PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
32478940-6	2020	We found that 1,4-BQ significantly decreased LC levels and downregulated Cpt1a, Cpt2, Crat, Hadha, Acaa2, and Acadvl mRNA expression in K562 cells.	quinone	14-20	carnitine O-acetyltransferase	Homo sapiens	86-90
35578012-2	2022	The carnitine acetyltransferase (CrAT) catalyzes the reaction between acetyl-CoA and L-carnitine to produce CoA which is difficult to detect directly by electrochemical methods owing to steric hindrance and electrostatic effect of CoA.	Acetyl Coenzyme A	70-80	carnitine O-acetyltransferase	Homo sapiens	4-31
35578012-2	2022	The carnitine acetyltransferase (CrAT) catalyzes the reaction between acetyl-CoA and L-carnitine to produce CoA which is difficult to detect directly by electrochemical methods owing to steric hindrance and electrostatic effect of CoA.	Acetyl Coenzyme A	70-80	carnitine O-acetyltransferase	Homo sapiens	33-37
35578012-2	2022	The carnitine acetyltransferase (CrAT) catalyzes the reaction between acetyl-CoA and L-carnitine to produce CoA which is difficult to detect directly by electrochemical methods owing to steric hindrance and electrostatic effect of CoA.	Carnitine	85-96	carnitine O-acetyltransferase	Homo sapiens	4-31
35578012-2	2022	The carnitine acetyltransferase (CrAT) catalyzes the reaction between acetyl-CoA and L-carnitine to produce CoA which is difficult to detect directly by electrochemical methods owing to steric hindrance and electrostatic effect of CoA.	Carnitine	85-96	carnitine O-acetyltransferase	Homo sapiens	33-37
33105059-0	2020	CR reprograms acetyl-CoA metabolism and induces long-chain acyl-CoA dehydrogenase and CrAT expression.	Chromium	0-2	carnitine O-acetyltransferase	Homo sapiens	86-90
33105059-10	2020	Carnitine acetyltransferase (CrAT) is a bidirectional enzyme that interconverts short-chain acyl-CoAs and their corresponding acylcarnitines.	Acyl Coenzyme A	92-101	carnitine O-acetyltransferase	Homo sapiens	0-27
33105059-10	2020	Carnitine acetyltransferase (CrAT) is a bidirectional enzyme that interconverts short-chain acyl-CoAs and their corresponding acylcarnitines.	Acyl Coenzyme A	92-101	carnitine O-acetyltransferase	Homo sapiens	29-33
33105059-10	2020	Carnitine acetyltransferase (CrAT) is a bidirectional enzyme that interconverts short-chain acyl-CoAs and their corresponding acylcarnitines.	acylcarnitine	126-140	carnitine O-acetyltransferase	Homo sapiens	0-27
33105059-10	2020	Carnitine acetyltransferase (CrAT) is a bidirectional enzyme that interconverts short-chain acyl-CoAs and their corresponding acylcarnitines.	acylcarnitine	126-140	carnitine O-acetyltransferase	Homo sapiens	29-33
33105059-11	2020	CrAT expression was induced in CR liver supporting the increased acetylcarnitine and short-chain acylcarnitine production.	Acetylcarnitine	65-80	carnitine O-acetyltransferase	Homo sapiens	0-4
33105059-11	2020	CrAT expression was induced in CR liver supporting the increased acetylcarnitine and short-chain acylcarnitine production.	acylcarnitine	97-110	carnitine O-acetyltransferase	Homo sapiens	0-4
28965027-0	2018	l-carnitine supplementation during vitrification or warming of in vivo-produced ovine embryos does not affect embryonic survival rates, but alters CrAT and PRDX1 expression.	Carnitine	0-11	carnitine O-acetyltransferase	Homo sapiens	147-151
32641979-8	2020	CPT 1A, CPT 2, and CRAT, which are extensively involved in carnitine system-mediated fatty acid beta-oxidation pathway were also found to be abnormally expressed in breast cancer.	Carnitine	59-68	carnitine O-acetyltransferase	Homo sapiens	19-23
