SecB is a bona fide generalized chaperone in Escherichia coli - Wikidata - wikimedia - TriplyDB

SecB is a bona fide generalized chaperone in Escherichia coli

SecB is a bona fide generalized chaperone in Escherichia coli

http://www.wikidata.org/entity/Q34336036

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Macromolecule-assisted de novo protein folding An essential nonredundant role for mycobacterial DnaK in native protein folding Structural basis for the antifolding activity of a molecular chaperone Evolutionary conservation in biogenesis of β-barrel proteins allows mitochondria to assemble a functional bacterial trimeric autotransporter protein.Cotranslational protein folding--fact or fiction?Molecular Determinants of Mutant Phenotypes, Inferred from Saturation Mutagenesis Data Protein solubility and folding enhancement by interaction with RNA The ISG15 conjugation system broadly targets newly synthesized proteins: implications for the antiviral function of ISG15.Lon protease quality control of presecretory proteins in Escherichia coli and its dependence on the SecB and DnaJ (Hsp40) chaperones.Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins.The structural view of bacterial translocation-specific chaperone SecB: implications for function.Multitasking SecB chaperones in bacteria Stress down south: meeting report of the fifth International Workshop on the Molecular Biology of Stress Responses.Distinguishing features of delta-proteobacterial genomes.SecB-like chaperone controls a toxin-antitoxin stress-responsive system in Mycobacterium tuberculosis.Chaperoning roles of macromolecules interacting with proteins in vivo.Large-scale evolutionary analyses on SecB subunits of bacterial sec system.Conserved, disordered C terminus of DnaK enhances cellular survival upon stress and DnaK in vitro chaperone activity Toothpicks, serendipity and the emergence of the Escherichia coli DnaK (Hsp70) and GroEL (Hsp60) chaperone machines.Trigger Factor can antagonize both SecB and DnaK/DnaJ chaperone functions in Escherichia coli.A little help from my friends: quality control of presecretory proteins in bacteria Chaperone-assisted folding of newly synthesized proteins in the cytosol.Sec-dependent protein translocation across biological membranes: evolutionary conservation of an essential protein transport pathway (review).Hsp33 controls elongation factor-Tu stability and allows Escherichia coli growth in the absence of the major DnaK and trigger factor chaperones TAC from Mycobacterium tuberculosis: a paradigm for stress-responsive toxin-antitoxin systems controlled by SecB-like chaperones.Secretion of GOB metallo-beta-lactamase in Escherichia coli depends strictly on the cooperation between the cytoplasmic DnaK chaperone system and the Sec machinery: completion of folding and Zn(II) ion acquisition occur in the bacterial periplasm.Multilevel interaction of the DnaK/DnaJ(HSP70/HSP40) stress-responsive chaperone machine with the central metabolism.SecB--a chaperone dedicated to protein translocation.Integrating protein homeostasis strategies in prokaryotes.Breaking on through to the other side: protein export through the bacterial Sec system.Folding while bound to chaperones.M1 RNA is important for the in-cell solubility of its cognate C5 protein: Implications for RNA-mediated protein folding.Identification of nascent chain interaction sites on trigger factor.The folding competence of HIV-1 Tat mediated by interaction with TAR RNA.Sequence-specific interactions of nascent Escherichia coli polypeptides with trigger factor and signal recognition particle.GroES/GroEL and DnaK/DnaJ have distinct roles in stress responses and during cell cycle progression in Caulobacter crescentus.Comparison of the RpoH-dependent regulon and general stress response in Neisseria gonorrhoeae.N-terminal domains of native multidomain proteins have the potential to assist de novo folding of their downstream domains in vivo by acting as solubility enhancers Early encounters of a nascent membrane protein: specificity and timing of contacts inside and outside the ribosome.Chaperone addiction of toxin-antitoxin systems.

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SecB is a bona fide generalized chaperone in Escherichia coli

http://www.wikidata.org/entity/Q34336036

description

2004 nî lūn-bûn

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2004 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2004 թվականի մայիսին հրատարակված գիտական հոդված

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2004年の論文

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2004年論文

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2004年論文

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2004年論文

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2004年論文

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2004年论文

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name

SecB is a bona fide generalized chaperone in Escherichia coli

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SecB is a bona fide generalized chaperone in Escherichia coli

@en

SecB is a bona fide generalized chaperone in Escherichia coli

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type

label

SecB is a bona fide generalized chaperone in Escherichia coli

@ast

SecB is a bona fide generalized chaperone in Escherichia coli

@en

SecB is a bona fide generalized chaperone in Escherichia coli

@nl

prefLabel

SecB is a bona fide generalized chaperone in Escherichia coli

@ast

SecB is a bona fide generalized chaperone in Escherichia coli

@en

SecB is a bona fide generalized chaperone in Escherichia coli

@nl

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

P1476

SecB is a bona fide generalized chaperone in Escherichia coli

@en

P2093

Costa Georgopoulos

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

Françoise Schwager

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

Joen Luirink

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

Nellie Harms

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

Ronald S Ullers

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

P2860

Cytosolic factor purified from Escherichia coli is necessary and sufficient for the export of a preprotein and is a homotetramer of SecB

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

Substrate specificity of the SecB chaperone.

SecA-dependent quality control of intracellular protein localization.

Trigger Factor and DnaK possess overlapping substrate pools and binding specificities.

Sec-dependent membrane protein insertion: sequential interaction of nascent FtsQ with SecY and YidC.

Getting newly synthesized proteins into shape.

Sec-dependent protein export and the involvement of the molecular chaperone SecB.

Protein traffic in bacteria: multiple routes from the ribosome to and across the membrane.

In vivo analysis of the overlapping functions of DnaK and trigger factor

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scholarly article

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10.1073/PNAS.0402398101

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20

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101

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Pierre Genevaux

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2004-05-05T00:00:00Z

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8576598

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15128935

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P921

Escherichia coli

molecular chaperones

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419649

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