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

New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH.

Molecular microbiology - 1 Aug 1996

Missiakas D, Betton J M, Raina S

Abstract excerpt

A global search for extracytoplasmic folding catalysts in Escherichia coli was undertaken using different genetic systems that produce unstable or misfolded proteins in the periplasm. The extent of misfolding was monitored by the increased activity of the sigma E regulon that is specifically induced by misfolded proteins in the periplasm. Using multicopy libraries, we cloned two genes, surA and fkpA, that...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Proteins
Share to Carrier Proteins
Share to DNA-Binding Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Escherichia coli

Share to Escherichia coli Proteins

Share to Genetic Complementation Test

Share to Membrane Proteins

Share to Mutation

Source

Identifiers

PMID: 8878048
DOI: 10.1046/j.1365-2958.1996.561412.x

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

New components of protein folding in extracytoplasmic compartments of Escherichia coli SurA, FkpA and Skp/OmpH.PMID 8878048Read ↗

Dissecting the Escherichia coli periplasmic chaperone network using differential proteomics.Semantic proximity Read ↗

Genetic evidence for parallel pathways of chaperone activity in the periplasm of Escherichia coli.Semantic proximity Read ↗

Identification of Substrates of Cytoplasmic Peptidyl-Prolyl Cis/Trans Isomerases and Their Collective Essentiality in Escherichia Coli.Semantic proximity Read ↗

Role of the periplasmic chaperones Skp, SurA, and DegQ in outer membrane protein biogenesis in Neisseria meningitidis.Semantic proximity Read ↗

Insights into the function and structural flexibility of the periplasmic molecular chaperone SurA.Semantic proximity Read ↗

Porin biogenesis activates the sigma(E) response in Salmonella hfq mutants.Semantic proximity Read ↗

Role for Skp in LptD assembly in Escherichia coli.Semantic proximity Read ↗

Skp, a molecular chaperone of gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins.Semantic proximity Read ↗

Identification of FkpA as a key quality control factor for the biogenesis of outer membrane proteins under heat shock conditions.Semantic proximity Read ↗

A pair of circularly permutated PDZ domains control RseP, the S2P family intramembrane protease of Escherichia coli.Semantic proximity Read ↗

The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity.Semantic proximity Read ↗

Diverse sequences are functional at the C-terminus of the E. coli periplasmic chaperone SurA.Semantic proximity Read ↗

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