32641979-8	2020	CPT 1A, CPT 2, and CRAT, which are extensively involved in carnitine system-mediated fatty acid beta-oxidation pathway were also found to be abnormally expressed in breast cancer.	Fatty Acids	85-95	carnitine O-acetyltransferase	Homo sapiens	19-23
30266950-6	2018	One single-nucleotide polymorphism, rs10988217, which is located 15-kb upstream of carnitine O-acetyltransferase (CRAT), was significantly associated with DQB1*06:02-negative EHS (P = 7.5 x 10-9, odds ratio = 2.63).	ehs	175-178	carnitine O-acetyltransferase	Homo sapiens	83-112
30266950-6	2018	One single-nucleotide polymorphism, rs10988217, which is located 15-kb upstream of carnitine O-acetyltransferase (CRAT), was significantly associated with DQB1*06:02-negative EHS (P = 7.5 x 10-9, odds ratio = 2.63).	ehs	175-178	carnitine O-acetyltransferase	Homo sapiens	114-118
32710884-1	2020	Mammalian carnitine acetyltransferase (CrAT) is a mitochondrial enzyme that catalyzes the reversible transfer of an acetyl group from acetyl-CoA to carnitine.	Acetyl Coenzyme A	134-144	carnitine O-acetyltransferase	Homo sapiens	10-37
32710884-1	2020	Mammalian carnitine acetyltransferase (CrAT) is a mitochondrial enzyme that catalyzes the reversible transfer of an acetyl group from acetyl-CoA to carnitine.	Acetyl Coenzyme A	134-144	carnitine O-acetyltransferase	Homo sapiens	39-43
32710884-1	2020	Mammalian carnitine acetyltransferase (CrAT) is a mitochondrial enzyme that catalyzes the reversible transfer of an acetyl group from acetyl-CoA to carnitine.	Carnitine	10-19	carnitine O-acetyltransferase	Homo sapiens	39-43
32710884-6	2020	A great preference for ordered binding is supported by stopped-flow double mixing experiments such that premixed CrAT with acetyl-CoA or CoA demonstrated a biphasic decrease in initial rate that produces about a 100-fold attenuation in catalysis.	Acetyl Coenzyme A	123-133	carnitine O-acetyltransferase	Homo sapiens	113-117
32710884-7	2020	Double mixing experiments also revealed that the CrAT initial rate is inhibited by 50% in approximately 8 s by either acetyl-CoA or CoA premixing.	Acetyl Coenzyme A	118-128	carnitine O-acetyltransferase	Homo sapiens	49-53
31448845-4	2020	Functional analyses of recombinant-purified CRAT proteins demonstrated that both missense variants, located in the acyl-group binding site of the enzyme, severely impair its catalytic function toward acetyl-CoA, and the p.Val569Met variant also toward propionyl-CoA and octanoyl-CoA.	Acetyl Coenzyme A	200-210	carnitine O-acetyltransferase	Homo sapiens	44-48
31448845-4	2020	Functional analyses of recombinant-purified CRAT proteins demonstrated that both missense variants, located in the acyl-group binding site of the enzyme, severely impair its catalytic function toward acetyl-CoA, and the p.Val569Met variant also toward propionyl-CoA and octanoyl-CoA.	propionyl-coenzyme A	252-265	carnitine O-acetyltransferase	Homo sapiens	44-48
31448845-4	2020	Functional analyses of recombinant-purified CRAT proteins demonstrated that both missense variants, located in the acyl-group binding site of the enzyme, severely impair its catalytic function toward acetyl-CoA, and the p.Val569Met variant also toward propionyl-CoA and octanoyl-CoA.	octanoyl-coenzyme A	270-282	carnitine O-acetyltransferase	Homo sapiens	44-48
31448845-5	2020	Although a single recessive variant in CRAT has been recently associated with neurodegeneration with brain iron accumulation, our study reports the first kinetic analysis of naturally occurring CRAT variants and demonstrates the genetic basis of carnitine acetyltransferase deficiency in a case of mitochondrial encephalopathy.	Iron	107-111	carnitine O-acetyltransferase	Homo sapiens	39-43
