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

CcdA chaperones CcdB against irreversible misfolding and aggregation via a cotranslational folding mechanism.

The FEBS journal - 1 Apr 2026

Bajaj Priyanka, Kohli Pehu, Varadarajan Raghavan

Abstract excerpt

Cotranslational subunit assembly is thought to be a prominent feature throughout the proteome, but, in bacteria, there are only a limited number of experimentally confirmed examples and most involve the addition of extraneous tag sequences for experimental convenience. Toxin CcdA and Antitoxin CcdB are components of the ccdAB operon. They assemble in a hetero-multimeric complex in vivo. Building on a previously...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Toxins
Share to Escherichia coli
Share to Escherichia coli Proteins

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

Share to Molecular Chaperones

Share to Operon

Share to Protein Aggregates

Share to Protein Biosynthesis

Share to Protein Folding

Source

Identifiers

PMID: 41389277
DOI: 10.1111/febs.70359

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 18 Oct 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

CcdA chaperones CcdB against irreversible misfolding and aggregation via a cotranslational folding mechanism.PMID 41389277Read ↗

Structural and functional determinants inferred from deep mutational scans.Semantic proximity Read ↗

The High Mutational Sensitivity of ccdA Antitoxin Is Linked to Codon Optimality.Semantic proximity Read ↗

Molecular bases for strong phenotypic effects of single synonymous codon substitutions in the E. coli ccdB toxin gene.Semantic proximity Read ↗

Ter-Seq: A high-throughput method to stabilize transient ternary complexes and measure associated kinetics.Semantic proximity Read ↗

Structural correlates of the temperature sensitive phenotype derived from saturation mutagenesis studies of CcdB.Semantic proximity Read ↗

Decoding toxicity: deducing the sequence requirements of IbsC, a type I toxin in Escherichia coli.Semantic proximity Read ↗

Directed evolution of SecB chaperones toward toxin-antitoxin systems.Semantic proximity Read ↗

Membrane topology and mutational analysis of Escherichia coli CydDC, an ABC-type cysteine exporter required for cytochrome assembly.Semantic proximity Read ↗

Mechanism of CcdA-Mediated Rejuvenation of DNA Gyrase.Semantic proximity Read ↗

The molecular basis of protein toxin HicA–dependent binding of the protein antitoxin HicB to DNASemantic proximity Read ↗

Mechanistic insights into global suppressors of protein folding defects.Semantic proximity Read ↗

Molecular Determinants of Mutant Phenotypes, Inferred from Saturation Mutagenesis Data.Semantic proximity Read ↗

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