The small heat-shock protein, alphaB-crystallin, has a variable quaternary structure.
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Structural basis of nucleotide exchange and client binding by the Hsp70 cochaperone Bag2Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens functionSolid-state NMR and SAXS studies provide a structural basis for the activation of αB-crystallin oligomersN-terminal domain of B-crystallin provides a conformational switch for multimerization and structural heterogeneityMultiple molecular architectures of the eye lens chaperone B-crystallin elucidated by a triple hybrid approachCrystal Structure of an Activated Variant of Small Heat Shock Protein Hsp16.5Preferential and Specific Binding of Human αB-Crystallin to a Cataract-Related Variant of γS-CrystallinMyofibrillar myopathiesStudy of the chaperoning mechanism of bovine lens alpha-crystallin, a member of the alpha-small heat shock superfamily.Interactive domains in the molecular chaperone human alphaB crystallin modulate microtubule assembly and disassemblyFunctional similarities between the small heat shock proteins Mycobacterium tuberculosis HSP 16.3 and human alphaB-crystallinalphaB-Crystallin-coated MAP microtubule resists nocodazole and calcium-induced disassemblyNMR-detected brownian dynamics of αB-crystallin over a wide range of concentrations.The cardiomyopathy and lens cataract mutation in alphaB-crystallin alters its protein structure, chaperone activity, and interaction with intermediate filaments in vitro.Oxidative stress-dependent structural and functional switching of a human 2-Cys peroxiredoxin isotype II that enhances HeLa cell resistance to H2O2-induced cell death.Behavioral defects in chaperone-deficient Alzheimer's disease model mice.The eye lens chaperone alpha-crystallin forms defined globular assemblies.Multiscale natural moves refine macromolecules using single-particle electron microscopy projection imagesElectron tomography of fiber cell cytoplasm and dense cores of multilamellar bodies from human age-related nuclear cataracts.Thermally induced injury and heat-shock protein expression in cells and tissues.Role of alphaBI5 and alphaBT162 residues in subunit interaction during oligomerization of alphaB-crystallin.The structure of the cytoplasm of lens fibers as determined by conical tomography.Dynamic subunit exchange and the regulation of microtubule assembly by the stress response protein human alphaB crystallin.The interaction of alphaB-crystallin with mature alpha-synuclein amyloid fibrils inhibits their elongation.Biochemical characterization of the small heat shock protein IbpB from Escherichia coli.A novel quaternary structure of the dimeric alpha-crystallin domain with chaperone-like activity.Alpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network.The three-dimensional distribution of αA-crystalline in rat lenses and its possible relation to transparencyMultiple sites in αB-crystallin modulate its interactions with desmin filaments assembled in vitro.Molecular chaperones--cellular machines for protein folding.Molecular basis for the polymerization of octopus lens S-crystallinThe interaction of unfolding α-lactalbumin and malate dehydrogenase with the molecular chaperone αB-crystallin: a light and X-ray scattering investigation.Functional switching of a novel prokaryotic 2-Cys peroxiredoxin (PpPrx) under oxidative stressFunctional characterization of Xenopus small heat shock protein, Hsp30C: the carboxyl end is required for stability and chaperone activitySequestration of toxic oligomers by HspB1 as a cytoprotective mechanism.Binding of the molecular chaperone αB-crystallin to Aβ amyloid fibrils inhibits fibril elongationThe lens in hereditary hyperferritinaemia cataract syndrome contains crystalline deposits of L-ferritinThree-dimensional structure of low density lipoproteins by electron cryomicroscopyExtensive Charge Reduction and Dissociation of Intact Protein Complexes Following Electron Transfer on a Quadrupole-Ion Mobility-Time-of-Flight MS.Molecular characterization of hsp20, encoding a small heat shock protein of bifidobacterium breve UCC2003
P2860
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P2860
The small heat-shock protein, alphaB-crystallin, has a variable quaternary structure.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
1998年论文
@zh
1998年论文
@zh-cn
name
The small heat-shock protein, alphaB-crystallin, has a variable quaternary structure.
@en
type
label
The small heat-shock protein, alphaB-crystallin, has a variable quaternary structure.
@en
prefLabel
The small heat-shock protein, alphaB-crystallin, has a variable quaternary structure.
@en
P2093
P356
P1476
The small heat-shock protein, alphaB-crystallin, has a variable quaternary structure.
@en
P2093
P356
10.1006/JMBI.1997.1611
P407
P577
1998-03-01T00:00:00Z