Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange - Wikidata - awgldk - TriplyDB

Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange

Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange

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Not all J domains are created equal: implications for the specificity of Hsp40-Hsp70 interactions The nucleotide exchange factors of Hsp70 molecular chaperones BiP and its nucleotide exchange factors Grp170 and Sil1: mechanisms of action and biological functions Insights into Hsp70 Chaperone Activity from a Crystal Structure of the Yeast Hsp110 Sse1 Structure of the Hsp110:Hsc70 nucleotide exchange machine.Structural basis of nucleotide exchange and client binding by the Hsp70 cochaperone Bag2 Structural and Functional Analysis of the Globular Head Domain of p115 Provides Insight into Membrane Tethering Biochemical and structural studies on the high affinity of Hsp70 for ADP The Hsp70 homolog Ssb is essential for glucose sensing via the SNF1 kinase network Saccharomyces cerevisiae Rot1p is an ER-localized membrane protein that may function with BiP/Kar2p in protein folding.A lysine-rich region within fungal BAG domain-containing proteins mediates a novel association with ribosomes.Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s.The yeast Hsp110, Sse1p, exhibits high-affinity peptide binding.Prion-impairing mutations in Hsp70 chaperone Ssa1: effects on ATPase and chaperone activities.Hsp70 nucleotide exchange factor Fes1 is essential for ubiquitin-dependent degradation of misfolded cytosolic proteins.Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor.Plasmodium falciparum Hsp70-z, an Hsp110 homologue, exhibits independent chaperone activity and interacts with Hsp70-1 in a nucleotide-dependent fashion The human HSP70 family of chaperones: where do we stand?Allostery in the Hsp70 chaperone proteins Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro Changes in protein structure at the interface accompanying complex formation.Structure of the Tuberous Sclerosis Complex 2 (TSC2) N Terminus Provides Insight into Complex Assembly and Tuberous Sclerosis Pathogenesis.ATP-induced conformational changes in Hsp70: molecular dynamics and experimental validation of an in silico predicted conformation.Detection of alpha-rod protein repeats using a neural network and application to huntingtin.A nationwide survey on Marinesco-Sjögren syndrome in Japan.Hierarchical functional specificity of cytosolic heat shock protein 70 (Hsp70) nucleotide exchange factors in yeast.Role of Hsp70 ATPase domain intrinsic dynamics and sequence evolution in enabling its functional interactions with NEFs.Quantitative shotgun proteomics using a uniform ¹⁵N-labeled standard to monitor proteome dynamics in time course experiments reveals new insights into the heat stress response of Chlamydomonas reinhardtii HSP70-binding protein HSPBP1 regulates chaperone expression at a posttranslational level and is essential for spermatogenesis.Functional and genomic analyses of alpha-solenoid proteins.Overexpressed heat shock protein 70 protects cells against DNA damage caused by ultraviolet C in a dose-dependent manner.Role of Hsc70 binding cycle in CFTR folding and endoplasmic reticulum-associated degradation.Importance of the Hsp70 ATPase domain in yeast prion propagation Keep the traffic moving: mechanism of the Hsp70 motor.Molecular and functional characterization of the only known hemiascomycete ortholog of the carboxyl terminus of Hsc70-interacting protein CHIP in the yeast Yarrowia lipolytica.All in the family: atypical Hsp70 chaperones are conserved modulators of Hsp70 activity.The Hsp40 molecular chaperone Ydj1p, along with the protein kinase C pathway, affects cell-wall integrity in the yeast Saccharomyces cerevisiae.C-terminal mutations destabilize SIL1/BAP and can cause Marinesco-Sjögren syndrome.The structural and functional diversity of Hsp70 proteins from Plasmodium falciparum HSP70 binding protein 1 (HspBP1) suppresses HIV-1 replication by inhibiting NF-κB mediated activation of viral gene expression.

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P2860

Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange

http://www.wikidata.org/entity/Q28305976

description

2005 nî lūn-bûn

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2005 թուականի Փետրուարին հրատարակուած գիտական յօդուած

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2005 թվականի փետրվարին հրատարակված գիտական հոդված

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2005年の論文

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2005年論文

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2005年論文

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name

Regulation of Hsp70 function b ...... for Hsp70 nucleotide exchange

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Regulation of Hsp70 function b ...... for Hsp70 nucleotide exchange

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Regulation of Hsp70 function b ...... for Hsp70 nucleotide exchange

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Regulation of Hsp70 function b ...... for Hsp70 nucleotide exchange

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Regulation of Hsp70 function b ...... for Hsp70 nucleotide exchange

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Regulation of Hsp70 function b ...... for Hsp70 nucleotide exchange

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Regulation of Hsp70 function b ...... for Hsp70 nucleotide exchange

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Regulation of Hsp70 Function by HspBP1

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Regulation of Hsp70 function b ...... for Hsp70 nucleotide exchange

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P2093

Andreas Bracher

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F Ulrich Hartl

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F.Ulrich Hartl

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Hung-Chun Chang

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Jason C Young

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Jeffrey L Brodsky

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Jeffrey L. Brodsky

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Nikolay Tzvetkov

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Vince Guerriero

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