|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
18
|
|
pubmed:dateCreated |
1999-2-2
|
|
pubmed:abstractText |
Peptide deformylase catalyzes the removal of the N-terminal formyl group from nascent polypeptides during prokaryotic protein maturation and is essential for bacterial survival. Its absence from eukaryotic organisms makes it an attractive target for designing novel antibacterial agents. Peptidyl H-phosphonates were synthesized and shown to be competitive inhibitors of the deformylase.
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pubmed:grant |
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Sep
|
|
pubmed:issn |
0960-894X
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:day |
22
|
|
pubmed:volume |
8
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
2479-82
|
|
pubmed:dateRevised |
2007-11-14
|
|
pubmed:meshHeading |
|
|
pubmed:year |
1998
|
|
pubmed:articleTitle |
H-phosphonate derivatives as novel peptide deformylase inhibitors.
|
|
pubmed:affiliation |
Department of Chemistry, Ohio State University, Columbus 43210, USA.
|
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|
