Molecular analysis of the multiple GroEL proteins of Chlamydiae.
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Genomic insights into methanotrophy: the complete genome sequence of Methylococcus capsulatus (Bath)Multiple chaperonins in bacteria--novel functions and non-canonical behaviorsA novel nucleoid-associated protein of Mycobacterium tuberculosis is a sequence homolog of GroELIn silico identification of functional divergence between the multiple groEL gene paralogs in Chlamydiae.Chlamydial GroEL autoregulates its own expression through direct interactions with the HrcA repressor proteinStress response gene regulation in Chlamydia is dependent on HrcA-CIRCE interactions.Immunopathogenic consequences of Chlamydia trachomatis 60 kDa heat shock protein expression in the female reproductive tractProtein multifunctionality: principles and mechanisms.Secretion of the chlamydial virulence factor CPAF requires the Sec-dependent pathwayChlamydia trachomatis secretion of an immunodominant hypothetical protein (CT795) into host cell cytoplasm.Bacterial virulence in the moonlight: multitasking bacterial moonlighting proteins are virulence determinants in infectious diseaseProtective effect of human heat shock protein 60 suggested by its association with decreased seropositivity to pathogensChlamydial Hsp60-2 is iron responsive in Chlamydia trachomatis serovar E-infected human endometrial epithelial cells in vitroTranscriptional regulation of the Chlamydia heat shock stress response in an intracellular infectionTryptophan Codon-Dependent Transcription in Chlamydia pneumoniae during Gamma Interferon-Mediated Tryptophan Limitation.Comparative analysis of gene expression among low G+C gram-positive genomes.Biochemical and Genetic Analysis of the Chlamydia GroEL Chaperonins.Chlamydia pneumoniae GroEL1 protein is cell surface associated and required for infection of HEp-2 cellsThe intermediate domain defines broad nucleotide selectivity for protein folding in Chlamydophila GroEL1.Protein expression profiles of Chlamydia pneumoniae in models of persistence versus those of heat shock stress response.Chaperonin 60: a paradoxical, evolutionarily conserved protein family with multiple moonlighting functions.The evolution of protein moonlighting: adaptive traps and promiscuity in the chaperonins.Only one of five groEL genes is required for viability and successful symbiosis in Sinorhizobium meliloti.Homologous cpn60 genes in Rhizobium leguminosarum are not functionally equivalentFacilitated oligomerization of mycobacterial GroEL: evidence for phosphorylation-mediated oligomerization.The chaperone GroESL enhances the accumulation of soluble, active TraR protein, a quorum-sensing transcription factor from Agrobacterium tumefaciens.Regulation of heat-shock genes in bacteria: from signal sensing to gene expression output.The htpAB operon of Legionella pneumophila cannot be deleted in the presence of the groE chaperonin operon of Escherichia coli.Functional coevolutionary networks of the Hsp70-Hop-Hsp90 system revealed through computational analyses
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P2860
Molecular analysis of the multiple GroEL proteins of Chlamydiae.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on March 2003
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vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
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vědecký článek
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name
Molecular analysis of the multiple GroEL proteins of Chlamydiae.
@en
Molecular analysis of the multiple GroEL proteins of Chlamydiae.
@nl
type
label
Molecular analysis of the multiple GroEL proteins of Chlamydiae.
@en
Molecular analysis of the multiple GroEL proteins of Chlamydiae.
@nl
prefLabel
Molecular analysis of the multiple GroEL proteins of Chlamydiae.
@en
Molecular analysis of the multiple GroEL proteins of Chlamydiae.
@nl
P2093
P2860
P1476
Molecular analysis of the multiple GroEL proteins of Chlamydiae.
@en
P2093
Artem Cherkasov
Caixia Shen
Colleen C Nelson
Jeffrey Kwee
Karuna P Karunakaran
Robert C Brunham
Timothy D Read
Yasuyuki Noguchi
P2860
P304
P356
10.1128/JB.185.6.1958-1966.2003
P407
P577
2003-03-01T00:00:00Z