Multiple molecular architectures of the eye lens chaperone B-crystallin elucidated by a triple hybrid approach
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Binding determinants of the small heat shock protein, αB-crystallin: recognition of the 'IxI' motifAlternative bacterial two-component small heat shock protein systemsStructural basis for microtubule recognition by the human kinetochore Ska complexFunctions of crystallins in and out of lens: roles in elongated and post-mitotic cellsTryptophan and Non-Tryptophan Fluorescence of the Eye Lens Proteins Provides Diagnostics of Cataract at the Molecular LevelIn Vitro Structural and Functional Characterization of the Small Heat Shock Proteins (sHSP) of the Cyanophage S-ShM2 and Its Host, Synechococcus sp. WH7803Crystallin-αB regulates skeletal muscle homeostasis via modulation of argonaute2 activity.A Mechanism of Subunit Recruitment in Human Small Heat Shock Protein OligomersThe novel αB-crystallin (CRYAB) mutation p.D109G causes restrictive cardiomyopathy.Characterization and expression of genes encoding three small heat shock proteins in Sesamia inferens (Lepidoptera: Noctuidae).Analysis of the dominant effects mediated by wild type or R120G mutant of αB-crystallin (HspB5) towards Hsp27 (HspB1)A first line of stress defense: small heat shock proteins and their function in protein homeostasis.A conserved histidine modulates HSPB5 structure to trigger chaperone activity in response to stress-related acidosisA novel molecular dynamics approach to evaluate the effect of phosphorylation on multimeric protein interface: the αB-Crystallin case study.The mitosis and neurodevelopment proteins NDE1 and NDEL1 form dimers, tetramers, and polymers with a folded back structure in solution.Effect of N-terminal region of nuclear Drosophila melanogaster small heat shock protein DmHsp27 on function and quaternary structure.Evolution of crystallins for a role in the vertebrate eye lens.Phenotype of cardiomyopathy in cardiac-specific heat shock protein B8 K141N transgenic mouse.High-Density Peptide Microarray Analysis of IgG Autoantibody Reactivities in Serum and Cerebrospinal Fluid of Multiple Sclerosis Patients.Regulated structural transitions unleash the chaperone activity of αB-crystallinFive small heat shock protein genes from Chilo suppressalis: characteristics of gene, genomic organization, structural analysis, and transcription profiles.One size does not fit all: the oligomeric states of αB crystallin.A novel dominant D109A CRYAB mutation in a family with myofibrillar myopathy affects αB-crystallin structure.Small heat-shock proteins: important players in regulating cellular proteostasis.Medical implications of understanding the functions of human small heat shock proteins.Regulation of αA- and αB-crystallins via phosphorylation in cellular homeostasis.Regulating levels of the neuromodulator d-serine in human brain: structural insight into pLG72 and d-amino acid oxidase interaction.A Study into the Collision-induced Dissociation (CID) Behavior of Cross-Linked Peptides.C-terminal interactions mediate the quaternary dynamics of αB-crystallin.Hydrodynamic modelling of protein conformation in solution: ELLIPS and HYDRO.Structure of the α-crystallin domain from the redox-sensitive chaperone, HSPB1.Oligomer-dependent and -independent chaperone activity of sHsps in different stressed conditions.The small heat shock protein Hsp27 affects assembly dynamics and structure of keratin intermediate filament networks.BAG3 Is a Modular, Scaffolding Protein that physically Links Heat Shock Protein 70 (Hsp70) to the Small Heat Shock Proteins.An alternative splice variant of human αA-crystallin modulates the oligomer ensemble and the chaperone activity of α-crystallins.Molecular cloning, bioinformatics analysis, and expression of small heat shock protein beta-1 from Camelus dromedarius, Arabian camel.The role of αB-crystallin in skeletal and cardiac muscle tissues.Chronic fatigue and immune deficiency syndrome (CFIDS), cellular metabolism, and ionizing radiation: a review of contemporary scientific literature and suggested directions for future research.The chaperone αB-crystallin uses different interfaces to capture an amorphous and an amyloid client.Co-chaperoning by amyloid-forming proteins: cystatins vs. crystallins.
P2860
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P2860
Multiple molecular architectures of the eye lens chaperone B-crystallin elucidated by a triple hybrid approach
description
2011 nî lūn-bûn
@nan
2011 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Multiple molecular architectur ...... ed by a triple hybrid approach
@ast
Multiple molecular architectur ...... ed by a triple hybrid approach
@en
Multiple molecular architectur ...... ed by a triple hybrid approach
@nl
type
label
Multiple molecular architectur ...... ed by a triple hybrid approach
@ast
Multiple molecular architectur ...... ed by a triple hybrid approach
@en
Multiple molecular architectur ...... ed by a triple hybrid approach
@nl
prefLabel
Multiple molecular architectur ...... ed by a triple hybrid approach
@ast
Multiple molecular architectur ...... ed by a triple hybrid approach
@en
Multiple molecular architectur ...... ed by a triple hybrid approach
@nl
P2093
P2860
P50
P921
P3181
P356
P1476
Multiple molecular architectur ...... ed by a triple hybrid approach
@en
P2093
Andreas Kastenmüller
Johannes Buchner
Marianne Hanzlik
Martin Haslbeck
Nathalie Braun
Sevil Weinkauf
P2860
P304
P3181
P356
10.1073/PNAS.1111014108
P407
P577
2011-12-20T00:00:00Z