Phosphorylation dependence of hsp27 multimeric size and molecular chaperone function - Wikidata - awgldk - TriplyDB

Phosphorylation dependence of hsp27 multimeric size and molecular chaperone function

Phosphorylation dependence of hsp27 multimeric size and molecular chaperone function

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Crystal Structure of R120G Disease Mutant of Human αB-Crystallin Domain Dimer Shows Closure of a Groove Alternative bacterial two-component small heat shock protein systems Characterization of Mutants of Human Small Heat Shock Protein HspB1 Carrying Replacements in the N-Terminal Domain and Associated with Hereditary Motor Neuron Diseases Heat shock proteins: cellular and molecular mechanisms in the central nervous system.Role of heat shock factor-1 activation in the doxorubicin-induced heart failure in mice.Heat shock protein 27 phosphorylation state is associated with cancer progression.Human-derived physiological heat shock protein 27 complex protects brain after focal cerebral ischemia in mice.Heat shock transcription factor 1-deficiency attenuates overloading-associated hypertrophy of mouse soleus muscle.Sequestration of toxic oligomers by HspB1 as a cytoprotective mechanism.A first line of stress defense: small heat shock proteins and their function in protein homeostasis.Hsp27-actin interaction.Heterooligomeric complexes of human small heat shock proteins Sequence, structure, and dynamic determinants of Hsp27 (HspB1) equilibrium dissociation are encoded by the N-terminal domain.Oligomers of Heat-Shock Proteins: Structures That Don't Imply Function.Effect of N-terminal region of nuclear Drosophila melanogaster small heat shock protein DmHsp27 on function and quaternary structure.Equilibrium self-association of tropomyosin.Structural and functional aspects of hetero-oligomers formed by the small heat shock proteins αB-crystallin and HSP27 Multi-kinase inhibitors can associate with heat shock proteins through their NH2-termini by which they suppress chaperone function αB-Crystallin overexpression in astrocytes modulates the phenotype of the BACHD mouse model of Huntington's disease Regulated structural transitions unleash the chaperone activity of αB-crystallin Regeneration of injured skeletal muscle in heat shock transcription factor 1-null mice Large potentials of small heat shock proteins.Small heat-shock proteins: important players in regulating cellular proteostasis.Medical implications of understanding the functions of human small heat shock proteins.Mammalian HspB1 (Hsp27) is a molecular sensor linked to the physiology and environment of the cell.Targeting Heat Shock Proteins in Cancer: A Promising Therapeutic Approach Small Heat-shock Proteins Prevent α-Synuclein Aggregation via Transient Interactions and Their Efficacy Is Affected by the Rate of Aggregation Effect of methylglyoxal modification on the structure and properties of human small heat shock protein HspB6 (Hsp20)The role of the cysteine residue in the chaperone and anti-apoptotic functions of human Hsp27.Disulfide cross-linked antiparallel actin dimer.pH-dependent structural modulation is conserved in the human small heat shock protein HSBP1.The role of αB-crystallin in skeletal and cardiac muscle tissues.A Novel Kinase Function of a Nucleoside-diphosphate-kinase Homolog in P. gingivalis is Critical in Subversion of Host Cell Apoptosis by Targeting Heat-Shock Protein 27.Deficiency of heat shock transcription factor 1 suppresses heat stress-associated increase in slow soleus muscle mass of mice.Characterization of human small heat shock protein HSPB1 α-crystallin domain localized mutants associated with hereditary motor neuron diseases.The small heat shock protein Hsp27 binds α-synuclein fibrils, preventing elongation and cytotoxicity.Effects of heat stress on muscle mass and the expression levels of heat shock proteins and lysosomal cathepsin L in soleus muscle of young and aged mice.The functional roles of the unstructured N- and C-terminal regions in αB-crystallin and other mammalian small heat-shock proteins.The Chaperone Activity and Substrate Spectrum of Human Small Heat Shock Proteins.Mild systemic thermal therapy ameliorates renal dysfunction in a rodent model of chronic kidney disease.

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Phosphorylation dependence of hsp27 multimeric size and molecular chaperone function

http://www.wikidata.org/entity/Q37254023

description

article científic

@ca

article scientifique

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articolo scientifico

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artigo científico

@pt

bilimsel makale

@tr

scientific article published on 30 April 2009

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Phosphorylation dependence of hsp27 multimeric size and molecular chaperone function

@en

Phosphorylation dependence of hsp27 multimeric size and molecular chaperone function.

@nl

type

label

Phosphorylation dependence of hsp27 multimeric size and molecular chaperone function

@en

Phosphorylation dependence of hsp27 multimeric size and molecular chaperone function.

@nl

prefLabel

Phosphorylation dependence of hsp27 multimeric size and molecular chaperone function

@en

Phosphorylation dependence of hsp27 multimeric size and molecular chaperone function.

@nl

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JBC.M109.011353

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Journal of Biological Chemistry

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Phosphorylation dependence of hsp27 multimeric size and molecular chaperone function

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Andrew Mazurkie

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David Hayes

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Philip Graceffa

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

Vanessa Napoli

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

Walter F Stafford

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

P2860

Fractionation of oxidized insulin

Stress- and mitogen-induced phosphorylation of the small heat shock protein Hsp25 by MAPKAP kinase 2 is not essential for chaperone properties and cellular thermoresistance

Modulation of cellular thermoresistance and actin filament stability accompanies phosphorylation-induced changes in the oligomeric structure of heat shock protein 27

Crystal structure of truncated human betaB1-crystallin

Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor alpha by phosphorylation

Structure and properties of small heat shock proteins (sHsp) and their interaction with cytoskeleton proteins

Structure and function of the small heat shock protein/alpha-crystallin family of molecular chaperones

Essential role of the NH2-terminal WD/EPF motif in the phosphorylation-activated protective function of mammalian Hsp27

Self-association of a small heat shock protein

On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation

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18801-18807

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scholarly article

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10.1074/JBC.M109.011353

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28

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19411251

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phosphorylation

molecular chaperones

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2707219

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