Role of disulfide bond formation in the folding and assembly of the envelope glycoproteins of a pestivirus.
Bovine viral diarrhea virus (BVDV) is a pestivirus member of the Flaviviridae family, closely related to, and used as a surrogate model for the hepatitis C virus. Its envelope contains the E1 and E2 glycoproteins, disulfide linked into homo- and heterodimers. In this study, we investigate the role o...
প্রধান লেখক: | Branza-Nichita, N, Lazar, C, Durantel, D, Dwek, R, Zitzmann, N |
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বিন্যাস: | Journal article |
ভাষা: | English |
প্রকাশিত: |
Elsevier
2002
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অনুরূপ উপাদানগুলি
অনুরূপ উপাদানগুলি
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The bovine viral diarrhoea virus: a model for the study of antiviral molecules interfering with N-glycosylation and folding of envelope glycoprotein
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Role of N-glycan trimming in the folding and secretion of the pestivirus protein E(rns)
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The pestivirus E(rns) glycoprotein interacts with E2 in both infected cells and mature virions.
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Brefeldin A inhibits pestivirus release from infected cells, without affecting its assembly and infectivity.
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Antiviral effect of N-butyldeoxynojirimycin against bovine viral diarrhea virus correlates with misfolding of E2 envelope proteins and impairment of their association into E1-E2 heterodimers.
অনুযায়ী: Branza-Nichita, N, অন্যান্য
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