Linked Life Data

20359522

Source:http://linkedlifedata.com/resource/pubmed/id/20359522

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
2010-8-4
pubmed:abstractText
While annexin A1 in nuclei is proposed to be involved in cell transformation, its functions remain poorly understood. Since annexin A1 has the consensus motif, ¹??LKRD, for SUMOylation as well as Ks, acceptors for ubiquitination that regulates localization and functions of proteins, we investigated SUMOylation and ubiquitination of annexin A1.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-3002
pubmed:author
pubmed:copyrightInfo
Copyright © 2010 Elsevier B.V. All rights reserved.
pubmed:issnType
Print
pubmed:volume
1800
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
899-905
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Ubiquitination and SUMOylation of annexin A1 and helicase activity.
pubmed:affiliation
Department of Pharmaceutical Sciences, Eugene Applebaum College of Pharmacy and Health Sciences, Wayne State University, Detroit, MI 48202, USA. fhirata@wayne.edu
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't