31448845-5	2020	Although a single recessive variant in CRAT has been recently associated with neurodegeneration with brain iron accumulation, our study reports the first kinetic analysis of naturally occurring CRAT variants and demonstrates the genetic basis of carnitine acetyltransferase deficiency in a case of mitochondrial encephalopathy.	Iron	107-111	carnitine O-acetyltransferase	Homo sapiens	194-198
30327559-3	2018	Here we demonstrate that mmBCFAs are de novo synthesized via mitochondrial BCAA catabolism, exported to the cytosol by adipose-specific expression of carnitine acetyltransferase (CrAT), and elongated by FASN.	mmbcfas	25-32	carnitine O-acetyltransferase	Homo sapiens	150-177
30327559-3	2018	Here we demonstrate that mmBCFAs are de novo synthesized via mitochondrial BCAA catabolism, exported to the cytosol by adipose-specific expression of carnitine acetyltransferase (CrAT), and elongated by FASN.	mmbcfas	25-32	carnitine O-acetyltransferase	Homo sapiens	179-183
29444428-3	2018	Crat deletion in AgRP neurons reduced food intake and feeding behavior and increased glycerol supply to the liver during fasting, as a gluconeogenic substrate, which was mediated by changes to sympathetic output and peripheral fatty acid metabolism in the liver.	Glycerol	85-93	carnitine O-acetyltransferase	Homo sapiens	0-4
29444428-3	2018	Crat deletion in AgRP neurons reduced food intake and feeding behavior and increased glycerol supply to the liver during fasting, as a gluconeogenic substrate, which was mediated by changes to sympathetic output and peripheral fatty acid metabolism in the liver.	Fatty Acids	227-237	carnitine O-acetyltransferase	Homo sapiens	0-4
29444428-4	2018	Crat deletion in AgRP neurons increased peripheral fatty acid substrate utilization and attenuated the switch to glucose utilization after refeeding, indicating altered nutrient partitioning.	Fatty Acids	51-61	carnitine O-acetyltransferase	Homo sapiens	0-4
29444428-4	2018	Crat deletion in AgRP neurons increased peripheral fatty acid substrate utilization and attenuated the switch to glucose utilization after refeeding, indicating altered nutrient partitioning.	Glucose	113-120	carnitine O-acetyltransferase	Homo sapiens	0-4
29395073-3	2018	After studying fibroblast cell lines from subjects carrying both known and unreported biallelic mutations in CRAT and REPS1, we ascribe iron overload to the abnormal recycling of transferrin receptor (TfR1) and the reduction of TfR1 palmitoylation in NBIA.	Iron	136-140	carnitine O-acetyltransferase	Homo sapiens	109-113
26154055-2	2015	Short-chain carnitine conjugates, including acetylcarnitine, derive from their corresponding acyl-CoA precursors via the action of carnitine acetyltransferase (CrAT), a bidirectional mitochondrial matrix enzyme.	Carnitine	12-21	carnitine O-acetyltransferase	Homo sapiens	131-158
28671672-7	2017	CPT1A, CACT and CrAT overexpression allow PCCs to be more prone on FA utilization than normal prostate cells, also in the presence of high pyruvate concentration.	Pyruvic Acid	139-147	carnitine O-acetyltransferase	Homo sapiens	16-20
26388708-4	2015	CLA supplementation also could increase the lipolysis and reduce the accumulation of fatty acids on the adipose tissue; the putative mechanisms involved may be its action in reducing the lipase lipoprotein activity and to increase the carnitine-palmitoil-transferase-1 (CAT-1) activity, its interaction with PPARgamma, and to raise the expression of UCP-1.	Linoleic Acids, Conjugated	0-3	carnitine O-acetyltransferase	Homo sapiens	235-268
