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Index « MeshFr.i » - entrée « Serine endopeptidases »
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List of bibliographic references indexed by Serine endopeptidases

Number of relevant bibliographic references: 23.
[0-20] [0 - 20][0 - 23][20-22][20-40]
Ident.Authors (with country if any)Title
000512 (2020) Sarah E. Henrickson [États-Unis]Learning from our immunological history: What can SARS-CoV teach us about SARS-CoV-2?
000675 (2020) Shutoku Matsuyama [Japon] ; Naganori Nao [Japon] ; Kazuya Shirato [Japon] ; Miyuki Kawase [Japon] ; Shinji Saito [Japon] ; Ikuyo Takayama [Japon] ; Noriyo Nagata [Japon] ; Tsuyoshi Sekizuka [Japon] ; Hiroshi Katoh [Japon] ; Fumihiro Kato [Japon] ; Masafumi Sakata [Japon] ; Maino Tahara [Japon] ; Satoshi Kutsuna [Japon] ; Norio Ohmagari [Japon] ; Makoto Kuroda [Japon] ; Tadaki Suzuki [Japon] ; Tsutomu Kageyama [Japon] ; Makoto Takeda [Japon]Enhanced isolation of SARS-CoV-2 by TMPRSS2-expressing cells.
000A85 (2019) Naoko Iwata-Yoshikawa [Japon] ; Tadashi Okamura [Japon] ; Yukiko Shimizu [Japon] ; Hideki Hasegawa [Japon] ; Makoto Takeda [Japon] ; Noriyo Nagata [Japon]TMPRSS2 Contributes to Virus Spread and Immunopathology in the Airways of Murine Models after Coronavirus Infection.
000D45 (2017) Woo-Jin Shin [États-Unis] ; Baik Lin Seong [Corée du Sud]Type II transmembrane serine proteases as potential target for anti-influenza drug discovery.
000E55 (2017) Lennart Michel Reinke [Allemagne] ; Martin Spiegel [Allemagne] ; Teresa Plegge [Allemagne] ; Anika Hartleib [Allemagne] ; Inga Nehlmeier [Allemagne] ; Stefanie Gierer [Allemagne] ; Markus Hoffmann [Allemagne] ; Heike Hofmann-Winkler [Allemagne] ; Michael Winkler [Allemagne] ; Stefan Pöhlmann [Allemagne]Different residues in the SARS-CoV spike protein determine cleavage and activation by the host cell protease TMPRSS2.
000E63 (2017) Kazuya Shirato [Japon] ; Kazuhiko Kanou [Japon] ; Miyuki Kawase [Japon] ; Shutoku Matsuyama [Japon]Clinical Isolates of Human Coronavirus 229E Bypass the Endosome for Cell Entry.
000E80 (2017) Ali A. Rabaan [Arabie saoudite] ; Shamsah H. Alahmed [Arabie saoudite] ; Ali M. Bazzi [Arabie saoudite] ; Hatem M. Alhani [Arabie saoudite]A review of candidate therapies for Middle East respiratory syndrome from a molecular perspective.
001229 (2015) Pawel Zmora ; Anna-Sophie Moldenhauer ; Heike Hofmann-Winkler ; Stefan PöhlmannTMPRSS2 Isoform 1 Activates Respiratory Viruses and Is Expressed in Viral Target Cells
001266 (2015) Yanchen Zhou [États-Unis] ; Punitha Vedantham [États-Unis] ; Kai Lu [États-Unis] ; Juliet Agudelo [États-Unis] ; Ricardo Carrion [États-Unis] ; Jerritt W. Nunneley [États-Unis] ; Dale Barnard [États-Unis] ; Stefan Pöhlmann [Allemagne] ; James H. Mckerrow [États-Unis] ; Adam R. Renslo [États-Unis] ; Graham Simmons [États-Unis]Protease inhibitors targeting coronavirus and filovirus entry.
001277 (2015) Garvita Gupta [Singapour] ; Liangzhong Lim [Singapour] ; Jianxing Song [Singapour]NMR and MD Studies Reveal That the Isolated Dengue NS3 Protease Is an Intrinsically Disordered Chymotrypsin Fold Which Absolutely Requests NS2B for Correct Folding and Functional Dynamics.
