Chaperonin complex with a newly folded protein encapsulated in the folding chamber.
about
Structure and assembly of bacteriophage T4 headStructure, assembly, and DNA packaging of the bacteriophage T4 headComparing protein folding in vitro and in vivo: foldability meets the fitness challengeChaperone machines for protein folding, unfolding and disaggregationPromiscuous Substrate Recognition in Folding and Assembly Activities of the Trigger Factor ChaperoneCrystal Structures of a Group II Chaperonin Reveal the Open and Closed States Associated with the Protein Folding CycleThe host outer membrane proteins OmpA and OmpC are associated with the Shigella phage Sf6 virionCrystal structure of the open conformation of the mammalian chaperonin CCT in complex with tubulinNewly folded substrates inside the molecular cage of the HtrA chaperone DegQATP-Triggered Conformational Changes Delineate Substrate-Binding and -Folding Mechanics of the GroEL ChaperoninFlexible interwoven termini determine the thermal stability of thermosomesVisualizing GroEL/ES in the Act of Encapsulating a Folding ProteinStructural basis for the antifolding activity of a molecular chaperoneDynamic Complexes in the Chaperonin-Mediated Protein Folding CycleDynamics, flexibility, and allostery in molecular chaperoninsChaperonin structure: the large multi-subunit protein complex.Single-molecule spectroscopy of protein folding in a chaperonin cage.Toward an atomic model of the 26S proteasome.Protein folding in the cytoplasm and the heat shock response.Mutagenesis of RpoE-like sigma factor genes in Bdellovibrio reveals differential control of groEL and two groES genesProtein folding in the cell: challenges and progress.A national facility for biological cryo-electron microscopyFunctional Subunits of Eukaryotic Chaperonin CCT/TRiC in Protein Folding.Decoding Structural Properties of a Partially Unfolded Protein Substrate: En Route to Chaperone Binding.An ORFan no more: the bacteriophage T4 39.2 gene product, NwgI, modulates GroEL chaperone functionExpression and functional characterization of the first bacteriophage-encoded chaperonin.Folding of large multidomain proteins by partial encapsulation in the chaperonin TRiC/CCT.GroEL-assisted protein folding: does it occur within the chaperonin inner cavity?The GroEL/GroES cis cavity as a passive anti-aggregation device.Intrinsically disordered chaperones in plants and animals.Diverse functional manifestations of intrinsic structural disorder in molecular chaperones.ATP-driven molecular chaperone machines.The chaperone toolbox at the single-molecule level: From clamping to confining.Chaperone-client interactions: Non-specificity engenders multifunctionality.Dynamics of the entropic insertion of a large sphere into a cylindrical vessel.Analysis of peptides and proteins in their binding to GroEL.Structural and mechanistic characterization of an archaeal-like chaperonin from a thermophilic bacteriumBlob-ology and biology of cryo-EM: an interview with Helen Saibil.Structure of GroEL in complex with an early folding intermediate of alanine glyoxylate aminotransferase.Molecular chaperones: providing a safe place to weather a midlife protein-folding crisis.
P2860
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P2860
Chaperonin complex with a newly folded protein encapsulated in the folding chamber.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
2009年论文
@zh
2009年论文
@zh-cn
name
Chaperonin complex with a newly folded protein encapsulated in the folding chamber.
@en
type
label
Chaperonin complex with a newly folded protein encapsulated in the folding chamber.
@en
prefLabel
Chaperonin complex with a newly folded protein encapsulated in the folding chamber.
@en
P2093
P2860
P356
P1433
P1476
Chaperonin complex with a newly folded protein encapsulated in the folding chamber.
@en
P2093
H R Saibil
H van Heerikhuizen
P J Bakkes
S M van der Vies
P2860
P2888
P304
P356
10.1038/NATURE07479
P407
P577
2009-01-01T00:00:00Z
P5875
P6179
1047340453