TMPRSS2 and TMPRSS4 facilitate trypsin-independent spread of influenza virus in Caco-2 cells.
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 proteinPlasminogen controls inflammation and pathogenesis of influenza virus infections via fibrinolysisDecoding protein networks during virus entry by quantitative proteomicsInfluenza and SARS-coronavirus activating proteases TMPRSS2 and HAT are expressed at multiple sites in human respiratory and gastrointestinal tractsProteolytic 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.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.Pseudotype-based neutralization assays for influenza: a systematic analysis.Inhibition of influenza virus infection in human airway cell cultures by an antisense peptide-conjugated morpholino oligomer targeting the hemagglutinin-activating protease TMPRSS2.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.Matriptase proteolytically activates influenza virus and promotes multicycle replication in the human airway epithelium.The host protease TMPRSS2 plays a major role in in vivo replication of emerging H7N9 and seasonal influenza viruses.Non-human primate orthologues of TMPRSS2 cleave and activate the influenza virus hemagglutinin.TMPRSS2 and MSPL Facilitate Trypsin-Independent Porcine Epidemic Diarrhea Virus Replication in Vero Cells.A chemokine gene expression signature derived from meta-analysis predicts the pathogenicity of viral respiratory infectionsReceptor usage and cell entry of bat coronavirus HKU4 provide insight into bat-to-human transmission of MERS coronavirus.Influenza virus-mediated membrane fusion: determinants of hemagglutinin fusogenic activity and experimental approaches for assessing virus fusion.Distinct gene loci control the host response to influenza H1N1 virus infection in a time-dependent manner.Influenza A virus does not encode a tetherin antagonist with Vpu-like activity and induces IFN-dependent tetherin expression in infected cellsHost cell entry of Middle East respiratory syndrome coronavirus after two-step, furin-mediated activation of the spike protein.PTB binds to the 3' untranslated region of the human astrovirus type 8: a possible role in viral replicationInhibition of lung serine proteases in mice: a potentially new approach to control influenza infection.Role of the spike glycoprotein of human Middle East respiratory syndrome coronavirus (MERS-CoV) in virus entry and syncytia formation.Evidence that TMPRSS2 activates the severe acute respiratory syndrome coronavirus spike protein for membrane fusion and reduces viral control by the humoral immune response.A serpin shapes the extracellular environment to prevent influenza A virus maturationInfluenza A virus encoding secreted Gaussia luciferase as useful tool to analyze viral replication and its inhibition by antiviral compounds and cellular proteins.Cleavage and activation of the severe acute respiratory syndrome coronavirus spike protein by human airway trypsin-like proteaseImpact of host proteases on reovirus infection in the respiratory tract.Epithelial Sodium Channel-Mediated Sodium Transport Is Not Dependent on the Membrane-Bound Serine Protease CAP2/Tmprss4.Simultaneous treatment of human bronchial epithelial cells with serine and cysteine protease inhibitors prevents severe acute respiratory syndrome coronavirus entry.Respiratory protease/antiprotease balance determines susceptibility to viral infection and can be modified by nutritional antioxidantsCleavage activation of the human-adapted influenza virus subtypes by matriptase reveals both subtype and strain specificities.The human Transmembrane Protease Serine 2 is necessary for the production of Group 2 influenza A virus pseudotypes.Acquisition of a novel eleven amino acid insertion directly N-terminal to a tetrabasic cleavage site confers intracellular cleavage of an H7N7 influenza virus hemagglutinin.The Proteolytic Activation of (H3N2) Influenza A Virus Hemagglutinin Is Facilitated by Different Type II Transmembrane Serine Proteases.