Lys169 of human glucokinase is a determinant for glucose phosphorylation: implication for the atomic mechanism of glucokinase catalysis.
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The active conformation of human glucokinase is not altered by allosteric activatorsThe mechanism of allosteric inhibition of protein tyrosine phosphatase 1BThe structural basis of ATP as an allosteric modulatorCarbohydrate force fieldsMolecular dynamics simulation of the interactions between EHD1 EH domain and multiple peptides.Harnessing allostery: a novel approach to drug discovery.Structural Variations of Human Glucokinase Glu256Lys in MODY2 Condition Using Molecular Dynamics Study.Glucokinase mutations in pediatric patients with impaired fasting glucose.Mechanism of kinase inactivation and nonbinding of FRATide to GSK3β due to K85M mutation: molecular dynamics simulation and normal mode analysis.
P2860
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P2860
Lys169 of human glucokinase is a determinant for glucose phosphorylation: implication for the atomic mechanism of glucokinase catalysis.
description
2009 nî lūn-bûn
@nan
2009 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Lys169 of human glucokinase is ...... nism of glucokinase catalysis.
@ast
Lys169 of human glucokinase is ...... nism of glucokinase catalysis.
@en
type
label
Lys169 of human glucokinase is ...... nism of glucokinase catalysis.
@ast
Lys169 of human glucokinase is ...... nism of glucokinase catalysis.
@en
prefLabel
Lys169 of human glucokinase is ...... nism of glucokinase catalysis.
@ast
Lys169 of human glucokinase is ...... nism of glucokinase catalysis.
@en
P2093
P2860
P1433
P1476
Lys169 of human glucokinase is ...... nism of glucokinase catalysis.
@en
P2093
Chenjing Li
Hualiang Jiang
Jian Zhang
Kaixian Chen
P2860
P356
10.1371/JOURNAL.PONE.0006304
P407
P50
P577
2009-07-20T00:00:00Z