Linked Life Data

2846533

Source:http://linkedlifedata.com/resource/pubmed/id/2846533

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
31
pubmed:dateCreated
1988-12-2
pubmed:abstractText
Herpes simplex virus (HSV) ribonucleotide reductase activity is specifically inhibited by a synthetic peptide, Tyr-Ala-Gly-Ala-Val-Val-Asn-Asp-Leu (HSV H2-(7-15], corresponding to the carboxyl terminus of its subunit 2 (H2). In order to elucidate the mechanism of action of the nonapeptide a photoreactive analog, [4'-azido-Phe6]HSV H2-(6-15), was synthesized. The photoaffinity probe inhibits HSV ribonucleotide reductase activity, and when radioiodinated, it specifically labeled three viral proteins of 144, 95, and 85 kDa. We demonstrated by immunoprecipitation of the 144- and 95-kDa photolabeled proteins with antibodies specific to subunit 1 (H1) of HSV ribonucleotide reductase that the nonapeptide interacts with H1 and probably with its degradation products. Moreover, we obtained evidence that this specific binding is directly responsible for the ribonucleotide reductase inhibition.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
5
pubmed:volume
263
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
16045-50
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Mechanism of inhibition of herpes simplex virus (HSV) ribonucleotide reductase by a nonapeptide corresponding to the carboxyl terminus of its subunit 2. Specific binding of a photoaffinity analog, [4'- azido-Phe6] HSV H2-6(6-15), to subunit 1.
pubmed:affiliation
Institut du Cancer de Montréal, Notre-Dame Hospital, Quebec, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't