Type II transmembrane serine proteases in cancer and viral infections.
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Combinatorial Enzyme Design Probes Allostery and Cooperativity in the Trypsin FoldMatriptase proteolytically activates influenza virus and promotes multicycle replication in the human airway epithelium.Plasmin-mediated activation of pandemic H1N1 influenza virus hemagglutinin is independent of the viral neuraminidase.The production and development of H7 Influenza virus pseudotypes for the study of humoral responses against avian virusesEfficient activation of the severe acute respiratory syndrome coronavirus spike protein by the transmembrane protease TMPRSS2.Changes in mouse uterine transcriptome in estrus and proestrus.Modifications to the hemagglutinin cleavage site control the virulence of a neurotropic H1N1 influenza virusTMPRSS2 and TMPRSS4 facilitate trypsin-independent spread of influenza virus in Caco-2 cells.Evidence that TMPRSS2 activates the severe acute respiratory syndrome coronavirus spike protein for membrane fusion and reduces viral control by the humoral immune response.Cleavage and activation of the severe acute respiratory syndrome coronavirus spike protein by human airway trypsin-like proteaseLow expression levels of hepsin and TMPRSS3 are associated with poor breast cancer survivalTMPRSS3 is a novel poor prognostic factor for breast cancerTMPRSS4 facilitates epithelial-mesenchymal transition of hepatocellular carcinoma and is a predictive marker for poor prognosis of patients after curative resection.A novel cytoplasmic tail motif regulates mouse corin expression on the cell surface.Simultaneous treatment of human bronchial epithelial cells with serine and cysteine protease inhibitors prevents severe acute respiratory syndrome coronavirus entry.Cleavage activation of the human-adapted influenza virus subtypes by matriptase reveals both subtype and strain specificities.The cutting edge: membrane-anchored serine protease activities in the pericellular microenvironment.TMPRSS2 is an activating protease for respiratory parainfluenza viruses.Middle East respiratory syndrome coronavirus infection mediated by the transmembrane serine protease TMPRSS2.TMPRSS4 correlates with colorectal cancer pathological stage and regulates cell proliferation and self-renewal ability.Overexpression of TMPRSS4 promotes tumor proliferation and aggressiveness in breast cancerThe Transmembrane Serine Protease HAT-like 4 Is Important for Epidermal Barrier Function to Prevent Body Fluid Loss.TMPRSS13, a type II transmembrane serine protease, is inhibited by hepatocyte growth factor activator inhibitor type 1 and activates pro-hepatocyte growth factor.Transmembrane serine protease TMPRSS2 activates hepatitis C virus infection.Type II transmembrane serine proteases as potential target for anti-influenza drug discovery.Antithrombin controls tumor migration, invasion and angiogenesis by inhibition of enteropeptidase.Peptide self-assembly assisted signal labeling for an electrochemical assay of protease activity.Cell-surface marker discovery for lung cancer.Enterokinase Enhances Influenza A Virus Infection by Activating Trypsinogen in Human Cell Lines.
P2860
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P2860
Type II transmembrane serine proteases in cancer and viral infections.
description
article científic
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article scientifique
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articolo scientifico
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artigo científico
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bilimsel makale
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scientific article published on 04 July 2009
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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
Type II transmembrane serine proteases in cancer and viral infections.
@en
Type II transmembrane serine proteases in cancer and viral infections.
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type
label
Type II transmembrane serine proteases in cancer and viral infections.
@en
Type II transmembrane serine proteases in cancer and viral infections.
@nl
prefLabel
Type II transmembrane serine proteases in cancer and viral infections.
@en
Type II transmembrane serine proteases in cancer and viral infections.
@nl
P2093
P1476
Type II transmembrane serine proteases in cancer and viral infections
@en
P2093
Ilona Glowacka
So-Young Choi
Stephanie Bertram
Young Woo Park
P304
P356
10.1016/J.MOLMED.2009.05.003
P577
2009-07-04T00:00:00Z