Linked Life Data

20433201

Source:http://linkedlifedata.com/resource/pubmed/id/20433201

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2010-8-16
pubmed:abstractText
Enolase is a key glycolytic enzyme that catalyzes the dehydration of 2-phosphoglycerate to phosphoenolpyruvate. Recently, enolase was revealed as an important protein in pathophysiological processes since it was found on the surface of hematopoietic cells and overexpressed in several tumor cells. Our previous studies demonstrated that alpha-enolase is up-regulated in pancreatic ductal adenocarcinoma (PDAC). In this present work, we further characterized the alpha-enolase from PDAC and normal pancreatic duct cells by mass spectrometry using LTQ-Orbitrap and identified multiple post-translational modifications of alpha-enolase, such as phosphorylation, acetylation, and methylation. The result showed that more acetylated lysines, methylated aspartic acids, and glutamic acids were found in PDAC cells than that of normal pancreatic duct cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1535-3907
pubmed:author
pubmed:issnType
Electronic
pubmed:day
4
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2929-36
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Mass spectrometry analysis of the post-translational modifications of alpha-enolase from pancreatic ductal adenocarcinoma cells.
pubmed:affiliation
Center for Applied Proteomics and Molecular Medicine, George Mason University, Manassas, Virginia 20110, USA. wzhou@gmu.edu
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't