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Caspases < Catalyse < Catastrophes  Facettes :

List of bibliographic references indexed by Catalyse

Number of relevant bibliographic references: 24.
[0-20] [0 - 20][0 - 24][20-23][20-40]
Ident.Authors (with country if any)Title
000A99 (2019) Deeksha Munnur [Royaume-Uni] ; Edward Bartlett [Royaume-Uni] ; Petra Mikol Evi [Croatie] ; Ilsa T. Kirby [États-Unis] ; Johannes Gregor Matthias Rack [Royaume-Uni] ; Andreja Miko [Croatie] ; Michael S. Cohen [États-Unis] ; Ivan Ahel [Royaume-Uni]Reversible ADP-ribosylation of RNA.
000F39 (2016) Gang Ye [République populaire de Chine] ; Feng Deng [République populaire de Chine] ; Zhou Shen [République populaire de Chine] ; Rui Luo [République populaire de Chine] ; Ling Zhao [République populaire de Chine] ; Shaobo Xiao [République populaire de Chine] ; Zhen F. Fu [République populaire de Chine, États-Unis] ; Guiqing Peng [République populaire de Chine]Structural basis for the dimerization and substrate recognition specificity of porcine epidemic diarrhea virus 3C-like protease
001063 (2016) Chunmei Li [République populaire de Chine] ; Xin Teng [République populaire de Chine] ; Yifei Qi [République populaire de Chine] ; Bo Tang [République populaire de Chine] ; Hailing Shi [République populaire de Chine] ; Xiaomin Ma [République populaire de Chine] ; Luhua Lai [République populaire de Chine]Conformational Flexibility of a Short Loop near the Active Site of the SARS-3CLpro is Essential to Maintain Catalytic Activity.
002496 (2010) Jennifer Barrila [États-Unis] ; Sandra B. Gabelli ; Usman Bacha ; L Mario Amzel ; Ernesto FreireMutation of Asn28 disrupts the dimerization and enzymatic activity of SARS 3CL(pro) .
002A19 (2009) Cromwell T. Cornillez-Ty [États-Unis] ; Lujian Liao ; John R. Yates ; Peter Kuhn ; Michael J. BuchmeierSevere acute respiratory syndrome coronavirus nonstructural protein 2 interacts with a host protein complex involved in mitochondrial biogenesis and intracellular signaling.
003007 (2008) Kanchan Bhardwaj [États-Unis] ; Satheesh Palaninathan ; Joanna Maria Ortiz Alcantara ; Lillian Li Yi ; Linda Guarino ; James C. Sacchettini ; C Cheng KaoStructural and functional analyses of the severe acute respiratory syndrome coronavirus endoribonuclease Nsp15.
003049 (2008) Alex G. Taranto [Brésil] ; Paulo Carvalho ; Mitchell A. AveryQM/QM studies for Michael reaction in coronavirus main protease (3CL Pro).
003057 (2008) Marcin Drag [États-Unis] ; Jowita Mikolajczyk ; Miklos Bekes ; Francisca E. Reyes-Turcu ; Jonathan A. Ellman ; Keith D. Wilkinson ; Guy S. SalvesenPositional-scanning fluorigenic substrate libraries reveal unexpected specificity determinants of DUBs (deubiquitinating enzymes).
003071 (2008) Veena Nukoolkarn [Thaïlande] ; Vannajan Sanghiran Lee ; Maturos Malaisree ; Ornjira Aruksakulwong ; Supot HannongbuaMolecular dynamic simulations analysis of ritonavir and lopinavir as SARS-CoV 3CL(pro) inhibitors.
003078 (2008) Jiahai Shi [Singapour] ; J. Sivaraman ; Jianxing SongMechanism for controlling the dimer-monomer switch and coupling dimerization to catalysis of the severe acute respiratory syndrome coronavirus 3C-like protease.
003192 (2008) James Solowiej [États-Unis] ; James A. Thomson [États-Unis] ; Kevin Ryan [États-Unis] ; Chun Luo [États-Unis] ; Mingying He [États-Unis] ; Jihong Lou [États-Unis] ; Brion W. Murray [États-Unis, Oman]Steady-State and Pre-Steady-State Kinetic Evaluation of Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV) 3CLpro Cysteine Protease:  Development of an Ion-Pair Model for Catalysis
003784 (2007) Jiang Yin [Canada] ; Chunying Niu [Canada] ; Maia M. Cherney [Canada] ; Jianmin Zhang [Canada] ; Carly Huitema [Canada] ; Lindsay D. Eltis [Canada] ; John C. Vederas [Canada] ; Michael N. G. James [Canada]A Mechanistic View of Enzyme Inhibition and Peptide Hydrolysis in the Active Site of the SARS-CoV 3C-like Peptidase
003C69 (2006) Jiahai Shi [Singapour] ; Jianxing SongThe catalysis of the SARS 3C-like protease is under extensive regulation by its extra domain.
003C79 (2006) Xingnan Li [États-Unis] ; Robert VinceSynthesis and biological evaluation of purine derivatives incorporating metal chelating ligands as HIV integrase inhibitors.
003D96 (2006) Hao Chen [République populaire de Chine] ; Ping Wei ; Changkang Huang ; Lei Tan ; Ying Liu ; Luhua LaiOnly one protomer is active in the dimer of SARS 3C-like proteinase.
004611 (2005) Ting Xu [Singapour] ; Amy Ooi ; Hooi Chen Lee ; Rupert Wilmouth ; Ding Xiang Liu ; Julien LescarStructure of the SARS coronavirus main proteinase as an active C2 crystallographic dimer.
004806 (2005) Jodie L. Guy [Royaume-Uni] ; Richard M. Jackson ; Hanne A. Jensen ; Nigel M. Hooper ; Anthony J. TurnerIdentification of critical active-site residues in angiotensin-converting enzyme-2 (ACE2) by site-directed mutagenesis.
004854 (2005) Jun Han [République populaire de Chine] ; Lan Chen ; Shu-Min Duan ; Qing-Xiang Yang ; Min Yang ; Chen Gao ; Bao-Yun Zhang ; Hong He ; Xiao-Ping DongEfficient and quick inactivation of SARS coronavirus and other microbes exposed to the surfaces of some metal catalysts.
004875 (2005) Ting-Wai Lee [Canada] ; Maia M. Cherney ; Carly Huitema ; Jie Liu ; Karen Ellis James ; James C. Powers ; Lindsay D. Eltis ; Michael N G. JamesCrystal structures of the main peptidase from the SARS coronavirus inhibited by a substrate-like aza-peptide epoxide.
004878 (2005) Wen-Chi Hsu [Taïwan] ; Hui-Chuan Chang ; Chi-Yuan Chou ; Pui-Jen Tsai ; Pei-In Lin ; Gu-Gang ChangCritical assessment of important regions in the subunit association and catalytic action of the severe acute respiratory syndrome coronavirus main protease.
004973 (2005) Yu-San Han [République populaire de Chine] ; Gu-Gang Chang [République populaire de Chine] ; Chiun-Gung Juo [République populaire de Chine] ; Hong-Jen Lee [République populaire de Chine] ; Shiou-Hwei Yeh [République populaire de Chine] ; John Tsu-An Hsu [République populaire de Chine] ; Xin Chen [République populaire de Chine, Taïwan]Papain-Like Protease 2 (PLP2) from Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV):  Expression, Purification, Characterization, and Inhibition†

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