26388708-4	2015	CLA supplementation also could increase the lipolysis and reduce the accumulation of fatty acids on the adipose tissue; the putative mechanisms involved may be its action in reducing the lipase lipoprotein activity and to increase the carnitine-palmitoil-transferase-1 (CAT-1) activity, its interaction with PPARgamma, and to raise the expression of UCP-1.	Linoleic Acids, Conjugated	0-3	carnitine O-acetyltransferase	Homo sapiens	270-275
26154055-2	2015	Short-chain carnitine conjugates, including acetylcarnitine, derive from their corresponding acyl-CoA precursors via the action of carnitine acetyltransferase (CrAT), a bidirectional mitochondrial matrix enzyme.	Carnitine	12-21	carnitine O-acetyltransferase	Homo sapiens	160-164
26154055-2	2015	Short-chain carnitine conjugates, including acetylcarnitine, derive from their corresponding acyl-CoA precursors via the action of carnitine acetyltransferase (CrAT), a bidirectional mitochondrial matrix enzyme.	Acetylcarnitine	44-59	carnitine O-acetyltransferase	Homo sapiens	131-158
26154055-2	2015	Short-chain carnitine conjugates, including acetylcarnitine, derive from their corresponding acyl-CoA precursors via the action of carnitine acetyltransferase (CrAT), a bidirectional mitochondrial matrix enzyme.	Acetylcarnitine	44-59	carnitine O-acetyltransferase	Homo sapiens	160-164
26154055-2	2015	Short-chain carnitine conjugates, including acetylcarnitine, derive from their corresponding acyl-CoA precursors via the action of carnitine acetyltransferase (CrAT), a bidirectional mitochondrial matrix enzyme.	Coenzyme A	98-101	carnitine O-acetyltransferase	Homo sapiens	131-158
26154055-2	2015	Short-chain carnitine conjugates, including acetylcarnitine, derive from their corresponding acyl-CoA precursors via the action of carnitine acetyltransferase (CrAT), a bidirectional mitochondrial matrix enzyme.	Coenzyme A	98-101	carnitine O-acetyltransferase	Homo sapiens	160-164
26154055-5	2015	Likewise, in exercise-trained compared to untrained humans, post-exercise phosphocreatine recovery rates were positively associated with CrAT activity and coincided with dramatic shifts in muscle acetylcarnitine dynamics.	Phosphocreatine	74-89	carnitine O-acetyltransferase	Homo sapiens	137-141
24395925-1	2014	Carnitine acetyltransferase (CrAT) is a mitochondrial matrix enzyme that catalyzes the interconversion of acetyl-CoA and acetylcarnitine.	Acetyl Coenzyme A	106-116	carnitine O-acetyltransferase	Homo sapiens	0-27
26010953-3	2015	A group of genes, namely CPT1A, CPT1B, CPT1C, CPT2, CRAT and CROT, encode for three carnitine acyltransferases that are important for the oxidation of fatty acids, a critical step in their metabolism.	Fatty Acids	151-162	carnitine O-acetyltransferase	Homo sapiens	52-56
24395925-1	2014	Carnitine acetyltransferase (CrAT) is a mitochondrial matrix enzyme that catalyzes the interconversion of acetyl-CoA and acetylcarnitine.	Acetyl Coenzyme A	106-116	carnitine O-acetyltransferase	Homo sapiens	29-33
24395925-1	2014	Carnitine acetyltransferase (CrAT) is a mitochondrial matrix enzyme that catalyzes the interconversion of acetyl-CoA and acetylcarnitine.	Acetylcarnitine	121-136	carnitine O-acetyltransferase	Homo sapiens	0-27
24395925-1	2014	Carnitine acetyltransferase (CrAT) is a mitochondrial matrix enzyme that catalyzes the interconversion of acetyl-CoA and acetylcarnitine.	Acetylcarnitine	121-136	carnitine O-acetyltransferase	Homo sapiens	29-33
