Lysine 71 of the chaperone protein Hsc70 Is essential for ATP hydrolysis - Wikidata - thesis-toulmin - TriplyDB

Lysine 71 of the chaperone protein Hsc70 Is essential for ATP hydrolysis

Lysine 71 of the chaperone protein Hsc70 Is essential for ATP hydrolysis

http://www.wikidata.org/entity/Q27732843

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Engineering and Evolution of Molecular Chaperones and Protein Disaggregases with Enhanced Activity Insights into the molecular mechanism of allostery in Hsp70s.Insights into Hsp70 Chaperone Activity from a Crystal Structure of the Yeast Hsp110 Sse1 Crystal Structures of the 70-kDa Heat Shock Proteins in Domain Disjoining Conformation Biochemical and structural studies on the high affinity of Hsp70 for ADP Functional analysis of Hsp70 inhibitors Structural characterization of a eukaryotic chaperone--the ribosome-associated complex Allostery in the Hsp70 chaperone proteins Identification of key hinge residues important for nucleotide-dependent allostery in E. coli Hsp70/DnaK Hsc70 regulates accumulation of cyclin D1 and cyclin D1-dependent protein kinase Allostery in Hsp70 chaperones is transduced by subdomain rotations ATP-induced conformational changes in Hsp70: molecular dynamics and experimental validation of an in silico predicted conformation.Free ATP inhibits thimet oligopeptidase (EC 3.4.24.15) activity, induces autophosphorylation in vitro, and controls oligopeptide degradation in macrophage.Hsc70 focus formation at the periphery of HSV-1 transcription sites requires ICP27.Measurement and interpretation of 15N-1H residual dipolar couplings in larger proteins.ATPgammaS disrupts human immunodeficiency virus type 1 virion core integrity.Mutagenesis reveals the complex relationships between ATPase rate and the chaperone activities of Escherichia coli heat shock protein 70 (Hsp70/DnaK)ATPase-defective derivatives of Escherichia coli DnaK that behave differently with respect to ATP-induced conformational change and peptide release Uncoating ATPase Hsc70 is recruited by invariant chain and controls the size of endocytic compartments Heat shock protein 72 is associated with the hepatitis C virus replicase complex and enhances viral RNA replication.Hsp70/Hsp90 chaperone machinery is involved in the assembly of the purinosome.Chemical screens against a reconstituted multiprotein complex: myricetin blocks DnaJ regulation of DnaK through an allosteric mechanism Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones Common functionally important motions of the nucleotide-binding domain of Hsp70 Decipher the mechanisms of protein conformational changes induced by nucleotide binding through free-energy landscape analysis: ATP binding to Hsp70.Intercellular chaperone transmission via exosomes contributes to maintenance of protein homeostasis at the organismal level.Isoform-selective Genetic Inhibition of Constitutive Cytosolic Hsp70 Activity Promotes Client Tau Degradation Using an Altered Co-chaperone Complement Tetratricopeptide repeat cochaperones in steroid receptor complexes Subcellular distribution of non-muscle myosin IIb is controlled by FILIP through Hsc70 Dominant-interfering Hsc70 mutants disrupt multiple stages of the clathrin-coated vesicle cycle in vivo.Experimentally biased model structure of the Hsc70/auxilin complex: substrate transfer and interdomain structural change The 70-kDa heat shock protein chaperone nucleotide-binding domain in solution unveiled as a molecular machine that can reorient its functional subdomains.Tissue-specific expression of dominant negative mutant Drosophila HSC70 causes developmental defects and lethality.Hsp70 structure, function, regulation and influence on yeast prions.Interaction of the cotranslational Hsp70 Ssb with ribosomal proteins and rRNA depends on its lid domain.Modeling and docking studies on novel mutants (K71L and T204V) of the ATPase domain of human heat shock 70 kDa protein 1.The cellular chaperone hsc70 is specifically recruited to reovirus viral factories independently of its chaperone function.Mutation of Hip's carboxy-terminal region inhibits a transitional stage of progesterone receptor assembly.Defining Hsp70 Subnetworks in Dengue Virus Replication Reveals Key Vulnerability in Flavivirus Infection.The peptide-binding and ATPase domains of recombinant hsc70 are required to interact with rotavirus and reduce its infectivity.

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P2860

Lysine 71 of the chaperone protein Hsc70 Is essential for ATP hydrolysis

http://www.wikidata.org/entity/Q27732843

description

1996 nî lūn-bûn

@nan

1996 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

1996 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

1996年の論文

@ja

1996年論文

@yue

1996年論文

@zh-hant

1996年論文

@zh-hk

1996年論文

@zh-mo

1996年論文

@zh-tw

1996年论文

@wuu

name

Lysine 71 of the chaperone protein Hsc70 Is essential for ATP hydrolysis

@ast

Lysine 71 of the chaperone protein Hsc70 Is essential for ATP hydrolysis

@en

Lysine 71 of the chaperone protein Hsc70 Is essential for ATP hydrolysis

@nl

type

label

Lysine 71 of the chaperone protein Hsc70 Is essential for ATP hydrolysis

@ast

Lysine 71 of the chaperone protein Hsc70 Is essential for ATP hydrolysis

@en

Lysine 71 of the chaperone protein Hsc70 Is essential for ATP hydrolysis

@nl

prefLabel

Lysine 71 of the chaperone protein Hsc70 Is essential for ATP hydrolysis

@ast

Lysine 71 of the chaperone protein Hsc70 Is essential for ATP hydrolysis

@en

Lysine 71 of the chaperone protein Hsc70 Is essential for ATP hydrolysis

@nl

P1433

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P356

JBC.271.27.15874

P1433

Journal of Biological Chemistry

P1476

Lysine 71 of the chaperone protein Hsc70 Is essential for ATP hydrolysis

@en

P2093

D B McKay

http://www.w3.org/2001/XMLSchema#string

K M Flaherty

http://www.w3.org/2001/XMLSchema#string

M C O'Brien

http://www.w3.org/2001/XMLSchema#string

P2860

DNA sequencing with chain-terminating inhibitors

Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein

Crystallographic R factor refinement by molecular dynamics

Uncoating protein (hsc70) binds a conformationally labile domain of clathrin light chain LCa to stimulate ATP hydrolysis

Protein folding in the cell

A graphics model building and refinement system for macromolecules

An enzyme that removes clathrin coats: purification of an uncoating ATPase.

Hsc70-binding peptides selected from a phage display peptide library that resemble organellar targeting sequences.

How potassium affects the activity of the molecular chaperone Hsc70. I. Potassium is required for optimal ATPase activity.

ATP-induced protein-Hsp70 complex dissociation requires K+ but not ATP hydrolysis.

P304

15874-8

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scholarly article

P356

10.1074/JBC.271.27.15874

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P433

27

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271

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1996-07-05T00:00:00Z

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P5875

14538197

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P698

8663302

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P921

molecular chaperones