetaldehyde intake group (AcH) was given a 2% aqueous solution of acetaldehyde for the first time on the first day of pregnancy.	Acetaldehyde	71-83	acyl-CoA thioesterase 12	Rattus norvegicus	31-34
1590750-9	1992	The results suggest that individuals with high Vmax beta 2-ADH and deficient in low-Km mitochondrial ALDH2, accounting for approximately 45% of the Chinese population, may end up with acetaldehyde accumulation during alcohol consumption, rendering them vulnerable to tissue injury caused by this highly reactive and toxic metabolite.	Acetaldehyde	184-196	aldo-keto reductase family 1 member A1	Homo sapiens	59-62
1590750-9	1992	The results suggest that individuals with high Vmax beta 2-ADH and deficient in low-Km mitochondrial ALDH2, accounting for approximately 45% of the Chinese population, may end up with acetaldehyde accumulation during alcohol consumption, rendering them vulnerable to tissue injury caused by this highly reactive and toxic metabolite.	Acetaldehyde	184-196	aldehyde dehydrogenase 2 family member	Homo sapiens	101-106
1759148-2	1991	One factor governing the production of acetaldehyde is the genetically determined pattern of class I alcohol dehydrogenase isoenzymes, consisting of "fast" beta 2 and gamma 1 and "slow" beta 1 and gamma 2 subunits.	Acetaldehyde	39-51	potassium calcium-activated channel subfamily M regulatory beta subunit 2	Homo sapiens	156-192
1551237-1	1992	We developed a simple, kinetic method for the determination of catalase activity in which i) the enzyme catalyzes the peroxidation of ethanol by hydrogen peroxide to acetaldehyde and water, and ii) the acetaldehyde so formed is rapidly oxidized to acetic acid and NADPH by the addition of an excess of NADP+ and aldehyde dehydrogenase.	Acetaldehyde	166-178	catalase	Homo sapiens	63-71
1551237-1	1992	We developed a simple, kinetic method for the determination of catalase activity in which i) the enzyme catalyzes the peroxidation of ethanol by hydrogen peroxide to acetaldehyde and water, and ii) the acetaldehyde so formed is rapidly oxidized to acetic acid and NADPH by the addition of an excess of NADP+ and aldehyde dehydrogenase.	Acetaldehyde	202-214	catalase	Homo sapiens	63-71
1580923-0	1992	Acetaldehyde, ethanol and acetone concentrations in blood of alcohol-treated mice receiving aldehyde dehydrogenase-loaded erythrocytes.	Acetaldehyde	0-12	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	92-114
1615467-8	1992	AcH adducts formation severely impaired platelet aggregation and shape change induced by ADP, collagen and thrombin.	Acetaldehyde	0-3	coagulation factor II, thrombin	Homo sapiens	107-115
1292933-2	1992	The Km of ALDH1 for retinal is about 0.06 mumol/l at pH 7.5, and the catalytic efficiency (Vmax/Km) for retinal is about 600 times higher than that for acetaldehyde.	Acetaldehyde	152-164	aldehyde dehydrogenase 1 family member A1	Homo sapiens	10-15
1822117-0	1991	Acetaldehyde as a substrate for ethanol-inducible cytochrome P450 (CYP2E1).	Acetaldehyde	0-12	cytochrome P450, family 2, subfamily e, polypeptide 1	Rattus norvegicus	67-73
1898355-5	1991	In hepatocytes from fed rats the Flux Control Coefficient for alcohol dehydrogenase decreases with increasing acetaldehyde concentration.	Acetaldehyde	110-122	aldo-keto reductase family 1 member A1	Rattus norvegicus	62-83
1898355-6	1991	This suggests that, as acetaldehyde concentrations rise, control of the pathway shifts from alcohol dehydrogenase to other enzymes, particularly aldehyde dehydrogenase.	Acetaldehyde	23-35	aldo-keto reductase family 1 member A1	Rattus norvegicus	92-113
1822117-4	1991	Gas chromatographic/mass spectrometric analysis of products formed from [2H4]-acetaldehyde with CYP2E1-containing reconstituted membrane vesicles revealed the formation of acetate as the only detectable product, although other water soluble products were also formed as evidenced from incubations with [1,2-14C]acetaldehyde.	Acetaldehyde	78-90	cytochrome P450, family 2, subfamily e, polypeptide 1	Rattus norvegicus	96-102
1916152-1	1991	About half of all Japanese lack the activity of aldehyde dehydrogenase 2 (ALDH2), and suffer a flush after alcohol intake due to the marked elevation of blood acetaldehyde concentration.	Acetaldehyde	159-171	aldehyde dehydrogenase 2 family member	Homo sapiens	74-79
1650222-10	1991	At concentrations of 100 micrograms/ml or greater, CRP also inhibited superoxide production in a cell-free xanthine oxidase-acetaldehyde system.	Acetaldehyde	124-136	C-reactive protein	Homo sapiens	51-54
1804132-1	1991	A new biological alcohol marker, the ratio between the acetaldehyde-induced haemoglobin fraction HbA1ach and the glycated haemoglobin fraction HbA1c (HbA1ach/HbA1c), was studied in association with data obtained in a questionnaire, the Malmo modified Michigan alcoholism screening test (Mm-MAST), completed by 270 consecutive middle-aged men participating in a voluntary health screening.	Acetaldehyde	55-67	hemoglobin subunit alpha 1	Homo sapiens	97-101
2043614-1	1991	Class III alcohol dehydrogenase (chi chi-ADH) from human liver binds both ethanol and acetaldehyde so poorly that their Km values cannot be determined, even at ethanol concentrations up to 3 M. However, long-chain carboxylates, e.g., pentanoate, octanoate, deoxycholate, and other anions, substantially enhance the binding of ethanol and other substrates and hence the activity of class III ADH up to 30-fold.	Acetaldehyde	86-98	aldo-keto reductase family 1 member A1	Homo sapiens	10-31
2010168-0	1991	Inhibition of rat hepatic mitochondrial aldehyde dehydrogenase-mediated acetaldehyde oxidation by trans-4-hydroxy-2-nonenal.	Acetaldehyde	72-84	aldehyde dehydrogenase 2 family member	Rattus norvegicus	26-62
2010168-2	1991	It was the purpose of this study to evaluate the cooxidation of the lipid peroxidation product, trans-4-hydroxy-2-nonenal, and acetaldehyde by high-affinity mitochondrial aldehyde dehydrogenase, which is of prominent importance in the oxidation of ethanol-derived acetaldehyde.	Acetaldehyde	127-139	aldehyde dehydrogenase 2 family member	Rattus norvegicus	157-193
2010168-2	1991	It was the purpose of this study to evaluate the cooxidation of the lipid peroxidation product, trans-4-hydroxy-2-nonenal, and acetaldehyde by high-affinity mitochondrial aldehyde dehydrogenase, which is of prominent importance in the oxidation of ethanol-derived acetaldehyde.	Acetaldehyde	264-276	aldehyde dehydrogenase 2 family member	Rattus norvegicus	157-193
2010168-3	1991	Experiments were performed for determination of kinetic parameters for uninhibited acetaldehyde and 4-hydroxynonenal oxidation by semi-purified mitochondrial aldehyde dehydrogenase prepared from male Sprague-Dawley rat liver.	Acetaldehyde	83-95	aldehyde dehydrogenase 2 family member	Rattus norvegicus	144-180
2010168-4	1991	The affinity of the enzyme for the substrate at low substrate concentrations and the Michaelis-Menten constant of mitochondrial aldehyde dehydrogenase for acetaldehyde were 25 and 10 times greater, respectively, than those determined for 4-hydroxynonenal.	Acetaldehyde	155-167	aldehyde dehydrogenase 2 family member	Rattus norvegicus	114-150
2010171-0	1991	Acetaldehyde increases procollagen type I and fibronectin gene transcription in cultured rat fat-storing cells through a protein synthesis-dependent mechanism.	Acetaldehyde	0-12	fibronectin 1	Rattus norvegicus	46-57