24395925-6	2014	In vitro assays demonstrated that palmitoyl-CoA acts as a direct mixed-model inhibitor of CrAT.	Palmitoyl Coenzyme A	34-47	carnitine O-acetyltransferase	Homo sapiens	90-94
24395925-7	2014	Similarly, in primary human myocytes grown in culture, nutritional and genetic manipulations that promoted mitochondrial influx of fatty acids resulted in accumulation of LCACs but a pronounced decrease of CrAT-derived short-chain acylcarnitines.	acylcarnitine	231-245	carnitine O-acetyltransferase	Homo sapiens	206-210
24395925-8	2014	These results suggest that lipid-induced antagonism of CrAT might contribute to decreased PDH activity and glucose disposal in the context of obesity and diabetes.	Glucose	107-114	carnitine O-acetyltransferase	Homo sapiens	55-59
22560225-0	2012	Muscle-specific deletion of carnitine acetyltransferase compromises glucose tolerance and metabolic flexibility.	Glucose	68-75	carnitine O-acetyltransferase	Homo sapiens	28-55
23485643-0	2013	Substrate specificity of human carnitine acetyltransferase: Implications for fatty acid and branched-chain amino acid metabolism.	Fatty Acids	77-87	carnitine O-acetyltransferase	Homo sapiens	31-58
23485643-0	2013	Substrate specificity of human carnitine acetyltransferase: Implications for fatty acid and branched-chain amino acid metabolism.	Amino Acids, Branched-Chain	92-117	carnitine O-acetyltransferase	Homo sapiens	31-58
23485643-6	2013	In order to explore the origin of short-chain and branched-chain acylcarnitines that may accumulate in various organic acidemias, we performed substrate specificity studies using purified recombinant human CrAT.	acylcarnitine	65-79	carnitine O-acetyltransferase	Homo sapiens	206-210
23485643-8	2013	We show that CrAT converts short- and medium-chain acyl-CoAs (C2 to C10-CoA), whereas no activity was observed with long-chain species.	Acyl Coenzyme A	51-60	carnitine O-acetyltransferase	Homo sapiens	13-17
23485643-8	2013	We show that CrAT converts short- and medium-chain acyl-CoAs (C2 to C10-CoA), whereas no activity was observed with long-chain species.	c10-coa	68-75	carnitine O-acetyltransferase	Homo sapiens	13-17
23485643-10	2013	Furthermore, CrAT turned out to be active towards some but not all the BCAAO intermediates tested and no activity was found with dicarboxylic acyl-CoA esters.	bcaao	71-76	carnitine O-acetyltransferase	Homo sapiens	13-17
23485643-11	2013	This suggests the existence of another enzyme able to handle the acyl-CoAs that are not substrates for CrAT and CPT2, but for which the corresponding acylcarnitines are well recognized as diagnostic markers in inborn errors of metabolism.	Acyl Coenzyme A	65-74	carnitine O-acetyltransferase	Homo sapiens	103-107
23344032-0	2012	Role of carnitine acetyl transferase in regulation of nitric oxide signaling in pulmonary arterial endothelial cells.	Nitric Oxide	54-66	carnitine O-acetyltransferase	Homo sapiens	8-36
23344032-2	2012	Utilizing a lamb model with left-to-right shunting of blood and increased PBF that mimics the human disease, we have recently shown that a disruption in carnitine homeostasis, due to a decreased carnitine acetyl transferase (CrAT) activity, correlates with decreased bioavailable NO.	Carnitine	153-162	carnitine O-acetyltransferase	Homo sapiens	195-223
23344032-2	2012	Utilizing a lamb model with left-to-right shunting of blood and increased PBF that mimics the human disease, we have recently shown that a disruption in carnitine homeostasis, due to a decreased carnitine acetyl transferase (CrAT) activity, correlates with decreased bioavailable NO.	Carnitine	153-162	carnitine O-acetyltransferase	Homo sapiens	225-229
