Mechanism of chaperone function in small heat-shock proteins. Phosphorylation-induced activation of two-mode binding in alphaB-crystallin.
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Cataract-linked γD-crystallin mutants have weak affinity to lens chaperones α-crystallinsTranslocation of human ribosomal protein S3 to sites of DNA damage is dependant on ERK-mediated phosphorylation following genotoxic stressSolid-state NMR and SAXS studies provide a structural basis for the activation of αB-crystallin oligomersCrystal Structure of an Activated Variant of Small Heat Shock Protein Hsp16.5Heat shock proteins and heat shock factor 1 in carcinogenesis and tumor development: an updateDisulfide cross-links in the interaction of a cataract-linked alphaA-crystallin mutant with betaB1-crystallinDistribution of bovine and rabbit lens alpha-crystallin products by MALDI imaging mass spectrometryFree-solution label-free detection of alpha-crystallin chaperone interactions by back-scattering interferometry.Mechanistic differences between two conserved classes of small heat shock proteins found in the plant cytosol.Gene duplication and separation of functions in alphaB-crystallin from zebrafish (Danio rerio).Cystic fibrosis transmembrane conductance regulator degradation: cross-talk between the ubiquitylation and SUMOylation pathways.Heat shock protein 27 phosphorylation state is associated with cancer progression.Activation of PKN mediates survival of cardiac myocytes in the heart during ischemia/reperfusion.Analysis of the dominant effects mediated by wild type or R120G mutant of αB-crystallin (HspB5) towards Hsp27 (HspB1)Pseudophosphorylated αB-crystallin is a nuclear chaperone imported into the nucleus with help of the SMN complexSmall heat-shock proteins select deltaF508-CFTR for endoplasmic reticulum-associated degradation.Sequence, structure, and dynamic determinants of Hsp27 (HspB1) equilibrium dissociation are encoded by the N-terminal domain.A conserved role of αA-crystallin in the development of the zebrafish embryonic lens.Novel roles for α-crystallins in retinal function and disease.Small heat shock proteins target mutant cystic fibrosis transmembrane conductance regulator for degradation via a small ubiquitin-like modifier-dependent pathway.A proteome map of the zebrafish (Danio rerio) lens reveals similarities between zebrafish and mammalian crystallin expressionCryoelectron microscopy analysis of small heat shock protein 16.5 (Hsp16.5) complexes with T4 lysozyme reveals the structural basis of multimode bindingAICAR reduces the collagen-stimulated secretion of PDGF-AB and release of soluble CD40 ligand from human platelets: Suppression of HSP27 phosphorylation via p44/p42 MAP kinase.Regulated structural transitions unleash the chaperone activity of αB-crystallinαB-crystallin: Portrait of a malignant chaperone as a cancer therapeutic targetStructure and mechanism of protein stability sensors: chaperone activity of small heat shock proteins.Species-Specific Structural and Functional Divergence of α-Crystallins: Zebrafish αBa- and Rodent αA(ins)-Crystallin Encode Activated ChaperonesPotential synergy between tau aggregation inhibitors and tau chaperone modulators.Small heat-shock proteins: important players in regulating cellular proteostasis.Regulation of αA- and αB-crystallins via phosphorylation in cellular homeostasis.Mimicking phosphorylation of alphaB-crystallin affects its chaperone activityThe microtubule-associated protein, NUD-1, exhibits chaperone activity in vitro.The molecular chaperone, alpha-crystallin, protects against loss of antigenicity and activity of esterase caused by sugars, sugar phosphate and a steroid.Role of ATP on the interaction of alpha-crystallin with its substrates and its implications for the molecular chaperone function.Expression of Cataract-linked γ-Crystallin Variants in Zebrafish Reveals a Proteostasis Network That Senses Protein Stability.Analysis of HspB1 (Hsp27) Oligomerization and Phosphorylation Patterns and Its Interaction with Specific Client Polypeptides.The effect of small molecules in modulating the chaperone activity of alphaB-crystallin against ordered and disordered protein aggregation.The minimal α-crystallin domain of Mj Hsp16.5 is functional at non-heat-shock conditions.Loss of αB-crystallin function in zebrafish reveals critical roles in the development of the lens and stress resistance of the heart.αB-Crystallin interacts and attenuates the tyrosine phosphatase activity of Shp2 in cardiomyocytes under mechanical stress.
P2860
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P2860
Mechanism of chaperone function in small heat-shock proteins. Phosphorylation-induced activation of two-mode binding in alphaB-crystallin.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
2003年學術文章
@zh-hant
name
Mechanism of chaperone functio ...... binding in alphaB-crystallin.
@en
Mechanism of chaperone functio ...... binding in alphaB-crystallin.
@nl
type
label
Mechanism of chaperone functio ...... binding in alphaB-crystallin.
@en
Mechanism of chaperone functio ...... binding in alphaB-crystallin.
@nl
prefLabel
Mechanism of chaperone functio ...... binding in alphaB-crystallin.
@en
Mechanism of chaperone functio ...... binding in alphaB-crystallin.
@nl
P2860
P356
P1476
Mechanism of chaperone functio ...... binding in alphaB-crystallin.
@en
P2093
Hanane A Koteiche
Hassane S McHaourab
P2860
P304
10361-10367
P356
10.1074/JBC.M211851200
P407
P577
2003-01-14T00:00:00Z