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

The structure of a ring-opened proliferating cell nuclear antigen-replication factor C complex revealed by fluorescence energy transfer.

Proceedings of the National Academy of Sciences of the United States of America - 21 Feb 2006

Zhuang Zhihao, Yoder Bonita L, Burgers Peter M J, Benkovic Stephen J

Abstract excerpt

Numerous proteins that function in DNA metabolic pathways are known to interact with the proliferating cell nuclear antigen (PCNA). The important function of PCNA in stimulating various cellular activities requires its topological linkage with DNA. Loading of the circular PCNA onto duplex DNA requires the activity of a clamp-loader [replication factor C (RFC)] complex and the energy derived from ATP hydrolysis....

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphate
Share to DNA Replication

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Fluorescence Resonance Energy Transfer

Share to Proliferating Cell Nuclear Antigen

Share to Protein Conformation

Share to Replication Protein C

Share to Saccharomyces cerevisiae

Share to Saccharomyces cerevisiae Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 16476998
DOI: 10.1073/pnas.0511263103
PMCID: PMC1413853

Genes

PCNA

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

The structure of a ring-opened proliferating cell nuclear antigen-replication factor C complex revealed by fluorescence energy transfer.PMID 16476998Read ↗

A central swivel point in the RFC clamp loader controls PCNA opening and loading on DNA.Semantic proximity Read ↗

Mechanism of proliferating cell nuclear antigen clamp opening by replication factor C.Semantic proximity Read ↗

Nuclear dynamics of PCNA in DNA replication and repair.Semantic proximity Read ↗

Kinetic analysis of PCNA clamp binding and release in the clamp loading reaction catalyzed by Saccharomyces cerevisiae replication factor C.Semantic proximity Read ↗

Structure of the human clamp loader bound to the sliding clamp: a further twist on AAA+ mechanismSemantic proximity Read ↗

Understanding and re-engineering nucleoprotein machines to cure human disease.Semantic proximity Read ↗

Recruitment of DNA repair synthesis machinery to sites of DNA damage/repair in living human cellsSemantic proximity Read ↗

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

Monitoring the Retention of Human Proliferating Cell Nuclear Antigen at Primer/Template Junctions by Proteins That Bind Single-Stranded DNA.Semantic proximity Read ↗

Cryo-EM reveals a nearly complete PCNA loading process and unique features of the human alternative clamp loader CTF18-RFCSemantic proximity Read ↗

Structure of eukaryotic DNA polymerase δ bound to the PCNA clamp while encircling DNA.Semantic proximity Read ↗

Photo-activatable Ub-PCNA probes reveal new structural features of the Saccharomyces cerevisiae Polη/PCNA complex.Semantic proximity Read ↗

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