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ACADM wt Allele
Known as:
FLJ99884
, FLJ18227
, FLJ93013
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Human ACADM wild-type allele is located in the vicinity of 1p31 and is approximately 39 kb in length. This allele, which encodes medium-chain…
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National Institutes of Health
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Related topics
Related topics
6 relations
Broader (1)
ACADM gene
CDH15 gene
Medium-Chain Specific Acyl-CoA Dehydrogenase, Mitochondrial
Medium-chain acyl-coenzyme A dehydrogenase deficiency
Oxidation-Reduction
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Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
1999
1999
Mechanism of activation of acyl-CoA substrates by medium chain acyl-CoA dehydrogenase: interaction of the thioester carbonyl with the flavin adenine dinucleotide ribityl side chain.
S. Engst
,
P. Vock
,
M. Wang
,
J. J. Kim
,
S. Ghisla
Biochemistry
1999
Corpus ID: 10365171
The flavin adenine dinucleotide (FAD) cofactor of pig kidney medium-chain specific acyl-coenzyme A (CoA) dehydrogenase (MCADH…
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1999
1999
Biochemical characterization of a variant human medium-chain acyl-CoA dehydrogenase with a disease-associated mutation localized in the active site.
B. Küchler
,
A. Abdel-Ghany
,
P. Bross
,
A. Nandy
,
I. Rasched
,
S. Ghisla
Biochemical Journal
1999
Corpus ID: 9106396
Medium-chain acyl-CoA dehydrogenase (MCADH) deficiency, an autosomal recessive inherited disorder, is the most common genetic…
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1998
1998
Substrate activation by acyl-CoA dehydrogenases: transition-state stabilization and pKs of involved functional groups.
P. Vock
,
S. Engst
,
M. Eder
,
S. Ghisla
Biochemistry
1998
Corpus ID: 13388051
The mechanism by which acyl-CoA dehydrogenases initiate catalysis was studied by using p-substituted phenylacetyl-CoAs…
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1997
1997
Biochemical characterization of purified, human recombinant Lys304-->Glu medium-chain acyl-CoA dehydrogenase containing the common disease-causing mutation and comparison with the normal enzyme.
V. Kieweg
,
F. Kräutle
,
+8 authors
S. Ghisla
European Journal of Biochemistry
1997
Corpus ID: 16616328
Recombinant, normal human medium-chain acyl-CoA dehydrogenase (MCADH) and the common, human disease-causing K304E mutant ([Glu304…
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Highly Cited
1996
Highly Cited
1996
Crystal structures of the wild type and the Glu376Gly/Thr255Glu mutant of human medium-chain acyl-CoA dehydrogenase: influence of the location of the catalytic base on substrate specificity.
H. Lee
,
M. Wang
,
R. Paschke
,
A. Nandy
,
S. Ghisla
,
J. J. Kim
Biochemistry
1996
Corpus ID: 12900887
Crystal structures of the wild type human medium-chain acyl-CoA dehydrogenase (MCADH) and a double mutant in which its active…
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1996
1996
Medium-long-chain chimeric human Acyl-CoA dehydrogenase: medium-chain enzyme with the active center base arrangement of long-chain Acyl-CoA dehydrogenase.
A. Nandy
,
V. Kieweg
,
+6 authors
S. Ghisla
Biochemistry
1996
Corpus ID: 7406274
The catalytically essential glutamate residue that initiates catalysis by abstracting the substrate alpha-hydrogen as H+ is…
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Highly Cited
1990
Highly Cited
1990
Characterization of wild-type and an active site mutant of human medium chain acyl-CoA dehydrogenase after expression in Escherichia coli.
P. Bross
,
S. Engst
,
A. Strauss
,
D. Kelly
,
I. Rasched
,
S. Ghisla
Journal of Biological Chemistry
1990
Corpus ID: 17118807
1990
1990
Selective inactivation of various acyl-CoA dehydrogenases by (methylenecyclopropyl)acetyl-CoA.
Y. Ikeda
,
K. Tanaka
Biochimica et Biophysica Acta
1990
Corpus ID: 25007833
Highly Cited
1987
Highly Cited
1987
Short-chain acyl-coenzyme A dehydrogenase deficiency. Clinical and biochemical studies in two patients.
B. Amendt
,
C. Greene
,
+5 authors
W. Rhead
Journal of Clinical Investigation
1987
Corpus ID: 29681901
We describe two patients with short-chain acyl-coenzyme A (CoA) dehydrogenase (SCADH) deficiency. Neonate I excreted large…
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1985
1985
Catalytic defect of medium-chain acyl-coenzyme A dehydrogenase deficiency. Lack of both cofactor responsiveness and biochemical heterogeneity in eight patients.
B. Amendt
,
W. Rhead
Journal of Clinical Investigation
1985
Corpus ID: 2908814
Medium-chain acyl-coenzyme A (CoA) dehydrogenase (MCADH; EC 1.3.99.3) deficiency (MCD) is an inborn error of beta-oxidation. We…
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