On the maximum size of proteins to stay and fold in the cavity of GroEL underneath GroES.
about
Chaperonin GroEL uses asymmetric and symmetric reaction cycles in response to the concentration of non-native substrate proteinsMultiple chaperonins in bacteria--novel functions and non-canonical behaviorsIdentification of novel in vivo obligate GroEL/ES substrates based on data from a cell-free proteomics approach.Substrate-induced gene-expression screening of environmental metagenome libraries for isolation of catabolic genes.Stress genes and proteins in the archaea.Side effects of chaperone gene co-expression in recombinant protein production.Cytosolic chaperonin protects folding intermediates of Gbeta from aggregation by recognizing hydrophobic beta-strandsCo-production of GroELS discriminates between intrinsic and thermally-induced recombinant protein aggregation during substrate quality control.Concerted ATP-induced allosteric transitions in GroEL facilitate release of protein substrate domains in an all-or-none manner.Global analysis of chaperone effects using a reconstituted cell-free translation system.Functional bacteriorhodopsin is efficiently solubilized and delivered to membranes by the chaperonin GroELBacterial expression strategies for several Sus scrofa diacylglycerol kinase alpha constructs: solubility challenges.Molecular clamp mechanism of substrate binding by hydrophobic coiled-coil residues of the archaeal chaperone prefoldin.A systematic survey of in vivo obligate chaperonin-dependent substrates.Effect of the C-terminal truncation on the functional cycle of chaperonin GroEL: implication that the C-terminal region facilitates the transition from the folding-arrested to the folding-competent state.Revisiting the GroEL-GroES reaction cycle via the symmetric intermediate implied by novel aspects of the GroEL(D398A) mutant.Single-molecule observation of protein folding in symmetric GroEL-(GroES)2 complexes.Filamentous morphology in GroE-depleted Escherichia coli induced by impaired folding of FtsE.Facilitated oligomerization of mycobacterial GroEL: evidence for phosphorylation-mediated oligomerization.The 28.3 kDa FK506 binding protein from a thermophilic archaeum, Methanobacterium thermoautotrophicum, protects the denaturation of proteins in vitro.Trigger factor from Thermus thermophilus is a Zn2+-dependent chaperone.Nucleotide specificity of an archaeal group II chaperonin from Thermococcus strain KS-1 with reference to the ATP-dependent protein folding cycle.Encapsulation of an 86-kDa assembly intermediate inside the cavities of GroEL and its single-ring variant SR1 by GroES.Role of the helical protrusion in the conformational change and molecular chaperone activity of the archaeal group II chaperonin.BeF(x) stops the chaperonin cycle of GroEL-GroES and generates a complex with double folding chambers.Facilitated release of substrate protein from prefoldin by chaperonin.Determination of the number of active GroES subunits in the fused heptamer GroES required for interactions with GroEL.Characterization of archaeal group II chaperonin-ADP-metal fluoride complexes: implications that group II chaperonins operate as a "two-stroke engine".Hydrophilic residues 526 KNDAAD 531 in the flexible C-terminal region of the chaperonin GroEL are critical for substrate protein folding within the central cavity.Kinetics and binding sites for interaction of the prefoldin with a group II chaperonin: contiguous non-native substrate and chaperonin binding sites in the archaeal prefoldin.Protein Catenation Enhances Both the Stability and Activity of Folded Structural Domains.A more precise characterization of chaperonin substrates.GroEL-substrate-GroES ternary complexes are an important transient intermediate of the chaperonin cycle.Partial Occlusion of Both Cavities of the Eukaryotic Chaperonin with Antibody Has No Effect upon the Rates of β-Actin or α-Tubulin Folding
P2860
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P2860
On the maximum size of proteins to stay and fold in the cavity of GroEL underneath GroES.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh-hant
name
On the maximum size of proteins to stay and fold in the cavity of GroEL underneath GroES.
@en
On the maximum size of proteins to stay and fold in the cavity of GroEL underneath GroES.
@nl
type
label
On the maximum size of proteins to stay and fold in the cavity of GroEL underneath GroES.
@en
On the maximum size of proteins to stay and fold in the cavity of GroEL underneath GroES.
@nl
prefLabel
On the maximum size of proteins to stay and fold in the cavity of GroEL underneath GroES.
@en
On the maximum size of proteins to stay and fold in the cavity of GroEL underneath GroES.
@nl
P2093
P2860
P356
P1476
On the maximum size of proteins to stay and fold in the cavity of GroEL underneath GroES.
@en
P2093
P2860
P304
21251-21256
P356
10.1074/JBC.274.30.21251
P407
P577
1999-07-01T00:00:00Z