2010171-3	1991	By 6 hr, acetaldehyde increased the steady-state levels of alpha 1 procollagen type I messenger RNA 3.2-fold and of fibronectin messenger RNA 2.8-fold above control values.	Acetaldehyde	9-21	fibronectin 1	Rattus norvegicus	116-127
2010171-10	1991	In the presence of methylene blue, a scavenger of reducing equivalents, the effect of acetaldehyde on alpha 1(I) procollagen and fibronectin gene expression was totally inhibited.	Acetaldehyde	86-98	fibronectin 1	Rattus norvegicus	129-140
2010171-11	1991	Transcription run-on assay showed that acetaldehyde increased both procollagen type I and fibronectin transcriptional activity threefold and 2.5-fold, respectively.	Acetaldehyde	39-51	fibronectin 1	Rattus norvegicus	90-101
2010171-12	1991	We conclude that acetaldehyde increases alpha 1(I) procollagen and fibronectin gene expression through enhanced transcription by a mechanism dependent on newly synthesized proteins.	Acetaldehyde	17-29	fibronectin 1	Rattus norvegicus	67-78
1946823-6	1991	The stomach ALDH3 isozymes exhibited a Km value for acetaldehyde of 75 mM, and an optimum for acetaldehyde oxidation at pH 8.5.	Acetaldehyde	52-64	aldehyde dehydrogenase 3 family member A1	Homo sapiens	12-17
1946823-6	1991	The stomach ALDH3 isozymes exhibited a Km value for acetaldehyde of 75 mM, and an optimum for acetaldehyde oxidation at pH 8.5.	Acetaldehyde	94-106	aldehyde dehydrogenase 3 family member A1	Homo sapiens	12-17
1946823-9	1991	These results indicate that Chinese lacking ALDH2 activity may have a lower acetaldehyde oxidation rate in the stomach during alcohol consumption.	Acetaldehyde	76-88	aldehyde dehydrogenase 2 family member	Homo sapiens	44-49
2024727-1	1991	In order to clarify the relationships between acetaldehyde (Ac-CHO) metabolism and low Km (mitochondrial) aldehyde dehydrogenase (ALDH2) genotypes, hepatic ALDH2 activity was determined and serial changes of blood Ac-CHO levels after ethanol administration were analyzed in the individuals homozygous for the normal ALDH2 genes, heterozygous for the normal and mutant ALDH2 genes, and homozygous for the mutant ALDH2 genes.	Acetaldehyde	46-58	aldehyde dehydrogenase 2 family member	Homo sapiens	130-135
1845546-0	1991	Alcohol abusers exhibit a higher IgA response to acetaldehyde-modified proteins.	Acetaldehyde	49-61	CD79a molecule	Homo sapiens	33-36
1845546-4	1991	Thus measurement of IgA binding to acetaldehyde-modified proteins may be a marker for alcohol abuse.	Acetaldehyde	35-47	CD79a molecule	Homo sapiens	20-23
1661206-4	1991	With the first substrate the ALDH activities found in the crude cytoplasmic extracts were lower in hepatoma cells than in normal hepatocytes, especially when measured with NADP as coenzyme (ACA/NADP).	Acetaldehyde	190-193	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	29-33
2050324-10	1991	These results indicate that alcoholic liver disease develops even with moderate amounts of alcohol intake in heterozygotes of the aldehyde dehydrogenase-2 genes, in which acetaldehyde metabolism in the liver is impaired and liver damage in the heterozygotes is more severe than that in the normal homozygotes, suggesting that habitual drinkers who are heterozygotes of the aldehyde dehydrogenase-2 genes may be at high risk for alcoholic liver disease.	Acetaldehyde	171-183	aldehyde dehydrogenase 2 family member	Homo sapiens	130-154
2014795-5	1991	The alcoholics had significantly lower frequencies of the ADH2*2, ADH3*1, and ALDH2*2 alleles than did the nonalcoholics, suggesting that genetic variation in both ADH and ALDH, by modulating the rate of metabolism of ethanol and acetaldehyde, influences drinking behavior and the risk of developing alcoholism.	Acetaldehyde	230-242	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	58-61
2058789-11	1991	They also confirm the presence and generation of H2O2 in the rat brain in vivo, and overall seem to support the notion that centrally formed acetaldehyde via brain catalase may be responsible for some of the psychopharmacological actions of ethanol.	Acetaldehyde	141-153	catalase	Rattus norvegicus	164-172
2383209-2	1990	At the same time, blood ethanol and acetaldehyde levels were measured to consider their correlation to the changes in ALDH activities.	Acetaldehyde	36-48	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	118-122
2058934-7	1991	In addition to alpha-tubulin, calmodulin and actin have also been found to have enhanced reactivity toward acetaldehyde.	Acetaldehyde	107-119	calmodulin 1	Homo sapiens	30-40
1673427-6	1991	On the contrary, citral was found to be a potent inhibitor of acetaldehyde oxidation by the low-KM mitochondrial form of ALDH.	Acetaldehyde	62-74	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	121-125
2394940-0	1990	delta-Aminolevulinic acid dehydratase in rat liver: studies on the effects of ethanol, acetaldehyde, and B6 vitamers.	Acetaldehyde	87-99	aminolevulinate dehydratase	Rattus norvegicus	0-37
2394940-1	1990	Because ethanol ingestion lowers delta-aminolevulinic acid dehydratase (ALAD) activity in liver and red cells, effects of ethanol and acetaldehyde on ALAD in rat liver cytosol were studied.	Acetaldehyde	134-146	aminolevulinate dehydratase	Rattus norvegicus	150-154
2394940-2	1990	When added to the assay mix, as little as 0.5 mmol/L acetaldehyde competitively inhibited ALAD even in the presence of dithiothreitol, a sulfhydryl reagent.	Acetaldehyde	53-65	aminolevulinate dehydratase	Rattus norvegicus	90-94
2394940-3	1990	ALAD activity also fell when undiluted cytosol was incubated at 37 degrees with as little as 0.25 mmol/L acetaldehyde for 8 hours before enzyme assay.	Acetaldehyde	105-117	aminolevulinate dehydratase	Rattus norvegicus	0-4
2394940-4	1990	Inactivation of ALAD by acetaldehyde was prevented by the metabolic inhibitor NaF but not by the aldehyde dehydrogenase inhibitor cyanamide.	Acetaldehyde	24-36	aminolevulinate dehydratase	Rattus norvegicus	16-20
2372948-3	1990	Catalase oxidizes ethanol to acetaldehyde in the presence of hydrogen peroxide.	Acetaldehyde	29-41	catalase	Homo sapiens	0-8
2193925-3	1990	Analysis of the glucose metabolism of adh0 cells shows that the lack of all known ADH isozymes results in the formation of glycerol as a major fermentation product, accompanied by a significant production of acetaldehyde and acetate.	Acetaldehyde	208-220	alcohol dehydrogenase ADH4	Saccharomyces cerevisiae S288C	82-85
2378434-4	1990	Short-term addition of ethanol or acetaldehyde to the incubations markedly increased the sensitivity of CPT-I to inhibition by malonyl-CoA in a subsequent assay in hepatocytes isolated from ethanol-treated rats, but not in cells from control animals.	Acetaldehyde	34-46	carnitine palmitoyltransferase 1B	Rattus norvegicus	104-109
2222285-7	1990	The plasma gastrin level is certified to increase after the ingestion of ethanol and this is not mediated by acetaldehyde because the intra-venous infusion of acetaldehyde was not increased the plasma gastrin level in dogs.	Acetaldehyde	159-171	gastrin	Canis lupus familiaris	11-18
2266114-1	1990	Activation parameters for each reaction step in the kinetic mechanism of liver alcohol dehydrogenase have been measured for the oxidation of ethanol and the reduction of acetaldehyde.	Acetaldehyde	170-182	aldo-keto reductase family 1 member A1	Homo sapiens	79-100
