N-terminal residues regulate the catalytic efficiency of the Hsp90 ATPase cycle.
about
Structure insights into mechanisms of ATP hydrolysis and the activation of human heat-shock protein 90Structural Asymmetry in the Closed State of Mitochondrial Hsp90 (TRAP1) Supports a Two-Step ATP Hydrolysis MechanismCrystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complexDynamics of heat shock protein 90 C-terminal dimerization is an important part of its conformational cycle.Downregulation of the Hsp90 system causes defects in muscle cells of Caenorhabditis elegansLigand-induced conformational shift in the N-terminal domain of GRP94, an Hsp90 chaperone.Enforced N-domain proximity stimulates Hsp90 ATPase activity and is compatible with function in vivo.Heat shock protein 90's mechanochemical cycle is dominated by thermal fluctuations.Fungal heat-shock proteins in human disease.The regulatory mechanism of a client kinase controlling its own release from Hsp90 chaperone machinery through phosphorylationThe Mechanism of Hsp90 ATPase Stimulation by Aha1Spatially and kinetically resolved changes in the conformational dynamics of the Hsp90 chaperone machine.Chaperone activation of the hepadnaviral reverse transcriptase for template RNA binding is established by the Hsp70 and stimulated by the Hsp90 system.Cooperation of local motions in the Hsp90 molecular chaperone ATPase mechanism.The charged linker region is an important regulator of Hsp90 function.A novel N-terminal extension in mitochondrial TRAP1 serves as a thermal regulator of chaperone activity.Structure of unliganded GRP94, the endoplasmic reticulum Hsp90. Basis for nucleotide-induced conformational change.Both the charged linker region and ATPase domain of Hsp90 are essential for Rad51-dependent DNA repair.Dissection of the contribution of individual domains to the ATPase mechanism of Hsp90.NMR chemical shift perturbation study of the N-terminal domain of Hsp90 upon binding of ADP, AMP-PNP, geldanamycin, and radicicol.Conserved conformational changes in the ATPase cycle of human Hsp90.Intrinsic inhibition of the Hsp90 ATPase activity.The ATPase cycle of the endoplasmic chaperone Grp94.Protein conformational flexibility modulates kinetics and thermodynamics of drug binding.Importance of cycle timing for the function of the molecular chaperone Hsp90.Improvement of catalytic efficiency and thermostability of recombinant Streptomyces griseus trypsin by introducing artificial peptide.Artificial Accelerators of the Molecular Chaperone Hsp90 Facilitate Rate-Limiting Conformational Transitions
P2860
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P2860
N-terminal residues regulate the catalytic efficiency of the Hsp90 ATPase cycle.
description
2002 nî lūn-bûn
@nan
2002 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
N-terminal residues regulate the catalytic efficiency of the Hsp90 ATPase cycle.
@ast
N-terminal residues regulate the catalytic efficiency of the Hsp90 ATPase cycle.
@en
N-terminal residues regulate the catalytic efficiency of the Hsp90 ATPase cycle.
@nl
type
label
N-terminal residues regulate the catalytic efficiency of the Hsp90 ATPase cycle.
@ast
N-terminal residues regulate the catalytic efficiency of the Hsp90 ATPase cycle.
@en
N-terminal residues regulate the catalytic efficiency of the Hsp90 ATPase cycle.
@nl
prefLabel
N-terminal residues regulate the catalytic efficiency of the Hsp90 ATPase cycle.
@ast
N-terminal residues regulate the catalytic efficiency of the Hsp90 ATPase cycle.
@en
N-terminal residues regulate the catalytic efficiency of the Hsp90 ATPase cycle.
@nl
P3181
P356
P1476
N-terminal residues regulate the catalytic efficiency of the Hsp90 ATPase cycle.
@en
P2093
Jochen Reinstein
Johannes Buchner
P304
P3181
P356
10.1074/JBC.M208457200
P407
P577
2002-11-22T00:00:00Z