PMID-sentid	Pub_year	Sent_text	comp_official_name	comp_offset	protein_name	organism	prot_offset
30935417-11	2019	The upregulation of atrial and ventricular expression of PPARalpha, ACADM, natriuretic peptides (NPPA and NPPB), and TNF-alpha in SHR, was all restored by treatment of empagliflozin.	empagliflozin	168-181	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	68-73
3611054-4	1987	The identity of the medium chain acyl-CoA dehydrogenase clone was confirmed by matching the amino acid sequence predicted from the cDNA to the NH2-terminal and nine internal tryptic peptide sequences derived from pure rat liver medium chain acyl-CoA dehydrogenase.	Peptides	182-189	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	20-55
3611054-8	1987	Comparison of medium chain acyl-CoA dehydrogenase sequence to other flavoproteins and enzymes which act on coenzyme A ester substrates did not lead to unambiguous identification of a possible FAD-binding site nor a coenzyme A-binding domain.	Esters	118-123	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	14-49
33755174-6	2021	Furthermore, ERRalpha/PGC-1beta and their target genes MCAD and CPT-1 were increased and regulated by AMPK, which coincided with increased fatty acid oxidation (FAO) and autophagy in TAM-resistant cells.	Fatty Acids	139-149	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	55-59
33755174-6	2021	Furthermore, ERRalpha/PGC-1beta and their target genes MCAD and CPT-1 were increased and regulated by AMPK, which coincided with increased fatty acid oxidation (FAO) and autophagy in TAM-resistant cells.	Tamoxifen	183-186	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	55-59
33755174-7	2021	Inhibition of AKT feedback activates AMPK and ERRalpha/PGC-1beta-MCAD/CPT-1 with a consequent increase in FAO and autophagy that counters the therapeutic effect of endoxifen and AKT inhibitors.	4-hydroxy-N-desmethyltamoxifen	164-173	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	65-69
22738961-7	2012	Treatment with AE enhanced the expression of the acyl-CoA oxidase 1 (ACO1), medium-chain acyl-CoA dehydrogenase (MCAD), ATP-binding membrane cassette transporter A1 (ABCA1) and apolipoprotein A1 (Apo-A1) genes.	alanylglutamic acid	15-17	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	76-111
29278547-9	2018	In salt-loaded SHRSPs, we observed severe morphological mitochondrial alterations, reduced SDH activity, and down-regulation of genes regulating mitochondrial fatty-acid oxidation (i.e. PPARalpha, SIRT3, and Acadm).	Salts	3-7	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	208-213
22874759-7	2012	Among the enzymes of fatty acid metabolism, expressions of medium-chain acyl-CoA dehydrogenase (MCAD) and cytochrome P-450 (CYP)4A significantly decreased in PTECs of PAN-treated SDRs.	Fatty Acids	21-31	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	59-94
22874759-7	2012	Among the enzymes of fatty acid metabolism, expressions of medium-chain acyl-CoA dehydrogenase (MCAD) and cytochrome P-450 (CYP)4A significantly decreased in PTECs of PAN-treated SDRs.	Fatty Acids	21-31	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	96-100
30138942-13	2018	Fenofibrate prevented PE-induced down regulation of PPARalpha-target genes like CPT-I and MCAD.	Fenofibrate	0-11	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	90-94
26949064-11	2016	Clofibrate minimized changes in MCAD, CYP4A, PGC-1alpha and ERRalpha expressions with increased PPARalpha, very long-chain acyl-CoA dehydrogenase (VLCAD) and long-chain acyl-CoA dehydrogenase (LCAD) expressions.	Clofibrate	0-10	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	32-36
26068433-7	2015	Treatment with GGH(4), the individual components or curcmumin increased mRNA levels of mitochondrial (CPT-1, MCAD, and VLCAD) and peroxisomal (ACOX and thiolase) PPARalpha target genes.	curcmumin	52-61	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	109-113
25132363-8	2014	Carnitine palmitoyltransferase (CPT) 2 levels in liver and medium-chain acyl-CoA dehydrogenase (MCAD) levels in gastrocnemius and liver were significantly increased by the supplementation of flavan-3-ols.	flavan-3-ol	191-203	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	59-94
