Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary chain tracing at 2.8-A resolution.

Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary chain tracing at 2.8-A resolution.

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http://www.wikidata.org/entity/Q34180382
The Hotdog fold: wrapping up a superfamily of thioesterases and dehydratasesNAD(+)-dependent formate dehydrogenaseStructure of a bacterial enzyme regulated by phosphorylation, isocitrate dehydrogenasePig heart short chain L-3-hydroxyacyl-CoA dehydrogenase revisited: Sequence analysis and crystal structure determinationGlutamate 170 of human l-3-hydroxyacyl-CoA dehydrogenase is required for proper orientation of the catalytic histidine and structural integrity of the enzymeA human brain L-3-hydroxyacyl-coenzyme A dehydrogenase is identical to an amyloid beta-peptide-binding protein involved in Alzheimer's diseaseCrystal structure of NAD-dependent formate dehydrogenaseAnalysis of proteins with the 'hot dog' fold: prediction of function and identification of catalytic residues of hypothetical proteins.Enhancement of L-3-hydroxybutyryl-CoA dehydrogenase activity and circulating ketone body levels by pantethine. Relevance to dopaminergic injury.Aerobic degradation of mercaptosuccinate by the gram-negative bacterium Variovorax paradoxus strain B4.The molecular basis of pediatric long chain 3-hydroxyacyl-CoA dehydrogenase deficiency associated with maternal acute fatty liver of pregnancyCloning, sequencing, and expression of clustered genes encoding beta-hydroxybutyryl-coenzyme A (CoA) dehydrogenase, crotonase, and butyryl-CoA dehydrogenase from Clostridium acetobutylicum ATCC 824Homology between hydroxybutyryl and hydroxyacyl coenzyme A dehydrogenase enzymes from Clostridium acetobutylicum fermentation and vertebrate fatty acid beta-oxidation pathways.Purification and properties of 3-hydroxybutyryl-coenzyme A dehydrogenase from Clostridium beijerinckii ("Clostridium butylicum") NRRL B593.Alanine-scanning mutation approach for classification of the roles of conserved residues in the activity and substrate affinity of L-carnitine dehydrogenase.Identification of residues essential for the activity and substrate affinity of L-carnitine dehydrogenase.
P2860

Structure of L-3-hydroxyacyl-coenzyme A dehydrogenase: preliminary chain tracing at 2.8-A resolution.

Item
http://www.wikidata.org/entity/Q34180382
description
1987 nî lūn-bûn
@nan
1987 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1987 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1987年の論文
@ja
1987年学术文章
@wuu
1987年学术文章
@zh-cn
1987年学术文章
@zh-hans
1987年学术文章
@zh-my
1987年学术文章
@zh-sg
1987年學術文章
@yue
name
Structure of L-3-hydroxyacyl-c ...... n tracing at 2.8-A resolution.
@ast
Structure of L-3-hydroxyacyl-c ...... n tracing at 2.8-A resolution.
@en
Structure of L-3-hydroxyacyl-c ...... n tracing at 2.8-A resolution.
@nl
type
label
Structure of L-3-hydroxyacyl-c ...... n tracing at 2.8-A resolution.
@ast
Structure of L-3-hydroxyacyl-c ...... n tracing at 2.8-A resolution.
@en
Structure of L-3-hydroxyacyl-c ...... n tracing at 2.8-A resolution.
@nl
prefLabel
Structure of L-3-hydroxyacyl-c ...... n tracing at 2.8-A resolution.
@ast
Structure of L-3-hydroxyacyl-c ...... n tracing at 2.8-A resolution.
@en
Structure of L-3-hydroxyacyl-c ...... n tracing at 2.8-A resolution.
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P5875
P698
P932
P356
P1433
P1476
Structure of L-3-hydroxyacyl-c ...... n tracing at 2.8-A resolution.
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P5875
P698
P932