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OB Fold Contributes to Telomere Maintenance.

Cohn, Marita LU (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:
author
organization
publishing date
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
2020-08-19 01:38:51
@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},
}