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.Cleavage activation of human-adapted influenza virus subtypes by kallikrein-related peptidases 5 and 12
P2860
Q24306622-D95F898C-7640-4F14-B835-523C067F4C88Q24339582-EB3B3A63-AC42-4207-854D-141140C648B8Q27335814-F5567B9C-B995-4068-8BA1-38352E0C9F0DQ27469058-EAD1009F-2972-44BD-B010-7959793A9432Q28730201-B201C061-3379-4F0C-8F74-BB7190E36355Q30354466-3CC993FE-F550-4F00-8663-9C8F76001BCCQ30356975-729E3EC1-5DED-4E1A-A238-9A11AAE55BE5Q30364158-DD675347-87A4-4C75-BC06-828F806881DCQ30365699-DAD0BEC6-0B8A-4C80-B9B7-095399AA7865Q30374662-C90B4270-8E54-4A70-94A1-0C1987D29B9FQ30396910-A266FFAB-2393-448E-908E-5C60D1924802Q30415297-43D55DBB-D3A5-434D-A5B5-A2B3EBE486D9Q30424187-11238F8C-9770-4F2E-865B-F5FE935358B5Q30426551-7E610461-7E2D-4F84-9ADF-549DEA5FA6D7Q33602849-4ED3E4E4-8DDA-4EB5-9462-258845AF2E21Q33663432-6DF48D70-7C36-4A3C-927C-FEA6796D52FBQ33753975-CBD02F17-33C4-4370-A96B-556E07332FABQ34107952-A1800D07-3B48-412E-9F4B-276645D6EADCQ34120263-5BF13B19-72CA-424C-9519-2ACF3F7EEF67Q34360974-573F81C0-ED41-48CE-95BB-A2959F6A4229Q34385369-9A17C6B7-6645-43A5-A235-F5A5FDAEA3B8Q34405097-0CA70A1D-BB4C-481B-843A-352ADAFD8BFEQ34408840-A25C3347-C7E8-4827-9371-F7163F0FC5F1Q34535820-7B04299E-282E-4E5B-8B3E-073BE3921ADAQ34556193-B024A2BD-C471-4AA5-ADE9-AE9F97DF25E6Q35009468-3FD8D527-5A53-4742-A7F8-A10641CACB00Q35076795-CB37E81D-30AC-41C5-8557-4D0FA195569DQ35083702-D2ED917C-30B2-45EC-8E82-A1EA381C5ADEQ35171172-15870BE3-B07D-4AAD-BC36-E16C7C2EEBE6Q35599437-CE180F04-C4A5-4B4F-BB5D-5A8159F227BBQ35665861-0A0335B4-DD63-4881-B6FF-01300C668890Q35756115-9B504142-342B-4C63-B291-6DCC57D247D9Q36086649-77B4A2C4-5034-4761-B0D5-E10C1F27EE6AQ36104532-323286AC-FCF0-49D9-BF1A-43A0A570AC7EQ36276614-F8FE7E8F-85D3-4BE1-AA2D-61427B8FDE20Q36734159-0E959FCF-9EC1-47CB-B884-11E81EBFBFC0Q36765363-2C4B3C2B-15B1-418E-98EC-62FFB730F6AAQ36811980-28A31618-CF46-433A-84F9-97D7F4A701BFQ36827306-C72D820C-3B07-4D8D-933A-ED57C7C6E9F8Q36929003-6567D896-BBC8-4891-B5F7-CAA451C3C22A
P2860
TMPRSS2 and TMPRSS4 facilitate trypsin-independent spread of influenza virus in Caco-2 cells.
description
2010 nî lūn-bûn
@nan
2010 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
TMPRSS2 and TMPRSS4 facilitate ...... fluenza virus in Caco-2 cells.
@ast
TMPRSS2 and TMPRSS4 facilitate ...... fluenza virus in Caco-2 cells.
@en
TMPRSS2 and TMPRSS4 facilitate ...... fluenza virus in Caco-2 cells.
@nl
type
label
TMPRSS2 and TMPRSS4 facilitate ...... fluenza virus in Caco-2 cells.
@ast
TMPRSS2 and TMPRSS4 facilitate ...... fluenza virus in Caco-2 cells.
@en
TMPRSS2 and TMPRSS4 facilitate ...... fluenza virus in Caco-2 cells.
@nl
prefLabel
TMPRSS2 and TMPRSS4 facilitate ...... fluenza virus in Caco-2 cells.
@ast
TMPRSS2 and TMPRSS4 facilitate ...... fluenza virus in Caco-2 cells.
@en
TMPRSS2 and TMPRSS4 facilitate ...... fluenza virus in Caco-2 cells.
@nl
P2093
P2860
P50
P356
P1433
P1476
TMPRSS2 and TMPRSS4 facilitate ...... nfluenza virus in Caco-2 cells
@en
P2093
Heike Schneider
Ilona Glowacka
Imke Steffen
Paul Allen
Paulina Blazejewska
Simon Danisch
So-Young Choi
Stephanie Bertram
Youngwoo Park
P2860
P304
10016-10025
P356
10.1128/JVI.00239-10
P407
P577
2010-07-14T00:00:00Z