25132363-8	2014	Carnitine palmitoyltransferase (CPT) 2 levels in liver and medium-chain acyl-CoA dehydrogenase (MCAD) levels in gastrocnemius and liver were significantly increased by the supplementation of flavan-3-ols.	flavan-3-ol	191-203	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	96-100
22738961-7	2012	Treatment with AE enhanced the expression of the acyl-CoA oxidase 1 (ACO1), medium-chain acyl-CoA dehydrogenase (MCAD), ATP-binding membrane cassette transporter A1 (ABCA1) and apolipoprotein A1 (Apo-A1) genes.	alanylglutamic acid	15-17	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	113-117
21700370-6	2011	Muscle genes controlling mitochondrial beta-oxidation (PPARs, MCAD and CPT-1b) were up-regulated in the HFO group.	1,3,3,3-tetrafluoropropene	104-107	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	62-66
21310443-4	2011	Despite an attempt to compensate by increasing expression of genes of fatty acid oxidation (carnitine palmitoyl transferase-1/medium chain acyl-CoA dehydrogenase), the HFD and diabetic groups developed marked steatosis and suffered a significant reduction in mitochondrial biogenesis gene expression (nuclear respiratory factor 1/transcriptional factor A, mitochondrial).	Fatty Acids	70-80	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	112-161
21169901-14	2011	mRNA and protein expression of PPARalpha, CPT-I, MCAD, ANT1 and ATPase expressions were gradually altered in groups following alcohol feeding.	Alcohols	126-133	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	49-53
21169901-16	2011	Carnitine may improve myocardial metabolism by elevating the content of PPARalpha, CPT-I and MCAD.	Carnitine	0-9	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	93-97
19699196-5	2009	Treatment of TAC animals with 5-aminoimidazole 1 carboxamide ribonucleoside (AICAR, 0.5 mg/g body wt), a specific activator of AMPK, inhibited cardiac hypertrophy in TAC and reversed PPARalpha, CPT-I and MCAD expression and fatty acid oxidation.	4-aminoimidazole	30-46	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	204-208
19699196-5	2009	Treatment of TAC animals with 5-aminoimidazole 1 carboxamide ribonucleoside (AICAR, 0.5 mg/g body wt), a specific activator of AMPK, inhibited cardiac hypertrophy in TAC and reversed PPARalpha, CPT-I and MCAD expression and fatty acid oxidation.	carboxamide ribonucleoside	49-75	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	204-208
19699196-5	2009	Treatment of TAC animals with 5-aminoimidazole 1 carboxamide ribonucleoside (AICAR, 0.5 mg/g body wt), a specific activator of AMPK, inhibited cardiac hypertrophy in TAC and reversed PPARalpha, CPT-I and MCAD expression and fatty acid oxidation.	acadesine	77-82	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	204-208
20011657-4	2009	Here we demonstrate that fasting of rats increased mRNA concentrations of typical PPARalpha target genes implicated in beta-oxidation of fatty acids (acyl-CoA oxidase, carnitine palmitoyltransferase-1, medium chain acyl-CoA dehydrogenase) and ketogenesis (mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase) in pituitary gland and partially also in frontal cortex and diencephalon compared to nonfasted animals.	Fatty Acids	137-148	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	168-237
17352811-6	2007	In addition, in both experiments fetuses of the oxidized fat group and the clofibrate group also had markedly higher relative mRNA concentrations of ACO, CYP4A1, CPT I, MCAD, and LCAD in the liver than those of the control group (P < 0.05), whereas the relative mRNA concentrations of PPARalpha, SREBP-1c, and FAS did not differ between treatment groups.	Clofibrate	75-85	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	169-173
18456726-8	2008	Administration of MCT of SHRs reversed the LCT-induced reduction in the cardiac FA metabolic enzymatic activities of long-chain 3-hydroxyacyl-CoA dehydrogenase (LCHAD) and medium-chain acyl-CoA dehydrogenase (MCAD).	N-[5-(4-Nitrophenyl)-1,3,4-thiadiazol-2-yl]acetamide	43-46	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	172-207
