Source:http://linkedlifedata.com/resource/pubmed/id/10476882
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
16
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pubmed:dateCreated |
1999-10-14
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pubmed:abstractText |
The importance of each side chain of a cross-linked interfacial peptide inhibitor of HIV-1 protease was evaluated using an alanine scanning approach. Whereas the parent inhibitor has an IC50 value of 350 nM, values for the mutations reported here range from 280-9200 nM. The relative importance or each residue was thus assigned and correlated to the solvent accessible surface area (SASA) exposed upon mutation.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0960-894X
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
16
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2431-6
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading | |
pubmed:year |
1999
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pubmed:articleTitle |
Probing the role of interfacial residues in a dimerization inhibitor of HIV-1 protease.
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pubmed:affiliation |
Department of Chemistry, Purdue University, West Lafayette, IN 47907, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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