2088119-0	1990	Detection of a new acetaldehyde-induced hemoglobin fraction HbA1ach by cation exchange liquid chromatography.	Acetaldehyde	19-31	hemoglobin subunit alpha 1	Homo sapiens	60-64
2175175-0	1990	Acetaldehyde-collagen adducts in CCl4-induced liver injury in rats.	Acetaldehyde	0-12	C-C motif chemokine ligand 4	Rattus norvegicus	33-37
2394940-8	1990	However, these vitamers increased ALAD activity and decreased acetaldehyde-mediated inactivation of ALAD when incubated for 8 hours with undiluted cytosol.	Acetaldehyde	62-74	aminolevulinate dehydratase	Rattus norvegicus	100-104
2394940-9	1990	We conclude that (1) acetaldehyde decreases ALAD activity both by competitive inhibition with substrate and by inactivation of enzyme protein and that (2) inactivation of ALAD by acetaldehyde may require nonoxidative metabolism of acetaldehyde.	Acetaldehyde	21-33	aminolevulinate dehydratase	Rattus norvegicus	44-48
2394940-9	1990	We conclude that (1) acetaldehyde decreases ALAD activity both by competitive inhibition with substrate and by inactivation of enzyme protein and that (2) inactivation of ALAD by acetaldehyde may require nonoxidative metabolism of acetaldehyde.	Acetaldehyde	179-191	aminolevulinate dehydratase	Rattus norvegicus	44-48
2394940-10	1990	The net pharmacologic effect of B6 vitamers on ALAD activity and on inactivation of ALAD by acetaldehyde remains to be determined.	Acetaldehyde	92-104	aminolevulinate dehydratase	Rattus norvegicus	84-88
2222203-2	1990	AlDH activity (acetaldehyde is used as a substrate) in the barrier structures of the brain (vascular and villous ependymocytes of the cerebral ventricles, endothelium of blood capillaries) makes only 10-30% during the antenatal period and then increases gradually, reaching the activity specific for mature animals by the 20th-40th day after birth.	Acetaldehyde	15-27	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	0-4
2383209-10	1990	These drastic decreases in acetaldehyde elimination rate appear to be caused by reduction of the granule low Km ALDH activity.	Acetaldehyde	27-39	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	112-116
2193901-2	1990	K. marxianus ADH1 has an optimal temperature higher than the S. cerevisiae enzyme (45-50 degrees vs 35 degrees C), a better stability to pH variations in the oxidative reaction (pH optimum 7.5), a lower Michaelis constant for acetaldehyde, and a good catalytic activity both for fermentative and oxidative reactions.	Acetaldehyde	226-238	alcohol dehydrogenase ADH1	Saccharomyces cerevisiae S288C	13-17
2371231-3	1990	The apparent isotope effects declined rapidly with time when acetaldehyde was present in the medium as a result of the reduction to ethanol of the [14C]-acetaldehyde formed from the double labelled ethanol by alcohol dehydrogenase (ADH).	Acetaldehyde	61-73	aldo-keto reductase family 1 member A1	Rattus norvegicus	209-230
2371231-3	1990	The apparent isotope effects declined rapidly with time when acetaldehyde was present in the medium as a result of the reduction to ethanol of the [14C]-acetaldehyde formed from the double labelled ethanol by alcohol dehydrogenase (ADH).	Acetaldehyde	61-73	aldo-keto reductase family 1 member A1	Rattus norvegicus	232-235
2371231-3	1990	The apparent isotope effects declined rapidly with time when acetaldehyde was present in the medium as a result of the reduction to ethanol of the [14C]-acetaldehyde formed from the double labelled ethanol by alcohol dehydrogenase (ADH).	Acetaldehyde	153-165	aldo-keto reductase family 1 member A1	Rattus norvegicus	209-230
2371231-3	1990	The apparent isotope effects declined rapidly with time when acetaldehyde was present in the medium as a result of the reduction to ethanol of the [14C]-acetaldehyde formed from the double labelled ethanol by alcohol dehydrogenase (ADH).	Acetaldehyde	153-165	aldo-keto reductase family 1 member A1	Rattus norvegicus	232-235
2371231-5	1990	The apparent first order rate constant for the reverse ADH reaction, assuming the reactants to be acetaldehyde and the ADH-NADH complex, was determined by two methods giving comparable results.	Acetaldehyde	98-110	aldo-keto reductase family 1 member A1	Rattus norvegicus	55-58
2331431-1	1990	We tested the effect of ethanol and its metabolite, acetaldehyde, on bone formation as measured by [3H]proline incorporation into collagenase digestible protein (CDP) and noncollagen protein (NCP), and on DNA synthesis as measured by [3H]thymidine (TdR) incorporation in fetal rat calvaria.	Acetaldehyde	52-64	cut-like homeobox 1	Rattus norvegicus	162-165
2334855-4	1990	Although the etiology is not yet fully understood, the direct toxic effects of ethanol and acetaldehyde upon the structure and function of the myocardium due to the decreased functional activity of alcohol dehydrogenase and catalase are known to be involved in the development of alcoholic diseases of the heart.	Acetaldehyde	91-103	catalase	Homo sapiens	224-232
2198030-4	1990	Expression of an inactive form of the ALDH2 isoenzyme, the so-called Oriental variant, results in impaired acetaldehyde metabolizing capacity.	Acetaldehyde	107-119	aldehyde dehydrogenase 2 family member	Homo sapiens	38-43
2087903-0	1990	Influence of ethanol and acetaldehyde on the activity and release of cathepsin A from liver lysosomes.	Acetaldehyde	25-37	cathepsin A	Rattus norvegicus	69-80
2087903-1	1990	Ethanol and acetaldehyde inhibited the activity of cathepsin A.	Acetaldehyde	12-24	cathepsin A	Rattus norvegicus	51-62
2087903-3	1990	Intoxication of rats with ethanol and acetaldehyde evoked a transient increase of free and bound cathepsin A.	Acetaldehyde	38-50	cathepsin A	Rattus norvegicus	97-108
2222572-14	1990	The observed steady state level of AHD-2 mRNA and the increase in ALDH activity after ethanol feeding, which is unique to C57BL/6J mice, is expected to offer a faster clearance (metabolism) of acetaldehyde, the toxic metabolite, and may be responsible for, or contribute to, the relative resistance of this strain to ethanol.	Acetaldehyde	193-205	aldehyde dehydrogenase family 1, subfamily A1	Mus musculus	35-40
2222572-14	1990	The observed steady state level of AHD-2 mRNA and the increase in ALDH activity after ethanol feeding, which is unique to C57BL/6J mice, is expected to offer a faster clearance (metabolism) of acetaldehyde, the toxic metabolite, and may be responsible for, or contribute to, the relative resistance of this strain to ethanol.	Acetaldehyde	193-205	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	66-70
2331431-10	1990	At 0.01% and 0.03% acetaldehyde inhibited proline incorporation into CDP by 48% and 94% and NCP by 40% and 74% respectively.	Acetaldehyde	19-31	cut-like homeobox 1	Rattus norvegicus	69-72
2170242-4	1990	Iron mobilization due to the metabolism of ethanol to acetaldehyde by alcohol dehydrogenase was increased 100% by the addition of aldehyde oxidase.	Acetaldehyde	54-66	aldehyde oxidase 1	Homo sapiens	130-146
2209564-0	1990	Acetaldehyde-induced mutation at the hprt locus in human lymphocytes in vitro.	Acetaldehyde	0-12	hypoxanthine phosphoribosyltransferase 1	Homo sapiens	37-41
2170242-6	1990	Mobilization of iron due to acetaldehyde metabolism by aldehyde oxidase was completely inhibited by superoxide dismutase but not by catalase suggesting that superoxide radicals mediate mobilization.	Acetaldehyde	28-40	aldehyde oxidase 1	Homo sapiens	55-71
