The effect of small molecules in modulating the chaperone activity of alphaB-crystallin against ordered and disordered protein aggregation.
about
Advanced protein formulationsThe structured core domain of B-crystallin can prevent amyloid fibrillation and associated toxicityQuantification of anti-aggregation activity of chaperones: a test-system based on dithiothreitol-induced aggregation of bovine serum albuminThe interaction of unfolding α-lactalbumin and malate dehydrogenase with the molecular chaperone αB-crystallin: a light and X-ray scattering investigation.Changes in αB-crystallin, tubulin, and MHC isoforms by hindlimb unloading show different expression patterns in various hindlimb muscles.Binding of the molecular chaperone αB-crystallin to Aβ amyloid fibrils inhibits fibril elongationαB-crystallin, an effector of unfolded protein response, confers anti-VEGF resistance to breast cancer via maintenance of intracrine VEGF in endothelial cells.Monitoring the interaction between β2-microglobulin and the molecular chaperone αB-crystallin by NMR and mass spectrometry: αB-crystallin dissociates β2-microglobulin oligomers.alpha-Synuclein: a therapeutic target for Parkinson's disease?Structure/function studies of dogfish alpha-crystallin, comparison with bovine alpha-crystallin.Heat-shock proteins in clinical neurology.Chaperone potential of Pulicaria undulata extract in preventing aggregation of stressed proteins.Functional Amyloid Protection in the Eye Lens: Retention of α-Crystallin Molecular Chaperone Activity after Modification into Amyloid Fibrils.Effect of αB-crystallin on protein aggregation in Drosophila.NMR spectroscopy of 14-3-3ζ reveals a flexible C-terminal extension: differentiation of the chaperone and phosphoserine-binding activities of 14-3-3ζ.Glutamic acid residues in the C-terminal extension of small heat shock protein 25 are critical for structural and functional integrity.The influence of the N-terminal region proximal to the core domain on the assembly and chaperone activity of αB-crystallin.
P2860
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P2860
The effect of small molecules in modulating the chaperone activity of alphaB-crystallin against ordered and disordered protein aggregation.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年学术文章
@wuu
2008年学术文章
@zh
2008年学术文章
@zh-cn
2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
@zh-sg
2008年學術文章
@yue
2008年學術文章
@zh-hant
name
The effect of small molecules ...... isordered protein aggregation.
@en
The effect of small molecules ...... isordered protein aggregation.
@nl
type
label
The effect of small molecules ...... isordered protein aggregation.
@en
The effect of small molecules ...... isordered protein aggregation.
@nl
prefLabel
The effect of small molecules ...... isordered protein aggregation.
@en
The effect of small molecules ...... isordered protein aggregation.
@nl
P2860
P1433
P1476
The effect of small molecules ...... isordered protein aggregation.
@en
P2860
P304
P356
10.1111/J.1742-4658.2008.06257.X
P407
P577
2008-01-23T00:00:00Z