The cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domains - Test2 - elhamkhani - TriplyDB

The cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domains

The cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domains

http://www.wikidata.org/entity/Q30157376

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A growing toolbox of techniques for studying β-barrel outer membrane protein folding and biogenesis Protein plasticity underlines activation and function of ATP-independent chaperones Structural Basis for Protein Antiaggregation Activity of the Trigger Factor Chaperone Mitochondrial-bacterial hybrids of BamA/Tob55 suggest variable requirements for the membrane integration of β-barrel proteins.From Chaperones to the Membrane with a BAM!Outer membrane protein biogenesis in Gram-negative bacteria Looks can be deceiving: recent insights into the mechanism of protein secretion by the autotransporter pathway.Bipartite Topology of Treponema pallidum Repeat Proteins C/D and I: OUTER MEMBRANE INSERTION, TRIMERIZATION, AND PORIN FUNCTION REQUIRE A C-TERMINAL β-BARREL DOMAIN Evolutionary conservation in biogenesis of β-barrel proteins allows mitochondria to assemble a functional bacterial trimeric autotransporter protein.Involvement of Neisseria meningitidis lipoprotein GNA2091 in the assembly of a subset of outer membrane proteins Identification of FkpA as a key quality control factor for the biogenesis of outer membrane proteins under heat shock conditions Dissecting the effects of periplasmic chaperones on the in vitro folding of the outer membrane protein PagP SurA is involved in the targeting to the outer membrane of a Tat signal sequence-anchored protein.Insights into the structure and assembly of Escherichia coli outer membrane protein A Alternative folding pathways of the major porin OprF of Pseudomonas aeruginosa.Assembly of Outer Membrane β-Barrel Proteins: the Bam Complex.The Bam machine: a molecular cooper.The soluble, periplasmic domain of OmpA folds as an independent unit and displays chaperone activity by reducing the self-association propensity of the unfolded OmpA transmembrane β-barrel.Sequential and spatially restricted interactions of assembly factors with an autotransporter beta domain.Factors affecting the folding of Pseudomonas aeruginosa OprF porin into the one-domain open conformer Biogenesis of beta-barrel membrane proteins in bacteria and eukaryotes: evolutionary conservation and divergence.Periplasmic expression of soluble single chain T cell receptors is rescued by the chaperone FkpA.The bacterial cell envelope.ATP-independent reversal of a membrane protein aggregate by a chloroplast SRP subunit Direct observation of the uptake of outer membrane proteins by the periplasmic chaperone Skp.Role of the periplasmic chaperones Skp, SurA, and DegQ in outer membrane protein biogenesis in Neisseria meningitidis.Cross-linking measurements of in vivo protein complex topologies.Membrane protein thermodynamic stability may serve as the energy sink for sorting in the periplasm Conformational dynamics of a membrane protein chaperone enables spatially regulated substrate capture and release.In vivo protein complex topologies: sights through a cross-linking lens Deuterium Labeling Together with Contrast Variation Small-Angle Neutron Scattering Suggests How Skp Captures and Releases Unfolded Outer Membrane Proteins Role for Skp in LptD assembly in Escherichia coli.Immunoglobulin domains in Escherichia coli and other enterobacteria: from pathogenesis to applications in antibody technologies.Mechanistic studies of the biogenesis and folding of outer membrane proteins in vitro and in vivo: what have we learned to date?The β-Barrel Assembly Machinery Complex.Skp is a multivalent chaperone of outer-membrane proteins The Skp chaperone helps fold soluble proteins in vitro by inhibiting aggregation.Skp Trimer Formation Is Insensitive to Salts in the Physiological Range.Role of periplasmic chaperones and BamA (YaeT/Omp85) in folding and secretion of intimin from enteropathogenic Escherichia coli strains.Outer membrane protein folding from an energy landscape perspective.

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The cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domains

http://www.wikidata.org/entity/Q30157376

description

2009 nî lūn-bûn

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2009 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2009 թվականի հունվարին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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name

The cavity-chaperone Skp prote ...... t folding of substrate domains

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The cavity-chaperone Skp prote ...... t folding of substrate domains

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The cavity-chaperone Skp prote ...... t folding of substrate domains

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The cavity-chaperone Skp prote ...... t folding of substrate domains

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The cavity-chaperone Skp prote ...... t folding of substrate domains

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The cavity-chaperone Skp prote ...... t folding of substrate domains

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PNAS.0809275106

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Proceedings of the National Academy of Sciences of the United States of America

P1476

The cavity-chaperone Skp prote ...... t folding of substrate domains

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P2093

Arthur Pardi

http://www.w3.org/2001/XMLSchema#string

Cristina M Sandoval

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Marcelo C Sousa

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Troy A Walton

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P2860

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

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

Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

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

Structure of the OmpA-like domain of RmpM from Neisseria meningitidis

Structure and function of an essential component of the outer membrane protein assembly machine

The Periplasmic Bacterial Molecular Chaperone SurA Adapts its Structure to Bind Peptides in Different Conformations to Assert a Sequence Preference for Aromatic Residues

Fold and function of polypeptide transport-associated domains responsible for delivering unfolded proteins to membranes

Crystal Structure of YaeT: Conformational Flexibility and Substrate Recognition

Structure of the outer membrane protein A transmembrane domain

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6

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106

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23963764

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19181847

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P921

molecular chaperones

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2644113

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