18456726-8	2008	Administration of MCT of SHRs reversed the LCT-induced reduction in the cardiac FA metabolic enzymatic activities of long-chain 3-hydroxyacyl-CoA dehydrogenase (LCHAD) and medium-chain acyl-CoA dehydrogenase (MCAD).	N-[5-(4-Nitrophenyl)-1,3,4-thiadiazol-2-yl]acetamide	43-46	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	209-213
18171348-10	2008	However, the treatment-induced modulation of fatty-acid beta-oxidation enzymes was confined to FATP and MCAD in group IV.	Fatty Acids	45-55	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	104-108
15927499-2	2005	MCAD is a mitochondrial enzyme involved in the fatty acid metabolism and previous studies in isolated rat mitochondria or prokaryotic expression systems have shown that Hsp60 and GroEL are involved in the folding of MCAD proteins.	Fatty Acids	47-57	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	0-4
15927499-2	2005	MCAD is a mitochondrial enzyme involved in the fatty acid metabolism and previous studies in isolated rat mitochondria or prokaryotic expression systems have shown that Hsp60 and GroEL are involved in the folding of MCAD proteins.	Fatty Acids	47-57	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	216-220
15863369-4	2005	Supplementation with ALADG significantly inhibited hepatic triglyceride accumulation; this was accompanied by the up-regulation of beta-oxidation activity, and acyl-CoA oxidase (ACO) and medium-chain acyl-CoA dehydrogenase (MCAD) mRNA levels.	aladg	21-26	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	187-222
15863369-4	2005	Supplementation with ALADG significantly inhibited hepatic triglyceride accumulation; this was accompanied by the up-regulation of beta-oxidation activity, and acyl-CoA oxidase (ACO) and medium-chain acyl-CoA dehydrogenase (MCAD) mRNA levels.	aladg	21-26	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	224-228
15852996-11	2005	CONCLUSIONS: Ketamine induces various metabolic effects due to changes in adipose LPL activity and MCAD levels in muscles.	Ketamine	13-21	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	99-103
15358373-0	2004	Expression and purification of His-tagged rat mitochondrial medium-chain acyl-CoA dehydrogenase wild-type and Arg256 mutant proteins.	Histidine	31-34	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	60-95
15358373-1	2004	Mitochondrial medium-chain acyl-CoA dehydrogenase is a key enzyme for the beta-oxidation of fatty acids, and the deficiency of this enzyme in patient has been previously reported.	Fatty Acids	92-103	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	14-49
15358373-2	2004	We cloned the gene of rat mitochondrial medium-chain acyl-CoA dehydrogenase into a bacterial expression vector pLM1 with six continuous histidine codons attached to the 3" of the gene.	Histidine	136-145	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	40-75
11872165-5	2002	However, the N-terminal alpha- and beta-domains rotate by 13 with respect to the C-terminal alpha-domain compared with those in MCAD to give a long and large crevice that accommodates the cofactor FAD and the substrate acyl-CoA.	Flavin-Adenine Dinucleotide	197-200	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	128-132
15018640-7	2004	Similarly, clofibrate and WY14643 increased expression of MCAD, a downstream target protein of PPARalpha by 123 +/- 8% (p < 0.05) and 143 +/- 8% (p < 0.05), respectively.	Clofibrate	11-21	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	58-62
15018640-7	2004	Similarly, clofibrate and WY14643 increased expression of MCAD, a downstream target protein of PPARalpha by 123 +/- 8% (p < 0.05) and 143 +/- 8% (p < 0.05), respectively.	pirinixic acid	26-33	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	58-62
11872165-7	2002	The flavin ring of FAD resides at the active site with its si-face attached to the beta-domain, and is surrounded by active-site residues in a mode similar to that found in MCAD.	4,6-dinitro-o-cresol	4-10	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	173-177
11872165-7	2002	The flavin ring of FAD resides at the active site with its si-face attached to the beta-domain, and is surrounded by active-site residues in a mode similar to that found in MCAD.	Flavin-Adenine Dinucleotide	19-22	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	173-177
