|
rdf:type |
|
|
lifeskim:mentions |
umls-concept:C0001044,
umls-concept:C0008425,
umls-concept:C0205145,
umls-concept:C0205250,
umls-concept:C0205314,
umls-concept:C0205369,
umls-concept:C0524637,
umls-concept:C0599894,
umls-concept:C0679622,
umls-concept:C0728810,
umls-concept:C1707689
|
|
pubmed:issue |
1
|
|
pubmed:dateCreated |
2002-12-27
|
|
pubmed:abstractText |
Tacrine-based AChE and BuChE inhibitors were designed by investigating the topology of the active site gorge of the two enzymes. The homobivalent ligands characterized by a nitrogen-bridged atom at the tether level could be considered among the most potent and selective cholinesterase inhibitors described to date. The nitrogen-containing homobivalent ligands 3e,g and the sulfur-containing 3h validated the hypothesis of extra sites of interaction in the AChE and BuChE active site gorges.
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Jan
|
|
pubmed:issn |
0022-2623
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
2
|
|
pubmed:volume |
46
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
1-4
|
|
pubmed:meshHeading |
|
|
pubmed:year |
2003
|
|
pubmed:articleTitle |
Specific targeting of acetylcholinesterase and butyrylcholinesterase recognition sites. Rational design of novel, selective, and highly potent cholinesterase inhibitors.
|
|
pubmed:affiliation |
Dipartimento Farmaco Chimico Tecnologico, Università di Siena, via Aldo Moro, 53100 Siena, Italy.
|
|
pubmed:publicationType |
Journal Article
|
