Direct evidence of conformational heterogeneity in human pancreatic glucokinase from high-resolution nuclear magnetic resonance.
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Homotropic allosteric regulation in monomeric mammalian glucokinaseCooperativity in monomeric enzymes with single ligand-binding sitesThe active conformation of human glucokinase is not altered by allosteric activatorsInsights into Mechanism of Glucokinase ActivationA phospho-BAD BH3 helix activates glucokinase by a mechanism distinct from that of allosteric activatorsThe relationship between folding and activity in UreG, an intrinsically disordered enzyme.Analysis of the co-operative interaction between the allosterically regulated proteins GK and GKRP using tryptophan fluorescenceThermal stability of glucokinase (GK) as influenced by the substrate glucose, an allosteric glucokinase activator drug (GKA) and the osmolytes glycerol and ureaOrder-disorder transitions govern kinetic cooperativity and allostery of monomeric human glucokinaseDual allosteric activation mechanisms in monomeric human glucokinase.Kinetic Cooperativity in Human Pancreatic Glucokinase Originates from Millisecond Dynamics of the Small Domain.GCK-MODY diabetes associated with protein misfolding, cellular self-association and degradation.Biochemical and biophysical investigations of the interaction between human glucokinase and pro-apoptotic BAD.SUMOylation of pancreatic glucokinase regulates its cellular stability and activityUsing NMR spectroscopy to elucidate the role of molecular motions in enzyme functionSolution NMR Spectroscopy for the Study of Enzyme Allostery.Mutational analysis of allosteric activation and inhibition of glucokinase.Role of connecting loop I in catalysis and allosteric regulation of human glucokinase.Conformational heterogeneity and intrinsic disorder in enzyme regulation: Glucokinase as a case study.Binding of ATP at the active site of human pancreatic glucokinase--nucleotide-induced conformational changes with possible implications for its kinetic cooperativity.Tryptophan Fluorescence Yields and Lifetimes as a Probe of Conformational Changes in Human Glucokinase.Kinetic Cooperativity in Human Pancreatic Glucokinase Originates from Millisecond Dynamics of the Small Domain
P2860
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P2860
Direct evidence of conformational heterogeneity in human pancreatic glucokinase from high-resolution nuclear magnetic resonance.
description
2010 nî lūn-bûn
@nan
2010 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Direct evidence of conformatio ...... on nuclear magnetic resonance.
@ast
Direct evidence of conformatio ...... on nuclear magnetic resonance.
@en
Direct evidence of conformatio ...... on nuclear magnetic resonance.
@nl
type
label
Direct evidence of conformatio ...... on nuclear magnetic resonance.
@ast
Direct evidence of conformatio ...... on nuclear magnetic resonance.
@en
Direct evidence of conformatio ...... on nuclear magnetic resonance.
@nl
prefLabel
Direct evidence of conformatio ...... on nuclear magnetic resonance.
@ast
Direct evidence of conformatio ...... on nuclear magnetic resonance.
@en
Direct evidence of conformatio ...... on nuclear magnetic resonance.
@nl
P2093
P2860
P356
P1433
P1476
Direct evidence of conformatio ...... on nuclear magnetic resonance.
@en
P2093
Brian G Miller
Lei Bruschweiler-Li
Mioara Larion
Rafael Brüschweiler
Roberto K Salinas
P2860
P304
P356
10.1021/BI101098F
P407
P577
2010-09-01T00:00:00Z