2170242-7	1990	Acetaldehyde-aldehyde oxidase mediated reduction of ferritin iron was facilitated by incubation with menadione, an electron acceptor for aldehyde oxidase.	Acetaldehyde	0-12	aldehyde oxidase 1	Homo sapiens	13-29
2170242-7	1990	Acetaldehyde-aldehyde oxidase mediated reduction of ferritin iron was facilitated by incubation with menadione, an electron acceptor for aldehyde oxidase.	Acetaldehyde	0-12	aldehyde oxidase 1	Homo sapiens	137-153
2170242-8	1990	Mobilization of ferritin iron due to the metabolism of acetaldehyde by aldehyde oxidase may be a fundamental mechanism of alcohol-induced liver injury.	Acetaldehyde	55-67	aldehyde oxidase 1	Homo sapiens	71-87
2125096-0	1990	Impairment of histone H1 DNA binding by adduct formation with acetaldehyde.	Acetaldehyde	62-74	H1.0 linker histone	Rattus norvegicus	14-24
2182564-2	1990	While three forms display low affinity for acetaldehyde, the fourth is active at extremely low aldehyde concentrations (Km less than or equal to 2 microM) and allows the oxidation of the acetaldehyde formed by catalysis of alcohol dehydrogenase at pH 7.4.	Acetaldehyde	43-55	aldo-keto reductase family 1 member A1	Rattus norvegicus	223-244
2182564-2	1990	While three forms display low affinity for acetaldehyde, the fourth is active at extremely low aldehyde concentrations (Km less than or equal to 2 microM) and allows the oxidation of the acetaldehyde formed by catalysis of alcohol dehydrogenase at pH 7.4.	Acetaldehyde	187-199	aldo-keto reductase family 1 member A1	Rattus norvegicus	223-244
2182564-4	1990	According to the only acceptable model, when the acetaldehyde concentration is kept low by the action of aldehyde dehydrogenase, NADH no longer binds to alcohol dehydrogenase, but acetaldehyde still competes with ethanol for the active site of the enzyme.	Acetaldehyde	49-61	aldo-keto reductase family 1 member A1	Rattus norvegicus	153-174
2272522-2	1990	On the other hand, rates of acetaldehyde metabolism by mitochondrial aldehyde dehydrogenase (ALDH) were 15-20% lower in livers of old rats than in those of younger ones.	Acetaldehyde	28-40	aldehyde dehydrogenase 2 family member	Rattus norvegicus	55-91
2272522-2	1990	On the other hand, rates of acetaldehyde metabolism by mitochondrial aldehyde dehydrogenase (ALDH) were 15-20% lower in livers of old rats than in those of younger ones.	Acetaldehyde	28-40	aldehyde dehydrogenase 3 family, member A1	Rattus norvegicus	93-97
2125096-1	1990	Incubation of histone H1 with pharmacologically relevant concentrations of acetaldehyde resulted in the formation of spontaneously stable acetaldehyde-protein linkages.	Acetaldehyde	75-87	H1.0 linker histone	Rattus norvegicus	14-24
2125096-1	1990	Incubation of histone H1 with pharmacologically relevant concentrations of acetaldehyde resulted in the formation of spontaneously stable acetaldehyde-protein linkages.	Acetaldehyde	138-150	H1.0 linker histone	Rattus norvegicus	14-24
6705976-3	1984	The ALDH activity in the cerebellum, which was measured spectrophotometrically with 0.1 and 5 mM acetaldehyde as the substrates, was the highest of the three regions and it was about 2-fold higher than that in the cortex in both strains.	Acetaldehyde	97-109	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	4-8
2237274-2	1990	Acetaldehyde, which is derived from alcohol by the action of alcohol dehydrogenase, is apparently the most important factor leading to alcohol-induced liver injury.	Acetaldehyde	0-12	aldo-keto reductase family 1 member A1	Homo sapiens	61-82
6705976-6	1984	Electrophoretic analysis of cortex ALDH revealed that strain differences were observed in the isozyme pattern between pH 7.2 and 7.8 with either acetaldehyde or propionaldehyde as substrate.	Acetaldehyde	145-157	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	35-39
34587326-4	2021	Aldehyde profiling in leaves of 24-days old plants revealed higher accumulation of acrolein, crotonaldehyde, 3Z-hexenal, hexanal and acetaldehyde in aao3 mutants compared to wild-type leaves.	Acetaldehyde	133-145	abscisic aldehyde oxidase 3	Arabidopsis thaliana	149-153
33764154-10	2021	Nuclear ALDH1A3 converted acetaldehyde to acetate to produce acetyl-CoA to acetylate H3K27, marking active enhancers.	Acetaldehyde	26-38	aldehyde dehydrogenase family 1, subfamily A3	Mus musculus	8-15
22922648-5	2012	Mice with combined inactivation of aldehyde catabolism (through Aldh2 knockout) and the Fanconi anaemia DNA-repair pathway (Fancd2 knockout) display developmental defects, a predisposition to leukaemia, and are susceptible to the toxic effects of ethanol-an exogenous source of acetaldehyde.	Acetaldehyde	278-290	Fanconi anemia, complementation group D2	Mus musculus	124-130
22922648-7	2012	Unexpectedly, we find that only HSPCs, and not more mature blood precursors, require Aldh2 for protection against acetaldehyde toxicity.	Acetaldehyde	114-126	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	85-90
21156189-8	2011	In cultured human or mouse HSC, production of CTGF, alpha-SMA and/or collagen was increased by ethanol treatment, an effect mimicked by acetaldehyde and blocked by 4-methylpyrazole (4-MP) or N-acetylcysteine (NAC).	Acetaldehyde	136-148	cellular communication network factor 2	Mus musculus	46-50
21156189-8	2011	In cultured human or mouse HSC, production of CTGF, alpha-SMA and/or collagen was increased by ethanol treatment, an effect mimicked by acetaldehyde and blocked by 4-methylpyrazole (4-MP) or N-acetylcysteine (NAC).	Acetaldehyde	136-148	actin alpha 2, smooth muscle, aorta	Mus musculus	52-61
21156189-11	2011	Administration of TGF-beta1 siRNA or CTGF siRNA significantly decreased ethanol- or acetaldehyde-stimulated mRNA or protein levels of CTGF, alpha-SMA or collagen I in LX-2 cells.	Acetaldehyde	84-96	transforming growth factor beta 1	Homo sapiens	18-27
21156189-11	2011	Administration of TGF-beta1 siRNA or CTGF siRNA significantly decreased ethanol- or acetaldehyde-stimulated mRNA or protein levels of CTGF, alpha-SMA or collagen I in LX-2 cells.	Acetaldehyde	84-96	cellular communication network factor 2	Homo sapiens	37-41
21156189-11	2011	Administration of TGF-beta1 siRNA or CTGF siRNA significantly decreased ethanol- or acetaldehyde-stimulated mRNA or protein levels of CTGF, alpha-SMA or collagen I in LX-2 cells.	Acetaldehyde	84-96	cellular communication network factor 2	Homo sapiens	134-138
21156189-11	2011	Administration of TGF-beta1 siRNA or CTGF siRNA significantly decreased ethanol- or acetaldehyde-stimulated mRNA or protein levels of CTGF, alpha-SMA or collagen I in LX-2 cells.	Acetaldehyde	84-96	actin alpha 2, smooth muscle, aorta	Mus musculus	140-149
17718407-2	2006	UChB animals carry efficient variants of the aldehyde dehydrogenase 2 (ALDH2) genes and have active mitochondria, resulting in fast removal of acetaldehyde.	Acetaldehyde	143-155	aldehyde dehydrogenase 1 family, member A1	Rattus norvegicus	45-69
17718407-2	2006	UChB animals carry efficient variants of the aldehyde dehydrogenase 2 (ALDH2) genes and have active mitochondria, resulting in fast removal of acetaldehyde.	Acetaldehyde	143-155	aldehyde dehydrogenase 1 family, member A1	Rattus norvegicus	71-76
