Protease-mediated entry via the endosome of human coronavirus 229E.
about
Mechanisms of viral entry: sneaking in the front doorProteolytic activation of the SARS-coronavirus spike protein: cutting enzymes at the cutting edge of antiviral research.Two-step conformational changes in a coronavirus envelope glycoprotein mediated by receptor binding and proteolysisTransport to late endosomes is required for efficient reovirus infectionInsulin degrading enzyme induces a conformational change in varicella-zoster virus gE, and enhances virus infectivity and stabilityTMPRSS2 and MSPL Facilitate Trypsin-Independent Porcine Epidemic Diarrhea Virus Replication in Vero Cells.Different potential of C-type lectin-mediated entry between Marburg virus strainsRole of the spike glycoprotein of human Middle East respiratory syndrome coronavirus (MERS-CoV) in virus entry and syncytia formation.Role of proteases in the release of porcine epidemic diarrhea virus from infected cells.Host cell proteases: Critical determinants of coronavirus tropism and pathogenesisThe Hemagglutinin of Bat-Associated Influenza Viruses Is Activated by TMPRSS2 for pH-Dependent Entry into Bat but Not Human Cells.Simultaneous treatment of human bronchial epithelial cells with serine and cysteine protease inhibitors prevents severe acute respiratory syndrome coronavirus entry.Neutralization interfering antibodies: a "novel" example of humoral immune dysfunction facilitating viral escape?Development of novel entry inhibitors targeting emerging viruses.SARS-coronavirus spike S2 domain flanked by cysteine residues C822 and C833 is important for activation of membrane fusion.The spike protein of the emerging betacoronavirus EMC uses a novel coronavirus receptor for entry, can be activated by TMPRSS2, and is targeted by neutralizing antibodies.Proteolytic activation of the spike protein at a novel RRRR/S motif is implicated in furin-dependent entry, syncytium formation, and infectivity of coronavirus infectious bronchitis virus in cultured cellsMiddle East respiratory syndrome coronavirus infection mediated by the transmembrane serine protease TMPRSS2.Clinical Isolates of Human Coronavirus 229E Bypass the Endosome for Cell Entry.The role of cysteine proteinases and their inhibitors in the host-pathogen cross talk.TMPRSS2 activates the human coronavirus 229E for cathepsin-independent host cell entry and is expressed in viral target cells in the respiratory epithelium.Coronavirus and influenza virus proteolytic priming takes place in tetraspanin-enriched membrane microdomainsProteolytic activation of the porcine epidemic diarrhea coronavirus spike fusion protein by trypsin in cell culture.Possible involvement of infection with human coronavirus 229E, but not NL63, in Kawasaki disease.Receptor-bound porcine epidemic diarrhea virus spike protein cleaved by trypsin induces membrane fusion.Peptide-Based Membrane Fusion Inhibitors Targeting HCoV-229E Spike Protein HR1 and HR2 Domains.Technical considerations for the generation of novel pseudotyped viruses
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Protease-mediated entry via the endosome of human coronavirus 229E.
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
@pt
bilimsel makale
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scientific article published on 29 October 2008
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vedecký článok
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vetenskaplig artikel
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videnskabelig artikel
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vědecký článek
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name
Protease-mediated entry via the endosome of human coronavirus 229E.
@en
Protease-mediated entry via the endosome of human coronavirus 229E.
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type
label
Protease-mediated entry via the endosome of human coronavirus 229E.
@en
Protease-mediated entry via the endosome of human coronavirus 229E.
@nl
prefLabel
Protease-mediated entry via the endosome of human coronavirus 229E.
@en
Protease-mediated entry via the endosome of human coronavirus 229E.
@nl
P2093
P2860
P356
P1433
P1476
Protease-mediated entry via the endosome of human coronavirus 229E.
@en
P2093
Fumihiro Taguchi
Kazuya Shirato
Miyuki Kawase
Shutoku Matsuyama
P2860
P304
P356
10.1128/JVI.01933-08
P407
P577
2008-10-29T00:00:00Z