Chaperonin-catalyzed rescue of kinetically trapped states in protein folding.
about
Macromolecule-assisted de novo protein foldingProtein homeostasis at the plasma membraneThe Role of Protein Denaturation Energetics and Molecular Chaperones in the Aggregation and Mistargeting of Mutants Causing Primary Hyperoxaluria Type IStructural Basis for Protein Antiaggregation Activity of the Trigger Factor ChaperoneGroEL/ES Chaperonin Modulates the Mechanism and Accelerates the Rate of TIM-Barrel Domain FoldingMultiple chaperonins in bacteria--novel functions and non-canonical behaviorsFunctional assembly of protein fragments induced by spatial confinementCapturing the mechanical unfolding pathway of a large protein with coiled-coil probes.Protein folding at single-molecule resolution.Counteracting chemical chaperone effects on the single-molecule α-synuclein structural landscape.FoldEco: a model for proteostasis in E. coli.Probing water density and dynamics in the chaperonin GroEL cavity.GroEL actively stimulates folding of the endogenous substrate protein PepQUNC-45B chaperone: the role of its domains in the interaction with the myosin motor domain.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.Combining MFD and PIE for accurate single-pair Förster resonance energy transfer measurements.Signaling the mitochondrial unfolded protein response.Chaperones rescue luciferase folding by separating its domains.Mechanisms of cellular proteostasis: insights from single-molecule approachesOpposing effects of folding and assembly chaperones on evolvability of Rubisco.Protein folding in the cell: challenges and progress.Forced folding of a disordered protein accesses an alternative folding landscape.Chaperoning roles of macromolecules interacting with proteins in vivo.Decoding Structural Properties of a Partially Unfolded Protein Substrate: En Route to Chaperone Binding.Indole-3-glycerol-phosphate synthase is recognized by a cold-inducible group II chaperonin in Thermococcus kodakarensis.Revisiting the contribution of negative charges on the chaperonin cage wall to the acceleration of protein folding.Folding of newly translated membrane protein CCR5 is assisted by the chaperonin GroEL-GroES.Protein quality control acts on folding intermediates to shape the effects of mutations on organismal fitness.Shedding light on protein folding landscapes by single-molecule fluorescence.Mitochondrial quality control and communications with the nucleus are important in maintaining mitochondrial function and cell health.How do chaperonins fold protein?The chaperone toolbox at the single-molecule level: From clamping to confining.Chaperone-client interactions: Non-specificity engenders multifunctionality.Replacement of GroEL in Escherichia coli by the Group II Chaperonin from the Archaeon Methanococcus maripaludis.The folding competence of HIV-1 Tat mediated by interaction with TAR RNA.Trigger factor chaperone acts as a mechanical foldase.Is catalytic activity of chaperones a selectable trait for the emergence of heat shock response?Chemical chaperones assist intracellular folding to buffer mutational variations.Catalysis of protein folding by chaperones accelerates evolutionary dynamics in adapting cell populations
P2860
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P2860
Chaperonin-catalyzed rescue of kinetically trapped states in protein folding.
description
2010 nî lūn-bûn
@nan
2010 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Chaperonin-catalyzed rescue of kinetically trapped states in protein folding.
@ast
Chaperonin-catalyzed rescue of kinetically trapped states in protein folding.
@en
Chaperonin-catalyzed rescue of kinetically trapped states in protein folding.
@nl
type
label
Chaperonin-catalyzed rescue of kinetically trapped states in protein folding.
@ast
Chaperonin-catalyzed rescue of kinetically trapped states in protein folding.
@en
Chaperonin-catalyzed rescue of kinetically trapped states in protein folding.
@nl
prefLabel
Chaperonin-catalyzed rescue of kinetically trapped states in protein folding.
@ast
Chaperonin-catalyzed rescue of kinetically trapped states in protein folding.
@en
Chaperonin-catalyzed rescue of kinetically trapped states in protein folding.
@nl
P2093
P50
P1433
P1476
Chaperonin-catalyzed rescue of kinetically trapped states in protein folding.
@en
P2093
Bernhard C Poschner
Guoxin Jiang
Jyoti Sinha
Manal Chatila
Martin Sikor
Qiaoyun Shi
P304
P356
10.1016/J.CELL.2010.05.027
P407
P577
2010-07-01T00:00:00Z