OB Fold Contributes to Telomere Maintenance.
(2013) In Structure 21(1). p.3-4- Abstract
- The essential Cdc13 protein is part of the trimeric CST complex that confers genome stability by binding to and protecting yeast telomeres. In this issue of Structure, Mason and colleagues characterize an OB fold domain of Cdc13 (named OB2) and propose that homo-dimerization of OB2 is required for proper assembly of the CST complex and telomere maintenance.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/3438799
- author
- Cohn, Marita LU
- organization
- publishing date
- 2013
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Structure
- volume
- 21
- issue
- 1
- pages
- 3 - 4
- publisher
- Cell Press
- external identifiers
-
- wos:000313383400002
- pmid:23312029
- scopus:84872166841
- pmid:23312029
- ISSN
- 0969-2126
- DOI
- 10.1016/j.str.2012.12.005
- language
- English
- LU publication?
- yes
- id
- fd555a06-1207-4e3a-b19e-ae72f14aa214 (old id 3438799)
- date added to LUP
- 2016-04-01 10:18:11
- date last changed
- 2022-01-25 21:56:09
@article{fd555a06-1207-4e3a-b19e-ae72f14aa214,
abstract = {{The essential Cdc13 protein is part of the trimeric CST complex that confers genome stability by binding to and protecting yeast telomeres. In this issue of Structure, Mason and colleagues characterize an OB fold domain of Cdc13 (named OB2) and propose that homo-dimerization of OB2 is required for proper assembly of the CST complex and telomere maintenance.}},
author = {{Cohn, Marita}},
issn = {{0969-2126}},
language = {{eng}},
number = {{1}},
pages = {{3--4}},
publisher = {{Cell Press}},
series = {{Structure}},
title = {{OB Fold Contributes to Telomere Maintenance.}},
url = {{http://dx.doi.org/10.1016/j.str.2012.12.005}},
doi = {{10.1016/j.str.2012.12.005}},
volume = {{21}},
year = {{2013}},
}