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Structures and Functions of Pestivirus Glycoproteins: Not Simply Surface Matters

Structures and Functions of Pestivirus Glycoproteins: Not Simply Surface Matters

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Molecular Characterization of a Novel Bovine Viral Diarrhea Virus Isolate SD-15.Deciphering the emergence, genetic diversity and evolution of classical swine fever virus.Tracking the Origin and Deciphering the Phylogenetic Relationship of Porcine Epidemic Diarrhea Virus in Ecuador.Genetic evolution of classical swine fever virus under immune environments conditioned by genotype 1-based modified live virus vaccine.DDX5 RNA Helicases: Emerging Roles in Viral Infection.The Occurrence of a Commercial Npro and Erns Double Mutant BVDV-1 Live-Vaccine Strain in Newborn Calves.

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P2860

Structures and Functions of Pestivirus Glycoproteins: Not Simply Surface Matters

http://www.wikidata.org/entity/Q26860412

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2015 nî lūn-bûn

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2015 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2015 թվականի հունիսին հրատարակված գիտական հոդված

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年论文

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name

Structures and Functions of Pestivirus Glycoproteins: Not Simply Surface Matters

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Structures and Functions of Pestivirus Glycoproteins: Not Simply Surface Matters

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Structures and Functions of Pestivirus Glycoproteins: Not Simply Surface Matters

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Structures and Functions of Pestivirus Glycoproteins: Not Simply Surface Matters

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Structures and Functions of Pestivirus Glycoproteins: Not Simply Surface Matters

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Structures and Functions of Pestivirus Glycoproteins: Not Simply Surface Matters

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Structures and Functions of Pestivirus Glycoproteins: Not Simply Surface Matters

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Structures and Functions of Pestivirus Glycoproteins: Not Simply Surface Matters

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Structures and Functions of Pestivirus Glycoproteins: Not Simply Surface Matters

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Structures and Functions of Pestivirus Glycoproteins: Not Simply Surface Matters

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Chia-Yi Chang

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Ming-Chung Deng

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Yu-Liang Huang

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Creative Commons Attribution

P2860

Approaches to define the viral genetic basis of classical swine fever virus virulence

Glycoprotein E1 of hog cholera virus expressed in insect cells protects swine from hog cholera

Acid-resistant bovine pestivirus requires activation for pH-triggered fusion during entry.

The E2 glycoprotein of classical swine fever virus is a virulence determinant in swine.

Inactivation of the RNase activity of glycoprotein E(rns) of classical swine fever virus results in a cytopathogenic virus

Passage of classical swine fever virus in cultured swine kidney cells selects virus variants that bind to heparan sulfate due to a single amino acid change in envelope protein E(rns)

Deletions of structural glycoprotein E2 of classical swine fever virus strain alfort/187 resolve a linear epitope of monoclonal antibody WH303 and the minimal N-terminal domain essential for binding immunoglobulin G antibodies of a pig hyperimmune s

Mutations abrogating the RNase activity in glycoprotein E(rns) of the pestivirus classical swine fever virus lead to virus attenuation

Interaction of classical swine fever virus with membrane-associated heparan sulfate: role for virus replication in vivo and virulence.

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.

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3506-29

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scholarly article

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10.3390/V7072783

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2015-06-29T00:00:00Z

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280030629

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26131960

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viral envelope proteins

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4517112

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