Mini-alphaB-crystallin: a functional element of alphaB-crystallin with chaperone-like activity
about
Aging and age-related diseases of the ocular lens and vitreous bodySolid-state NMR and SAXS studies provide a structural basis for the activation of αB-crystallin oligomersThe structured core domain of B-crystallin can prevent amyloid fibrillation and associated toxicityFunctions of crystallins in and out of lens: roles in elongated and post-mitotic cellsAnti-chaperone betaA3/A1(102-117) peptide interacting sites in human alphaB-crystallinDetection and architecture of small heat shock protein monomers.Cataract-causing αAG98R-crystallin mutant dissociates into monomers having chaperone activity.Protein polymer nanoparticles engineered as chaperones protect against apoptosis in human retinal pigment epithelial cellsFunctional insights by comparison of modeled structures of 18kDa small heat shock protein and its mutant in Mycobacterium lepraeComparison of modification sites in glycated crystallin in vitro and in vivo.Interaction of amyloid inhibitor proteins with amyloid beta peptides: insight from molecular dynamics simulationsIdentification of peptides in human Hsp20 and Hsp27 that possess molecular chaperone and anti-apoptotic activitiesNovel roles for α-crystallins in retinal function and disease.Alpha crystallins in the retinal pigment epithelium and implications for the pathogenesis and treatment of age-related macular degenerationChaperone activity of small heat shock proteins underlies therapeutic efficacy in experimental autoimmune encephalomyelitis.Crystallins and neuroinflammation: The glial side of the story.Alpha-crystallin-derived peptides as therapeutic chaperones.Conserved F84 and P86 residues in alphaB-crystallin are essential to effectively prevent the aggregation of substrate proteins.Antiapoptotic properties of α-crystallin-derived peptide chaperones and characterization of their uptake transporters in human RPE cells.Chaperone peptides of α-crystallin inhibit epithelial cell apoptosis, protein insolubilization, and opacification in experimental cataractsInteractive sequences in the molecular chaperone, human alphaB crystallin modulate the fibrillation of amyloidogenic proteins.alphaB-crystallin: a hybrid solid-state/solution-state NMR investigation reveals structural aspects of the heterogeneous oligomer.The αA66-80 peptide interacts with soluble α-crystallin and induces its aggregation and precipitation: a contribution to age-related cataract formation.αB-crystallin: Portrait of a malignant chaperone as a cancer therapeutic targetIndoleamine 2,3-dioxygenase overexpression causes kynurenine-modification of proteins, fiber cell apoptosis and cataract formation in the mouse lensLens aging: effects of crystallins.One size does not fit all: the oligomeric states of αB crystallin.Impact of diabetes on alpha-crystallins and other heat shock proteins in the eye.Small heat-shock proteins: important players in regulating cellular proteostasis.RNA aptamers targeted for human αA-crystallin do not bind αB-crystallin, and spare the α-crystallin domain.Structural and functional properties of NH(2)-terminal domain, core domain, and COOH-terminal extension of αA- and αB-crystallins.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.Deletion of (54)FLRAPSWF(61) residues decreases the oligomeric size and enhances the chaperone function of alphaB-crystallinTruncation attenuates molecular chaperoning and apoptosis inhibition by p26, a small heat shock protein from Artemia franciscana.Self-assembly of protein aggregates in ageing disorders: the lens and cataract model.Structural and mechanistic implications of metal binding in the small heat-shock protein αB-crystallinAge-related cleavages of crystallins in human lens cortical fiber cells generate a plethora of endogenous peptides and high molecular weight complexes.Functional Amyloid Protection in the Eye Lens: Retention of α-Crystallin Molecular Chaperone Activity after Modification into Amyloid Fibrils.
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Mini-alphaB-crystallin: a functional element of alphaB-crystallin with chaperone-like activity
description
article científic
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article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on March 2006
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
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vědecký článek
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name
Mini-alphaB-crystallin: a func ...... n with chaperone-like activity
@en
Mini-alphaB-crystallin: a func ...... with chaperone-like activity.
@nl
type
label
Mini-alphaB-crystallin: a func ...... n with chaperone-like activity
@en
Mini-alphaB-crystallin: a func ...... with chaperone-like activity.
@nl
prefLabel
Mini-alphaB-crystallin: a func ...... n with chaperone-like activity
@en
Mini-alphaB-crystallin: a func ...... with chaperone-like activity.
@nl
P2093
P2860
P356
P1433
P1476
Mini-alphaB-crystallin: a func ...... n with chaperone-like activity
@en
P2093
E G Padmanabha Udupa
Jaya Bhattacharyya
K Krishna Sharma
P2860
P304
P356
10.1021/BI0518141
P407
P577
2006-03-01T00:00:00Z