Proteolytic activation of influenza viruses by serine proteases TMPRSS2 and HAT from human airway epithelium - sprookjes - yvandenbroek - TriplyDB

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

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

http://www.wikidata.org/entity/Q24671018

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A transmembrane serine protease is linked to the severe acute respiratory syndrome coronavirus receptor and activates virus entry TMPRSS2 and ADAM17 cleave ACE2 differentially and only proteolysis by TMPRSS2 augments entry driven by the severe acute respiratory syndrome coronavirus spike protein Influenza virus pathogenicity regulated by host cellular proteases, cytokines and metabolites, and its therapeutic options Mechanisms of coronavirus cell entry mediated by the viral spike protein Mechanisms of hemagglutinin targeted influenza virus neutralization Plasminogen controls inflammation and pathogenesis of influenza virus infections via fibrinolysis Ifitm3 limits the severity of acute influenza in mice Insights 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 Cleavage Differentiated human alveolar type II cells secrete antiviral IL-29 (IFN-lambda 1) in response to influenza A infection MicroRNA regulation of human protease genes essential for influenza virus replication Influenza and SARS-coronavirus activating proteases TMPRSS2 and HAT are expressed at multiple sites in human respiratory and gastrointestinal tracts Innate immune response of human alveolar macrophages during influenza A infection Influenza hemagglutinin stem-fragment immunogen elicits broadly neutralizing antibodies and confers heterologous protection 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.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 course Inhibition 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 Subtype Molecular pathogenesis of H5 highly pathogenic avian influenza: the role of the haemagglutinin cleavage site motif Cleavage of influenza virus hemagglutinin by airway proteases TMPRSS2 and HAT differs in subcellular localization and susceptibility to protease inhibitors Cross-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 eggs Inhibition 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 infection Matriptase, 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 adaptation Synthetic 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

http://www.wikidata.org/entity/Q24671018

description

2006 nî lūn-bûn

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2006 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年論文

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2006年论文

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name

Proteolytic activation of infl ...... T from human airway epithelium

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Proteolytic activation of infl ...... T from human airway epithelium

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Proteolytic activation of infl ...... T from human airway epithelium

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type

label

Proteolytic activation of infl ...... T from human airway epithelium

@ast

Proteolytic activation of infl ...... T from human airway epithelium

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Proteolytic activation of infl ...... T from human airway epithelium

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prefLabel

Proteolytic activation of infl ...... T from human airway epithelium

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Proteolytic activation of infl ...... T from human airway epithelium

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Proteolytic activation of infl ...... T from human airway epithelium

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Journal of Virology

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Proteolytic activation of infl ...... T from human airway epithelium

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P2093

Eva Böttcher

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Michaela Beyerle

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Mikhail Matrosovich

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Tatyana Matrosovich

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Wolfgang Garten

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P2860

Pandemic Threat Posed by Avian Influenza A Viruses

Cloning and characterization of the cDNA for human airway trypsin-like protease

Cloning of the TMPRSS2 gene, which encodes a novel serine protease with transmembrane, LDLRA, and SRCR domains and maps to 21q22.3

The membrane-anchored serine protease, TMPRSS2, activates PAR-2 in prostate cancer cells

Efficient selection for high-expression transfectants with a novel eukaryotic vector

Type II transmembrane serine proteases. Insights into an emerging class of cell surface proteolytic enzymes

Localization of human airway trypsin-like protease in the airway: an immunohistochemical study

Membrane anchored serine proteases: a rapidly expanding group of cell surface proteolytic enzymes with potential roles in cancer

Human airway trypsin-like protease stimulates human bronchial fibroblast proliferation in a protease-activated receptor-2-dependent pathway

Purification, characterization, and localization of a novel trypsin-like protease found in the human airway

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9896-8

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scholarly article

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172011

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10.1128/JVI.01118-06

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P433

19

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80

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Hans-Dieter Klenk

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2006-10-01T00:00:00Z

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16973594

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P932

1617224

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