Convergent evolution of clamp-like binding sites in diverse chaperones (Q36614878)

15 August 2017

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title

Convergent evolution of clamp-like binding sites in diverse chaperones (English)

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15 August 2017

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1

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15 August 2017

Samuel F Bakhoum

2

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15 August 2017

Andrea B Feigl

series ordinal

3

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15 August 2017

Michel R Leroux

series ordinal

4

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15 August 2017

publication date

1 October 2006

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Nature Structural & Molecular Biology

15 August 2017

published in

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15 August 2017

volume

13

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15 August 2017

issue

10

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15 August 2017

page(s)

865-870

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Folding of newly translated proteins in vivo: the role of molecular chaperones

15 August 2017

cites work

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Molecular chaperones in the cytosol: from nascent chain to folded protein

21 January 2018

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Getting a grip on non-native proteins

21 January 2018

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Posttranslational quality control: folding, refolding, and degrading proteins.

21 January 2018

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Protein import into mitochondria

21 January 2018

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Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains.

21 January 2018

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L23 protein functions as a chaperone docking site on the ribosome

21 January 2018

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RAC, a stable ribosome-associated complex in yeast formed by the DnaK-DnaJ homologs Ssz1p and zuotin.

21 January 2018

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A functional chaperone triad on the yeast ribosome

21 January 2018

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Human Mpp11 J protein: ribosome-tethered molecular chaperones are ubiquitous

21 January 2018

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The molecular chaperone system and other anti-stress mechanisms in archaea

21 January 2018

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A novel protein complex promoting formation of functional alpha- and gamma-tubulin

21 January 2018

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Structure of eukaryotic prefoldin and of its complexes with unfolded actin and the cytosolic chaperonin CCT.

21 January 2018

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MtGimC, a novel archaeal chaperone related to the eukaryotic chaperonin cofactor GimC/prefoldin

21 January 2018

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Compartmentation of protein folding in vivo: sequestration of non-native polypeptide by the chaperonin-GimC system

21 January 2018

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Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin

21 January 2018

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Protein folding: versatility of the cytosolic chaperonin TRiC/CCT.

21 January 2018

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Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets.

21 January 2018

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From the cradle to the grave: molecular chaperones that may choose between folding and degradation

21 January 2018

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Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide

21 January 2018

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Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins

21 January 2018

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Crystal structure of the mitochondrial chaperone TIM9.10 reveals a six-bladed alpha-propeller

21 January 2018

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Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins.

21 January 2018

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Structure of the periplasmic chaperone Skp suggests functional similarity with cytosolic chaperones despite differing architecture.

21 January 2018

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The crystal structure of the yeast Hsp40 Ydj1 complexed with its peptide substrate

21 January 2018

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The crystal structure of ribosomal chaperone trigger factor from Vibrio cholerae

21 January 2018

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The crystal structure of the peptide-binding fragment from the yeast Hsp40 protein Sis1

21 January 2018

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Structure of the molecular chaperone prefoldin: unique interaction of multiple coiled coil tentacles with unfolded proteins

21 January 2018

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Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation

21 January 2018

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The crystal structure of the carboxy-terminal dimerization domain of htpG, the Escherichia coli Hsp90, reveals a potential substrate binding site

21 January 2018

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Structures of the N-terminal and middle domains of E. coli Hsp90 and conformation changes upon ADP binding

21 January 2018

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Structural analysis of substrate binding by the molecular chaperone DnaK

21 January 2018

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Crystal structure of an Hsp90-nucleotide-p23/Sba1 closed chaperone complex

21 January 2018

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Folding zones inside the ribosomal exit tunnel

21 January 2018

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Nascent membrane and secretory proteins differ in FRET-detected folding far inside the ribosome and in their exposure to ribosomal proteins.

21 January 2018

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The complete atomic structure of the large ribosomal subunit at 2.4 A resolution

21 January 2018

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Trigger factor peptidyl-prolyl cis/trans isomerase activity is not essential for the folding of cytosolic proteins in Escherichia coli

21 January 2018

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The amino-terminal 118 amino acids of Escherichia coli trigger factor constitute a domain that is necessary and sufficient for binding to ribosomes.

21 January 2018

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The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity

21 January 2018

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Structure of the hypothetical Mycoplasma protein MPN555 suggests a chaperone function

21 January 2018

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Structural basis of interdomain communication in the Hsc70 chaperone.

21 January 2018

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Identification of essential residues in the type II Hsp40 Sis1 that function in polypeptide binding

21 January 2018

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Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries

21 January 2018

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Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone.

21 January 2018

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Kinetics and binding sites for interaction of the prefoldin with a group II chaperonin: contiguous non-native substrate and chaperonin binding sites in the archaeal prefoldin.

21 January 2018

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Molecular clamp mechanism of substrate binding by hydrophobic coiled-coil residues of the archaeal chaperone prefoldin

21 January 2018

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TRiC/CCT cooperates with different upstream chaperones in the folding of distinct protein classes

21 January 2018

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Tim9p, an essential partner subunit of Tim10p for the import of mitochondrial carrier proteins

21 January 2018

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Assembly of Tim9 and Tim10 into a functional chaperone.

21 January 2018

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Mitochondrial import and the twin-pore translocase

21 January 2018

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Chaperoning through the mitochondrial intermembrane space

21 January 2018

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Molecular chaperones Hsp90 and Hsp70 deliver preproteins to the mitochondrial import receptor Tom70

21 January 2018

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Navigating the chaperone network: an integrative map of physical and genetic interactions mediated by the hsp90 chaperone

21 January 2018

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The ATPase cycle of Hsp90 drives a molecular 'clamp' via transient dimerization of the N-terminal domains

21 January 2018

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Structural and functional analysis of the middle segment of hsp90: implications for ATP hydrolysis and client protein and cochaperone interactions

21 January 2018

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Polypeptide release by Hsp90 involves ATP hydrolysis and is enhanced by the co-chaperone p23.

21 January 2018

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The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state

21 January 2018

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The structures of HsIU and the ATP-dependent protease HsIU-HsIV

21 January 2018

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Crystal and solution structures of an HslUV protease-chaperone complex

21 January 2018

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Some like it hot: the structure and function of small heat-shock proteins.

21 January 2018

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Distinct Domains of Small Tims Involved in Subunit Interaction and Substrate Recognition

21 January 2018

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Multistep mechanism of substrate binding determines chaperone activity of Hsp70

21 January 2018

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Skp, a molecular chaperone of gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins

31 March 2020

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Hsp90 structure: when two ends meet

31 March 2020

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31 March 2020

Identifiers

DOI

10.1038/NSMB1153

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Dimensions Publication ID

15 August 2017

1006818989

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