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Serine endopeptidases (immunologie) < Serine endopeptidases (métabolisme) < Serine endopeptidases (physiologie)  Facettes :

List of bibliographic references indexed by Serine endopeptidases (métabolisme)

Number of relevant bibliographic references: 21.
[0-20] [0 - 20][0 - 21][20-20][20-40]
Ident.Authors (with country if any)Title
000340 (2019) Zhemin Zhang [République populaire de Chine] ; Qi Huang [République populaire de Chine] ; Xuan Tao [République populaire de Chine] ; Guobing Song [République populaire de Chine] ; Peng Zheng [République populaire de Chine] ; Hongyan Li ; Hongzhe Sun ; Wei Xia [République populaire de Chine]The unique trimeric assembly of the virulence factor HtrA from Helicobacter pylori occurs via N-terminal domain swapping.
000354 (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.
000790 (2018) Pawel Zmora [Allemagne] ; Markus Hoffmann [Allemagne] ; Heike Kollmus [Allemagne] ; Anna-Sophie Moldenhauer [Allemagne] ; Olga Danov ; Armin Braun ; Michael Winkler [Allemagne] ; Klaus Schughart [Allemagne] ; Stefan PöhlmannTMPRSS11A activates the influenza A virus hemagglutinin and the MERS coronavirus spike protein and is insensitive against blockade by HAI-1.
000896 (2018) Shutoku Matsuyama [Japon] ; Kazuya Shirato [Japon] ; Miyuki Kawase [Japon] ; Yutaka Terada [Japon] ; Kengo Kawachi [Japon] ; Shuetsu Fukushi [Japon] ; Wataru Kamitani [Japon]Middle East Respiratory Syndrome Coronavirus Spike Protein Is Not Activated Directly by Cellular Furin during Viral Entry into Target Cells.
000965 (2018) Hannah Kleine-Weber [Allemagne] ; Mahmoud Tarek Elzayat [Allemagne] ; Markus Hoffmann [Allemagne] ; Stefan Pöhlmann [Allemagne]Functional analysis of potential cleavage sites in the MERS-coronavirus spike protein
000B34 (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.
000B43 (2017) James T. Earnest [États-Unis] ; Michael P. Hantak [États-Unis] ; Kun Li [États-Unis] ; Paul B. Mccray [États-Unis] ; Stanley Perlman [États-Unis] ; Tom Gallagher [États-Unis]The tetraspanin CD9 facilitates MERS-coronavirus entry by scaffolding host cell receptors and proteases
000D38 (2017) Yoshiyuki Fukuda [Allemagne] ; Florian Beck [Allemagne] ; Jürgen M. Plitzko [Allemagne] ; Wolfgang Baumeister [Allemagne]In situ structural studies of tripeptidyl peptidase II (TPPII) reveal spatial association with proteasomes.
000F06 (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.
001214 (2016) Mizuki Yamamoto [Japon] ; Shutoku Matsuyama [Japon] ; Xiao Li [République populaire de Chine] ; Makoto Takeda [Japon] ; Yasushi Kawaguchi [Japon] ; Jun-Ichiro Inoue [Japon] ; Zene Matsuda [Japon]Identification of Nafamostat as a Potent Inhibitor of Middle East Respiratory Syndrome Coronavirus S Protein-Mediated Membrane Fusion Using the Split-Protein-Based Cell-Cell Fusion Assay.
001612 (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
001A49 (2014) Shanshan Li ; Rui Wang ; Deyong Li ; Jing Ma ; Heng Li ; Xiaochuan He ; Zengyi Chang ; Yuxiang WengThermal-triggerd Proteinquake Leads to Disassembly of DegP Hexamer as an Imperative Activation Step
001A51 (2014) Kouji Sakai [Japon] ; Yasushi Ami ; Maino Tahara ; Toru Kubota ; Masaki Anraku ; Masako Abe ; Noriko Nakajima ; Tsuyoshi Sekizuka ; Kazuya Shirato ; Yuriko Suzaki ; Akira Ainai ; Yuichiro Nakatsu ; Kazuhiko Kanou ; Kazuya Nakamura ; Tadaki Suzuki ; Katsuhiro Komase ; Eri Nobusawa ; Katsumi Maenaka ; Makoto Kuroda ; Hideki Hasegawa ; Yoshihiro Kawaoka [États-Unis] ; Masato Tashiro ; Makoto TakedaThe host protease TMPRSS2 plays a major role in in vivo replication of emerging H7N9 and seasonal influenza viruses.
001F26 (2013) James W. Marsh ; William B. Lott ; Joel D. A. Tyndall ; Wilhelmina Willa M. HustonProteolytic activation of Chlamydia trachomatis HTRA is mediated by PDZ1 domain interactions with protease domain loops L3 and LC and beta strand β5
001F42 (2013) Kazuya Shirato [Japon] ; Miyuki Kawase ; Shutoku MatsuyamaMiddle East respiratory syndrome coronavirus infection mediated by the transmembrane serine protease TMPRSS2.
002052 (2013) Guido Hansen [Allemagne] ; Rolf HilgenfeldArchitecture and regulation of HtrA-family proteins involved in protein quality control and stress response.
002175 (2013) Graham Simmons [États-Unis] ; Pawel Zmora [Allemagne] ; Stefanie Gierer [Allemagne] ; Adeline Heurich [Allemagne] ; Stefan Pöhlmann [Allemagne]Proteolytic activation of the SARS-coronavirus spike protein: Cutting enzymes at the cutting edge of antiviral research
002451 (2011) Justyna Sawa [Autriche] ; Hélène Malet ; Tobias Krojer ; Flavia Canellas ; Michael Ehrmann ; Tim ClausenMolecular adaptation of the DegQ protease to exert protein quality control in the bacterial cell envelope.
002453 (2011) Catherine Baud [France] ; Irina Gutsche ; Eve Willery ; Diane De Paepe ; Hervé Drobecq ; Martine Gilleron ; Camille Locht ; Marc Jamin ; Françoise Jacob-DubuissonMembrane-associated DegP in Bordetella chaperones a repeat-rich secretory protein.
002629 (2010) Tobias Krojer [Autriche] ; Justyna Sawa ; Robert Huber ; Tim ClausenHtrA proteases have a conserved activation mechanism that can be triggered by distinct molecular cues.
002A09 (2008) Jiansen Jiang [République populaire de Chine] ; Xuefeng Zhang ; Yong Chen ; Yi Wu ; Z Hong Zhou ; Zengyi Chang ; Sen-Fang SuiActivation of DegP chaperone-protease via formation of large cage-like oligomers upon binding to substrate proteins.

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