Linked Life Data

10327885

Source:http://linkedlifedata.com/resource/pubmed/id/10327885

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1999-5-27
pubmed:abstractText
In a series of CAAX-tetrapeptide based farnesyltransferase inhibitors it has been shown that the central AA-dipeptide can be replaced by tranexamic acid, 4-aminobenzenesulfonic acid, and 3-amino-N-(2,3-dimethylphenyl)benzenesulfonamide, respectively, yielding inhibitors active in the low micromolar range. Lipophilic derivatives of these compounds showed moderate anti-proliferative activity against different tumor cell lines. A promising class of peptidomimetic farnesyltransferase inhibitors was discovered through the replacement of the terminal AAX motif of the CAAX-tetrapeptide by 2-acylamino-5-aminobenzophenones.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0365-6233
pubmed:author
pubmed:issnType
Print
pubmed:volume
332
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
124-32
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Different amino acid replacements in CAAX-tetrapeptide based peptidomimetic farnesyltransferase inhibitors.
pubmed:affiliation
Institut für Parmazeutische Chemie, Philipps-Universität Marburg, Germany.
pubmed:publicationType
Journal Article