Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
19
pubmed:dateCreated
1999-2-2
pubmed:abstractText
Replacement of the C-terminal carboxylic acid functionality of peptide inhibitors of hepatitis C virus (HCV) NS3 protease (complexed with NS4A peptide cofactor) by activated carbonyl groups does not produce any substantial increase in potency. These latter inhibitors also inhibit a variety of other serine and cysteine proteases whereas the carboxylic acids are specific. Norvaline was identified as a chemically stable replacement for the P1 residue of Ac-DDIVPC-OH which was also compatible with activated carbonyl functionalities.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0960-894X
pubmed:author
pubmed:issnType
Print
pubmed:day
6
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2719-24
pubmed:dateRevised
2001-11-2
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Studies on the C-terminal of hexapeptide inhibitors of the hepatitis C virus serine protease.
pubmed:affiliation
Boehringer Ingelheim (Canada) Ltd, Bio-Méga Research Division, Laval, Québec, Canada.
pubmed:publicationType
Journal Article