GroEL stimulates protein folding through forced unfolding.
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Chaperonin chamber accelerates protein folding through passive action of preventing aggregationEngineering and Evolution of Molecular Chaperones and Protein Disaggregases with Enhanced ActivityChaperone machines for protein folding, unfolding and disaggregationConformational sampling and nucleotide-dependent transitions of the GroEL subunit probed by unbiased molecular dynamics simulationsATP-Triggered Conformational Changes Delineate Substrate-Binding and -Folding Mechanics of the GroEL ChaperoninVisualizing GroEL/ES in the Act of Encapsulating a Folding ProteinGroEL/ES Chaperonin Modulates the Mechanism and Accelerates the Rate of TIM-Barrel Domain FoldingDynamics, flexibility, and allostery in molecular chaperoninsProteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasisRevealing the functions of the transketolase enzyme isoforms in Rhodopseudomonas palustris using a systems biology approachIntrinsic unfoldase/foldase activity of the chaperonin GroEL directly demonstrated using multinuclear relaxation-based NMR.Novel insights into protein misfolding diseases revealed by ion mobility-mass spectrometry.FoldEco: a model for proteostasis in E. coli.GroEL dependency affects codon usage--support for a critical role of misfolding in gene evolution.Differential protein acetylation assists import of excess SOD2 into mitochondria and mediates SOD2 aggregation associated with cardiac hypertrophy in the murine SOD2-tg heart.GroEL actively stimulates folding of the endogenous substrate protein PepQSingle-molecule spectroscopy of protein folding in a chaperonin cage.Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins.The C-terminal tails of the bacterial chaperonin GroEL stimulate protein folding by directly altering the conformation of a substrate proteinProtein folding in the cytoplasm and the heat shock response.Protein folding in the cell: challenges and progress.A hypothesis for bacteriophage DNA packaging motors.The DNA methylation-regulated miR-193a-3p dictates the multi-chemoresistance of bladder cancer via repression of SRSF2/PLAU/HIC2 expressionEngineering a nanopore with co-chaperonin function.Multiplex H. pylori Serology and Risk of Gastric Cardia and Noncardia Adenocarcinomas.GroEL and CCT are catalytic unfoldases mediating out-of-cage polypeptide refolding without ATPSetting the chaperonin timer: a two-stroke, two-speed, protein machine.Setting the chaperonin timer: the effects of K+ and substrate protein on ATP hydrolysis.Requirement for binding multiple ATPs to convert a GroEL ring to the folding-active state.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.Symmetric GroEL:GroES2 complexes are the protein-folding functional form of the chaperonin nanomachineGroEL/GroES cycling: ATP binds to an open ring before substrate protein favoring protein binding and production of the native state.Molecular chaperones and proteostasis regulation during redox imbalance.Chromatin density and splicing destiny: on the cross-talk between chromatin structure and splicing.Integrating protein homeostasis strategies in prokaryotes.Molecular chaperones as enzymes that catalytically unfold misfolded polypeptides.ATP-driven molecular chaperone machines.How do chaperonins fold protein?The transcriptional co-activator SND1 is a novel regulator of alternative splicing in prostate cancer cells.
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GroEL stimulates protein folding through forced unfolding.
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article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 02 March 2008
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
GroEL stimulates protein folding through forced unfolding.
@en
GroEL stimulates protein folding through forced unfolding.
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type
label
GroEL stimulates protein folding through forced unfolding.
@en
GroEL stimulates protein folding through forced unfolding.
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prefLabel
GroEL stimulates protein folding through forced unfolding.
@en
GroEL stimulates protein folding through forced unfolding.
@nl
P2093
P2860
P356
P1476
GroEL stimulates protein folding through forced unfolding.
@en
P2093
Damian Madan
Hays S Rye
P2860
P2888
P304
P356
10.1038/NSMB.1394
P577
2008-03-02T00:00:00Z