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1       Mutations that inhibit the activity of viral proteinase 2A were dominant, arguing that inhibiti
2  sensitivity is dramatically enhanced by the viral proteinase 2A, due, most likely, to inhibition of
3 rsor protein (P1-2A) and wild-type or mutant viral proteinase 3C (plasmids P12X3C or P12X3C-mut, resp
4 that this cleavage event was mediated by the viral proteinases 3C/3CD.
5 rhinovirus infection, AUF1 is cleaved by the viral proteinase 3CD and that AUF1 can interact with the
6                   It has been shown that the viral proteinase 3CD cleaves PCBP2 and contributes to vi
7  through proteolytic cleavage of AUF1 by the viral proteinase 3CD.
8                                          The viral proteinase 3Cpro was not found to interact with ot
9 omain and to demonstrate that three distinct viral proteinase activities process the MHV replicase po
10 ody disruption correlated with production of viral proteinases and required substantial viral gene pr
11         Late in an adenovirus infection, the viral proteinase (AVP) becomes activated to process viri
12                           One such target of viral proteinase cleavage is AU-rich binding factor 1 (A
13 yproteins are cotranslationally processed by viral proteinases into at least 15 mature proteins, incl
14 to a polyprotein that is cleaved by host and viral proteinases into functional, structural and non-st
15 co- and post-translationally by cellular and viral proteinases into three structural and at least six
16 of polyprotein processing are performed by a viral proteinase located in the N-terminal one-third of
17 argeting the nucleating factor G3BP1 via the viral proteinase NS6(Pro) This work provides new insight
18 t signal peptidase and a novel two-component viral proteinase of the serine proteinase family, NS2B/N
19  In contrast to inhibitors that act upon the viral proteinase, PA-457 appears to block only the final
20     The gene 1 polyproteins are processed by viral proteinases to yield at least 15 mature products,
21  work is the first instance of engineering a viral proteinase with switched cleavage preferences and

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