Monomerization of RepA dimers by heat shock proteins activates binding to DNA replication origin.
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Negative regulation of the heat shock transcriptional response by HSBP1Genome of bacteriophage P1Mechanisms for regulation of Hsp70 function by Hsp40Molecular chaperones as HSF1-specific transcriptional repressorsEukaryotic homologues of Escherichia coli dnaJ: a diverse protein family that functions with hsp70 stress proteinsCrystal structure of 12-oxophytodienoate reductase 3 from tomato: self-inhibition by dimerizationThe influence of C-terminal extension on the structure of the “J-domain” in E. coli DnaJThe nucleotide exchange factor MGE exerts a key function in the ATP-dependent cycle of mt-Hsp70-Tim44 interaction driving mitochondrial protein import.Opening the Strands of Replication Origins-Still an Open QuestionRandom versus Cell Cycle-Regulated Replication Initiation in Bacteria: Insights from Studying Vibrio cholerae Chromosome 2The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpEThe cellular inhibitor of the PKR protein kinase, P58(IPK), is an influenza virus-activated co-chaperone that modulates heat shock protein 70 activityThe DnaK Chaperone Uses Different Mechanisms To Promote and Inhibit Replication of Vibrio cholerae Chromosome 2.The replication initiator of the cholera pathogen's second chromosome shows structural similarity to plasmid initiators.Handcuffing reversal is facilitated by proteases and replication initiator monomers.Two forms of replication initiator protein: positive and negative controls.Identification and characterization of a novel allele of Escherichia coli dnaB helicase that compromises the stability of plasmid P1.Dimers of pi protein bind the A+T-rich region of the R6K gamma origin near the leading-strand synthesis start sites: regulatory implicationsDeep sequencing-based analysis of the anaerobic stimulon in Neisseria gonorrhoeae.Multiple homeostatic mechanisms in the control of P1 plasmid replicationATPase-defective derivatives of Escherichia coli DnaK that behave differently with respect to ATP-induced conformational change and peptide releaseThe P1 phage replication protein RepA contacts an otherwise inaccessible thymine N3 proton by DNA distortion or base flipping.Chaperones in cell cycle regulation and mitogenic signal transduction: a review.(1,4,7-trimethyl-1,4,7-triazacyclononane)iron (III)-mediated cleavage of DNA: detection of selected protein-DNA interactions.Interplay between E. coli DnaK, ClpB and GrpE during protein disaggregation.Molecular basis for semidominance of missense mutations in the XANTHA-H (42-kDa) subunit of magnesium chelataseTranscriptional inactivation of a regulatory site for replication of Vibrio cholerae chromosome II.Common domains in the initiators of DNA replication in Bacteria, Archaea and Eukarya: combined structural, functional and phylogenetic perspectives.Chromosome I controls chromosome II replication in Vibrio choleraeReplication-induced transcription of an autorepressed gene: the replication initiator gene of plasmid P1.Replication initiator protein RepE of mini-F plasmid: functional differentiation between monomers (initiator) and dimers (autogenous repressor).Translocation pathway of protein substrates in ClpAP protease.In vitro inhibitory activity of RepC/C*, the inactivated form of the pT181 plasmid initiation protein, RepC.Structure-function analyses of the Ssc1p, Mdj1p, and Mge1p Saccharomyces cerevisiae mitochondrial proteins in Escherichia coliRegulation by proteolysis: energy-dependent proteases and their targets.Toxoplasma gondii Sis1-like J-domain protein is a cytosolic chaperone associated to HSP90/HSP70 complexSimilarities between the DNA replication initiators of Gram-negative bacteria plasmids (RepA) and eukaryotes (Orc4p)/archaea (Cdc6p)A molecular chaperone, ClpA, functions like DnaK and DnaJ.Collaboration between the ClpB AAA+ remodeling protein and the DnaK chaperone system.Heat shock proteins DnaJ, DnaK, and GrpE stimulate P1 plasmid replication by promoting initiator binding to the origin.
P2860
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P2860
Monomerization of RepA dimers by heat shock proteins activates binding to DNA replication origin.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on September 1991
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Monomerization of RepA dimers ...... ing to DNA replication origin.
@en
Monomerization of RepA dimers ...... ing to DNA replication origin.
@nl
type
label
Monomerization of RepA dimers ...... ing to DNA replication origin.
@en
Monomerization of RepA dimers ...... ing to DNA replication origin.
@nl
prefLabel
Monomerization of RepA dimers ...... ing to DNA replication origin.
@en
Monomerization of RepA dimers ...... ing to DNA replication origin.
@nl
P2093
P2860
P356
P1476
Monomerization of RepA dimers ...... ing to DNA replication origin.
@en
P2093
P2860
P304
P356
10.1073/PNAS.88.18.7903
P407
P577
1991-09-01T00:00:00Z