Charged linker sequence modulates eukaryotic heat shock protein 90 (Hsp90) chaperone activity
about
Molecular chaperones: guardians of the proteome in normal and disease statesAtomic structure of Hsp90-Cdc37-Cdk4 reveals that Hsp90 traps and stabilizes an unfolded kinasePosttranslational modification and conformational state of heat shock protein 90 differentially affect binding of chemically diverse small molecule inhibitorsConsiderations in the analysis of hydrogen exchange mass spectrometry data.Trans-spliced heat shock protein 90 modulates encystation in Giardia lambliaProbing molecular mechanisms of the Hsp90 chaperone: biophysical modeling identifies key regulators of functional dynamics.Cellulase linkers are optimized based on domain type and function: insights from sequence analysis, biophysical measurements, and molecular simulation.The charged linker of the molecular chaperone Hsp90 modulates domain contacts and biological function.Hsp70 forms antiparallel dimers stabilized by post-translational modifications to position clients for transfer to Hsp90.Chaperoning the chaperone: a role for the co-chaperone Cpr7 in modulating Hsp90 function in Saccharomyces cerevisiae.Molecular and thermodynamic insights into the conformational transitions of Hsp90.Solubility-promoting function of Hsp90 contributes to client maturation and robust cell growth.How bacteria survive an acid trip.The Role of Sulfhydryl Reactivity of Small Molecules for the Activation of the KEAP1/NRF2 Pathway and the Heat Shock ResponseDiverse functional manifestations of intrinsic structural disorder in molecular chaperones.Computational methods and challenges in hydrogen/deuterium exchange mass spectrometry.Hsp90 regulates the dynamics of its cochaperone Sti1 and the transfer of Hsp70 between modules.Modulation of domain-domain interaction and protein function by a charged linker: a case study of mycobacteriophage D29 endolysin.The joining of the Hsp90 and Hsp70 chaperone cycles yields transient interactions and stable intermediates: insights from mass spectrometry.Atomistic simulations and network-based modeling of the Hsp90-Cdc37 chaperone binding with Cdk4 client protein: A mechanism of chaperoning kinase clients by exploiting weak spots of intrinsically dynamic kinase domains.Importance of cycle timing for the function of the molecular chaperone Hsp90.Molecular evolutionary mechanisms driving functional diversification of the HSP90A family of heat shock proteins in eukaryotes.The HSP90 chaperone machinery.HSP90 gene expression induced by aspirin is associated with damage remission in a chicken myocardial cell culture exposed to heat stress.The HSP90 Family: Structure, Regulation, Function, and Implications in Health and Disease
P2860
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P2860
Charged linker sequence modulates eukaryotic heat shock protein 90 (Hsp90) chaperone activity
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Charged linker sequence modula ...... 90 (Hsp90) chaperone activity
@ast
Charged linker sequence modula ...... 90 (Hsp90) chaperone activity
@en
type
label
Charged linker sequence modula ...... 90 (Hsp90) chaperone activity
@ast
Charged linker sequence modula ...... 90 (Hsp90) chaperone activity
@en
prefLabel
Charged linker sequence modula ...... 90 (Hsp90) chaperone activity
@ast
Charged linker sequence modula ...... 90 (Hsp90) chaperone activity
@en
P2093
P2860
P356
P1476
Charged linker sequence modula ...... 90 (Hsp90) chaperone activity
@en
P2093
Barry Panaretou
Chung-Tien Lee
Leonard M Neckers
Mehdi Mollapour
Shinji Tsutsumi
Soichiro Yoshida
P2860
P304
P356
10.1073/PNAS.1114414109
P407
P577
2012-02-06T00:00:00Z