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

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

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

http://www.wikidata.org/entity/Q27667422

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Binding determinants of the small heat shock protein, αB-crystallin: recognition of the 'IxI' motif Multiple molecular architectures of the eye lens chaperone B-crystallin elucidated by a triple hybrid approach Atomic View of a Toxic Amyloid Small Oligomer Crystal Structure of an Activated Variant of Small Heat Shock Protein Hsp16.5 Characterization of Mutants of Human Small Heat Shock Protein HspB1 Carrying Replacements in the N-Terminal Domain and Associated with Hereditary Motor Neuron Diseases Functions of crystallins in and out of lens: roles in elongated and post-mitotic cells A hierarchical algorithm for fast Debye summation with applications to small angle scattering Rapid prediction of multi-dimensional NMR data sets.Massive expansion and differential evolution of small heat shock proteins with wheat (Triticum aestivum L.) polyploidization.The small heat shock protein p26 aids development of encysting Artemia embryos, prevents spontaneous diapause termination and protects against stress.Kinetic evidence against partitioning of the ubiquinone pool and the catalytic relevance of respiratory-chain supercomplexes.A Mechanism of Subunit Recruitment in Human Small Heat Shock Protein Oligomers A first line of stress defense: small heat shock proteins and their function in protein homeostasis.Dissecting the functional role of the N-terminal domain of the human small heat shock protein HSPB6.Tobacco class I cytosolic small heat shock proteins are under transcriptional and translational regulations in expression and heterocomplex prevails under the high-temperature stress condition in vitro.A conserved histidine modulates HSPB5 structure to trigger chaperone activity in response to stress-related acidosis Heterooligomeric complexes of human small heat shock proteins Sequence, structure, and dynamic determinants of Hsp27 (HspB1) equilibrium dissociation are encoded by the N-terminal domain.Small heat shock proteins and α-crystallins: dynamic proteins with flexible functions.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.Pharmacoinformatic and molecular docking studies reveal potential novel antidepressants against neurodegenerative disorders by targeting HSPB8.New insight into the dynamical system of αB-crystallin oligomers.Regulated structural transitions unleash the chaperone activity of αB-crystallin αB-crystallin: Portrait of a malignant chaperone as a cancer therapeutic target 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.Species-Specific Structural and Functional Divergence of α-Crystallins: Zebrafish αBa- and Rodent αA(ins)-Crystallin Encode Activated Chaperones Large potentials of small heat shock proteins.The protective and therapeutic function of small heat shock proteins in neurological diseases.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.Hierarchical O(N) computation of small-angle scattering profiles and their associated derivatives.Structure and properties of chimeric small heat shock proteins containing yellow fluorescent protein attached to their C-terminal ends.C-terminal interactions mediate the quaternary dynamics of αB-crystallin.Structural and mechanistic implications of metal binding in the small heat-shock protein αB-crystallin Structure of the α-crystallin domain from the redox-sensitive chaperone, HSPB1.Monomeric 14-3-3ζ has a chaperone-like activity and is stabilized by phosphorylated HspB6.Plantation forestry under global warming: hybrid poplars with improved thermotolerance provide new insights on the in vivo function of small heat shock protein chaperones.

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

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N-terminal domain of B-crysta ...... n and structural heterogeneity

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N-terminal domain of B-crysta ...... n and structural heterogeneity

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N-terminal domain of B-crysta ...... n and structural heterogeneity

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N-terminal domain of B-crysta ...... n and structural heterogeneity

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N-terminal domain of B-crysta ...... n and structural heterogeneity

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N-terminal domain of B-crysta ...... n and structural heterogeneity

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N-terminal domain of B-crysta ...... n and structural heterogeneity

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N-terminal domain of B-crysta ...... n and structural heterogeneity

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

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N-terminal domain of B-crysta ...... n and structural heterogeneity

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Breanna S Vollmar

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Katja K Dove

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Ponni Rajagopal

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Rachel E Klevit

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Tamir Gonen

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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

Shotgun identification of protein modifications from protein complexes and lens tissue

TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts

Crystal structure and assembly of a eukaryotic small heat shock protein

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 a small heat-shock protein

SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields

Molecular chaperones and protein quality control

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10.1073/PNAS.1014656108

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16

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108

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Hartmut Oschkinat

Benjamin Bardiaux

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2011-04-19T00:00:00Z

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50999541

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21464278

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identical protein binding

Crystallin alpha B

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3081008

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