Molecular mechanism of the allosteric regulation of the αγ heterodimer of human NAD-dependent isocitrate dehydrogenase.
about
The β and γ subunits play distinct functional roles in the α2βγ heterotetramer of human NAD-dependent isocitrate dehydrogenase.Controlling ligand binding for tunable and switchable catalysis: cation-modulated hemilability in pincer-crown ether ligands.Insights into the inhibitory mechanisms of NADH on the αγ heterodimer of human NAD-dependent isocitrate dehydrogenase.
P2860
Molecular mechanism of the allosteric regulation of the αγ heterodimer of human NAD-dependent isocitrate dehydrogenase.
description
2017 nî lūn-bûn
@nan
2017 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2017 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2017年の論文
@ja
2017年論文
@yue
2017年論文
@zh-hant
2017年論文
@zh-hk
2017年論文
@zh-mo
2017年論文
@zh-tw
2017年论文
@wuu
name
Molecular mechanism of the all ...... dent isocitrate dehydrogenase.
@ast
Molecular mechanism of the all ...... dent isocitrate dehydrogenase.
@en
type
label
Molecular mechanism of the all ...... dent isocitrate dehydrogenase.
@ast
Molecular mechanism of the all ...... dent isocitrate dehydrogenase.
@en
prefLabel
Molecular mechanism of the all ...... dent isocitrate dehydrogenase.
@ast
Molecular mechanism of the all ...... dent isocitrate dehydrogenase.
@en
P2093
P2860
P921
P356
P1433
P1476
Molecular mechanism of the all ...... dent isocitrate dehydrogenase.
@en
P2093
Jianping Ding
Tengfei Ma
Yingjie Peng
P2860
P2888
P356
10.1038/SREP40921
P407
P577
2017-01-18T00:00:00Z
P6179
1034246617