23344032-5	2012	Our data indicate that silencing the CrAT gene disrupted cellular carnitine homeostasis, reduced the expression of mitochondrial superoxide dismutase-and resulted in an increase in oxidative stress within the mitochondrion.	Carnitine	66-75	carnitine O-acetyltransferase	Homo sapiens	37-41
23344032-6	2012	CrAT gene silencing also disrupted mitochondrial bioenergetics resulting in reduced ATP generation and decreased NO signaling secondary to a reduction in eNOS/Hsp90 interactions.	Adenosine Triphosphate	84-87	carnitine O-acetyltransferase	Homo sapiens	0-4
22560225-3	2012	Here, we identify an essential role for the mitochondrial matrix enzyme, carnitine acetyltransferase (CrAT), in regulating substrate switching and glucose tolerance.	Glucose	147-154	carnitine O-acetyltransferase	Homo sapiens	73-100
22560225-3	2012	Here, we identify an essential role for the mitochondrial matrix enzyme, carnitine acetyltransferase (CrAT), in regulating substrate switching and glucose tolerance.	Glucose	147-154	carnitine O-acetyltransferase	Homo sapiens	102-106
22560225-4	2012	By converting acetyl-CoA to its membrane permeant acetylcarnitine ester, CrAT regulates mitochondrial and intracellular carbon trafficking.	Acetyl Coenzyme A	14-24	carnitine O-acetyltransferase	Homo sapiens	73-77
22560225-4	2012	By converting acetyl-CoA to its membrane permeant acetylcarnitine ester, CrAT regulates mitochondrial and intracellular carbon trafficking.	acetylcarnitine ester	50-71	carnitine O-acetyltransferase	Homo sapiens	73-77
22560225-4	2012	By converting acetyl-CoA to its membrane permeant acetylcarnitine ester, CrAT regulates mitochondrial and intracellular carbon trafficking.	Carbon	120-126	carnitine O-acetyltransferase	Homo sapiens	73-77
22560225-5	2012	Studies in muscle-specific Crat knockout mice, primary human skeletal myocytes, and human subjects undergoing L-carnitine supplementation support a model wherein CrAT combats nutrient stress, promotes metabolic flexibility, and enhances insulin action by permitting mitochondrial efflux of excess acetyl moieties that otherwise inhibit key regulatory enzymes such as pyruvate dehydrogenase.	Carnitine	110-121	carnitine O-acetyltransferase	Homo sapiens	162-166
22560225-5	2012	Studies in muscle-specific Crat knockout mice, primary human skeletal myocytes, and human subjects undergoing L-carnitine supplementation support a model wherein CrAT combats nutrient stress, promotes metabolic flexibility, and enhances insulin action by permitting mitochondrial efflux of excess acetyl moieties that otherwise inhibit key regulatory enzymes such as pyruvate dehydrogenase.	Cysteine	297-303	carnitine O-acetyltransferase	Homo sapiens	162-166
19912061-0	2009	Inhibition of carnitine acetyltransferase by mildronate, a regulator of energy metabolism.	3-(2,2,2-trimethylhydrazine)propionate	45-55	carnitine O-acetyltransferase	Homo sapiens	14-41
19912061-1	2009	Carnitine acetyltransferase (CrAT; EC 2.3.1.7) catalyzes the reversible transfer of acetyl groups between acetyl-coenzyme A (acetyl-CoA) and L-carnitine; it also regulates the cellular pool of CoA and the availability of activated acetyl groups.	Acetyl Coenzyme A	125-135	carnitine O-acetyltransferase	Homo sapiens	0-27
19912061-1	2009	Carnitine acetyltransferase (CrAT; EC 2.3.1.7) catalyzes the reversible transfer of acetyl groups between acetyl-coenzyme A (acetyl-CoA) and L-carnitine; it also regulates the cellular pool of CoA and the availability of activated acetyl groups.	Acetyl Coenzyme A	125-135	carnitine O-acetyltransferase	Homo sapiens	29-33
