MecA, an adaptor protein necessary for ClpC chaperone activity. - Wikidata - wikimedia - TriplyDB

MecA, an adaptor protein necessary for ClpC chaperone activity.

MecA, an adaptor protein necessary for ClpC chaperone activity.

http://www.wikidata.org/entity/Q34804953

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Unscrambling an egg: protein disaggregation by AAA+ proteins Structural and Motional Contributions of the Bacillus subtilis ClpC N-Domain to Adaptor Protein Interactions Structural Dynamics of the MecA-ClpC Complex: A TYPE II AAA+ PROTEIN UNFOLDING MACHINE Structural Basis of Mycobacterial Inhibition by Cyclomarin A Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation Arginine phosphorylation marks proteins for degradation by a Clp protease YjbH-enhanced proteolysis of Spx by ClpXP in Bacillus subtilis is inhibited by the small protein YirB (YuzO)Adaptor protein controlled oligomerization activates the AAA+ protein ClpC Clp-dependent proteolysis down-regulates central metabolic pathways in glucose-starved Bacillus subtilis.Heat resistance mediated by a new plasmid encoded Clp ATPase, ClpK, as a possible novel mechanism for nosocomial persistence of Klebsiella pneumoniae.Crystal structure of the MecA degradation tag.Adaptor bypass mutations of Bacillus subtilis spx suggest a mechanism for YjbH-enhanced proteolysis of the regulator Spx by ClpXP Genome-wide identification of genes essential for the survival of Streptococcus pneumoniae in human saliva.ATP-independent reversal of a membrane protein aggregate by a chloroplast SRP subunit The M-domain controls Hsp104 protein remodeling activity in an Hsp70/Hsp40-dependent manner.The extracytoplasmic adaptor protein CpxP is degraded with substrate by DegP.Sortase B, a new class of sortase in Listeria monocytogenes.Dysregulation of bacterial proteolytic machinery by a new class of antibiotics.FliT selectively enhances proteolysis of FlhC subunit in FlhD4C2 complex by an ATP-dependent protease, ClpXP.The antibiotic ADEP reprogrammes ClpP, switching it from a regulated to an uncontrolled protease.The IbpA and IbpB small heat-shock proteins are substrates of the AAA+ Lon protease Regulated proteolysis of the alternative sigma factor SigX in Streptococcus mutans: implication in the escape from competence.Characterization of the accessory protein ClpT1 from Arabidopsis thaliana: oligomerization status and interaction with Hsp100 chaperones.A Clp/Hsp100 chaperone functions in Myxococcus xanthus sporulation and self-organization Sculpting the proteome with AAA(+) proteases and disassembly machines.Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis Novel insights into the mechanism of chaperone-assisted protein disaggregation.A new tyrosine phosphorylation mechanism involved in signal transduction in Bacillus subtilis.The purification of the Chlamydomonas reinhardtii chloroplast ClpP complex: additional subunits and structural features Geobacillus thermodenitrificans YjbH recognizes the C-terminal end of Bacillus subtilis Spx to accelerate Spx proteolysis by ClpXP.Clp ATPases and ClpP proteolytic complexes regulate vital biological processes in low GC, Gram-positive bacteria.Genome sequencing and analysis of the first complete genome of Lactobacillus kunkeei strain MP2, an Apis mellifera gut isolate.Degradation of SsrA-tagged proteins in streptococci.Differential Regulation of Genes Coding for Organelle and Cytosolic ClpATPases under Biotic and Abiotic Stresses in Wheat.Localization of general and regulatory proteolysis in Bacillus subtilis cells.Trapping and identification of cellular substrates of the Staphylococcus aureus ClpC chaperone SspB delivery of substrates for ClpXP proteolysis probed by the design of improved degradation tags Integrating protein homeostasis strategies in prokaryotes.The elusive middle domain of Hsp104 and ClpB: location and function.Regulated proteolysis in Gram-negative bacteria--how and when?

P2860

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P2860

MecA, an adaptor protein necessary for ClpC chaperone activity.

http://www.wikidata.org/entity/Q34804953

description

2003 nî lūn-bûn

@nan

2003 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2003年の論文

@ja

2003年論文

@yue

2003年論文

@zh-hant

2003年論文

@zh-hk

2003年論文

@zh-mo

2003年論文

@zh-tw

2003年论文

@wuu

name

MecA, an adaptor protein necessary for ClpC chaperone activity.

@ast

MecA, an adaptor protein necessary for ClpC chaperone activity.

@en

MecA, an adaptor protein necessary for ClpC chaperone activity.

@nl

type

label

MecA, an adaptor protein necessary for ClpC chaperone activity.

@ast

MecA, an adaptor protein necessary for ClpC chaperone activity.

@en

MecA, an adaptor protein necessary for ClpC chaperone activity.

@nl

prefLabel

MecA, an adaptor protein necessary for ClpC chaperone activity.

@ast

MecA, an adaptor protein necessary for ClpC chaperone activity.

@en

MecA, an adaptor protein necessary for ClpC chaperone activity.

@nl

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PNAS.0535717100

P1433

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

P1476

MecA, an adaptor protein necessary for ClpC chaperone activity.

@en

P2093

Tilman Schlothauer

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

P2860

Competence in Bacillus subtilis is controlled by regulated proteolysis of a transcription factor.

Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins.

Protein disaggregation mediated by heat-shock protein Hsp104.

AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes

DNA uptake in bacteria

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

AAA+ superfamily ATPases: common structure--diverse function

The ClpX heat-shock protein of Escherichia coli, the ATP-dependent substrate specificity component of the ClpP-ClpX protease, is a novel molecular chaperone

Clp-mediated proteolysis in Gram-positive bacteria is autoregulated by the stability of a repressor.

The RssB response regulator directly targets sigma(S) for degradation by ClpXP

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2306-2311

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scholarly article

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10.1073/PNAS.0535717100

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P433

5

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P478

100

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P50

David A. Dougan

Kürşad Turgay

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2003-02-21T00:00:00Z

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10889117

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12598648

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molecular chaperones

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151336

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