Proteolytic activation of the porcine epidemic diarrhea coronavirus spike fusion protein by trypsin in cell culture. - Wikidata - wikimedia - TriplyDB

Proteolytic activation of the porcine epidemic diarrhea coronavirus spike fusion protein by trypsin in cell culture.

Proteolytic activation of the porcine epidemic diarrhea coronavirus spike fusion protein by trypsin in cell culture.

http://www.wikidata.org/entity/Q41975503

about

Cryo-electron microscopy structure of a coronavirus spike glycoprotein trimer Fusion of Enveloped Viruses in Endosomes.TMPRSS2 and MSPL Facilitate Trypsin-Independent Porcine Epidemic Diarrhea Virus Replication in Vero Cells.Receptor usage and cell entry of porcine epidemic diarrhea coronavirus Host cell proteases: Critical determinants of coronavirus tropism and pathogenesis Isolation and characterization of porcine epidemic diarrhea virus associated with the 2014 disease outbreak in Mexico: case report.Porcine epidemic diarrhea virus: An emerging and re-emerging epizootic swine virus S1 domain of the porcine epidemic diarrhea virus spike protein as a vaccine antigen Cell Entry of Porcine Epidemic Diarrhea Coronavirus Is Activated by Lysosomal Proteases.Deletion of a 197-Amino-Acid Region in the N-Terminal Domain of Spike Protein Attenuates Porcine Epidemic Diarrhea Virus in Piglets.Isolation and characterization of porcine deltacoronavirus from pigs with diarrhea in the United States Identification of two mutation sites in spike and envelope proteins mediating optimal cellular infection of porcine epidemic diarrhea virus from different pathways.Cell Attachment Domains of the Porcine Epidemic Diarrhea Virus Spike Protein Are Key Targets of Neutralizing Antibodies.Immunogenicity and antigenic relationships among spike proteins of porcine epidemic diarrhea virus subtypes G1 and G2.A Single Point Mutation Creating a Furin Cleavage Site in the Spike Protein Renders Porcine Epidemic Diarrhea Coronavirus Trypsin Independent for Cell Entry and Fusion.Phylogenetic Analysis of the Spike (S) Gene of the New Variants of Porcine Epidemic Diarrhoea Virus in Taiwan.Antigenic relationships among porcine epidemic diarrhea virus and transmissible gastroenteritis virus strains.Glycan shield and fusion activation of a deltacoronavirus spike glycoprotein fine-tuned for enteric infections.Trypsin-independent porcine epidemic diarrhea virus US strain with altered virus entry mechanism.Oral Delivery of Probiotics Expressing Dendritic Cell-Targeting Peptide Fused with Porcine Epidemic Diarrhea Virus COE Antigen: A Promising Vaccine Strategy against PEDV.The S gene is necessary but not sufficient for the virulence of porcine epidemic diarrhea virus novel variant strain BJ2011C.Display of Porcine Epidemic Diarrhea Virus Spike Protein on Baculovirus to Improve Immunogenicity and Protective Efficacy

P2860

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P2860

Proteolytic activation of the porcine epidemic diarrhea coronavirus spike fusion protein by trypsin in cell culture.

http://www.wikidata.org/entity/Q41975503

description

2014 nî lūn-bûn

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2014年の論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年论文

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2014年论文

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2014年论文

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name

Proteolytic activation of the ...... in by trypsin in cell culture.

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Proteolytic activation of the ...... in by trypsin in cell culture.

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Proteolytic activation of the ...... in by trypsin in cell culture.

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Journal of Virology

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Proteolytic activation of the ...... in by trypsin in cell culture.

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P2093

Lione Willems

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Oliver Wicht

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Richard W Wubbolts

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Tom J Meuleman

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Wentao Li

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P2860

Proteolytic activation of influenza viruses by serine proteases TMPRSS2 and HAT from human airway epithelium

Mechanisms of coronavirus cell entry mediated by the viral spike protein

Host cell entry of respiratory syncytial virus involves macropinocytosis followed by proteolytic activation of the F protein

The Coronavirus Spike Protein Is a Class I Virus Fusion Protein: Structural and Functional Characterization of the Fusion Core Complex

Viral membrane fusion

Structures and Mechanisms of Viral Membrane Fusion Proteins: Multiple Variations on a Common Theme

Influenza and SARS-coronavirus activating proteases TMPRSS2 and HAT are expressed at multiple sites in human respiratory and gastrointestinal tracts

Host envelope glycoprotein processing proteases are indispensable for entry into human cells by seasonal and highly pathogenic avian influenza viruses.

Proteolytic activation of the SARS-coronavirus spike protein: cutting enzymes at the cutting edge of antiviral research.

Efficient activation of the severe acute respiratory syndrome coronavirus spike protein by the transmembrane protease TMPRSS2.

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7952-7961

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scholarly article

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10.1128/JVI.00297-14

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14

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88

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Frank J M van Kuppeveld

Peter J M Rottier

Berend Jan Bosch

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2014-05-07T00:00:00Z

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24807723

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Afọ ọsịsa

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4097775

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