Phenotypic analysis of mice lacking the Tmprss2-encoded protease
about
A transmembrane serine protease is linked to the severe acute respiratory syndrome coronavirus receptor and activates virus entryThree-color FISH analysis of TMPRSS2/ERG fusions in prostate cancer indicates that genomic microdeletion of chromosome 21 is associated with rearrangementInfluenza 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 proprotein convertases abrogates processing of the middle eastern respiratory syndrome coronavirus spike protein in infected cells but does not reduce viral infectivity.DESC1 and MSPL activate influenza A viruses and emerging coronaviruses for host cell entry.Inhibition of influenza virus infection in human airway cell cultures by an antisense peptide-conjugated morpholino oligomer targeting the hemagglutinin-activating protease TMPRSS2.The host protease TMPRSS2 plays a major role in in vivo replication of emerging H7N9 and seasonal influenza viruses.Quantitative expression of TMPRSS2 transcript in prostate tumor cells reflects TMPRSS2-ERG fusion status.Non-human primate orthologues of TMPRSS2 cleave and activate the influenza virus hemagglutinin.TMPRSS2, a serine protease expressed in the prostate on the apical surface of luminal epithelial cells and released into semen in prostasomes, is misregulated in prostate cancer cellsMembrane-anchored serine proteases in vertebrate cell and developmental biologyExpression and genetic loss of function analysis of the HAT/DESC cluster proteases TMPRSS11A and HATTMPRSS2 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.The androgen-regulated protease TMPRSS2 activates a proteolytic cascade involving components of the tumor microenvironment and promotes prostate cancer metastasis.Ready, set, fuse! The coronavirus spike protein and acquisition of fusion competenceA Tmprss2-CreERT2 Knock-In Mouse Model for Cancer Genetic Studies on Prostate and Colon.The Proteolytic Activation of (H3N2) Influenza A Virus Hemagglutinin Is Facilitated by Different Type II Transmembrane Serine Proteases.The cutting edge: membrane-anchored serine protease activities in the pericellular microenvironment.Membrane-anchored serine proteases in health and disease.Type II transmembrane serine proteases as potential targets for cancer therapy.Recurrent gene fusions in prostate cancerTMPRSS2 is an activating protease for respiratory parainfluenza viruses.Matriptase-2 (TMPRSS6): a proteolytic regulator of iron homeostasisA proteolytic modification of AIM promotes its renal excretion.TMPRSS2 is a host factor that is essential for pneumotropism and pathogenicity of H7N9 influenza A virus in mice.Activation of influenza viruses by proteases from host cells and bacteria in the human airway epithelium.The oncogene ERG: a key factor in prostate cancer.Androgen receptor: acting in the three-dimensional chromatin landscape of prostate cancer cells.TMPRSS2 Isoform 1 Activates Respiratory Viruses and Is Expressed in Viral Target Cells.The role of type II transmembrane serine protease-mediated signaling in cancer.TMPRSS2 activates the human coronavirus 229E for cathepsin-independent host cell entry and is expressed in viral target cells in the respiratory epithelium.Identification of the first synthetic inhibitors of the type II transmembrane serine protease TMPRSS2 suitable for inhibition of influenza virus activation.Mutation G827R in matriptase causing autosomal recessive ichthyosis with hypotrichosis yields an inactive protease.Type II transmembrane serine proteases as potential target for anti-influenza drug discovery.In vitro characterization of TMPRSS2 inhibition in IPEC-J2 cells.Coronavirus and influenza virus proteolytic priming takes place in tetraspanin-enriched membrane microdomainsActivation of influenza A viruses by host proteases from swine airway epithelium
P2860
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P2860
Phenotypic analysis of mice lacking the Tmprss2-encoded protease
description
2006 nî lūn-bûn
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2006 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի փետրվարին 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
Phenotypic analysis of mice lacking the Tmprss2-encoded protease
@ast
Phenotypic analysis of mice lacking the Tmprss2-encoded protease
@en
Phenotypic analysis of mice lacking the Tmprss2-encoded protease
@nl
type
label
Phenotypic analysis of mice lacking the Tmprss2-encoded protease
@ast
Phenotypic analysis of mice lacking the Tmprss2-encoded protease
@en
Phenotypic analysis of mice lacking the Tmprss2-encoded protease
@nl
prefLabel
Phenotypic analysis of mice lacking the Tmprss2-encoded protease
@ast
Phenotypic analysis of mice lacking the Tmprss2-encoded protease
@en
Phenotypic analysis of mice lacking the Tmprss2-encoded protease
@nl
P2093
P2860
P1476
Phenotypic analysis of mice lacking the Tmprss2-encoded protease
@en
P2093
Cynthia Heinlein
Peter S Nelson
Robert C Hackman
P2860
P304
P356
10.1128/MCB.26.3.965-975.2006
P407
P577
2006-02-01T00:00:00Z