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Article

Structural bases of dimerization of yeast telomere protein Cdc13 and its interaction with the catalytic subunit of DNA polymerase α.

Cell research - 1 Feb 2011

Sun Jia, Yang Yuting, Wan Ke, Mao Ninghui, Yu Tai-Yuan, Lin Yi-Chien, DeZwaan Diane C, Freeman Brian C, Lin Jing-Jer, Lue Neal F, Lei Ming

Abstract excerpt

Budding yeast Cdc13-Stn1-Ten1 (CST) complex plays an essential role in telomere protection and maintenance, and has been proposed to be a telomere-specific replication protein A (RPA)-like complex. Previous genetic and structural studies revealed a close resemblance between Stn1-Ten1 and RPA32-RPA14. However, the relationship between Cdc13 and RPA70, the largest subunit of RPA, has remained unclear. Here, we...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 20877309
DOI: 10.1038/cr.2010.138
PMCID: PMC3193437

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

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Structural bases of dimerization of yeast telomere protein Cdc13 and its interaction with the catalytic subunit of DNA polymerase α.PMID 20877309Read ↗

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