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rdf:type |
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lifeskim:mentions |
umls-concept:C0026882,
umls-concept:C0030705,
umls-concept:C0033684,
umls-concept:C0087111,
umls-concept:C0220847,
umls-concept:C0332281,
umls-concept:C0332307,
umls-concept:C0871261,
umls-concept:C1514562,
umls-concept:C1704632,
umls-concept:C1706817,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2911692
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pubmed:issue |
2
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pubmed:dateCreated |
2000-4-13
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pubmed:abstractText |
An interaction of the hepatitis C virus (HCV) NS5A protein with the interferon (IFN)-alpha-inducible double-stranded RNA-activated protein kinase (PKR) was demonstrated in vitro. The clinical correlation between amino acid mutations within the HCV NS5A region and response to antiviral treatment is controversial. Thirty-two patients chronically infected with HCV-1a, who were treated with IFN-alpha with or without ribavirin, were studied. The carboxy-terminal half of HCV NS5A was sequenced and was investigated by phylogenetic and conformational analyses. Eight patients achieved a sustained virologic response. An end-of-treatment response but relapse thereafter was observed among 8 patients, whereas 16 patients were nonresponders. The median number of mutations within the PKR-binding domain but not within the previously described IFN sensitivity-determining region was significantly higher for patients with sustained (3 mutations [range, 1-5]) or end-of-treatment (4 mutations [range, 1-5]) virologic response than for nonresponders (2 mutations [range, 0-3]) (P=.0087). Phylogenetic and conformational analyses of NS5A sequences allowed no differentiation between sensitive and resistant strains.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antiviral Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Hepatitis C Antibodies,
http://linkedlifedata.com/resource/pubmed/chemical/Interferon Type I,
http://linkedlifedata.com/resource/pubmed/chemical/NS-5 protein, hepatitis C virus,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ribavirin,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Nonstructural Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/eIF-2 Kinase
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0022-1899
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
181
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
432-41
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:10669323-Adult,
pubmed-meshheading:10669323-Amino Acid Sequence,
pubmed-meshheading:10669323-Antiviral Agents,
pubmed-meshheading:10669323-Binding Sites,
pubmed-meshheading:10669323-Drug Therapy, Combination,
pubmed-meshheading:10669323-Female,
pubmed-meshheading:10669323-Hepacivirus,
pubmed-meshheading:10669323-Hepatitis C, Chronic,
pubmed-meshheading:10669323-Hepatitis C Antibodies,
pubmed-meshheading:10669323-Humans,
pubmed-meshheading:10669323-Interferon Type I,
pubmed-meshheading:10669323-Male,
pubmed-meshheading:10669323-Middle Aged,
pubmed-meshheading:10669323-Molecular Sequence Data,
pubmed-meshheading:10669323-Mutation,
pubmed-meshheading:10669323-Phylogeny,
pubmed-meshheading:10669323-Protein Structure, Secondary,
pubmed-meshheading:10669323-Protein Structure, Tertiary,
pubmed-meshheading:10669323-RNA, Viral,
pubmed-meshheading:10669323-Recombinant Proteins,
pubmed-meshheading:10669323-Reverse Transcriptase Polymerase Chain Reaction,
pubmed-meshheading:10669323-Ribavirin,
pubmed-meshheading:10669323-Viral Nonstructural Proteins,
pubmed-meshheading:10669323-eIF-2 Kinase
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pubmed:year |
2000
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pubmed:articleTitle |
Mutations in the protein kinase-binding domain of the NS5A protein in patients infected with hepatitis C virus type 1a are associated with treatment response.
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pubmed:affiliation |
Medizinische Klinik II, J. W. Goethe-University, Frankfurt am Main, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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