Multiple molecular architectures of the eye lens chaperone B-crystallin elucidated by a triple hybrid approach - Test2 - elhamkhani - TriplyDB

Multiple molecular architectures of the eye lens chaperone B-crystallin elucidated by a triple hybrid approach

Multiple molecular architectures of the eye lens chaperone B-crystallin elucidated by a triple hybrid approach

http://www.wikidata.org/entity/Q27675996

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Binding determinants of the small heat shock protein, αB-crystallin: recognition of the 'IxI' motif Alternative bacterial two-component small heat shock protein systems Structural basis for microtubule recognition by the human kinetochore Ska complex Functions of crystallins in and out of lens: roles in elongated and post-mitotic cells Tryptophan and Non-Tryptophan Fluorescence of the Eye Lens Proteins Provides Diagnostics of Cataract at the Molecular Level In Vitro Structural and Functional Characterization of the Small Heat Shock Proteins (sHSP) of the Cyanophage S-ShM2 and Its Host, Synechococcus sp. WH7803 Crystallin-αB regulates skeletal muscle homeostasis via modulation of argonaute2 activity.A Mechanism of Subunit Recruitment in Human Small Heat Shock Protein Oligomers The 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 acidosis A 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-crystallin Five 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.

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Multiple molecular architectures of the eye lens chaperone B-crystallin elucidated by a triple hybrid approach

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Proceedings of the National Academy of Sciences of the United States of America

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Multiple molecular architectur ...... ed by a triple hybrid approach

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Andreas Kastenmüller

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Johannes Buchner

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Juan Zou

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Marianne Hanzlik

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Martin Haslbeck

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Nathalie Braun

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Sevil Weinkauf

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P2860

A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy

Crystal structures of alpha-crystallin domain dimers of alphaB-crystallin and Hsp20

Crystal structures of truncated alphaA and alphaB crystallins reveal structural mechanisms of polydispersity important for eye lens function

Solid-state NMR and SAXS studies provide a structural basis for the activation of αB-crystallin oligomers

Crystal Structure of R120G Disease Mutant of Human αB-Crystallin Domain Dimer Shows Closure of a Groove

N-terminal domain of B-crystallin provides a conformational switch for multimerization and structural heterogeneity

Crystal structure of a small heat-shock protein

EMAN: semiautomated software for high-resolution single-particle reconstructions

Size-Distribution Analysis of Macromolecules by Sedimentation Velocity Ultracentrifugation and Lamm Equation Modeling

Architecture of the RNA polymerase II-TFIIF complex revealed by cross-linking and mass spectrometry.

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10.1073/PNAS.1111014108

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51

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108

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Juri Rappsilber

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2011-12-20T00:00:00Z

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51854821

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identical protein binding

Crystallin alpha B

molecular chaperones

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