11872165-8	2002	However, the residues have weak interactions with the flavin ring due to the loss of some of the important hydrogen bonds with the flavin ring found in MCAD.	4,6-dinitro-o-cresol	54-60	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	152-156
11872165-8	2002	However, the residues have weak interactions with the flavin ring due to the loss of some of the important hydrogen bonds with the flavin ring found in MCAD.	Hydrogen	107-115	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	152-156
11872165-8	2002	However, the residues have weak interactions with the flavin ring due to the loss of some of the important hydrogen bonds with the flavin ring found in MCAD.	4,6-dinitro-o-cresol	131-137	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	152-156
11872165-10	2002	The pyrimidine moiety of flavin is exposed to the solvent and can readily be attacked by molecular oxygen, while that in MCAD is protected from the solvent.	pyrimidine	4-14	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	121-125
11872165-10	2002	The pyrimidine moiety of flavin is exposed to the solvent and can readily be attacked by molecular oxygen, while that in MCAD is protected from the solvent.	4,6-dinitro-o-cresol	25-31	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	121-125
10200137-11	1999	The most prominent effects were observed in mRNA levels involved in fatty acid oxidation (short-, medium- and long-chain acyl-CoA dehydrogenase).	Fatty Acids	68-78	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	98-143
11373342-8	2001	Finally, with the use of an established renal cell line, it was shown that glucocorticoids stimulate gene expression of PPARalpha and of medium chain acyl-CoA dehydrogenase (MCAD, a PPARalpha target gene) 2- to 4-fold and 1.5-fold, respectively, and that addition of fatty acids in the culture media led to a 2.2-fold increase in MCAD mRNA.	Fatty Acids	267-278	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	137-172
11373342-8	2001	Finally, with the use of an established renal cell line, it was shown that glucocorticoids stimulate gene expression of PPARalpha and of medium chain acyl-CoA dehydrogenase (MCAD, a PPARalpha target gene) 2- to 4-fold and 1.5-fold, respectively, and that addition of fatty acids in the culture media led to a 2.2-fold increase in MCAD mRNA.	Fatty Acids	267-278	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	174-178
11373342-9	2001	Altogether, these results demonstrated that glucocorticoids are potent regulators of PPARalpha development in the immature kidney and that these hormones act in concert with fatty acids to regulate MCAD gene expression in renal cells.	Fatty Acids	174-185	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	198-202
10958805-10	2000	F(1)F(0)-ATP synthase beta subunit and MCAD transcript levels remain low, which may contribute to impaired mitochondrial respiratory function, decreased fatty acid utilization and lipid droplet accumulation in hearts of copper-deficient rats.	Fatty Acids	153-163	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	39-43
10958805-10	2000	F(1)F(0)-ATP synthase beta subunit and MCAD transcript levels remain low, which may contribute to impaired mitochondrial respiratory function, decreased fatty acid utilization and lipid droplet accumulation in hearts of copper-deficient rats.	Copper	220-226	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	39-43
9852194-3	1998	Much of this work has focused on the gene encoding medium-chain acyl-CoA dehydrogenase (MCAD), which catalyzes a pivotal step in the mitochondrial fatty acid -oxidation (FAO) cycle.	Fatty Acids	147-157	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	51-86
9852194-3	1998	Much of this work has focused on the gene encoding medium-chain acyl-CoA dehydrogenase (MCAD), which catalyzes a pivotal step in the mitochondrial fatty acid -oxidation (FAO) cycle.	Fatty Acids	147-157	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	88-92
7829528-1	1995	We studied the role of FAD in the intramitochondrial folding and assembly of medium-chain acyl-CoA dehydrogenase (MCAD), a homotetrameric mitochondrial enzyme containing a molecule of non-covalently bound FAD/monomer.	Flavin-Adenine Dinucleotide	23-26	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	77-112
