Monitoring the prevention of amyloid fibril formation by alpha-crystallin. Temperature dependence and the nature of the aggregating species.
about
Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens functionThe 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.The interaction of unfolding α-lactalbumin and malate dehydrogenase with the molecular chaperone αB-crystallin: a light and X-ray scattering investigation.αB-Crystallin inhibits the cell toxicity associated with amyloid fibril formation by κ-casein and the amyloid-β peptide.Binding of the molecular chaperone αB-crystallin to Aβ amyloid fibrils inhibits fibril elongationMonitoring the interaction between β2-microglobulin and the molecular chaperone αB-crystallin by NMR and mass spectrometry: αB-crystallin dissociates β2-microglobulin oligomers.Survey of the year 2007 commercial optical biosensor literature.Amyloid fiber formation in human γD-Crystallin induced by UV-B photodamageStructure/function studies of dogfish alpha-crystallin, comparison with bovine alpha-crystallin.Mechanism of suppression of protein aggregation by α-crystallin.Protein Quality Control by Molecular Chaperones in Neurodegeneration.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.Gene expression profiling of light-induced retinal degeneration in phototransduction gene knockout mice.Chaperone-like activities of different molecular forms of beta-casein. Importance of polarity of N-terminal hydrophilic domain.Biophysical approaches for the study of interactions between molecular chaperones and protein aggregates.Expanding role of molecular chaperones in regulating α-synuclein misfolding; implications in Parkinson's disease.The molecular chaperone alpha-crystallin as an excipient in an insulin formulation.Small Heat-shock Proteins Prevent α-Synuclein Aggregation via Transient Interactions and Their Efficacy Is Affected by the Rate of AggregationEffect of αB-crystallin on protein aggregation in Drosophila.The small heat shock protein Hsp27 binds α-synuclein fibrils, preventing elongation and cytotoxicity.The functional roles of the unstructured N- and C-terminal regions in αB-crystallin and other mammalian small heat-shock proteins.Inhibition of α-synuclein aggregation by small heat shock proteins.PAMAM Dendrimers as Potential Agents against Fibrillation ofα-Synuclein, a Parkinson's Disease-Related Protein
P2860
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P2860
Monitoring the prevention of amyloid fibril formation by alpha-crystallin. Temperature dependence and the nature of the aggregating species.
description
2007 nî lūn-bûn
@nan
2007 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Monitoring the prevention of a ...... re of the aggregating species.
@ast
Monitoring the prevention of a ...... re of the aggregating species.
@en
Monitoring the prevention of a ...... re of the aggregating species.
@nl
type
label
Monitoring the prevention of a ...... re of the aggregating species.
@ast
Monitoring the prevention of a ...... re of the aggregating species.
@en
Monitoring the prevention of a ...... re of the aggregating species.
@nl
prefLabel
Monitoring the prevention of a ...... re of the aggregating species.
@ast
Monitoring the prevention of a ...... re of the aggregating species.
@en
Monitoring the prevention of a ...... re of the aggregating species.
@nl
P2093
P2860
P1433
P1476
Monitoring the prevention of a ...... re of the aggregating species.
@en
P2093
Agata Rekas
David C Thorn
Lucy Jankova
P2860
P304
P356
10.1111/J.1742-4658.2007.06144.X
P407
P577
2007-11-12T00:00:00Z