Linked Life Data

11676505

Source:http://linkedlifedata.com/resource/pubmed/id/11676505

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2001-10-25
pubmed:abstractText
Extensive protease digestion of delipidated [3H]mevalonate (MVA)-labeled proteins, followed by HPLC separation of the products, is one approach to identify and study prenyl cysteines. Using this methodology three major [3H]MVA-labeled peaks appeared. Two of them represent farnesyl cysteine (FC) and geranylgeranyl cysteine (GGC). The third peak represents unknown products that are considerably more hydrophobic than FC and GGC, here designated HPC. Previously, we provided evidence that cysteine residues may also be modified by dolichyl groups. Dolichyl cysteines (DolC) belong to HPC. However, as shown in the present study, DolC only represents a minor portion of HPC. Data obtained from different sets of experiments, including [3H]GGOH-labeling and use of prenyl transferase inhibitors, suggest that HPC mainly involves CXC or CC residues with double-linked GG groups. In turn this points to the possibility that proteins modified by double GG groups are quite common, and may probably involve other proteins than the rab family of GTPases.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0006-291X
pubmed:author
pubmed:copyrightInfo
Copyright 2001 Academic Press.
pubmed:issnType
Print
pubmed:day
2
pubmed:volume
288
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
736-41
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
Characterization of hydrophobic prenyl groups of isoprenylated proteins in human cancer cells.
pubmed:affiliation
Department of Oncology and Pathology, CCK R8:04, Karolinska Hospital, Stockholm, SE-171 76, Sweden.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't