Proteinase 3C-mediated processing of VP1-2A of two hepatitis A virus strains: in vivo evidence for cleavage at amino acid position 273/274 of VP1.
about
Hepatitis A virus capsid protein VP1 has a heterogeneous C terminus.Maturation of the hepatitis A virus capsid protein VP1 is not dependent on processing by the 3Cpro proteinase.Processing of proteinase precursors and their effect on hepatitis A virus particle formation.Improving proteolytic cleavage at the 3A/3B site of the hepatitis A virus polyprotein impairs processing and particle formation, and the impairment can be complemented in trans by 3AB and 3ABC.
P2860
Proteinase 3C-mediated processing of VP1-2A of two hepatitis A virus strains: in vivo evidence for cleavage at amino acid position 273/274 of VP1.
description
1997 nî lūn-bûn
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1997年の論文
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1997年学术文章
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1997年学术文章
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1997年学术文章
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1997年学术文章
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@zh-sg
1997年學術文章
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1997年學術文章
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1997年學術文章
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name
Proteinase 3C-mediated process ...... acid position 273/274 of VP1.
@en
Proteinase 3C-mediated process ...... acid position 273/274 of VP1.
@nl
type
label
Proteinase 3C-mediated process ...... acid position 273/274 of VP1.
@en
Proteinase 3C-mediated process ...... acid position 273/274 of VP1.
@nl
prefLabel
Proteinase 3C-mediated process ...... acid position 273/274 of VP1.
@en
Proteinase 3C-mediated process ...... acid position 273/274 of VP1.
@nl
P2093
P2860
P1433
P1476
Proteinase 3C-mediated process ...... o acid position 273/274 of VP1
@en
P2093
P2860
P304
P407
P577
1997-04-01T00:00:00Z