Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2004-12-6
pubmed:abstractText
Tamoxifen is a well-known antiestrogen used for the hormonotherapy of estrogen receptor positive breast cancer. In addition to its high affinity binding to the estrogen receptor (ER), tamoxifen binds with comparable affinity to the microsomal antiestrogen binding site (AEBS), and inhibits with a micromolar efficiency, protein kinase C (PKC), calmodulin (CaM)-dependent enzymes and Acyl CoenzymeA: Cholesterol Acyl Transferase (ACAT). Each of these tamoxifen targets might explain the genomic as well as non-genomic effects of tamoxifen. In this review, we will report current knowledge about the structural features of tamoxifen involved in this multiple targeting. These data provide a useful guide for the conception of selective ligands of ERs, AEBS, PKC, CaM or ACAT based on the chemical structure of tamoxifen.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1568-0118
pubmed:author
pubmed:issnType
Print
pubmed:volume
4
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
491-508
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Multiple targeting by the antitumor drug tamoxifen: a structure-activity study.
pubmed:affiliation
Département Innovation Thérapeutique et Oncologie Moléculaire, Centre de Physiopathologie de Toulouse Purpan, INSERM U 563, C.P.T.P., Institut Claudius Regaud, 20-24 rue du Pont Saint Pierre, 31052 Toulouse Cedex, France.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't