17718407-3	2006	UChA animals, in contrast, carry less efficient ALDH2 variants and less active mitochondria, which result in transient elevations of acetaldehyde levels after alcohol ingestion.	Acetaldehyde	133-145	aldehyde dehydrogenase 1 family, member A1	Rattus norvegicus	48-53
34587326-5	2021	Similarly, higher levels of acrolein, benzaldehyde, crotonaldehyde, propionaldehyde, trans-2-hexenal and acetaldehyde were accumulated in aao3 mutants upon UV-C irradiation.	Acetaldehyde	105-117	abscisic aldehyde oxidase 3	Arabidopsis thaliana	138-142
34328261-6	2021	At physiologically relevant concentrations, acetaldehyde activated the ATR-Chk1 pathway, leading to S- and G2/M-phase delay with accumulation of the FA complementation group D2 protein (FANCD2) at the sites of DNA synthesis, suggesting that acetaldehyde impedes replication fork progression.	Acetaldehyde	44-56	checkpoint kinase 1	Homo sapiens	75-79
34157622-6	2021	As pre-ozonation could oxidize natural organic matter to acetaldehydes, the concentration of acetaldehyde formed after pre-ozonation was used to calculate the HAL yields during ozonation-chlorination by the kinetic model, which fitted the experimental results well.	Acetaldehyde	57-70	histidine ammonia-lyase	Homo sapiens	159-162
34157622-6	2021	As pre-ozonation could oxidize natural organic matter to acetaldehydes, the concentration of acetaldehyde formed after pre-ozonation was used to calculate the HAL yields during ozonation-chlorination by the kinetic model, which fitted the experimental results well.	Acetaldehyde	93-105	histidine ammonia-lyase	Homo sapiens	159-162
34461491-4	2021	Serum anti-citrullinated (CIT) protein antibody (ACPA) and anti-malondialdehyde-acetaldehyde (MAA) antibodies were strikingly potentiated with co-exposure (CIA + LPS).	Acetaldehyde	80-92	nuclear receptor coactivator 5	Mus musculus	156-159
34886638-13	2021	Conclusion: Gas explosion can cause multi-organ system damage in rats, the mechanism of which may be related to the biosynthesis of alanine, tyrosine and tryptophan, metabolism of niacin and niacinamide, metabolism of acetaldehyde and dicarboxylic acid, and TCA cycle, etc.	Acetaldehyde	218-230	gastrin	Rattus norvegicus	12-15
34328261-0	2021	FANCD2 limits acetaldehyde-induced genomic instability during DNA replication in esophageal keratinocytes.	Acetaldehyde	14-26	FA complementation group D2	Homo sapiens	0-6
34328261-6	2021	At physiologically relevant concentrations, acetaldehyde activated the ATR-Chk1 pathway, leading to S- and G2/M-phase delay with accumulation of the FA complementation group D2 protein (FANCD2) at the sites of DNA synthesis, suggesting that acetaldehyde impedes replication fork progression.	Acetaldehyde	44-56	FA complementation group D2	Homo sapiens	186-192
34328261-5	2021	Acetaldehyde-exposed esophageal keratinocytes displayed accumulation of DNA damage foci consisting of 53BP1 and BRCA1.	Acetaldehyde	0-12	tumor protein p53 binding protein 1	Homo sapiens	102-107
34328261-5	2021	Acetaldehyde-exposed esophageal keratinocytes displayed accumulation of DNA damage foci consisting of 53BP1 and BRCA1.	Acetaldehyde	0-12	BRCA1 DNA repair associated	Homo sapiens	112-117
34328261-6	2021	At physiologically relevant concentrations, acetaldehyde activated the ATR-Chk1 pathway, leading to S- and G2/M-phase delay with accumulation of the FA complementation group D2 protein (FANCD2) at the sites of DNA synthesis, suggesting that acetaldehyde impedes replication fork progression.	Acetaldehyde	241-253	ATR serine/threonine kinase	Homo sapiens	71-74
34328261-6	2021	At physiologically relevant concentrations, acetaldehyde activated the ATR-Chk1 pathway, leading to S- and G2/M-phase delay with accumulation of the FA complementation group D2 protein (FANCD2) at the sites of DNA synthesis, suggesting that acetaldehyde impedes replication fork progression.	Acetaldehyde	44-56	ATR serine/threonine kinase	Homo sapiens	71-74
34328261-6	2021	At physiologically relevant concentrations, acetaldehyde activated the ATR-Chk1 pathway, leading to S- and G2/M-phase delay with accumulation of the FA complementation group D2 protein (FANCD2) at the sites of DNA synthesis, suggesting that acetaldehyde impedes replication fork progression.	Acetaldehyde	241-253	checkpoint kinase 1	Homo sapiens	75-79
34328261-6	2021	At physiologically relevant concentrations, acetaldehyde activated the ATR-Chk1 pathway, leading to S- and G2/M-phase delay with accumulation of the FA complementation group D2 protein (FANCD2) at the sites of DNA synthesis, suggesting that acetaldehyde impedes replication fork progression.	Acetaldehyde	241-253	FA complementation group D2	Homo sapiens	186-192
34328261-7	2021	Consistently, depletion of the replication fork protection protein Timeless led to elevated DNA damage upon acetaldehyde exposure.	Acetaldehyde	108-120	timeless circadian regulator	Homo sapiens	67-75
34328261-8	2021	Furthermore, FANCD2 depletion exacerbated replication abnormalities, elevated DNA damage, and led to apoptotic cell death, indicating that FANCD2 prevents acetaldehyde-induced genomic instability in esophageal keratinocytes.	Acetaldehyde	155-167	FA complementation group D2	Homo sapiens	139-145
34528981-1	2021	Alcohol consumption leads to acetaldehyde accumulation, especially in people with mutant aldehyde dehydrogenase 2 gene (ALDH2).	Acetaldehyde	29-41	aldehyde dehydrogenase 2 family member	Homo sapiens	89-113
34291576-3	2021	In the PEM reactor, a Pt/C catalyst promoted the electro-oxidation of ethanol to acetaldehyde.	Acetaldehyde	81-93	mucin 1, cell surface associated	Homo sapiens	7-10
34291576-4	2021	The Nafion membrane used as the PEM served as a solid acid catalyst for the acetalization of ethanol and electrochemically formed acetaldehyde.	Acetaldehyde	130-142	mucin 1, cell surface associated	Homo sapiens	32-35
34528981-1	2021	Alcohol consumption leads to acetaldehyde accumulation, especially in people with mutant aldehyde dehydrogenase 2 gene (ALDH2).	Acetaldehyde	29-41	aldehyde dehydrogenase 2 family member	Homo sapiens	120-125
34528981-8	2021	Interestingly, participants with mutant ALDH2 responded better than wild-type participants for salivary acetaldehyde (90% vs. 70%, p < 0.001).	Acetaldehyde	104-116	aldehyde dehydrogenase 2 family member	Homo sapiens	40-45
34528981-12	2021	The addition of exogenous capacity to detoxify acetaldehyde using the probiotic product could be a potential strategy to promote the alleviation of exposure to reactive and carcinogenic acetaldehyde associated with alcohol drinking in individuals with defective ALDH2 enzyme.	Acetaldehyde	47-59	aldehyde dehydrogenase 2 family member	Homo sapiens	262-267
34546339-5	2022	In an in vitro reaction setup with NER-proficient and NER-deficient xeroderma pigmentosum group A (XPA) cell extracts, NER reactions were observed in the presence of XPA recombinant proteins in acetaldehyde-treated plasmids.	Acetaldehyde	194-206	XPA, DNA damage recognition and repair factor	Homo sapiens	166-169
34546339-7	2022	Additionally, it was observed that DNA polymerase eta inserted dATP opposite guanine in acetaldehyde-treated oligonucleotides, suggesting that acetaldehyde induced GG to TT transversions.	Acetaldehyde	88-100	DNA polymerase eta	Homo sapiens	35-53
34546339-7	2022	Additionally, it was observed that DNA polymerase eta inserted dATP opposite guanine in acetaldehyde-treated oligonucleotides, suggesting that acetaldehyde induced GG to TT transversions.	Acetaldehyde	143-155	DNA polymerase eta	Homo sapiens	35-53
