GroEL-mediated protein folding: making the impossible, possible.
about
Fibrillogenic propensity of the GroEL apical domain: a Janus-faced minichaperoneMacromolecule-assisted de novo protein foldingVisualizing GroEL/ES in the Act of Encapsulating a Folding ProteinCrystal structure of a GroEL-ADP complex in the relaxed allosteric state at 2.7 A resolutionIntrinsic unfoldase/foldase activity of the chaperonin GroEL directly demonstrated using multinuclear relaxation-based NMR.Protein folding at single-molecule resolution.Legionella pneumophila requires polyamines for optimal intracellular growth.Fitting low-resolution cryo-EM maps of proteins using constrained geometric simulations.GroEL actively stimulates folding of the endogenous substrate protein PepQThe C-terminal tails of the bacterial chaperonin GroEL stimulate protein folding by directly altering the conformation of a substrate proteinAction of the chaperonin GroEL/ES on a non-native substrate observed with single-molecule FRET.Formation and structures of GroEL:GroES2 chaperonin footballs, the protein-folding functional formImmunodetection of the recombinant GroEL by the Nanobody NbBruc02.Archaeal-like chaperonins in bacteria.Mechanisms involved in the functional divergence of duplicated GroEL chaperonins in Myxococcus xanthus DK1622.Coevolution analyses illuminate the dependencies between amino acid sites in the chaperonin system GroES-L.Prolonged fasting identifies heat shock protein 10 as a Sirtuin 3 substrate: elucidating a new mechanism linking mitochondrial protein acetylation to fatty acid oxidation enzyme folding and function.The Legionella pneumophila Chaperonin - An Unusual Multifunctional Protein in Unusual Locations.Stimulating the substrate folding activity of a single ring GroEL variant by modulating the cochaperonin GroES.Functional Subunits of Eukaryotic Chaperonin CCT/TRiC in Protein Folding.Molecular and histological characterization of primary (betaproteobacteria) and secondary (gammaproteobacteria) endosymbionts of three mealybug speciesFolding of newly translated membrane protein CCR5 is assisted by the chaperonin GroEL-GroES.Do chaperonins boost protein yields by accelerating folding or preventing aggregation?Kinetic model for the coupling between allosteric transitions in GroEL and substrate protein folding and aggregation.Tea tree oil-induced transcriptional alterations in Staphylococcus aureusMultiplex H. pylori Serology and Risk of Gastric Cardia and Noncardia Adenocarcinomas.Mitochondrial protein import and human health and disease.Chaperone activation by unfolding.Folding versus aggregation: polypeptide conformations on competing pathwaysSetting the chaperonin timer: a two-stroke, two-speed, protein machine.Setting the chaperonin timer: the effects of K+ and substrate protein on ATP hydrolysis.Kinetic redistribution of native and misfolded RNAs by a DEAD-box chaperone.GroEL stimulates protein folding through forced unfolding.Structural frameworks for considering microbial protein- and nucleic acid-dependent motor ATPases.Development of free-energy-based models for chaperonin containing TCP-1 mediated folding of actin.Repetitive protein unfolding by the trans ring of the GroEL-GroES chaperonin complex stimulates folding.Substrate protein switches GroE chaperonins from asymmetric to symmetric cycling by catalyzing nucleotide exchange.Symmetric GroEL:GroES2 complexes are the protein-folding functional form of the chaperonin nanomachineStructure and mechanism of protein stability sensors: chaperone activity of small heat shock proteins.Chaperones GroEL/GroES accelerate the refolding of a multidomain protein through modulating on-pathway intermediates.
P2860
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P2860
GroEL-mediated protein folding: making the impossible, possible.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
GroEL-mediated protein folding: making the impossible, possible.
@ast
GroEL-mediated protein folding: making the impossible, possible.
@en
type
label
GroEL-mediated protein folding: making the impossible, possible.
@ast
GroEL-mediated protein folding: making the impossible, possible.
@en
prefLabel
GroEL-mediated protein folding: making the impossible, possible.
@ast
GroEL-mediated protein folding: making the impossible, possible.
@en
P2860
P1476
GroEL-mediated protein folding: making the impossible, possible.
@en
P2093
P2860
P304
P356
10.1080/10409230600760382
P577
2006-07-01T00:00:00Z