Structure of the subunit binding domain and dynamics of the di-domain region from the core of human branched chain alpha-ketoacid dehydrogenase complex.
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The two active sites in human branched-chain alpha-keto acid dehydrogenase operate independently without an obligatory alternating-site mechanismStructural and Thermodynamic Basis for Weak Interactions between Dihydrolipoamide Dehydrogenase and Subunit-binding Domain of the Branched-chain -Ketoacid Dehydrogenase ComplexMolecular basis of the recognition of the ap65-1 gene transcription promoter elements by a Myb protein from the protozoan parasite Trichomonas vaginalisNuclear magnetic resonance approaches in the study of 2-oxo acid dehydrogenase multienzyme complexes--a literature review.
P2860
Structure of the subunit binding domain and dynamics of the di-domain region from the core of human branched chain alpha-ketoacid dehydrogenase complex.
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2006年学术文章
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name
Structure of the subunit bindi ...... etoacid dehydrogenase complex.
@en
Structure of the subunit bindi ...... etoacid dehydrogenase complex.
@nl
type
label
Structure of the subunit bindi ...... etoacid dehydrogenase complex.
@en
Structure of the subunit bindi ...... etoacid dehydrogenase complex.
@nl
prefLabel
Structure of the subunit bindi ...... etoacid dehydrogenase complex.
@en
Structure of the subunit bindi ...... etoacid dehydrogenase complex.
@nl
P2093
P2860
P356
P1476
Structure of the subunit bindi ...... etoacid dehydrogenase complex.
@en
P2093
Chi-Fon Chang
David T Chuang
Hui-Ting Chou
Jacinta L Chuang
Shin-Jye Lee
Tai-Huang Huang
Yi-Jan Lin
P2860
P304
28345-28353
P356
10.1074/JBC.M605005200
P407
P577
2006-07-20T00:00:00Z