34411334-8	2021	Here, we show that 8-acetoxypyrene-1,3,6-trisulfonate (Ace), a fluorogenic derivative of the hepatic OATP substrate pyranine (8-hydroxypyrene-1,3,6-trisulfonate) enters the cells via OATP1B1/3 or OATP2B1 function.	Acetaldehyde	55-58	solute carrier organic anion transporter family, member 1a5	Mus musculus	183-192
34378958-9	2021	Ald has a broad range of substrates, including benzaldehyde, furfural, and acetaldehyde.	Acetaldehyde	75-87	AWN88_RS16050	Agrobacterium tumefaciens	0-3
34326141-6	2021	The results showed that intraperitoneal injection of acetaldehyde increased cFos protein expression within the LHb and that intra-LHb infusion of acetaldehyde induced conditioned place aversion in male rats.	Acetaldehyde	53-65	Fos proto-oncogene, AP-1 transcription factor subunit	Rattus norvegicus	76-80
34439848-7	2021	The principal findings are (1) dose-dependent increase of blood ethanol concentration, unaffected by ADH1B or ALDH2; (2) significant build-up of blood acetaldehyde, strikingly influenced by the ALDH2*2 gene allele and correlated with the dose of ingested alcohol; (3) the increased heart rate and subjective sensations caused by acetaldehyde accumulation in the ALDH2*2 heterozygotes; (4) no significant effect of ADH1B polymorphism in alcohol metabolism or producing the psychological responses.	Acetaldehyde	329-341	aldehyde dehydrogenase 2 family member	Homo sapiens	362-367
34410369-0	2021	Simultaneously deleting ADH2 and THI3 genes of Saccharomyces cerevisiae for reducing the yield of acetaldehyde and fusel alcohols.	Acetaldehyde	98-110	alcohol dehydrogenase ADH2	Saccharomyces cerevisiae S288C	24-28
34410369-0	2021	Simultaneously deleting ADH2 and THI3 genes of Saccharomyces cerevisiae for reducing the yield of acetaldehyde and fusel alcohols.	Acetaldehyde	98-110	branched-chain-2-oxoacid decarboxylase THI3	Saccharomyces cerevisiae S288C	33-37
34410369-3	2021	Results showed that single-gene-deletion mutants by separate gene deletion of ADH2 or THI3 led to a reduced production of the acetaldehyde or fusel alcohols, respectively.	Acetaldehyde	126-138	alcohol dehydrogenase ADH2	Saccharomyces cerevisiae S288C	78-82
34410369-3	2021	Results showed that single-gene-deletion mutants by separate gene deletion of ADH2 or THI3 led to a reduced production of the acetaldehyde or fusel alcohols, respectively.	Acetaldehyde	126-138	branched-chain-2-oxoacid decarboxylase THI3	Saccharomyces cerevisiae S288C	86-90
34441974-1	2021	Ethnic difference is known in genetic polymorphisms of aldehyde dehydrogenase 2 (ALDH2) and alcohol dehydrogenase 1B (ADH1B), which cause Asian flushing by blood vessel dilation due to accumulation of acetaldehyde.	Acetaldehyde	201-213	aldehyde dehydrogenase 2 family member	Homo sapiens	55-79
34441974-1	2021	Ethnic difference is known in genetic polymorphisms of aldehyde dehydrogenase 2 (ALDH2) and alcohol dehydrogenase 1B (ADH1B), which cause Asian flushing by blood vessel dilation due to accumulation of acetaldehyde.	Acetaldehyde	201-213	aldehyde dehydrogenase 2 family member	Homo sapiens	81-86
34441974-1	2021	Ethnic difference is known in genetic polymorphisms of aldehyde dehydrogenase 2 (ALDH2) and alcohol dehydrogenase 1B (ADH1B), which cause Asian flushing by blood vessel dilation due to accumulation of acetaldehyde.	Acetaldehyde	201-213	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	92-116
34441974-1	2021	Ethnic difference is known in genetic polymorphisms of aldehyde dehydrogenase 2 (ALDH2) and alcohol dehydrogenase 1B (ADH1B), which cause Asian flushing by blood vessel dilation due to accumulation of acetaldehyde.	Acetaldehyde	201-213	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	118-123
34351898-4	2021	In particular, the genetic polymorphisms of mitochondrial aldehyde dehydrogenase, ALDH2, play a large role in the metabolism of acetaldehyde.	Acetaldehyde	128-140	aldehyde dehydrogenase 2 family member	Homo sapiens	82-87
34351898-7	2021	This combined model was fit to clinical data and used to show the effect of alcohol concentrations, organ damage, ALDH2 enzyme polymorphisms, and ALDH2-inhibiting drug disulfiram on ethanol and acetaldehyde exposure.	Acetaldehyde	194-206	aldehyde dehydrogenase 2 family member	Homo sapiens	146-151
34351898-9	2021	Additionally, the model demonstrated that acetaldehyde exposure increased with higher dosages of disulfiram and decreased ALDH2 efficiency, and that moderate consumption rates of ethanol could lead to unexpected accumulations in acetaldehyde.	Acetaldehyde	42-54	aldehyde dehydrogenase 2 family member	Homo sapiens	122-127
34243819-2	2021	We reported that acetaldehyde (AcAld) is generated from Heme/Mb/Meat-Linoleate-EtOH model reaction mixtures, and thus could be a new plausible mechanism for the carcinogenesis (Kasai and Kawai, ACS Omega, 2021).	Acetaldehyde	17-29	myoglobin	Homo sapiens	61-63
34228649-1	2021	The mitochondrial enzyme acetaldehyde dehydrogenase 2 (ALDH2) catalyzes the detoxification of acetaldehyde and endogenous lipid aldehydes.	Acetaldehyde	94-106	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	55-60
34439969-1	2021	Mitochondrial aldehyde dehydrogenase 2 (ALDH2) is a critical enzyme involved in ethanol clearance in acetaldehyde metabolism and plays a key role in protecting the liver.	Acetaldehyde	101-113	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	40-45
34439969-2	2021	The ALDH2*2 mutation causes a significant decrease in acetaldehyde scavenging capacity, leading to the accumulation of acetaldehyde after consuming alcohol.	Acetaldehyde	54-66	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	4-9
34439969-2	2021	The ALDH2*2 mutation causes a significant decrease in acetaldehyde scavenging capacity, leading to the accumulation of acetaldehyde after consuming alcohol.	Acetaldehyde	119-131	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	4-9
34077272-9	2021	We also found that chronic exposure of NCM460 human colonic epithelial cells as well as human differentiated colonoid monolayers, to alcohol metabolites (acetaldehyde, ethyl palmitate, ethyl oleate) significantly inhibited biotin uptake and SMVT expression.	Acetaldehyde	154-166	solute carrier family 5 member 6	Homo sapiens	241-245
34260573-6	2021	The group with inactive aldehyde dehydrogenase-2 had a low odds ratio (OR = 0.75 (95% CI:0.69-0.80), P = 4.35 x 10-14) of hypertension, and low metabolism of acetaldehyde.	Acetaldehyde	158-170	aldehyde dehydrogenase 2 family member	Homo sapiens	24-48
34211048-7	2021	Notably, immune suppression was associated with ALDH2/ADH1B gene polymorphisms, and patients with a combination of ALDH2*1/*2 and ADH1B*2 genotypes, the most acetaldehyde-exposed group, demonstrated a deeply suppressed phenotype, suggesting a direct role of acetaldehyde.	Acetaldehyde	158-170	aldehyde dehydrogenase 2 family member	Homo sapiens	115-120
34211048-7	2021	Notably, immune suppression was associated with ALDH2/ADH1B gene polymorphisms, and patients with a combination of ALDH2*1/*2 and ADH1B*2 genotypes, the most acetaldehyde-exposed group, demonstrated a deeply suppressed phenotype, suggesting a direct role of acetaldehyde.	Acetaldehyde	158-170	alcohol dehydrogenase 1B (class I), beta polypeptide	Homo sapiens	130-135
