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| pubmed-article:7966638 | lifeskim:mentions | umls-concept:C1330957 | lld:lifeskim |
| pubmed-article:7966638 | lifeskim:mentions | umls-concept:C0032583 | lld:lifeskim |
| pubmed-article:7966638 | lifeskim:mentions | umls-concept:C0036720 | lld:lifeskim |
| pubmed-article:7966638 | lifeskim:mentions | umls-concept:C0022702 | lld:lifeskim |
| pubmed-article:7966638 | lifeskim:mentions | umls-concept:C0596311 | lld:lifeskim |
| pubmed-article:7966638 | lifeskim:mentions | umls-concept:C1709694 | lld:lifeskim |
| pubmed-article:7966638 | lifeskim:mentions | umls-concept:C0936012 | lld:lifeskim |
| pubmed-article:7966638 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:7966638 | pubmed:dateCreated | 1994-12-12 | lld:pubmed |
| pubmed-article:7966638 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7966638 | pubmed:abstractText | Hepatitis C virus (HCV) serine proteinase (Cpro-2) is responsible for the processing of HCV nonstructural (NS) protein processing. To clarify the mechanism of Cpro-2-dependent processing, pulse-chase and mutation analyses were performed by using a transient protein production system in cultured cells. Pulse-chase study revealed the sequential production of HCV-NS proteins. Production of p70(NS3) and p66(NS5B) were rapid. An 89-kDa processing intermediate protein (p89) was observed during the early part of the chase. p89 seemed to be cleaved first into a 31-kDa protein (p31) and a p58/56(NS5A). p31 was further processed into p4(NS4A) and p27(NS4B). Mutation analysis of cleavage sites of NS4A/4B, NS4B/5A, and NS5A/5B revealed that cleavage at each site is essentially independent from cleavage occurring at the other site. | lld:pubmed |
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| pubmed-article:7966638 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7966638 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7966638 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:7966638 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7966638 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:7966638 | pubmed:issn | 0022-538X | lld:pubmed |
| pubmed-article:7966638 | pubmed:author | pubmed-author:ShimotohnoKK | lld:pubmed |
| pubmed-article:7966638 | pubmed:author | pubmed-author:TanjiYY | lld:pubmed |
| pubmed-article:7966638 | pubmed:author | pubmed-author:HijikataMM | lld:pubmed |
| pubmed-article:7966638 | pubmed:author | pubmed-author:HirowatariYY | lld:pubmed |
| pubmed-article:7966638 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7966638 | pubmed:volume | 68 | lld:pubmed |
| pubmed-article:7966638 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7966638 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7966638 | pubmed:pagination | 8418-22 | lld:pubmed |
| pubmed-article:7966638 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:7966638 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:7966638 | pubmed:articleTitle | Hepatitis C virus polyprotein processing: kinetics and mutagenic analysis of serine proteinase-dependent cleavage. | lld:pubmed |
| pubmed-article:7966638 | pubmed:affiliation | Virology Division, National Cancer Center Research Institute, Tokyo, Japan. | lld:pubmed |
| pubmed-article:7966638 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:7966638 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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