The chaperone αB-crystallin uses different interfaces to capture an amorphous and an amyloid client.
about
Cataract-associated P23T γD-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH.Proline isomerization in the C-terminal region of HSP27.Multiple oligomeric structures of a bacterial small heat shock proteinThe Human 343delT HSPB5 Chaperone Associated with Early-onset Skeletal Myopathy Causes Defects in Protein SolubilityThe redox environment triggers conformational changes and aggregation of hIAPP in Type II Diabetes.Differential phosphorylation-based regulation of αB-crystallin chaperone activity for multipass transmembrane proteins.The growing world of small heat shock proteins: from structure to functions.Limits of Resolution and Sensitivity of Proton Detected MAS Solid-State NMR Experiments at 111 kHz in Deuterated and Protonated Proteins.Functional Amyloid Protection in the Eye Lens: Retention of α-Crystallin Molecular Chaperone Activity after Modification into Amyloid Fibrils.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.Small Heat-shock Proteins Prevent α-Synuclein Aggregation via Transient Interactions and Their Efficacy Is Affected by the Rate of AggregationBAG3 Is a Modular, Scaffolding Protein that physically Links Heat Shock Protein 70 (Hsp70) to the Small Heat Shock Proteins.An alternative splice variant of human αA-crystallin modulates the oligomer ensemble and the chaperone activity of α-crystallins.Bri2 BRICHOS client specificity and chaperone activity are governed by assembly state.HspB1 and Hsc70 chaperones engage distinct tau species and have different inhibitory effects on amyloid formation.Experimental Aspects of Polarization Optimized Experiments (POE) for Magic Angle Spinning Solid-State NMR of Microcrystalline and Membrane-Bound Proteins.Insights into protein misfolding and aggregation enabled by solid-state NMR spectroscopy.The functional roles of the unstructured N- and C-terminal regions in αB-crystallin and other mammalian small heat-shock proteins.Modulating the Effects of the Bacterial Chaperonin GroEL on Fibrillogenic Polypeptides through Modification of Domain Hinge Architecture.An in silico study of the effect of SOD1 electrostatic loop dynamics on amyloid‑like filament formation.The influence of the N-terminal region proximal to the core domain on the assembly and chaperone activity of αB-crystallin.Oligomerization of a molecular chaperone modulates its activity.New applications of solid-state NMR in structural biologyPost-diapause synthesis of ArHsp40-2, a type 2 J-domain protein from Artemia franciscana, is developmentally regulated and induced by stressCompeting protein-protein interactions regulate binding of Hsp27 to its client protein tauTerminal Regions Confer Plasticity to the Tetrameric Assembly of Human HspB2 and HspB3
P2860
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P2860
The chaperone αB-crystallin uses different interfaces to capture an amorphous and an amyloid client.
description
2015 nî lūn-bûn
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2015年の論文
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2015年学术文章
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2015年学术文章
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2015年学术文章
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2015年学术文章
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2015年学术文章
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2015年学术文章
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2015年學術文章
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2015年學術文章
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name
The chaperone αB-crystallin us ...... orphous and an amyloid client.
@en
The chaperone αB-crystallin us ...... orphous and an amyloid client.
@nl
type
label
The chaperone αB-crystallin us ...... orphous and an amyloid client.
@en
The chaperone αB-crystallin us ...... orphous and an amyloid client.
@nl
prefLabel
The chaperone αB-crystallin us ...... orphous and an amyloid client.
@en
The chaperone αB-crystallin us ...... orphous and an amyloid client.
@nl
P2093
P2860
P50
P356
P1476
The chaperone αB-crystallin us ...... orphous and an amyloid client.
@en
P2093
Andi Mainz
Carsten Peters
Elke Prade
Johannes Buchner
Katrin C Back
Maria Stavropoulou
Sevil Weinkauf
P2860
P2888
P304
P356
10.1038/NSMB.3108
P577
2015-10-12T00:00:00Z