34211048-9	2021	Consistently, hepatic macrophages of ethanol-administered ALDH2*2 transgenic mice exhibited suppressed inflammatory cytokines production in response to LPS compared to that in wild-type mice, reinforcing the contribution of acetaldehyde to liver macrophage function.	Acetaldehyde	224-236	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	58-63
34738133-2	2021	Commercial alumina (Al com), synthetic alumina (Al syn), commercial silica gel (Si com) and synthetic silica gel (Si syn) were used for the transformation of ethylene glycol to a mixture of diethylene glycol, 1,4-dioxane and 2-methyl-1,3-dioxolane via acetaldehyde by heating at 150  C under autogenous pressure without solvent.	Acetaldehyde	252-264	synemin	Homo sapiens	117-120
34262465-7	2021	By using primary hepatocytes and AML-12 cells, we confirmed that TLR9 activation by CpG ODN administration significantly ameliorated acetaldehyde-induced cell injury via suppressing ATF6-CHOP signaling.	Acetaldehyde	133-145	toll-like receptor 9	Mus musculus	65-69
34262465-7	2021	By using primary hepatocytes and AML-12 cells, we confirmed that TLR9 activation by CpG ODN administration significantly ameliorated acetaldehyde-induced cell injury via suppressing ATF6-CHOP signaling.	Acetaldehyde	133-145	activating transcription factor 6	Mus musculus	182-186
34262465-7	2021	By using primary hepatocytes and AML-12 cells, we confirmed that TLR9 activation by CpG ODN administration significantly ameliorated acetaldehyde-induced cell injury via suppressing ATF6-CHOP signaling.	Acetaldehyde	133-145	DNA-damage inducible transcript 3	Mus musculus	187-191
34262465-8	2021	By using STAT3 knockdown AML12 cells, we showed that TLR9-mediated STAT3 activation inhibited ATF6-CHOP signaling cascade and thereby protecting against acetaldehyde-induced mitochondrial dysfunction and cell injury.	Acetaldehyde	153-165	signal transducer and activator of transcription 3	Mus musculus	9-14
34262465-8	2021	By using STAT3 knockdown AML12 cells, we showed that TLR9-mediated STAT3 activation inhibited ATF6-CHOP signaling cascade and thereby protecting against acetaldehyde-induced mitochondrial dysfunction and cell injury.	Acetaldehyde	153-165	toll-like receptor 9	Mus musculus	53-57
34262465-8	2021	By using STAT3 knockdown AML12 cells, we showed that TLR9-mediated STAT3 activation inhibited ATF6-CHOP signaling cascade and thereby protecting against acetaldehyde-induced mitochondrial dysfunction and cell injury.	Acetaldehyde	153-165	signal transducer and activator of transcription 3	Mus musculus	67-72
34262465-8	2021	By using STAT3 knockdown AML12 cells, we showed that TLR9-mediated STAT3 activation inhibited ATF6-CHOP signaling cascade and thereby protecting against acetaldehyde-induced mitochondrial dysfunction and cell injury.	Acetaldehyde	153-165	DNA-damage inducible transcript 3	Mus musculus	99-103
34221859-1	2021	A major mitochondrial enzyme for protecting cells from acetaldehyde toxicity is aldehyde dehydrogenase 2 (ALDH2).	Acetaldehyde	55-67	aldehyde dehydrogenase 2 family member	Homo sapiens	80-104
34221859-1	2021	A major mitochondrial enzyme for protecting cells from acetaldehyde toxicity is aldehyde dehydrogenase 2 (ALDH2).	Acetaldehyde	55-67	aldehyde dehydrogenase 2 family member	Homo sapiens	106-111
34070917-11	2021	Blood levels of alcohol and acetaldehyde were significantly downregulated by probiotic supplementation in subjects with ALDH2*2/*1 genotype, but not in those with ALDH2*1/*1 genotype.	Acetaldehyde	28-40	aldehyde dehydrogenase 2 family member	Homo sapiens	120-125
35438433-7	2022	Acetaldehyde also promoted the accumulation of PINK1 and Parkin on mitochondria and caused a remarkable decrease of mitochondrial mass.	Acetaldehyde	0-12	PTEN induced kinase 1	Homo sapiens	47-52
34069398-5	2021	Analysis of the mechanism of action revealed that EHW inhibits the metabolism of ethanol to acetaldehyde by suppressing alcohol dehydrogenase.	Acetaldehyde	92-104	aldo-keto reductase family 1 member A1	Homo sapiens	120-141
34334796-1	2021	We report the detection of the oxygen-bearing complex organic molecules propenal (C2H3CHO), vinyl alcohol (C2H3OH), methyl formate (HCOOCH3), and dimethyl ether (CH3OCH3) toward the cyanopolyyne peak of the starless core TMC-1.	Acetaldehyde	92-105	transmembrane channel like 1	Homo sapiens	221-226
35438433-6	2022	The levels of light chain 3 (LC3)-II, Beclin1, autophagy-related protein (Atg) 5 and Atg16L1, PTEN-induced putative kinase (PINK)1, and Parkin were significantly elevated, while the level of p62 was reduced in acetaldehyde-treated cells.	Acetaldehyde	210-222	phosphatase and tensin homolog	Homo sapiens	94-98
35523338-9	2022	Furthermore, the levels of urinary DEN metabolite (acetaldehyde) and hepatic DNA damage markers (O6-ethyl-2-deoxyguanosine adducts and gamma-histone H2AX) after DEN treatment were elevated by Nrf2 agonist, 2-Cyano-3,12-dioxooleana-1,9-dien-28-imidazolide.	Acetaldehyde	51-63	nuclear factor, erythroid derived 2, like 2	Mus musculus	192-196
35595033-6	2022	Ferroptosis induced by ethanol- or acetaldehyde involving nuclear receptor co-activator 4 (NCOA4)-dependent autophagic degradation of ferritin, a protein for storing iron is rescued by silibinin.	Acetaldehyde	35-47	nuclear receptor coactivator 4	Homo sapiens	58-89
35595033-6	2022	Ferroptosis induced by ethanol- or acetaldehyde involving nuclear receptor co-activator 4 (NCOA4)-dependent autophagic degradation of ferritin, a protein for storing iron is rescued by silibinin.	Acetaldehyde	35-47	nuclear receptor coactivator 4	Homo sapiens	91-96
35595033-7	2022	PINK1 and Parkin-mediated mitophagy is arrested in ethanol- or acetaldehyde-treated cells but reversed by silibinin.	Acetaldehyde	63-75	PTEN induced kinase 1	Homo sapiens	0-5
35595033-8	2022	Ferritin degradation and ROS level are further increased when PINK1 or Parkin is silenced in the cells treated with ethanol or acetaldehyde.	Acetaldehyde	127-139	PTEN induced kinase 1	Homo sapiens	62-67
35504338-4	2022	We found that common protein-damaging agents such as endogenous/exogenous aldehydes (formaldehyde, acetaldehyde), moderate heat shock and the environmental toxicant cadmium cause inactivation of HIF1 and HIF2 due to structural damage to HIFalpha subunits.	Acetaldehyde	99-111	hypoxia inducible factor 1 subunit alpha	Homo sapiens	195-199
35318866-1	2022	Aldehyde dehydrogenase 2 (ALDH2) detoxifies acetaldehyde produced from ethanol.	Acetaldehyde	44-56	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	0-24
35318866-1	2022	Aldehyde dehydrogenase 2 (ALDH2) detoxifies acetaldehyde produced from ethanol.	Acetaldehyde	44-56	aldehyde dehydrogenase 2, mitochondrial	Mus musculus	26-31
35600274-5	2022	Compared with the acetaldehyde group, NR4A1 agonist upregulated E-cadherin and downregulated FN, FSP-1, vimentin, alpha-SMA, and COL1A1/COL1A2 (P < 0.05).	Acetaldehyde	18-30	cadherin 1	Rattus norvegicus	64-74
35600274-6	2022	After acetaldehyde stimulation, TGF-beta, Smad2/3/4, and zinc finger E-box-binding homeobox (ZEB) were upregulated, while Smad7 mRNA levels were downregulated (all P < 0.05).	Acetaldehyde	6-18	transforming growth factor alpha	Rattus norvegicus	32-40
