Variation in the organization and subunit composition of the mammalian pyruvate dehydrogenase complex E2/E3BP core assembly.
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Biochemical and structural characterization of the apicoplast dihydrolipoamide dehydrogenase of Plasmodium falciparumUniqueness of models from small-angle scattering data: the impact of a hydration shell and complementary NMR restraints.Regulation of pyruvate metabolism and human diseaseSpecific inhibition by synthetic analogs of pyruvate reveals that the pyruvate dehydrogenase reaction is essential for metabolism and viability of glioblastoma cells.Matchout deuterium labelling of proteins for small-angle neutron scattering studies using prokaryotic and eukaryotic expression systems and high cell-density cultures.Solution conformations of early intermediates in Mos1 transpositionThe Pyruvate Dehydrogenase Complex and Related Assemblies in Health and Disease.Atomic Structure of the E2 Inner Core of Human Pyruvate Dehydrogenase Complex.Mutagenesis of conserved active site residues of dihydrolipoamide succinyltransferase enhances the accumulation of α-ketoglutarate in Yarrowia lipolytica.
P2860
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P2860
Variation in the organization and subunit composition of the mammalian pyruvate dehydrogenase complex E2/E3BP core assembly.
description
2011 nî lūn-bûn
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2011年の論文
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2011年学术文章
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name
Variation in the organization ...... complex E2/E3BP core assembly.
@en
Variation in the organization ...... complex E2/E3BP core assembly.
@nl
type
label
Variation in the organization ...... complex E2/E3BP core assembly.
@en
Variation in the organization ...... complex E2/E3BP core assembly.
@nl
prefLabel
Variation in the organization ...... complex E2/E3BP core assembly.
@en
Variation in the organization ...... complex E2/E3BP core assembly.
@nl
P2093
P2860
P356
P1433
P1476
Variation in the organization ...... complex E2/E3BP core assembly
@en
P2093
David Gilbert
Donna P McGow
J Gordon Lindsay
Margaret A Nutley
Olwyn Byron
Peter Kropholler
Philip Callow
P2860
P304
P356
10.1042/BJ20101784
P407
P577
2011-08-01T00:00:00Z