about
Fibrillogenic propensity of the GroEL apical domain: a Janus-faced minichaperoneChaperonin chamber accelerates protein folding through passive action of preventing aggregationDynamics, flexibility and ligand-induced conformational changes in biological macromolecules: a computational approachConformational sampling and nucleotide-dependent transitions of the GroEL subunit probed by unbiased molecular dynamics simulationsUse of thallium to identify monovalent cation binding sites in GroELCrystal Structures of a Group II Chaperonin Reveal the Open and Closed States Associated with the Protein Folding CycleStructural Analysis of Protein Folding by the Long-Chain Archaeal Chaperone FKBP26Mechanism of nucleotide sensing in group II chaperoninsDynamic Complexes in the Chaperonin-Mediated Protein Folding CycleDynamics, flexibility, and allostery in molecular chaperoninsDisulfide formation as a probe of folding in GroEL-GroES reveals correct formation of long-range bonds and editing of incorrect short-range ones.Dynamics of allosteric transitions in GroEL.FoldEco: a model for proteostasis in E. coli.Bacterial proteostasis balances energy and chaperone utilization efficientlyMyxococcus xanthus DK1622 Coordinates Expressions of the Duplicate groEL and Single groES Genes for Synergistic Functions of GroELs and GroESA zinc-binding site by negative selection induces metallodrug susceptibility in an essential chaperonin.Structure of the human TRiC/CCT Subunit 5 associated with hereditary sensory neuropathy.Identification of S-nitrosylation of proteins of Helicobacter pylori in response to nitric oxide stress.Single-molecule spectroscopy of protein folding in a chaperonin cage.Probing the functional mechanism of Escherichia coli GroEL using circular permutation.Action of the chaperonin GroEL/ES on a non-native substrate observed with single-molecule FRET.Identification of elements that dictate the specificity of mitochondrial Hsp60 for its co-chaperonin.Sequencing and de novo assembly of the western tarnished plant bug (Lygus hesperus) transcriptome.Role of denatured-state properties in chaperonin action probed by single-molecule spectroscopyNitrogen recycling and nutritional provisioning by Blattabacterium, the cockroach endosymbiontGlobal aggregation of newly translated proteins in an Escherichia coli strain deficient of the chaperonin GroEL.Stimulating the substrate folding activity of a single ring GroEL variant by modulating the cochaperonin GroES.Management of cytoskeleton architecture by molecular chaperones and immunophilins.Nuclear magnetic resonance spectroscopy with the stringent substrate rhodanese bound to the single-ring variant SR1 of the E. coli chaperonin GroEL.Crystal structure of the human mitochondrial chaperonin symmetrical football complex.Football- and bullet-shaped GroEL-GroES complexes coexist during the reaction cycle.Perturbed ATPase activity and not "close confinement" of substrate in the cis cavity affects rates of folding by tail-multiplied GroEL.Coupling between allosteric transitions in GroEL and assisted folding of a substrate protein.Essential function of the built-in lid in the allosteric regulation of eukaryotic and archaeal chaperonins.Spontaneous conformational changes in the E. coli GroEL subunit from all-atom molecular dynamics simulations.Weak intra-ring allosteric communications of the archaeal chaperonin thermosome revealed by normal mode analysisHsp33 controls elongation factor-Tu stability and allows Escherichia coli growth in the absence of the major DnaK and trigger factor chaperonesDo chaperonins boost protein yields by accelerating folding or preventing aggregation?A gradient of ATP affinities generates an asymmetric power stroke driving the chaperonin TRIC/CCT folding cycle.Nucleotide-induced conformational changes of tetradecameric GroEL mapped by H/D exchange monitored by FT-ICR mass spectrometry
P2860
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P2860
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年学术文章
@wuu
2006年学术文章
@zh-cn
2006年学术文章
@zh-hans
2006年学术文章
@zh-my
2006年学术文章
@zh-sg
2006年學術文章
@yue
2006年學術文章
@zh
2006年學術文章
@zh-hant
name
GroEL-GroES-mediated protein folding.
@ast
GroEL-GroES-mediated protein folding.
@en
type
label
GroEL-GroES-mediated protein folding.
@ast
GroEL-GroES-mediated protein folding.
@en
prefLabel
GroEL-GroES-mediated protein folding.
@ast
GroEL-GroES-mediated protein folding.
@en
P356
P1433
P1476
GroEL-GroES-mediated protein folding.
@en
P2093
George W Farr
Wayne A Fenton
P304
P356
10.1021/CR040435V
P577
2006-05-01T00:00:00Z