9354389-17	1997	The band II of FAD in the complexes reveals a significant decrease in the frequency in comparison with the complexes of medium-chain acyl-CoA dehydrogenase (MCAD) with 3-ketoacyl-CoA.	3-ketoacyl-coa	168-182	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	120-155
9354389-17	1997	The band II of FAD in the complexes reveals a significant decrease in the frequency in comparison with the complexes of medium-chain acyl-CoA dehydrogenase (MCAD) with 3-ketoacyl-CoA.	3-ketoacyl-coa	168-182	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	157-161
9354389-18	1997	This observation suggests a difference between ACO and MCAD in the hydrogen-bonding network associated with enzyme-bound FAD.	Hydrogen	67-75	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	55-59
9354389-18	1997	This observation suggests a difference between ACO and MCAD in the hydrogen-bonding network associated with enzyme-bound FAD.	Flavin-Adenine Dinucleotide	121-124	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	55-59
8967442-1	1996	To determine whether expression of a nuclear gene encoding a mitochondrial fatty acid oxidation enzyme is regulated in parallel with skeletal muscle fibre-type-specific energy substrate preference, expression of the gene encoding medium-chain acyl-CoA dehydrogenase (MCAD) was delineated in canine latissimus dorsi muscle subjected to chronic motor nerve stimulation.	Fatty Acids	75-85	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	267-271
8967442-6	1996	The temporal pattern and magnitude of MCAD mRNA accumulation in response to muscle stimulation was distinct from that of mRNAs encoding other enzymes known to be regulated by this stimulus, including glyceraldehyde phosphate dehydrogenase, citrate synthase, and sarcoplasmic reticulum Ca-ATPase, but paralleled the protein levels of the peroxisome proliferator-activated receptor (PPAR), an orphan member of the nuclear hormone receptor superfamily known to regulate genes encoding fatty acid oxidation enzymes in liver.	Fatty Acids	482-492	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	38-42
7703241-0	1995	Medium-chain acyl-CoA dehydrogenase- and enoyl-CoA hydratase-dependent bioactivation of 5,6-dichloro-4-thia-5-hexenoyl-CoA.	5,6-dichloro-4-thia-5-hexenoyl-coenzyme A	88-122	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	0-35
7703241-3	1995	The objectives of the present experiments were to elaborate the bioactivation mechanism of DCTH and to examine the interaction of the coenzyme A thioester of DCTH (DCTH-CoA) with the medium-chain acyl-CoA dehydrogenase.	dcth	158-162	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	183-218
7703241-3	1995	The objectives of the present experiments were to elaborate the bioactivation mechanism of DCTH and to examine the interaction of the coenzyme A thioester of DCTH (DCTH-CoA) with the medium-chain acyl-CoA dehydrogenase.	dcth	158-162	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	183-218
7703241-7	1995	Incubation of DCTH-CoA with the medium-chain acyl-CoA dehydrogenase in the absence of FcPF6 gave 3-hydroxypropionyl-CoA as the major product and resulted in the irreversible inactivation of the enzyme.	dcth-coa	14-22	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	32-67
7703241-7	1995	Incubation of DCTH-CoA with the medium-chain acyl-CoA dehydrogenase in the absence of FcPF6 gave 3-hydroxypropionyl-CoA as the major product and resulted in the irreversible inactivation of the enzyme.	3-Hydroxypropanoyl-CoA	97-119	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	32-67
7703241-11	1995	The medium-chain acyl-CoA dehydrogenase was not inactivated by acryloyl-CoA, and little inactivation was observed in the presence of FcPF6.	fcpf6	133-138	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	4-39
7829528-2	1995	In the MCAD molecule, FAD is buried in a crevice containing the active center.	Flavin-Adenine Dinucleotide	22-25	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	7-11
