Site-directed mutations in the C-terminal extension of human alphaB-crystallin affect chaperone function and block amyloid fibril formation

Site-directed mutations in the C-terminal extension of human alphaB-crystallin affect chaperone function and block amyloid fibril formation

Item
http://www.wikidata.org/entity/Q33302904
Neuropathy- and myopathy-associated mutations in human small heat shock proteins: Characteristics and evolutionary history of the mutation sitesCrystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens functionAmyloid-β oligomers are sequestered by both intracellular and extracellular chaperonesLens proteomics: analysis of rat crystallins when lenses are exposed to dexamethasone.Role of alphaBI5 and alphaBT162 residues in subunit interaction during oligomerization of alphaB-crystallin.Functional validation of hydrophobic adaptation to physiological temperature in the small heat shock protein αA-crystallinA first line of stress defense: small heat shock proteins and their function in protein homeostasis.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.COOH-terminal truncations and site-directed mutations enhance thermostability and chaperone-like activity of porcine alphaB-crystallin.Structure/function studies of dogfish alpha-crystallin, comparison with bovine alpha-crystallin.Moonlighting chaperone-like activity of the universal regulatory 14-3-3 proteins.Truncation of alphaB-crystallin by the myopathy-causing Q151X mutation significantly destabilizes the protein leading to aggregate formation in transfected cells.C-terminal interactions mediate the quaternary dynamics of αB-crystallin.NMR spectroscopy of 14-3-3ζ reveals a flexible C-terminal extension: differentiation of the chaperone and phosphoserine-binding activities of 14-3-3ζ.The functional roles of the unstructured N- and C-terminal regions in αB-crystallin and other mammalian small heat-shock proteins.
P2860

Site-directed mutations in the C-terminal extension of human alphaB-crystallin affect chaperone function and block amyloid fibril formation

Item
http://www.wikidata.org/entity/Q33302904
description
2007 nî lūn-bûn
@nan
2007 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2007年の論文
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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
Site-directed mutations in the ...... block amyloid fibril formation
@ast
Site-directed mutations in the ...... block amyloid fibril formation
@en
Site-directed mutations in the ...... lock amyloid fibril formation.
@nl
type
label
Site-directed mutations in the ...... block amyloid fibril formation
@ast
Site-directed mutations in the ...... block amyloid fibril formation
@en
Site-directed mutations in the ...... lock amyloid fibril formation.
@nl
prefLabel
Site-directed mutations in the ...... block amyloid fibril formation
@ast
Site-directed mutations in the ...... block amyloid fibril formation
@en
Site-directed mutations in the ...... lock amyloid fibril formation.
@nl
P1433
P1476
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Site-directed mutations in the ...... block amyloid fibril formation
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10.1371/JOURNAL.PONE.0001046
P407
P433
P478
P50
P577
P5875
P698
P921
P932