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

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

Protein science : a publication of the Protein Society - 1 Jan 2023

Chattopadhyay Gopinath, Ahmed Shahbaz, Srilatha Nonavinakere Seetharam, Asok Aparna, Varadarajan Raghavan

Abstract excerpt

Regulation of biological processes by proteins often involves the formation of transient, multimeric complexes whose characterization is mechanistically important but challenging. The bacterial toxin CcdB binds and poisons DNA Gyrase. The corresponding antitoxin CcdA extracts CcdB from its complex with Gyrase through the formation of a transient ternary complex, thus rejuvenating Gyrase. We describe a high...

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 DNA Gyrase

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

Share to Escherichia coli

Share to Kinetics

Share to Mutation

Source

Open in PubMed Open full text

Identifiers

PMID: 36382921
DOI: 10.1002/pro.4514
PMCID: PMC9793979

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

Ter-Seq: A high-throughput method to stabilize transient ternary complexes and measure associated kinetics.PMID 36382921Read ↗

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

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

Ribosome Display: A Potent Display Technology used for Selecting and Evolving Specific Binders with Desired PropertiesSemantic proximity Read ↗

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

Prediction of residue-specific contributions to binding and thermal stability using yeast surface displaySemantic proximity Read ↗

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

Nucleic acid binding surface and dimer interface revealed by CRISPR-associated CasB protein structures.Semantic proximity Read ↗

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

Improved Prediction of Stabilizing Mutations in Proteins by Incorporation of Mutational Effects on Ligand Binding.Semantic proximity Read ↗

Identification of the Dimer Exchange Interface of the Bacterial DNA Damage Response Protein UmuD.Semantic proximity Read ↗

A Processive Protein Chimera Introduces Mutations across Defined DNA Regions In Vivo.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.