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

In vivo formation of Cu,Zn superoxide dismutase disulfide bond in Escherichia coli.

FEBS letters - 29 Jan 1999

Battistoni A, Mazzetti A P, Rotilio G

Abstract excerpt

We have found that the in vivo folding of periplasmic Escherichia coli Cu,Zn superoxide dismutase is assisted by DsbA, which catalyzes the efficient formation of its single disulfide bond, whose integrity is essential to ensure full catalytic activity to the enzyme. In line with these findings, we also report that the production of recombinant Xenopus laevis Cu,Zn superoxide dismutase is enhanced when the enzyme...

Read the complete abstract on PubMed

Topics

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

Share to Cytoplasm
Share to Disulfides
Share to Dithiothreitol

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

Share to Periplasm

Share to Protein Disulfide-Isomerases

Share to Superoxide Dismutase

Share to Thioredoxin-Disulfide Reductase

Share to Xenopus laevis

Source

Identifiers

PMID: 10025954
DOI: 10.1016/s0014-5793(98)01725-6

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

In vivo formation of Cu,Zn superoxide dismutase disulfide bond in Escherichia coli.PMID 10025954Read ↗

An in vivo pathway for disulfide bond isomerization in Escherichia coli.Semantic proximity Read ↗

Engineered pathways for correct disulfide bond oxidation.Semantic proximity Read ↗

Six conserved cysteines of the membrane protein DsbD are required for the transfer of electrons from the cytoplasm to the periplasm of Escherichia coli.Semantic proximity Read ↗

Temperature-dependent protein folding in vivo--lower growth temperature increases yield of two genetic variants of Xenopus laevis Cu,Zn superoxide dismutase in Escherichia coli.Semantic proximity Read ↗

Reduction of the periplasmic disulfide bond isomerase, DsbC, occurs by passage of electrons from cytoplasmic thioredoxin.Semantic proximity Read ↗

Effect of sequences of the active-site dipeptides of DsbA and DsbC on in vivo folding of multidisulfide proteins in Escherichia coli.Semantic proximity Read ↗

Identification and characterization of a new disulfide isomerase-like protein (DsbD) in Escherichia coli.Semantic proximity Read ↗

Complementation of DsbA deficiency with secreted thioredoxin variants reveals the crucial role of an efficient dithiol oxidant for catalyzed protein folding in the bacterial periplasm.Semantic proximity Read ↗

Identification of a protein required for disulfide bond formation in vivo.Semantic proximity Read ↗

The protein-disulfide isomerase DsbC cooperates with SurA and DsbA in the assembly of the essential β-barrel protein LptD.Semantic proximity Read ↗

An engineered pathway for the formation of protein disulfide bonds.Semantic proximity Read ↗

Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm.Semantic proximity Read ↗

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