eprintid: 39207
rev_number: 18
eprint_status: archive
userid: 11441
dir: disk0/00/03/92/07
datestamp: 2010-09-21 14:10:37
lastmod: 2022-10-24 14:45:33
status_changed: 2010-09-21 13:33:28
type: article
metadata_visibility: show
item_issues_count: 0
creators_name: Carter, S
creators_name: Vousden, KH
title: Modifications of p53: competing for the lysines
ispublished: pub
divisions: 25100000
abstract: The p53 tumour suppressor protein is subject to numerous post-translational modifications, which coalesce in various combinations and patterns to regulate its activity. In addition to a multitude of phosphorylated serines and threonines, many of the lysine residues in p53 can be modified to regulate activity, stability and subcellular localization of the protein. This complexity is amplified by the variety of modifications that can target the same lysine residue - often with opposing effects on p53 function
date: 2009
date_type: published
id_number: 10.1016/j.gde.2008.11.010
official_url: http://dx.doi.org/10.1016/j.gde.2008.11.010
uniqueid: glaseprints:2009-39207
scopus_impact: 30
scopus_cluster: 2-s2.0-61449190667
scopus_datestamp: 2013-05-23 01:44:29
wos_impact: 33
wos_cluster: WOS:000264430600004
wos_datestamp: 2013-10-25 02:36:04
full_text_status: none
publication: Current Opinion in Genetics and Development
volume: 19
number: 1
pagerange: 18-24
refereed: TRUE
issn: 0959437X
hoa_compliant: 305
hoa_date_pub: 2009
hoa_exclude: FALSE
hoa_gold: FALSE
citation:    Carter, S. <http://eprints.gla.ac.uk/view/author/12072.html> and Vousden, K. <http://eprints.gla.ac.uk/view/author/8560.html>  (2009)  Modifications of p53: competing for the lysines.   Current Opinion in Genetics and Development <https://eprints.gla.ac.uk/view/journal_volume/Current_Opinion_in_Genetics_and_Development.html>, 19(1),  pp. 18-24.   (doi: 10.1016/j.gde.2008.11.010 <https://doi.org/10.1016/j.gde.2008.11.010>)