Interaction of the molecular chaperone alphaB-crystallin with alpha-synuclein: effects on amyloid fibril formation and chaperone activity.
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Historical and Current Concepts of Fibrillogenesis and In vivo Amyloidogenesis: Implications of Amyloid Tissue TargetingPhysicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs)Potential roles for prions and protein-only inheritance in cancerMolecular chaperones and co-chaperones in Parkinson diseaseThe structured core domain of B-crystallin can prevent amyloid fibrillation and associated toxicityThe Synaptic Function of α-SynucleinProtein-metal interactions of calmodulin and alpha-synuclein monitored by selective noncovalent adduct protein probing mass spectrometry.Bovine PrPC directly interacts with alphaB-crystalline.Site-directed mutations in the C-terminal extension of human alphaB-crystallin affect chaperone function and block amyloid fibril formationIntrinsically disordered proteins display no preference for chaperone binding in vivo.Amyloidogenic and associated proteins in systemic amyloidosis proteome of adipose tissue.Interaction between oligomers of stefin B and amyloid-beta in vitro and in cells.The interaction of alphaB-crystallin with mature alpha-synuclein amyloid fibrils inhibits their elongation.Small heat-shock proteins interact with a flanking domain to suppress polyglutamine aggregation.Cataract-causing defect of a mutant γ-crystallin proceeds through an aggregation pathway which bypasses recognition by the α-crystallin chaperone.Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humansαB-Crystallin inhibits the cell toxicity associated with amyloid fibril formation by κ-casein and the amyloid-β peptide.Are heat shock proteins therapeutic target for Parkinson's disease?Neuropathology, biochemistry, and biophysics of alpha-synuclein aggregation.Monitoring the prevention of amyloid fibril formation by alpha-crystallin. Temperature dependence and the nature of the aggregating species.Dealing with misfolded proteins: examining the neuroprotective role of molecular chaperones in neurodegeneration.Binding of the molecular chaperone αB-crystallin to Aβ amyloid fibrils inhibits fibril elongationGenetic disorders involving molecular-chaperone genes: a perspective.Novel roles for α-crystallins in retinal function and disease.Crystallins and neuroinflammation: The glial side of the story.Differential regulation of small heat shock proteins in transgenic mouse models of neurodegenerative diseases.Structural and functional aspects of hetero-oligomers formed by the small heat shock proteins αB-crystallin and HSP27Monitoring the interaction between β2-microglobulin and the molecular chaperone αB-crystallin by NMR and mass spectrometry: αB-crystallin dissociates β2-microglobulin oligomers.Effects of α-synuclein overexpression in transgenic Caenorhabditis elegans strainsαB-Crystallin overexpression in astrocytes modulates the phenotype of the BACHD mouse model of Huntington's diseaseInteractive sequences in the molecular chaperone, human alphaB crystallin modulate the fibrillation of amyloidogenic proteins.Methionine sulfoxide reductase A (MsrA) restores alpha-crystallin chaperone activity lost upon methionine oxidationA novel function for proSAAS as an amyloid anti-aggregant in Alzheimer's disease.Alpha-synuclein structures from fluorescence energy-transfer kinetics: implications for the role of the protein in Parkinson's disease.Protein Quality Control by Molecular Chaperones in Neurodegeneration.Molecular chaperones and associated cellular clearance mechanisms against toxic protein conformers in Parkinson's disease.Different anti-aggregation and pro-degradative functions of the members of the mammalian sHSP family in neurological disorders.Small heat-shock proteins: important players in regulating cellular proteostasis.The transcription factor Pax6 regulates survival of dopaminergic olfactory bulb neurons via crystallin αA.Biophysical approaches for the study of interactions between molecular chaperones and protein aggregates.
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P2860
Interaction of the molecular chaperone alphaB-crystallin with alpha-synuclein: effects on amyloid fibril formation and chaperone activity.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
2004年學術文章
@zh-hant
name
Interaction of the molecular c ...... mation and chaperone activity.
@en
Interaction of the molecular c ...... mation and chaperone activity.
@nl
type
label
Interaction of the molecular c ...... mation and chaperone activity.
@en
Interaction of the molecular c ...... mation and chaperone activity.
@nl
prefLabel
Interaction of the molecular c ...... mation and chaperone activity.
@en
Interaction of the molecular c ...... mation and chaperone activity.
@nl
P2093
P50
P1476
Interaction of the molecular c ...... mation and chaperone activity.
@en
P2093
Agata Rekas
Denise Galatis
J Andrew Aquilina
Kevin J Barnham
P304
P356
10.1016/J.JMB.2004.05.054
P407
P50
P577
2004-07-01T00:00:00Z