35600274-4	2022	Compared with the control group, E-cadherin in the acetaldehyde group was downregulated, whereas FN, FSP-1, vimentin, alpha-SMA, and COL1A1/COL1A2 were upregulated (P < 0.05).	Acetaldehyde	51-63	cadherin 1	Rattus norvegicus	33-43
35600274-6	2022	After acetaldehyde stimulation, TGF-beta, Smad2/3/4, and zinc finger E-box-binding homeobox (ZEB) were upregulated, while Smad7 mRNA levels were downregulated (all P < 0.05).	Acetaldehyde	6-18	SMAD family member 2	Rattus norvegicus	42-51
35600274-6	2022	After acetaldehyde stimulation, TGF-beta, Smad2/3/4, and zinc finger E-box-binding homeobox (ZEB) were upregulated, while Smad7 mRNA levels were downregulated (all P < 0.05).	Acetaldehyde	6-18	SMAD family member 7	Rattus norvegicus	122-127
35600274-7	2022	Compared with acetaldehyde alone, NR4A1 agonist increased Smad7 mRNA levels and reduced TGF-beta, Smad2/3/4, and ZEB mRNA levels (all P < 0.05).	Acetaldehyde	14-26	SMAD family member 7	Rattus norvegicus	58-63
35600274-7	2022	Compared with acetaldehyde alone, NR4A1 agonist increased Smad7 mRNA levels and reduced TGF-beta, Smad2/3/4, and ZEB mRNA levels (all P < 0.05).	Acetaldehyde	14-26	transforming growth factor alpha	Rattus norvegicus	88-96
35600274-7	2022	Compared with acetaldehyde alone, NR4A1 agonist increased Smad7 mRNA levels and reduced TGF-beta, Smad2/3/4, and ZEB mRNA levels (all P < 0.05).	Acetaldehyde	14-26	SMAD family member 2	Rattus norvegicus	98-107
35600274-8	2022	NR4A1 activation suppresses acetaldehyde-induced EMT, as shown by epithelial and mesenchymal marker expression.	Acetaldehyde	28-40	nuclear receptor subfamily 4, group A, member 1	Rattus norvegicus	0-5
35158046-8	2022	Accordingly, inhibition of DRP1 activity with its pharmacological inhibitor or siDRP1 efficiently attenuated ethanol- or acetaldehyde-induced apoptosis, whereas activation of DRP1 by using staurosporine (STS) further increased apoptosis in ethanol- or acetaldehyde-treated HepG2 or HL7702 cells.	Acetaldehyde	121-133	dynamin 1 like	Homo sapiens	27-31
35443491-9	2022	Acetaldehyde binds exposed proteins which trigger immunoglobulin production.The antibodies directed against acetaldehyde adducts are predominantly IgA type.	Acetaldehyde	108-120	CD79a molecule	Homo sapiens	147-150
35114580-0	2022	Accumulation of acetaldehyde in aldh2.1-/- zebrafish causes increased retinal angiogenesis and impaired glucose metabolism.	Acetaldehyde	16-28	aldehyde dehydrogenase 2 family member, tandem duplicate 1	Danio rerio	32-39
35387552-7	2022	In addition, GZFL prevented acetaldehyde-induced activation of LX-2 cells via downregulation of TGF-beta1, p-Smad2, p-Smad3, CUGBP1, and upregulation of p-STAT1 and Smad7.	Acetaldehyde	28-40	transforming growth factor beta 1	Homo sapiens	96-105
35387552-7	2022	In addition, GZFL prevented acetaldehyde-induced activation of LX-2 cells via downregulation of TGF-beta1, p-Smad2, p-Smad3, CUGBP1, and upregulation of p-STAT1 and Smad7.	Acetaldehyde	28-40	CUGBP Elav-like family member 1	Homo sapiens	125-131
35158046-8	2022	Accordingly, inhibition of DRP1 activity with its pharmacological inhibitor or siDRP1 efficiently attenuated ethanol- or acetaldehyde-induced apoptosis, whereas activation of DRP1 by using staurosporine (STS) further increased apoptosis in ethanol- or acetaldehyde-treated HepG2 or HL7702 cells.	Acetaldehyde	252-264	dynamin 1 like	Homo sapiens	27-31
35158046-8	2022	Accordingly, inhibition of DRP1 activity with its pharmacological inhibitor or siDRP1 efficiently attenuated ethanol- or acetaldehyde-induced apoptosis, whereas activation of DRP1 by using staurosporine (STS) further increased apoptosis in ethanol- or acetaldehyde-treated HepG2 or HL7702 cells.	Acetaldehyde	252-264	dynamin 1 like	Homo sapiens	175-179
35425273-4	2022	It is found that a considerable blue-shift of Csp2 -H stretching frequency in the Csp2 -H O H-bond is mainly determined by an addition of water into the complexes along with the low polarity of the Csp2 -H covalent bond in formaldehyde and acetaldehyde.	Acetaldehyde	240-252	regulator of calcineurin 2	Homo sapiens	46-50
35159626-7	2022	A reproducible index by letting wine at pH 2 react with 35 mgL-1 of acetaldehyde for 7 days was obtained and applied to 12 wines.	Acetaldehyde	68-80	LLGL scribble cell polarity complex component 1	Homo sapiens	59-64
35114580-5	2022	aldh2.1-/- zebrafish displayed increased endogenous acetaldehyde (AA) inducing an increased angiogenesis in retinal vasculature.	Acetaldehyde	52-64	aldehyde dehydrogenase 2 family member, tandem duplicate 1	Danio rerio	0-7
35344413-2	2022	The most common variant allele, ALDH2*2, is present in 40-50% of East Asians, and causes acetaldehyde accumulation, flushing, and tachycardia after alcohol intake.	Acetaldehyde	89-101	aldehyde dehydrogenase 2 family member	Homo sapiens	32-37
35163684-2	2022	Since the ALDH polymorphism leads to the accumulation of acetaldehyde, we considered that the enhancement of the liver ALDH activity by certain food ingredients could help prevent alcohol-induced chronic diseases.	Acetaldehyde	57-69	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	10-14
35163684-2	2022	Since the ALDH polymorphism leads to the accumulation of acetaldehyde, we considered that the enhancement of the liver ALDH activity by certain food ingredients could help prevent alcohol-induced chronic diseases.	Acetaldehyde	57-69	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	119-123
35163684-7	2022	Silencing AhR impaired the resistant effect of OPAC against acetaldehyde.	Acetaldehyde	60-72	aryl hydrocarbon receptor	Homo sapiens	10-13
35163684-8	2022	These results strongly suggested that OPAC protects the cells from the acetaldehyde-induced cytotoxicity, mainly through the AhR-dependent and Nrf2-independent enhancement of the total ALDH activity.	Acetaldehyde	71-83	aryl hydrocarbon receptor	Homo sapiens	125-128
35163684-8	2022	These results strongly suggested that OPAC protects the cells from the acetaldehyde-induced cytotoxicity, mainly through the AhR-dependent and Nrf2-independent enhancement of the total ALDH activity.	Acetaldehyde	71-83	NFE2 like bZIP transcription factor 2	Homo sapiens	143-147
35163684-8	2022	These results strongly suggested that OPAC protects the cells from the acetaldehyde-induced cytotoxicity, mainly through the AhR-dependent and Nrf2-independent enhancement of the total ALDH activity.	Acetaldehyde	71-83	aldehyde dehydrogenase family 3, subfamily A1	Mus musculus	185-189
34940794-5	2022	The main objective of the study was to investigate retinaldehyde dehydrogenases (RALDHs), of which retinal is the main substrate and ALDH2, the mitochondrial isoform, having acetaldehyde as the main substrate.	Acetaldehyde	174-186	aldehyde dehydrogenase 2 family member	Homo sapiens	133-138
35425273-4	2022	It is found that a considerable blue-shift of Csp2 -H stretching frequency in the Csp2 -H O H-bond is mainly determined by an addition of water into the complexes along with the low polarity of the Csp2 -H covalent bond in formaldehyde and acetaldehyde.	Acetaldehyde	240-252	regulator of calcineurin 2	Homo sapiens	82-86
35425273-4	2022	It is found that a considerable blue-shift of Csp2 -H stretching frequency in the Csp2 -H O H-bond is mainly determined by an addition of water into the complexes along with the low polarity of the Csp2 -H covalent bond in formaldehyde and acetaldehyde.	Acetaldehyde	240-252	regulator of calcineurin 2	Homo sapiens	198-202