The structured core domain of B-crystallin can prevent amyloid fibrillation and associated toxicity
about
Extracellular Release and Signaling by Heat Shock Protein 27: Role in Modifying Vascular InflammationProline isomerization in the C-terminal region of HSP27.A Mechanism of Subunit Recruitment in Human Small Heat Shock Protein OligomersMolecular mechanism of the chaperone function of mini-α-crystallin, a 19-residue peptide of human α-crystallin.A first line of stress defense: small heat shock proteins and their function in protein homeostasis.Interaction of amyloid inhibitor proteins with amyloid beta peptides: insight from molecular dynamics simulationsA conserved histidine modulates HSPB5 structure to trigger chaperone activity in response to stress-related acidosisOligomers of Heat-Shock Proteins: Structures That Don't Imply Function.Truncated HSPB1 causes axonal neuropathy and impairs tolerance to unfolded protein stress.Alpha-crystallin-derived peptides as therapeutic chaperones.siRNA screen identifies QPCT as a druggable target for Huntington's disease.New insight into the dynamical system of αB-crystallin oligomers.The Human 343delT HSPB5 Chaperone Associated with Early-onset Skeletal Myopathy Causes Defects in Protein SolubilityαB-Crystallin overexpression in astrocytes modulates the phenotype of the BACHD mouse model of Huntington's diseaseSmall heat-shock proteins: important players in regulating cellular proteostasis.Therapeutic potential of α-crystallin.Medical implications of understanding the functions of human small heat shock proteins.Biophysical approaches for the study of interactions between molecular chaperones and protein aggregates.Non-neuronal Cells in ALS: Role of Glial, Immune cells and Blood-CNS Barriers.Small molecules, both dietary and endogenous, influence the onset of lens cataracts.The growing world of small heat shock proteins: from structure to functions.Ion mobility-mass spectrometry reveals conformational flexibility in the deubiquitinating enzyme USP5.Structure of the α-crystallin domain from the redox-sensitive chaperone, HSPB1.Oligomer-dependent and -independent chaperone activity of sHsps in different stressed conditions.Suppression of amyloid fibrils using the GroEL apical domain.Structural Basis for the Interaction of a Human Small Heat Shock Protein with the 14-3-3 Universal Signaling Regulator.Molecular Chaperones in the Pathogenesis of Amyotrophic Lateral Sclerosis: The Role of HSPB1.Small Heat-shock Proteins Prevent α-Synuclein Aggregation via Transient Interactions and Their Efficacy Is Affected by the Rate of AggregationMutant Huntingtin Inhibits αB-Crystallin Expression and Impairs Exosome Secretion from Astrocytes.BAG3 Is a Modular, Scaffolding Protein that physically Links Heat Shock Protein 70 (Hsp70) to the Small Heat Shock Proteins.pH-dependent structural modulation is conserved in the human small heat shock protein HSBP1.HspB1 and Hsc70 chaperones engage distinct tau species and have different inhibitory effects on amyloid formation.Propensity for cis-Proline Formation in Unfolded Proteins.The chaperone αB-crystallin uses different interfaces to capture an amorphous and an amyloid client.The small heat shock protein Hsp27 binds α-synuclein fibrils, preventing elongation and cytotoxicity.Specific sequences in the N-terminal domain of human small heat-shock protein HSPB6 dictate preferential hetero-oligomerization with the orthologue HSPB1.Denaturation induced aggregation in α-crystallin: differential action of chaotropes.Co-chaperoning by amyloid-forming proteins: cystatins vs. crystallins.Amyloid β-Sheet Secondary Structure Identified in UV-Induced Cataracts of Porcine Lenses using 2D IR Spectroscopy.The functional roles of the unstructured N- and C-terminal regions in αB-crystallin and other mammalian small heat-shock proteins.
P2860
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P2860
The structured core domain of B-crystallin can prevent amyloid fibrillation and associated toxicity
description
2014 nî lūn-bûn
@nan
2014 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2014年の論文
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2014年論文
@yue
2014年論文
@zh-hant
2014年論文
@zh-hk
2014年論文
@zh-mo
2014年論文
@zh-tw
2014年论文
@wuu
name
The structured core domain of ...... lation and associated toxicity
@ast
The structured core domain of ...... lation and associated toxicity
@en
The structured core domain of ...... lation and associated toxicity
@nl
type
label
The structured core domain of ...... lation and associated toxicity
@ast
The structured core domain of ...... lation and associated toxicity
@en
The structured core domain of ...... lation and associated toxicity
@nl
prefLabel
The structured core domain of ...... lation and associated toxicity
@ast
The structured core domain of ...... lation and associated toxicity
@en
The structured core domain of ...... lation and associated toxicity
@nl
P2093
P2860
P50
P3181
P356
P1476
The structured core domain of ...... lation and associated toxicity
@en
P2093
Andrew J Baldwin
David S Eisenberg
Georg K A Hochberg
Justin L P Benesch
Michael R Sawaya
Miranda P Collier
P2860
P304
P3181
P356
10.1073/PNAS.1322673111
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P50
P577
2014-04-22T00:00:00Z