Folding pattern of the alpha-crystallin domain in alphaA-crystallin determined by site-directed spin labeling.
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Detection of protein-protein interactions among lens crystallins in a mammalian two-hybrid system assayCell death triggered by a novel mutation in the alphaA-crystallin gene underlies autosomal dominant cataract linked to chromosome 21qDomain interaction sites of human lens betaB2-crystallinProtein-protein interactions among human lens acidic and basic beta-crystallinsCrystallin gene mutations in Indian families with inherited pediatric cataractSolid-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 Hsp16.5In vivo substrates of the lens molecular chaperones αA-crystallin and αB-crystallinCalculation of rigid-body conformational changes using restraint-driven Cartesian transformationsAccessibility and dynamics of nitroxide side chains in T4 lysozyme measured by saturation recovery EPR.De novo high-resolution protein structure determination from sparse spin-labeling EPR data.BCL::MP-fold: Membrane protein structure prediction guided by EPR restraintsAlgorithm for selection of optimized EPR distance restraints for de novo protein structure determinationThree-dimensional architecture of membrane-embedded MscS in the closed conformationRole of alphaBI5 and alphaBT162 residues in subunit interaction during oligomerization of alphaB-crystallin.Detection and architecture of small heat shock protein monomers.Alpha-crystallin-type heat shock proteins: socializing minichaperones in the context of a multichaperone network.Characterization of O-phosphohydroxyproline in rat {alpha}-crystallin A.The function of the beta3 interactive domain in the small heat shock protein and molecular chaperone, human alphaB crystallinFunctional insights by comparison of modeled structures of 18kDa small heat shock protein and its mutant in Mycobacterium lepraeSequence, structure, and dynamic determinants of Hsp27 (HspB1) equilibrium dissociation are encoded by the N-terminal domain.Inter- and intra-molecular distances determined by EPR spectroscopy and site-directed spin labeling reveal protein-protein and protein-oligonucleotide interaction.Cryoelectron microscopy analysis of small heat shock protein 16.5 (Hsp16.5) complexes with T4 lysozyme reveals the structural basis of multimode bindingProtein-protein interactions involving congenital cataract T5P gammaC-crystallin mutant: a confocal fluorescence microscopy study.alphaB-crystallin: a hybrid solid-state/solution-state NMR investigation reveals structural aspects of the heterogeneous oligomer.Structure 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 ChaperonesInteraction of mammalian Hsp22 with lipid membranes.Characteristics of super alphaA-crystallin, a product of in vitro exon shuffling.The lack of chaperonelike activity of Caenorhabditis elegans Hsp12.2 cannot be restored by domain swapping with human alphaB-crystallin.Insights into the domains required for dimerization and assembly of human alphaB crystallin.Mammalian Hsp22 is a heat-inducible small heat-shock protein with chaperone-like activity.The reaction of alpha-crystallin with the cross-linker 3,3'-dithiobis(sulfosuccinimidyl propionate) demonstrates close proximity of the C termini of alphaA and alphaB in the native assembly.Subunit exchange, conformational stability, and chaperone-like function of the small heat shock protein 16.5 from Methanococcus jannaschii.A critical motif for oligomerization and chaperone activity of bacterial alpha-heat shock proteins.Dap-SL: a new site-directed nitroxide spin labeling approach for determining structure and motions in synthesized peptides and proteins.Mechanism of chaperone function in small heat-shock proteins. Phosphorylation-induced activation of two-mode binding in alphaB-crystallin.Effect of a Paramagnetic Spin Label on the Intrinsically Disordered Peptide Ensemble of Amyloid-β.Cryoelectron microscopy and EPR analysis of engineered symmetric and polydisperse Hsp16.5 assemblies reveals determinants of polydispersity and substrate binding.Functional analysis of a small heat shock/alpha-crystallin protein from Artemia franciscana. Oligomerization and thermotolerance.
P2860
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P2860
Folding pattern of the alpha-crystallin domain in alphaA-crystallin determined by site-directed spin labeling.
description
1999 nî lūn-bûn
@nan
1999 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Folding pattern of the alpha-c ...... y site-directed spin labeling.
@ast
Folding pattern of the alpha-c ...... y site-directed spin labeling.
@en
type
label
Folding pattern of the alpha-c ...... y site-directed spin labeling.
@ast
Folding pattern of the alpha-c ...... y site-directed spin labeling.
@en
prefLabel
Folding pattern of the alpha-c ...... y site-directed spin labeling.
@ast
Folding pattern of the alpha-c ...... y site-directed spin labeling.
@en
P356
P1476
Folding pattern of the alpha-c ...... y site-directed spin labeling.
@en
P2093
Koteiche HA
Mchaourab HS
P304
P356
10.1006/JMBI.1999.3242
P407
P577
1999-11-01T00:00:00Z