001554 (2014) Adeline Heurich [Allemagne] ; Heike Hofmann-Winkler ; Stefanie Gierer ; Thomas Liepold ; Olaf Jahn ; Stefan PöhlmannTMPRSS2 and ADAM17 cleave ACE2 differentially and only proteolysis by TMPRSS2 augments entry driven by the severe acute respiratory syndrome coronavirus spike protein.
001880 (2013) Graham Simmons [États-Unis] ; Pawel Zmora ; Stefanie Gierer ; Adeline Heurich ; Stefan PöhlmannProteolytic activation of the SARS-coronavirus spike protein: cutting enzymes at the cutting edge of antiviral research.
001920 (2013) Daniela Meyer [Allemagne] ; Frank Sielaff ; Maya Hammami ; Eva Böttcher-Friebertsh User ; Wolfgang Garten ; Torsten SteinmetzerIdentification of the first synthetic inhibitors of the type II transmembrane serine protease TMPRSS2 suitable for inhibition of influenza virus activation.
001D02 (2012) Stephanie Bertram [Allemagne] ; Adeline Heurich [Allemagne] ; Hayley Lavender [Royaume-Uni] ; Stefanie Gierer [Allemagne] ; Simon Danisch [Allemagne] ; Paula Perin [Allemagne] ; Jared M. Lucas [États-Unis] ; Peter S. Nelson [États-Unis] ; Stefan Pöhlmann [Allemagne] ; Elizabeth J. Soilleux [Royaume-Uni]Influenza and SARS-Coronavirus Activating Proteases TMPRSS2 and HAT Are Expressed at Multiple Sites in Human Respiratory and Gastrointestinal Tracts
002003 (2011) Shutoku Matsuyama [Japon][Protease-dependent cell entry mechanism of coronaviruses].
002117 (2011) Ilona Glowacka [Allemagne] ; Stephanie Bertram ; Marcel A. Müller ; Paul Allen ; Elizabeth Soilleux ; Susanne Pfefferle ; Imke Steffen ; Theodros Solomon Tsegaye ; Yuxian He ; Kerstin Gnirss ; Daniela Niemeyer ; Heike Schneider ; Christian Drosten ; Stefan PöhlmannEvidence that TMPRSS2 activates the severe acute respiratory syndrome coronavirus spike protein for membrane fusion and reduces viral control by the humoral immune response.
002145 (2011) Stephanie Bertram [Allemagne] ; Ilona Glowacka ; Marcel A. Müller ; Hayley Lavender ; Kerstin Gnirss ; Inga Nehlmeier ; Daniela Niemeyer ; Yuxian He ; Graham Simmons ; Christian Drosten ; Elizabeth J. Soilleux ; Olaf Jahn ; Imke Steffen ; Stefan PöhlmannCleavage and activation of the severe acute respiratory syndrome coronavirus spike protein by human airway trypsin-like protease.
002157 (2011) Ana Shulla [États-Unis] ; Taylor Heald-Sargent ; Gitanjali Subramanya ; Jincun Zhao ; Stanley Perlman ; Tom GallagherA transmembrane serine protease is linked to the severe acute respiratory syndrome coronavirus receptor and activates virus entry.
002548 (2010) Shutoku Matsuyama [Japon] ; Noriyo Nagata ; Kazuya Shirato ; Miyuki Kawase ; Makoto Takeda ; Fumihiro TaguchiEfficient activation of the severe acute respiratory syndrome coronavirus spike protein by the transmembrane protease TMPRSS2.
003754 (2007) Hsin-Chieh Ma [République populaire de Chine] ; Yi-Yung Ku ; Yi-Ching Hsieh ; Shih-Yen LoCharacterization of the cleavage of signal peptide at the C-terminus of hepatitis C virus core protein by signal peptide peptidase.
003C43 (2006) D N Frick [États-Unis] ; A M I. LamUnderstanding helicases as a means of virus control.

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