Identification of the key structural motifs involved in HspB8/HspB6-Bag3 interaction
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A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathwaysGenome-wide studies of copy number variation and exome sequencing identify rare variants in BAG3 as a cause of dilated cardiomyopathyA genome-wide association study identifies two loci associated with heart failure due to dilated cardiomyopathyThe nucleotide exchange factors of Hsp70 molecular chaperonesHuman small heat shock proteins: protein interactomes of homo- and hetero-oligomeric complexes: an updateA Role for the Chaperone Complex BAG3-HSPB8 in Actin Dynamics, Spindle Orientation and Proper Chromosome Segregation during MitosisCrystal Structure of R120G Disease Mutant of Human αB-Crystallin Domain Dimer Shows Closure of a GrooveBAG3: a new player in the heart failure paradigmCardiomyocyte-Specific Human Bcl2-Associated Anthanogene 3 P209L Expression Induces Mitochondrial Fragmentation, Bcl2-Associated Anthanogene 3 Haploinsufficiency, and Activates p38 SignalingFunctions of crystallins in and out of lens: roles in elongated and post-mitotic cellsA BAG3 Coding Variant in Mice Determines Susceptibility to Ischemic Limb Muscle Myopathy by Directing Autophagy.Heat shock proteins: cellular and molecular mechanisms in the central nervous system.BAG3 directly interacts with mutated alphaB-crystallin to suppress its aggregation and toxicity.Inheritance patterns and phenotypic features of myofibrillar myopathy associated with a BAG3 mutationSmall heat shock protein 20 (HspB6) in cardiac hypertrophy and failureHeterooligomeric complexes of human small heat shock proteinsCordyceps sinensis attenuates renal fibrosis and suppresses BAG3 induction in obstructed rat kidneyThe Social Amoeba Dictyostelium discoideum Is Highly Resistant to Polyglutamine AggregationPoly-glutamine expanded huntingtin dramatically alters the genome wide binding of HSF1.Small heat shock protein IbpB acts as a robust chaperone in living cells by hierarchically activating its multi-type substrate-binding residues.Bcl2-associated athanogene 3 interactome analysis reveals a new role in modulating proteasome activity.ERK-mediated phosphorylation of BIS regulates nuclear translocation of HSF1 under oxidative stress.The prosurvival protein BAG3: a new participant in vascular homeostasisBAG3: a multifaceted protein that regulates major cell pathways.Large potentials of small heat shock proteins.Different anti-aggregation and pro-degradative functions of the members of the mammalian sHSP family in neurological disorders.Protein interactomes of three stress inducible small heat shock proteins: HspB1, HspB5 and HspB8.BAG3 regulates cell proliferation, migration, and invasion in human colorectal cancer.Inhibition of retrograde transport modulates misfolded protein accumulation and clearance in motoneuron diseases.An interaction study in mammalian cells demonstrates weak binding of HSPB2 to BAG3, which is regulated by HSPB3 and abrogated by HSPB8.BAG3 induces the sequestration of proteasomal clients into cytoplasmic puncta: implications for a proteasome-to-autophagy switch.Role of sHsps in organizing cytosolic protein aggregation and disaggregation.Decreased vulnerability of hippocampal neurons after neonatal hypoxia-ischemia in bis-deficient mice.The Role of the Multifunctional BAG3 Protein in Cellular Protein Quality Control and in Disease.Truncation attenuates molecular chaperoning and apoptosis inhibition by p26, a small heat shock protein from Artemia franciscana.Adenofection: A Method for Studying the Role of Molecular Chaperones in Cellular Morphodynamics by Depletion-Rescue Experiments.A BAG3 chaperone complex maintains cardiomyocyte function during proteotoxic stress.WW domain of BAG3 is required for the induction of autophagy in glioma cells.Multilevel structural characteristics for the natural substrate proteins of bacterial small heat shock proteins.Loss-of-function mutations in co-chaperone BAG3 destabilize small HSPs and cause cardiomyopathy.
P2860
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P2860
Identification of the key structural motifs involved in HspB8/HspB6-Bag3 interaction
description
2009 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2009
@ast
im Dezember 2009 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2009/12/14)
@sk
vědecký článek publikovaný v roce 2009
@cs
wetenschappelijk artikel (gepubliceerd op 2009/12/14)
@nl
наукова стаття, опублікована в грудні 2009
@uk
مقالة علمية (نشرت في 14-12-2009)
@ar
name
Identification of the key structural motifs involved in HspB8/HspB6-Bag3 interaction
@ast
Identification of the key structural motifs involved in HspB8/HspB6-Bag3 interaction
@en
Identification of the key structural motifs involved in HspB8/HspB6-Bag3 interaction
@nl
type
label
Identification of the key structural motifs involved in HspB8/HspB6-Bag3 interaction
@ast
Identification of the key structural motifs involved in HspB8/HspB6-Bag3 interaction
@en
Identification of the key structural motifs involved in HspB8/HspB6-Bag3 interaction
@nl
prefLabel
Identification of the key structural motifs involved in HspB8/HspB6-Bag3 interaction
@ast
Identification of the key structural motifs involved in HspB8/HspB6-Bag3 interaction
@en
Identification of the key structural motifs involved in HspB8/HspB6-Bag3 interaction
@nl
P2093
P2860
P3181
P356
P1433
P1476
Identification of the key structural motifs involved in HspB8/HspB6-Bag3 interaction
@en
P2093
Dominic J. Poirier
Herman Lambert
Jacques Landry
Margit Fuchs
Samuel J. Seguin
Serena Carra
Steve J. Charette
P2860
P304
P3181
P356
10.1042/BJ20090907
P407
P577
2009-12-14T00:00:00Z