Serine < Serine Endopeptidases < Serine Proteases

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List of bibliographic references

Number of relevant bibliographic references: 26.
[0-20] [0 - 20][0 - 26][20-25][20-40]

Ident.	Authors (with country if any)	Title
000588 (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.
000681 (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.
000736 (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.
000832 (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.
000844 (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 Pöhlmann	TMPRSS11A activates the influenza A virus hemagglutinin and the MERS coronavirus spike protein and is insensitive against blockade by HAI-1.
000B71 (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.
000B75 (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.
000C11 (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.
000D23 (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.
000F17 (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.
000F94 (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.
001702 (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.
001A00 (2014)	Shanshan Li ; Rui Wang [République populaire de Chine] ; Deyong Li ; Jing Ma [République populaire de Chine] ; Heng Li ; Xiaochuan He ; Zengyi Chang [République populaire de Chine] ; Yuxiang Weng	Thermal-triggerd proteinquake leads to disassembly of DegP hexamer as an imperative activation step.
001A33 (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 ; Masato Tashiro ; Makoto Takeda	The host protease TMPRSS2 plays a major role in in vivo replication of emerging H7N9 and seasonal influenza viruses.
001B00 (2014)	Natalie J. Thompson [Pays-Bas] ; Melisa Merdanovic [Allemagne] ; Michael Ehrmann [Royaume-Uni] ; Esther Van Duijn [Pays-Bas] ; Albert J R. Heck [Pays-Bas]	Substrate occupancy at the onset of oligomeric transitions of DegP.
001B61 (2013)	Graham Simmons [États-Unis] ; Pawel Zmora ; Stefanie Gierer ; Adeline Heurich ; Stefan Pöhlmann	Proteolytic activation of the SARS-coronavirus spike protein: cutting enzymes at the cutting edge of antiviral research.
001B89 (2013)	James W. Marsh ; William B. Lott ; Joel D A. Tyndall ; Wilhelmina Willa M. Huston	Proteolytic activation of Chlamydia trachomatis HTRA is mediated by PDZ1 domain interactions with protease domain loops L3 and LC and beta strand β5.
001B91 (2013)	Kazuya Shirato [Japon] ; Miyuki Kawase ; Shutoku Matsuyama	Middle East respiratory syndrome coronavirus infection mediated by the transmembrane serine protease TMPRSS2.
001D66 (2013)	Guido Hansen [Allemagne] ; Rolf Hilgenfeld	Architecture and regulation of HtrA-family proteins involved in protein quality control and stress response.
001E49 (2011)	Xiao-Chen Bai [République populaire de Chine] ; Xi-Jiang Pan ; Xiao-Jing Wang ; Yun-Ying Ye ; Lei-Fu Chang ; Dong Leng ; Jianlin Lei ; Sen-Fang Sui	Characterization of the structure and function of Escherichia coli DegQ as a representative of the DegQ-like proteases of bacterial HtrA family proteins.
001E66 (2011)	Justyna Sawa [Autriche] ; Hélène Malet ; Tobias Krojer ; Flavia Canellas ; Michael Ehrmann ; Tim Clausen	Molecular adaptation of the DegQ protease to exert protein quality control in the bacterial cell envelope.

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