Identification of the first synthetic inhibitors of the type II transmembrane serine protease TMPRSS2 suitable for inhibition of influenza virus activation.
about
Inhibition of Matriptase Activity Results in Decreased Intestinal Epithelial Monolayer Integrity In VitroProteolytic activation of the SARS-coronavirus spike protein: cutting enzymes at the cutting edge of antiviral research.DESC1 and MSPL activate influenza A viruses and emerging coronaviruses for host cell entry.Interplay between influenza A virus and host factors: targets for antiviral intervention.Type II transmembrane serine proteases as potential targets for cancer therapy.TMPRSS2 is a host factor that is essential for pneumotropism and pathogenicity of H7N9 influenza A virus in mice.New-generation screening assays for the detection of anti-influenza compounds targeting viral and host functions.Antiviral strategies against influenza virus: towards new therapeutic approaches.Interaction exists between matriptase inhibitors and intestinal epithelial cells.The role of type II transmembrane serine protease-mediated signaling in cancer.Type II transmembrane serine proteases as potential target for anti-influenza drug discovery.Limiting the Number of Potential Binding Modes by Introducing Symmetry into Ligands: Structure-Based Design of Inhibitors for Trypsin-Like Serine Proteases.In vitro characterization of TMPRSS2 inhibition in IPEC-J2 cells.Activation of influenza A viruses by host proteases from swine airway epitheliumFunctional analysis of corin protein domains required for PCSK6-mediated activation.Thrombin-Inhibiting Anticoagulant Liposomes: Development and Characterization.Changing the selectivity profile - from substrate analog inhibitors of thrombin and factor Xa to potent matriptase inhibitors.
P2860
Q28550435-F2B94C1A-6B47-4746-A861-D8C495C42D11Q30354466-A2674A6B-F316-4323-94B9-00FF543359D4Q30365699-52894B40-4208-42B9-B759-AA43BE44C35BQ30375026-94F07207-3DFD-495A-A2C0-1D3A7CE04C33Q37168351-0C533001-085D-49AD-B860-DF0E5FD77562Q37713993-44EBFC87-4FDB-4A24-B2A0-FAF5EB71DFB9Q38128093-CAB7B7D2-FF2F-4A52-B803-76A4EF55C484Q38202012-8E774477-94C4-4429-872D-965563125EAEQ38859369-1839DF2C-3465-48C2-8EA9-63A07DF5881AQ39015415-A2B7FCD6-FA57-4591-A7B5-8FDDD326FCC8Q40058871-2B4C2373-12BC-490C-BA93-A032E1474438Q40254260-843D429A-D4A9-4A30-B34E-0ACB1E27ABBFQ40640375-28081FEB-7DB8-44F3-BDD3-BCD274333D0DQ41820530-772A5E98-AC91-46EA-B11C-37E8CA5C9022Q47359170-582C84FF-1A6B-4099-90A1-A6AE2AC8E204Q48089546-9710857D-F463-49F9-BD28-C7C930F27888Q53099256-10C81431-4B74-4B6D-B6B6-73F21B51C101
P2860
Identification of the first synthetic inhibitors of the type II transmembrane serine protease TMPRSS2 suitable for inhibition of influenza virus activation.
description
2013 nî lūn-bûn
@nan
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
2013年论文
@zh
2013年论文
@zh-cn
name
Identification of the first sy ...... of influenza virus activation.
@en
Identification of the first sy ...... of influenza virus activation.
@nl
type
label
Identification of the first sy ...... of influenza virus activation.
@en
Identification of the first sy ...... of influenza virus activation.
@nl
prefLabel
Identification of the first sy ...... of influenza virus activation.
@en
Identification of the first sy ...... of influenza virus activation.
@nl
P2093
P2860
P356
P1433
P1476
Identification of the first sy ...... of influenza virus activation.
@en
P2093
Daniela Meyer
Eva Böttcher-Friebertshäuser
Frank Sielaff
Maya Hammami
Torsten Steinmetzer
Wolfgang Garten
P2860
P304
P356
10.1042/BJ20130101
P407
P577
2013-06-01T00:00:00Z