9164869-1	1997	During development, gene expression of medium-chain acyl-CoA dehydrogenase (MCAD), a nuclear-encoded mitochondrial enzyme that catalyses the first step of medium-chain fatty acid beta-oxidation, is highly regulated in tissues in accordance with fatty acid utilization, but the factors involved in this regulation are largely unknown.	chain fatty acid	162-178	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	39-74
9164869-1	1997	During development, gene expression of medium-chain acyl-CoA dehydrogenase (MCAD), a nuclear-encoded mitochondrial enzyme that catalyses the first step of medium-chain fatty acid beta-oxidation, is highly regulated in tissues in accordance with fatty acid utilization, but the factors involved in this regulation are largely unknown.	chain fatty acid	162-178	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	76-80
9164869-1	1997	During development, gene expression of medium-chain acyl-CoA dehydrogenase (MCAD), a nuclear-encoded mitochondrial enzyme that catalyses the first step of medium-chain fatty acid beta-oxidation, is highly regulated in tissues in accordance with fatty acid utilization, but the factors involved in this regulation are largely unknown.	Fatty Acids	168-178	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	39-74
9164869-1	1997	During development, gene expression of medium-chain acyl-CoA dehydrogenase (MCAD), a nuclear-encoded mitochondrial enzyme that catalyses the first step of medium-chain fatty acid beta-oxidation, is highly regulated in tissues in accordance with fatty acid utilization, but the factors involved in this regulation are largely unknown.	Fatty Acids	168-178	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	76-80
8615829-3	1996	We therefore studied the changes in the steady-state levels of mRNA encoding medium-chain acyl-CoA dehydrogenase (MCAD), which catalyses the initial step in mitochondrial fatty acid beta-oxidation, in the rat kidney cortex and medulla between postnatal days 10 and 30.	Fatty Acids	171-181	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	77-112
8615829-3	1996	We therefore studied the changes in the steady-state levels of mRNA encoding medium-chain acyl-CoA dehydrogenase (MCAD), which catalyses the initial step in mitochondrial fatty acid beta-oxidation, in the rat kidney cortex and medulla between postnatal days 10 and 30.	Fatty Acids	171-181	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	114-118
8615829-7	1996	Adrenalectomy prevented the 16-21-day developmental increases in MCAD and mMDH mRNA levels in the cortex and medulla; these could be restored by dexamethasone treatment.	Dexamethasone	145-158	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	65-69
8615829-8	1996	A single injection of dexamethasone into 10-day-old rats led to a rise in MCAD and mMDH mRNA levels in the renal cortex due to stimulation of gene transcription, as shown by nuclear run-on assays.	Dexamethasone	22-35	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	74-78
7829528-1	1995	We studied the role of FAD in the intramitochondrial folding and assembly of medium-chain acyl-CoA dehydrogenase (MCAD), a homotetrameric mitochondrial enzyme containing a molecule of non-covalently bound FAD/monomer.	Flavin-Adenine Dinucleotide	23-26	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	114-118
7829528-1	1995	We studied the role of FAD in the intramitochondrial folding and assembly of medium-chain acyl-CoA dehydrogenase (MCAD), a homotetrameric mitochondrial enzyme containing a molecule of non-covalently bound FAD/monomer.	Flavin-Adenine Dinucleotide	205-208	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	77-112
7829528-1	1995	We studied the role of FAD in the intramitochondrial folding and assembly of medium-chain acyl-CoA dehydrogenase (MCAD), a homotetrameric mitochondrial enzyme containing a molecule of non-covalently bound FAD/monomer.	Flavin-Adenine Dinucleotide	205-208	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	114-118
7829528-10	1995	After 60-min chase in the presence of FAD, the majority of MCAD in the complex with hsp60 was transferred to tetramer, whereas no such transfer occurred after the chase in the absence of FAD.	Flavin-Adenine Dinucleotide	38-41	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	59-63