19912061-1	2009	Carnitine acetyltransferase (CrAT; EC 2.3.1.7) catalyzes the reversible transfer of acetyl groups between acetyl-coenzyme A (acetyl-CoA) and L-carnitine; it also regulates the cellular pool of CoA and the availability of activated acetyl groups.	Carnitine	141-152	carnitine O-acetyltransferase	Homo sapiens	0-27
19912061-1	2009	Carnitine acetyltransferase (CrAT; EC 2.3.1.7) catalyzes the reversible transfer of acetyl groups between acetyl-coenzyme A (acetyl-CoA) and L-carnitine; it also regulates the cellular pool of CoA and the availability of activated acetyl groups.	Carnitine	141-152	carnitine O-acetyltransferase	Homo sapiens	29-33
19912061-2	2009	In this study, biochemical measurements, saturation transfer difference (STD) nuclear magnetic resonance (NMR) spectroscopy, and molecular docking were applied to give insights into the CrAT binding of a synthetic inhibitor, the cardioprotective drug mildronate (3-(2,2,2-trimethylhydrazinium)-propionate).	3-(2,2,2-trimethylhydrazine)propionate	251-261	carnitine O-acetyltransferase	Homo sapiens	186-190
19912061-2	2009	In this study, biochemical measurements, saturation transfer difference (STD) nuclear magnetic resonance (NMR) spectroscopy, and molecular docking were applied to give insights into the CrAT binding of a synthetic inhibitor, the cardioprotective drug mildronate (3-(2,2,2-trimethylhydrazinium)-propionate).	3-(2,2,2-trimethylhydrazine)propionate	263-304	carnitine O-acetyltransferase	Homo sapiens	186-190
19912061-3	2009	The obtained results show that mildronate inhibits CrAT in a competitive manner through binding to the carnitine binding site, not the acetyl-CoA binding site.	3-(2,2,2-trimethylhydrazine)propionate	31-41	carnitine O-acetyltransferase	Homo sapiens	51-55
19912061-3	2009	The obtained results show that mildronate inhibits CrAT in a competitive manner through binding to the carnitine binding site, not the acetyl-CoA binding site.	Carnitine	103-112	carnitine O-acetyltransferase	Homo sapiens	51-55
19912061-5	2009	The dissociation constant of the mildronate CrAT complex is approximately 0.1 mM, and the K(i) is 1.6 mM.	3-(2,2,2-trimethylhydrazine)propionate	33-43	carnitine O-acetyltransferase	Homo sapiens	44-48
19912061-6	2009	The results suggest that the cardioprotective effect of mildronate might be partially mediated by CrAT inhibition and concomitant regulation of cellular energy metabolism pathways.	3-(2,2,2-trimethylhydrazine)propionate	56-66	carnitine O-acetyltransferase	Homo sapiens	98-102
19553674-8	2009	Acetylcarnitine is produced by the mitochondrial matrix enzyme, carnitine acetyltransferase (CrAT).	Acetylcarnitine	0-15	carnitine O-acetyltransferase	Homo sapiens	64-91
19553674-8	2009	Acetylcarnitine is produced by the mitochondrial matrix enzyme, carnitine acetyltransferase (CrAT).	Acetylcarnitine	0-15	carnitine O-acetyltransferase	Homo sapiens	93-97
19553674-9	2009	A role for this enzyme in combating glucose intolerance was further supported by the finding that CrAT overexpression in primary human skeletal myocytes increased glucose uptake and attenuated lipid-induced suppression of glucose oxidation.	Glucose	36-43	carnitine O-acetyltransferase	Homo sapiens	98-102
19553674-9	2009	A role for this enzyme in combating glucose intolerance was further supported by the finding that CrAT overexpression in primary human skeletal myocytes increased glucose uptake and attenuated lipid-induced suppression of glucose oxidation.	Glucose	163-170	carnitine O-acetyltransferase	Homo sapiens	98-102