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

Structural and functional characterization of oligomeric states of proteins in RecFOR pathway.

International journal of biological macromolecules - 15 Nov 2020

Chaudhary Santosh Kumar, Elayappan Mohanapriya, Jeyakanthan Jeyaraman, Kanagaraj Sekar

Abstract excerpt

RecFOR pathway is the principal repair pathway for double strand break and single strand gap repair in Thermus thermophilus. RecF and RecR exist as monomer and dimer in solution, interestingly; they undergo condition-dependent dimerization and tetramerization, respectively during the DNA break repair. However, their importance in protein-protein and protein-DNA interactions remains elusive. In this study, the...

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 Repair

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to DNA, Single-Stranded

Share to Models, Molecular

Share to Protein Conformation

Share to Protein Multimerization

Share to Structure-Activity Relationship

Share to Thermus thermophilus

Source

Identifiers

PMID: 32659399
DOI: 10.1016/j.ijbiomac.2020.07.062

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural and functional characterization of oligomeric states of proteins in RecFOR pathway.PMID 32659399Read ↗

RecR forms a ring-like tetramer that encircles dsDNA by forming a complex with RecF.Semantic proximity Read ↗

Structural and functional characterization of Cys4 zinc finger motif in the recombination mediator protein RecR.Semantic proximity Read ↗

Differential requirement for RecFOR pathway components in Thermus thermophilus.Semantic proximity Read ↗

Endogenous Bos taurus RECQL is predominantly monomeric and more active than oligomers.Semantic proximity Read ↗

Monoclonal antibodies and mechanistic studies on recA protein.Semantic proximity Read ↗

Structural insights into the unique single-stranded DNA-binding mode of Helicobacter pylori DprASemantic proximity Read ↗

Helical interactions in homologous pairing and strand exchange driven by RecA protein.Semantic proximity Read ↗

Molecular design and functional organization of the RecA protein.Semantic proximity Read ↗

RecO and RecR are necessary for RecA loading in response to DNA damage and replication fork stress.Semantic proximity Read ↗

recF-dependent recombination as a SOS function.Semantic proximity Read ↗

RecFOR proteins are essential for Pol V-mediated translesion synthesis and mutagenesis.Semantic proximity Read ↗

The BLM dissolvasome in DNA replication and repair.Semantic proximity Read ↗

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