7829528-11	1995	When chase was done in the presence of FMN, a significant amount of MCAD was transferred from the complex with hsp60 to tetramer, but the transfer was not as efficient as in the presence of FAD.	Flavin-Adenine Dinucleotide	190-193	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	68-72
7829528-13	1995	These data suggest that isoalloxazine ring of FAD plays a critical role, exerting nucleating effect, in the hsp60-assisted folding of MCAD subunit into an assembly competent conformation, probably assisting the formation of the core.	isoalloxazine	24-37	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	134-138
7829528-13	1995	These data suggest that isoalloxazine ring of FAD plays a critical role, exerting nucleating effect, in the hsp60-assisted folding of MCAD subunit into an assembly competent conformation, probably assisting the formation of the core.	Flavin-Adenine Dinucleotide	46-49	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	134-138
7971999-1	1994	Medium-chain acyl-CoA dehydrogenase (MCAD) catalyzes a pivotal reaction in mitochondrial fatty acid (FA) beta-oxidation.	Fatty Acids	89-99	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	0-35
7971999-1	1994	Medium-chain acyl-CoA dehydrogenase (MCAD) catalyzes a pivotal reaction in mitochondrial fatty acid (FA) beta-oxidation.	Fatty Acids	89-99	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	37-41
7971999-2	1994	To examine the potential role of FAs and their metabolites in the regulation of MCAD gene expression, we measured MCAD mRNA levels in animals fed inhibitors of mitochondrial long-chain FA import.	ammonium ferrous sulfate	33-36	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	80-84
34732632-7	2021	First of all, we found that fish oil substitution increased plasma adiponectin levels, and then increasing MCAD and CPT-1 mRNA levels to accelerate fatty acid oxidation in liver, then further prevent ethanol-induced hepatosteatosis in rats with chronic alcohol-feeding.	Fish Oils	28-36	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	107-111
8109745-4	1993	The assay is specific for medium-chain acyl-CoA dehydrogenase because long-chain and short-chain acyl-CoA dehydrogenases exhibit little or no activity with 3-phenylpropionyl-CoA as substrate.	phenylpropionyl-coenzyme A	156-177	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	26-61
8109745-5	1993	Since absorbance changes at 308 nm caused by other reactions are less than 5% of the absorbance change due to cinnamoyl-CoA formation catalyzed by medium-chain acyl-CoA dehydrogenase, the assay can be used to measure the activity of this enzyme in crude tissue homogenates.	cinnamoyl-coenzyme A	110-123	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	147-182
8314750-1	1993	We have recently identified a complex transcriptional regulatory element in the medium chain acyl-CoA dehydrogenase (MCAD) gene promoter region that confers response to retinoids through interaction with receptors for all-trans-retinoic acid (RARs) and 9-cis-retinoic acid (RXRs) (Raisher, B. D., Gulick, T., Zhang, Z., Strauss, A. W., Moore, D. D., and Kelly, D. P. (1992) J. Biol.	Retinoids	169-178	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	80-115
8314750-1	1993	We have recently identified a complex transcriptional regulatory element in the medium chain acyl-CoA dehydrogenase (MCAD) gene promoter region that confers response to retinoids through interaction with receptors for all-trans-retinoic acid (RARs) and 9-cis-retinoic acid (RXRs) (Raisher, B. D., Gulick, T., Zhang, Z., Strauss, A. W., Moore, D. D., and Kelly, D. P. (1992) J. Biol.	Retinoids	169-178	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	117-121
8314750-1	1993	We have recently identified a complex transcriptional regulatory element in the medium chain acyl-CoA dehydrogenase (MCAD) gene promoter region that confers response to retinoids through interaction with receptors for all-trans-retinoic acid (RARs) and 9-cis-retinoic acid (RXRs) (Raisher, B. D., Gulick, T., Zhang, Z., Strauss, A. W., Moore, D. D., and Kelly, D. P. (1992) J. Biol.	Alitretinoin	253-272	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	80-115
