HspB8, a small heat shock protein mutated in human neuromuscular disorders, has in vivo chaperone activity in cultured cells.

scientific article published on 6 May 2005

HspB8, a small heat shock protein mutated in human neuromuscular disorders, has in vivo chaperone activity in cultured cells. is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1093/HMG/DDI174
P698PubMed publication ID15879436
P5875ResearchGate publication ID7862414

P50authorSerena CarraQ55136801
P2093author name stringJacques Landry
Herman Lambert
Aura T Chávez Zobel
Mitchel Sivilotti
P2860cites workMechanisms for regulation of Hsp70 function by Hsp40Q24563232
The human genome encodes 10 alpha-crystallin-related small heat shock proteins: HspB1-10Q24563241
Modulation of cellular thermoresistance and actin filament stability accompanies phosphorylation-induced changes in the oligomeric structure of heat shock protein 27Q24646796
Crystal structure of a small heat-shock proteinQ27765131
Polyglutamine length-dependent interaction of Hsp40 and Hsp70 family chaperones with truncated N-terminal huntingtin: their role in suppression of aggregation and cellular toxicityQ28143597
Molecular chaperones in the cytosol: from nascent chain to folded proteinQ28205903
Impairment of the ubiquitin-proteasome system by protein aggregationQ29614556
Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseasesQ29616535
Protein degradation and protection against misfolded or damaged proteinsQ29618400
Alpha-crystallin can function as a molecular chaperoneQ29618672
Formic acid dissolves aggregates of an N-terminal huntingtin fragment containing an expanded polyglutamine tract: applying to quantification of protein components of the aggregatesQ31460493
Polyglutamine-expanded androgen receptors form aggregates that sequester heat shock proteins, proteasome components and SRC-1, and are suppressed by the HDJ-2 chaperoneQ33858200
A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent stateQ33886098
Androgen receptor gene mutations in X-linked spinal and bulbar muscular atrophyQ34023072
Cellular defenses against unfolded proteins: a cell biologist thinks about neurodegenerative diseasesQ34142252
From the cradle to the grave: molecular chaperones that may choose between folding and degradationQ34400939
Polyglutamine fibrillogenesis: the pathway unfoldsQ34466014
Effects of heat shock, heat shock protein 40 (HDJ-2), and proteasome inhibition on protein aggregation in cellular models of Huntington's diseaseQ35084195
Hsp70 and hsp40 chaperones can inhibit self-assembly of polyglutamine proteins into amyloid-like fibrilsQ35169533
Alpha B-crystallin is expressed in non-lenticular tissues and accumulates in Alexander's disease brainQ35416428
CHIP: a link between the chaperone and proteasome systemsQ35759085
The sperm outer dense fiber protein is the 10th member of the superfamily of mammalian small stress proteinsQ37490527
Chaperone suppression of alpha-synuclein toxicity in a Drosophila model for Parkinson's diseaseQ43874109
Molecular chaperones enhance the degradation of expanded polyglutamine repeat androgen receptor in a cellular model of spinal and bulbar muscular atrophyQ43903236
Huntingtin-encoded polyglutamine expansions form amyloid-like protein aggregates in vitro and in vivoQ45294913
Molecular chaperones and the stress of oncogenesisQ47785215
P433issue12
P921main subjectmolecular chaperonesQ422496
P304page(s)1659-1669
P577publication date2005-05-06
P1433published inHuman Molecular GeneticsQ2720965
P1476titleHspB8, a small heat shock protein mutated in human neuromuscular disorders, has in vivo chaperone activity in cultured cells
P478volume14

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cites work (P2860)
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