The hydroxyl of threonine 13 of the bovine 70-kDa heat shock cognate protein is essential for transducing the ATP-induced conformational change
about
Hsp70 chaperones: cellular functions and molecular mechanismStructural basis for the catalytic mechanism of mammalian 25-kDa thiamine triphosphataseBiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functionsCrystal structure of monomeric actin in the ATP state. Structural basis of nucleotide-dependent actin dynamicsStructural characterization of a eukaryotic chaperone--the ribosome-associated complexThe function of the yeast molecular chaperone Sse1 is mechanistically distinct from the closely related hsp70 family.Allostery in the Hsp70 chaperone proteinsIdentification of key hinge residues important for nucleotide-dependent allostery in E. coli Hsp70/DnaKA motor neuron disease-associated mutation in p150Glued perturbs dynactin function and induces protein aggregation.ATP-induced conformational changes in Hsp70: molecular dynamics and experimental validation of an in silico predicted conformation.Dissection of the ATP-binding domain of the chaperone hsc70 for interaction with the cofactor Hap46.Stress genes and proteins in the archaea.Measurement and interpretation of 15N-1H residual dipolar couplings in larger proteins.Chemical screens against a reconstituted multiprotein complex: myricetin blocks DnaJ regulation of DnaK through an allosteric mechanismAllosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperonesDecipher the mechanisms of protein conformational changes induced by nucleotide binding through free-energy landscape analysis: ATP binding to Hsp70.Balance between folding and degradation for Hsp90-dependent client proteins: a key role for CHIP.Keep the traffic moving: mechanism of the Hsp70 motor.Experimentally biased model structure of the Hsc70/auxilin complex: substrate transfer and interdomain structural changeThe 70-kDa heat shock protein chaperone nucleotide-binding domain in solution unveiled as a molecular machine that can reorient its functional subdomains.In Silico Molecular Modeling and Docking Studies on Novel Mutants (E229V, H225P and D230C) of the Nucleotide-Binding Domain of Homo sapiens Hsp70.Structural basis of interdomain communication in the Hsc70 chaperone.Dimerisation-dependent GTPase reaction of MnmE: how potassium acts as GTPase-activating element.Protein surface representation and analysis by dimension reduction.Disrupted hydrogen bond network and impaired ATPase activity in an Hsc70 cysteine mutant.Hydration properties of magnesium and calcium ions from constrained first principles molecular dynamics.Amide hydrogen exchange reveals conformational changes in hsp70 chaperones important for allosteric regulation.
P2860
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P2860
The hydroxyl of threonine 13 of the bovine 70-kDa heat shock cognate protein is essential for transducing the ATP-induced conformational change
description
1998 nî lūn-bûn
@nan
1998 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
name
The hydroxyl of threonine 13 o ...... -induced conformational change
@ast
The hydroxyl of threonine 13 o ...... -induced conformational change
@en
The hydroxyl of threonine 13 o ...... -induced conformational change
@nl
type
label
The hydroxyl of threonine 13 o ...... -induced conformational change
@ast
The hydroxyl of threonine 13 o ...... -induced conformational change
@en
The hydroxyl of threonine 13 o ...... -induced conformational change
@nl
prefLabel
The hydroxyl of threonine 13 o ...... -induced conformational change
@ast
The hydroxyl of threonine 13 o ...... -induced conformational change
@en
The hydroxyl of threonine 13 o ...... -induced conformational change
@nl
P356
P1433
P1476
The hydroxyl of threonine 13 o ...... -induced conformational change
@en
P2093
P304
P356
10.1021/BI981510X
P407
P577
1998-11-03T00:00:00Z