Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Defense against protein carbonylation by DnaK/DnaJ and proteases of the heat shock regulon.

Journal of bacteriology - 1 Jun 2005

Fredriksson Asa, Ballesteros Manuel, Dukan Sam, Nyström Thomas

Abstract excerpt

Protein carbonylation is an irreversible oxidative modification that increases during organism aging and bacterial growth arrest. We analyzed whether the heat shock regulon has a role in defending Escherichia coli cells against this deleterious modification upon entry into stationary phase. Providing the cell with ectopically elevated levels of the heat shock transcription factor, sigma32, effectively reduced...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cell Cycle
Share to Heat-Shock Proteins
Share to HSP40 Heat-Shock Proteins

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to HSP70 Heat-Shock Proteins

Share to Molecular Chaperones

Share to Peptide Hydrolases

Share to Protein Denaturation

Share to Regulon

Source

Open in PubMed Open full text

Identifiers

PMID: 15937182
DOI: 10.1128/JB.187.12.4207-4213.2005
PMCID: PMC1151714

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Defense against protein carbonylation by DnaK/DnaJ and proteases of the heat shock regulon.PMID 15937182Read ↗

Bacterial senescence: stasis results in increased and differential oxidation of cytoplasmic proteins leading to developmental induction of the heat shock regulon.Semantic proximity Read ↗

Heat acclimation and the role of RpoS in prolonged heat shock of Escherichia coli O157.Semantic proximity Read ↗

Protein oxidation in response to increased transcriptional or translational errors.Semantic proximity Read ↗

Oxidative stress defense and deterioration of growth-arrested Escherichia coli cells.Semantic proximity Read ↗

The small heat-shock protein IbpB from Escherichia coli stabilizes stress-denatured proteins for subsequent refolding by a multichaperone network.Semantic proximity Read ↗

A temperature-dependent switch from chaperone to protease in a widely conserved heat shock protein.Semantic proximity Read ↗

Genetic dissection of the roles of chaperones and proteases in protein folding and degradation in the Escherichia coli cytosol.Semantic proximity Read ↗

The Escherichia coli heat shock protease HtrA participates in defense against oxidative stress.Semantic proximity Read ↗

Glutathionylation of the Bacterial Hsp70 Chaperone DnaK Provides a Link between Oxidative Stress and the Heat Shock Response.Semantic proximity Read ↗

Comparative analysis of the molecular mechanism of heat shock proteins from pathogenic and non-pathogenic <i>E.coli</i>Semantic proximity Read ↗

Proteomic survey of the DNA damage response in <i>Caulobacter crescentus</i>Semantic proximity Read ↗

AppppA-binding protein E89 is the Escherichia coli heat shock protein ClpB.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.