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

Human replication protein A (RPA) binds a primer-template junction in the absence of its major ssDNA-binding domains.

Nucleic acids research - 1 Jan 2004

Pestryakov Pavel E, Khlimankov Denis Y, Bochkareva Elena, Bochkarev Alexey, Lavrik Olga I

Abstract excerpt

The human nuclear single-stranded (ss) DNA- binding protein, replication protein A (RPA), is a heterotrimer consisting of three subunits: p70, p32 and p14. The protein-DNA interaction is mediated by several DNA-binding domains (DBDs): two major (A and B, also known as p70A and p70B) and several minor (C and D, also known as p70C and p32D, and, presumably, by p70N). Here, using crosslinking experiments, we...

Read the complete abstract on PubMed

Topics

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

Share to Binding Sites
Share to DNA-Binding Proteins

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

Share to DNA Primers

Share to DNA, Single-Stranded

Share to Protein Structure, Tertiary

Share to Protein Subunits

Share to Replication Protein A

Share to Templates, Genetic

Source

Open in PubMed Open full text

Identifiers

PMID: 15047856
DOI: 10.1093/nar/gkh346
PMCID: PMC390355

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

Human replication protein A (RPA) binds a primer-template junction in the absence of its major ssDNA-binding domains.PMID 15047856Read ↗

Replication Protein A, the Main Eukaryotic Single-Stranded DNA Binding Protein, a Focal Point in Cellular DNA MetabolismSemantic proximity Read ↗

Structural characterization of human RPA sequential binding to single-stranded DNA using ssDNA as a molecular ruler.Semantic proximity Read ↗

The Intriguing Mystery of RPA Phosphorylation in DNA Double-Strand Break RepairSemantic proximity Read ↗

Functional analysis of the four DNA binding domains of replication protein A. The role of RPA2 in ssDNA binding.Semantic proximity Read ↗

Replication protein A: single-stranded DNA's first responder: dynamic DNA-interactions allow replication protein A to direct single-strand DNA intermediates into different pathways for synthesis or repair.Semantic proximity Read ↗

Analysis of the human replication protein A:Rad52 complex: evidence for crosstalk between RPA32, RPA70, Rad52 and DNA.Semantic proximity Read ↗

Cellular functions of human RPA1. Multiple roles of domains in replication, repair, and checkpoints.Semantic proximity Read ↗

Replication protein A binds RNA and promotes R-loop formationSemantic proximity Read ↗

Functions of human replication protein A (RPA): From DNA replication to DNA damage and stress responsesSemantic proximity Read ↗

Fluorescent human RPA to track assembly dynamics on DNASemantic proximity Read ↗

Human primosome requires replication protein A when copying DNA with inverted repeatsSemantic proximity Read ↗

Regulatory functions of the N-terminal domain of the 70-kDa subunit of replication protein A (RPA).Semantic proximity Read ↗

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