GroEL/GroES: structure and function of a two-stroke folding machine.
about
The morph server: a standardized system for analyzing and visualizing macromolecular motions in a database framework.Dynamics, flexibility, and allostery in molecular chaperoninsConstructing fluorogenic Bacillus spores (F-spores) via hydrophobic decoration of coat proteinsChaperonin structure: the large multi-subunit protein complex.The archaeal molecular chaperone machine: peculiarities and paradoxesConditionally and transiently disordered proteins: awakening cryptic disorder to regulate protein function.A New Method for Coarse-Grained Elastic Normal-Mode Analysis.Coupling between allosteric transitions in GroEL and assisted folding of a substrate protein.Chaperone-assisted folding of newly synthesized proteins in the cytosol.Caging helps proteins foldWeak intra-ring allosteric communications of the archaeal chaperonin thermosome revealed by normal mode analysisDetermination of network of residues that regulate allostery in protein families using sequence analysis.Identifying natural substrates for chaperonins using a sequence-based approach.Kinetic model for the coupling between allosteric transitions in GroEL and substrate protein folding and aggregation.Setting the chaperonin timer: a two-stroke, two-speed, protein machine.Setting the chaperonin timer: the effects of K+ and substrate protein on ATP hydrolysis.Functional studies of N-terminally modified CYP2J2 epoxygenase in model lipid bilayersStructure and mechanism of protein stability sensors: chaperone activity of small heat shock proteins.Chaperonin 60: a paradoxical, evolutionarily conserved protein family with multiple moonlighting functions.The evolution of the heat-shock protein GroEL from Buchnera, the primary endosymbiont of aphids, is governed by positive selection.Hypothesis: The unfolding power of protein dielectricity.Efficient generation of feasible pathways for protein conformational transitions.Cryo-EM structure of dodecameric Vps4p and its 2:1 complex with Vta1p.Rigid-cluster models of conformational transitions in macromolecular machines and assembliesDesign of an optical switch for studying conformational dynamics in individual molecules of GroEL.High hydrostatic pressure can probe the effects of functionally related ligands on the quaternary structures of the chaperonins GroEL and GroES.Propionic acidemia: analysis of mutant propionyl-CoA carboxylase enzymes expressed in Escherichia coli.Response of heat-shock protein (HSP) genes to temperature and salinity stress in the antarctic psychrotrophic bacterium Psychrobacter sp. G.Expression and genomic organization of the zebrafish chaperonin gene complex.Application of a chaperone-based refolding method to two- and three-dimensional off-lattice protein models.Cryoelectron microscopy and EPR analysis of engineered symmetric and polydisperse Hsp16.5 assemblies reveals determinants of polydispersity and substrate binding.Effect of γ-irradiation on gene expression of heat shock proteins in the foodborne pathogen Escherichia coli O157:H7.Towards functional orthogonalisation of protein complexes: individualisation of GroEL monomers leads to distinct quasihomogeneous single rings.Chloroplast β chaperonins from A. thaliana function with endogenous cpn10 homologs in vitro.
P2860
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P2860
GroEL/GroES: structure and function of a two-stroke folding machine.
description
1998 nî lūn-bûn
@nan
1998 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
GroEL/GroES: structure and function of a two-stroke folding machine.
@ast
GroEL/GroES: structure and function of a two-stroke folding machine.
@en
GroEL/GroES: structure and function of a two-stroke folding machine.
@nl
type
label
GroEL/GroES: structure and function of a two-stroke folding machine.
@ast
GroEL/GroES: structure and function of a two-stroke folding machine.
@en
GroEL/GroES: structure and function of a two-stroke folding machine.
@nl
prefLabel
GroEL/GroES: structure and function of a two-stroke folding machine.
@ast
GroEL/GroES: structure and function of a two-stroke folding machine.
@en
GroEL/GroES: structure and function of a two-stroke folding machine.
@nl
P356
P1476
GroEL/GroES: structure and function of a two-stroke folding machine.
@en
P304
P356
10.1006/JSBI.1998.4060
P577
1998-12-01T00:00:00Z