about
NMR characterization of the interaction of GroEL with amyloid β as a model ligandEpolactaene binds human Hsp60 Cys442 resulting in the inhibition of chaperone activityChaperonin chamber accelerates protein folding through passive action of preventing aggregationEngineering and Evolution of Molecular Chaperones and Protein Disaggregases with Enhanced ActivityRole of the -phosphate of ATP in triggering protein folding by GroEL-GroES: function, structure and energeticsATP-Triggered Conformational Changes Delineate Substrate-Binding and -Folding Mechanics of the GroEL ChaperoninCrystal structure of a GroEL-ADP complex in the relaxed allosteric state at 2.7 A resolutionGroEL/ES Chaperonin Modulates the Mechanism and Accelerates the Rate of TIM-Barrel Domain FoldingMultiple chaperonins in bacteria--novel functions and non-canonical behaviorsHow EF-Tu can contribute to efficient proofreading of aa-tRNA by the ribosomeMapping pathways of allosteric communication in GroEL by analysis of correlated mutationsConfinement and Stabilization of Fyn SH3 Folding Intermediate Mimetics within the Cavity of the Chaperonin GroEL Demonstrated by Relaxation-Based NMR.Intrinsic unfoldase/foldase activity of the chaperonin GroEL directly demonstrated using multinuclear relaxation-based NMR.Effect of glycosylation on protein folding: a close look at thermodynamic stabilization.Disulfide 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.Conversion of the allosteric transition of GroEL from concerted to sequential by the single mutation Asp-155 -> Ala.Probing water density and dynamics in the chaperonin GroEL cavity.Genetic evidence for a link between glycolysis and DNA replication.Proinflammatory effect in whole blood by free soluble bacterial components released from planktonic and biofilm cells.Allosteric transitions of supramolecular systems explored by network models: application to chaperonin GroEL.Huperzine A derivative M3 protects PC12 cells against sodium nitroprusside-induced apoptosisOut-of-equilibrium conformational cycling of GroEL under saturating ATP concentrationsStructure of trigger factor binding domain in biologically homologous complex with eubacterial ribosome reveals its chaperone actionDirect NMR observation of a substrate protein bound to the chaperonin GroEL.Single-molecule spectroscopy of protein folding in a chaperonin cage.Formation and structures of GroEL:GroES2 chaperonin footballs, the protein-folding functional formProtein folding in the cytoplasm and the heat shock response.Molecular chaperones--cellular machines for protein folding.The unfolding action of GroEL on a protein substratePhi value analysis of heterogeneity in pathways of allosteric transitions: Evidence for parallel pathways of ATP-induced conformational changes in a GroEL ring.Visualizing transient dark states by NMR spectroscopy.Probing the sequence of conformationally induced polarity changes in the molecular chaperonin GroEL with fluorescence spectroscopy.Hsp70 chaperones accelerate protein translocation and the unfolding of stable protein aggregates by entropic pulling.Low-frequency normal modes that describe allosteric transitions in biological nanomachines are robust to sequence variationsRole of denatured-state properties in chaperonin action probed by single-molecule spectroscopyCapturing transition paths and transition states for conformational rearrangements in the ribosome.Allostery and cooperativity revisited.Coevolution analyses illuminate the dependencies between amino acid sites in the chaperonin system GroES-L.Type I chaperonins: not all are created equal.
P2860
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P2860
description
2001 nî lūn-bûn
@nan
2001 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Chaperonin-mediated protein folding.
@ast
Chaperonin-mediated protein folding.
@en
Chaperonin-mediated protein folding.
@nl
type
label
Chaperonin-mediated protein folding.
@ast
Chaperonin-mediated protein folding.
@en
Chaperonin-mediated protein folding.
@nl
prefLabel
Chaperonin-mediated protein folding.
@ast
Chaperonin-mediated protein folding.
@en
Chaperonin-mediated protein folding.
@nl
P1476
Chaperonin-mediated protein folding.
@en
P2093
Lorimer GH
Thirumalai D
P304
P356
10.1146/ANNUREV.BIOPHYS.30.1.245
P577
2001-01-01T00:00:00Z