8314750-1	1993	We have recently identified a complex transcriptional regulatory element in the medium chain acyl-CoA dehydrogenase (MCAD) gene promoter region that confers response to retinoids through interaction with receptors for all-trans-retinoic acid (RARs) and 9-cis-retinoic acid (RXRs) (Raisher, B. D., Gulick, T., Zhang, Z., Strauss, A. W., Moore, D. D., and Kelly, D. P. (1992) J. Biol.	Alitretinoin	253-272	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	117-121
1931995-0	1991	Spiropentaneacetic acid as a specific inhibitor of medium-chain acyl-CoA dehydrogenase.	spiropentaneacetic acid	0-23	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	51-86
1931995-7	1991	In contrast, MCPA inhibited both MCAD and short-chain acyl-CoA dehydrogenase with a stronger inhibition toward the latter.	methylenecyclopropylacetic acid	13-17	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	33-37
34939931-5	2021	Furthermore, we elucidated that 8C-promoted histone acetylation and heart repair were carried out by metabolic enzyme medium-chain acyl-CoA dehydrogenase (MCAD) and histone acetyltransferase Kat2a, suggesting that 8C dramatically improves cardiac function mainly through metabolic acetyl-CoA-mediated histone acetylation.	N-(4-bromophenyl) 3-(4-bromophenylaminosulfonyl)benzamide	32-34	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	118-153
34939931-5	2021	Furthermore, we elucidated that 8C-promoted histone acetylation and heart repair were carried out by metabolic enzyme medium-chain acyl-CoA dehydrogenase (MCAD) and histone acetyltransferase Kat2a, suggesting that 8C dramatically improves cardiac function mainly through metabolic acetyl-CoA-mediated histone acetylation.	N-(4-bromophenyl) 3-(4-bromophenylaminosulfonyl)benzamide	32-34	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	155-159
34939931-5	2021	Furthermore, we elucidated that 8C-promoted histone acetylation and heart repair were carried out by metabolic enzyme medium-chain acyl-CoA dehydrogenase (MCAD) and histone acetyltransferase Kat2a, suggesting that 8C dramatically improves cardiac function mainly through metabolic acetyl-CoA-mediated histone acetylation.	N-(4-bromophenyl) 3-(4-bromophenylaminosulfonyl)benzamide	214-216	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	118-153
34939931-5	2021	Furthermore, we elucidated that 8C-promoted histone acetylation and heart repair were carried out by metabolic enzyme medium-chain acyl-CoA dehydrogenase (MCAD) and histone acetyltransferase Kat2a, suggesting that 8C dramatically improves cardiac function mainly through metabolic acetyl-CoA-mediated histone acetylation.	N-(4-bromophenyl) 3-(4-bromophenylaminosulfonyl)benzamide	214-216	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	155-159
34939931-5	2021	Furthermore, we elucidated that 8C-promoted histone acetylation and heart repair were carried out by metabolic enzyme medium-chain acyl-CoA dehydrogenase (MCAD) and histone acetyltransferase Kat2a, suggesting that 8C dramatically improves cardiac function mainly through metabolic acetyl-CoA-mediated histone acetylation.	Acetyl Coenzyme A	281-291	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	118-153
34939931-5	2021	Furthermore, we elucidated that 8C-promoted histone acetylation and heart repair were carried out by metabolic enzyme medium-chain acyl-CoA dehydrogenase (MCAD) and histone acetyltransferase Kat2a, suggesting that 8C dramatically improves cardiac function mainly through metabolic acetyl-CoA-mediated histone acetylation.	Acetyl Coenzyme A	281-291	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	155-159
34923497-7	2022	The exercise upregulated the renal expressions of both medium-chain acyl-CoA dehydrogenase and peroxisome proliferator-activated receptor gamma coactivator-1alpha related to fatty acid metabolism.	Fatty Acids	174-184	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	55-90
34732632-7	2021	First of all, we found that fish oil substitution increased plasma adiponectin levels, and then increasing MCAD and CPT-1 mRNA levels to accelerate fatty acid oxidation in liver, then further prevent ethanol-induced hepatosteatosis in rats with chronic alcohol-feeding.	Fatty Acids	148-158	acyl-CoA dehydrogenase medium chain	Rattus norvegicus	107-111