Proteolytic activation of influenza viruses by serine proteases TMPRSS2 and HAT from human airway epithelium
about
A transmembrane serine protease is linked to the severe acute respiratory syndrome coronavirus receptor and activates virus entryTMPRSS2 and ADAM17 cleave ACE2 differentially and only proteolysis by TMPRSS2 augments entry driven by the severe acute respiratory syndrome coronavirus spike proteinInfluenza virus pathogenicity regulated by host cellular proteases, cytokines and metabolites, and its therapeutic optionsMechanisms of coronavirus cell entry mediated by the viral spike proteinMechanisms of hemagglutinin targeted influenza virus neutralizationPlasminogen controls inflammation and pathogenesis of influenza virus infections via fibrinolysisIfitm3 limits the severity of acute influenza in miceInsights into Avian Influenza Virus Pathogenicity: the Hemagglutinin Precursor HA0 of Subtype H16 Has an Alpha-Helix Structure in Its Cleavage Site with Inefficient HA1/HA2 CleavageDifferentiated human alveolar type II cells secrete antiviral IL-29 (IFN-lambda 1) in response to influenza A infectionMicroRNA regulation of human protease genes essential for influenza virus replicationInfluenza and SARS-coronavirus activating proteases TMPRSS2 and HAT are expressed at multiple sites in human respiratory and gastrointestinal tractsInnate immune response of human alveolar macrophages during influenza A infectionInfluenza hemagglutinin stem-fragment immunogen elicits broadly neutralizing antibodies and confers heterologous protectionHost 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.Tmprss2 is essential for influenza H1N1 virus pathogenesis in mice.Antigen-specific H1N1 influenza antibody responses in acute respiratory tract infections and their relation to influenza infection and disease courseInhibition of influenza virus infection and hemagglutinin cleavage by the protease inhibitor HAI-2.DESC1 and MSPL activate influenza A viruses and emerging coronaviruses for host cell entry.Identification of TMPRSS2 as a Susceptibility Gene for Severe 2009 Pandemic A(H1N1) Influenza and A(H7N9) Influenza.Pseudotype-based neutralization assays for influenza: a systematic analysis.Interplay between influenza A virus and host factors: targets for antiviral intervention.Hemagglutinin Sequence Conservation Guided Stem Immunogen Design from Influenza A H3 SubtypeMolecular pathogenesis of H5 highly pathogenic avian influenza: the role of the haemagglutinin cleavage site motifCleavage of influenza virus hemagglutinin by airway proteases TMPRSS2 and HAT differs in subcellular localization and susceptibility to protease inhibitorsCross-neutralization of 1918 and 2009 influenza viruses: role of glycans in viral evolution and vaccine design.TMPRSS2 Independency for Haemagglutinin Cleavage In Vivo Differentiates Influenza B Virus from Influenza A Virus.Mutations at positions 186 and 194 in the HA gene of the 2009 H1N1 pandemic influenza virus improve replication in cell culture and eggsInhibition of influenza virus infection in human airway cell cultures by an antisense peptide-conjugated morpholino oligomer targeting the hemagglutinin-activating protease TMPRSS2.Molecular mechanisms of interspecies transmission and pathogenicity of influenza viruses: Lessons from the 2009 pandemic.A peptide-based approach to evaluate the adaptability of influenza A virus to humans based on its hemagglutinin proteolytic cleavage site.Exposure to ozone modulates human airway protease/antiprotease balance contributing to increased influenza A infectionMatriptase, HAT, and TMPRSS2 activate the hemagglutinin of H9N2 influenza A viruses.[Evolution and infection biology of new influenza A viruses with pandemic potential].Matriptase proteolytically activates influenza virus and promotes multicycle replication in the human airway epithelium.H5N1 pathogenesis studies in mammalian models.Influenza HA subtypes demonstrate divergent phenotypes for cleavage activation and pH of fusion: implications for host range and adaptationSynthetic generation of influenza vaccine viruses for rapid response to pandemics.Efficient activation of the severe acute respiratory syndrome coronavirus spike protein by the transmembrane protease TMPRSS2.Cytopathogenesis of Sendai virus in well-differentiated primary pediatric bronchial epithelial cells.
P2860
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P2860
Proteolytic activation of influenza viruses by serine proteases TMPRSS2 and HAT from human airway epithelium
description
2006 nî lūn-bûn
@nan
2006 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Proteolytic activation of infl ...... T from human airway epithelium
@ast
Proteolytic activation of infl ...... T from human airway epithelium
@en
Proteolytic activation of infl ...... T from human airway epithelium
@nl
type
label
Proteolytic activation of infl ...... T from human airway epithelium
@ast
Proteolytic activation of infl ...... T from human airway epithelium
@en
Proteolytic activation of infl ...... T from human airway epithelium
@nl
prefLabel
Proteolytic activation of infl ...... T from human airway epithelium
@ast
Proteolytic activation of infl ...... T from human airway epithelium
@en
Proteolytic activation of infl ...... T from human airway epithelium
@nl
P2093
P2860
P3181
P356
P1433
P1476
Proteolytic activation of infl ...... T from human airway epithelium
@en
P2093
Eva Böttcher
Michaela Beyerle
Mikhail Matrosovich
Tatyana Matrosovich
Wolfgang Garten
P2860
P304
P3181
P356
10.1128/JVI.01118-06
P407
P577
2006-10-01T00:00:00Z