| dc.contributor.author |
Antonopoulou, G |
en |
| dc.contributor.author |
Barbayianni, E |
en |
| dc.contributor.author |
Magrioti, V |
en |
| dc.contributor.author |
Cotton, N |
en |
| dc.contributor.author |
Stephens, D |
en |
| dc.contributor.author |
Constantinou-Kokotou, V |
en |
| dc.contributor.author |
Dennis, EA |
en |
| dc.contributor.author |
Kokotos, G |
en |
| dc.date.accessioned |
2014-06-06T06:48:41Z |
|
| dc.date.available |
2014-06-06T06:48:41Z |
|
| dc.date.issued |
2008 |
en |
| dc.identifier.issn |
09680896 |
en |
| dc.identifier.uri |
http://dx.doi.org/10.1016/j.bmc.2008.10.046 |
en |
| dc.identifier.uri |
http://62.217.125.90/xmlui/handle/123456789/4235 |
|
| dc.subject |
2-Oxoamides |
en |
| dc.subject |
Amides |
en |
| dc.subject |
Amino acids |
en |
| dc.subject |
Inhibitors |
en |
| dc.subject |
Phospholipase A2 |
en |
| dc.subject.other |
amino acid derivative |
en |
| dc.subject.other |
phospholipase A2 |
en |
| dc.subject.other |
phospholipase A2 inhibitor |
en |
| dc.subject.other |
article |
en |
| dc.subject.other |
drug activity |
en |
| dc.subject.other |
drug structure |
en |
| dc.subject.other |
enzyme inhibition |
en |
| dc.subject.other |
structure activity relation |
en |
| dc.subject.other |
Amides |
en |
| dc.subject.other |
Amino Acids |
en |
| dc.subject.other |
Enzyme Inhibitors |
en |
| dc.subject.other |
Humans |
en |
| dc.subject.other |
Molecular Structure |
en |
| dc.subject.other |
Phospholipases A2 |
en |
| dc.subject.other |
Pyridines |
en |
| dc.subject.other |
Structure-Activity Relationship |
en |
| dc.title |
Structure-activity relationships of natural and non-natural amino acid-based amide and 2-oxoamide inhibitors of human phospholipase A2 enzymes |
en |
| heal.type |
journalArticle |
en |
| heal.identifier.primary |
10.1016/j.bmc.2008.10.046 |
en |
| heal.publicationDate |
2008 |
en |
| heal.abstract |
A variety of 2-oxoamides and related amides based on natural and non-natural amino acids were synthesized. Their activity on two human intracellular phospholipases (GIVA cPLA2 and GVIA iPLA2) and one human secretory phospholipase (GV sPLA2) was evaluated. We show that an amide based on (R)-γ-norleucine is a highly selective inhibitor of GV sPLA2. © 2008 Elsevier Ltd. All rights reserved. |
en |
| heal.journalName |
Bioorganic and Medicinal Chemistry |
en |
| dc.identifier.issue |
24 |
en |
| dc.identifier.volume |
16 |
en |
| dc.identifier.doi |
10.1016/j.bmc.2008.10.046 |
en |
| dc.identifier.spage |
10257 |
en |
| dc.identifier.epage |
10269 |
en |