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Details on Person Severe acute respiratory syndrome coronavirus 3C-like proteinase N terminus is indispensable for proteolytic activity but not for enzyme dimerization. Biochemical and thermodynamic investigation in conjunction with molecular dynamics simulations

Class:IdLiteratureReference:9686168
_displayNameSevere acute respiratory syndrome coronavirus 3C-like proteinase N terminus is indispensable for proteolytic activity but not for enzyme dimerization. Biochemical and thermodynamic investigation in conjunction with molecular dynamics simulations
_timestamp2020-04-28 13:55:04
author[Person:9684348] Chen, Shuai
[Person:9028576] Chen, Lili
[Person:9686166] Tan, Jinzhi
[Person:1679945] Chen, J
[Person:9686167] Du, Li
[Person:9684337] Sun, Tao
[Person:9028571] Shen, Jianhua
[Person:9028570] Chen, Kaixian
[Person:1273415] Jiang, H
[Person:9028548] Shen, Xu
created[InstanceEdit:9686165] Jassal, Bijay, 2020-04-28
journalJ. Biol. Chem.
pages164-73
pubMedIdentifier15507456
titleSevere acute respiratory syndrome coronavirus 3C-like proteinase N terminus is indispensable for proteolytic activity but not for enzyme dimerization. Biochemical and thermodynamic investigation in conjunction with molecular dynamics simulations
volume280
year2005
(literatureReference)[BlackBoxEvent:9681596] 3CLp dimer binds α-Ketoamides [Homo sapiens]
[BlackBoxEvent:9694592] 3CLp dimer binds 3CLp inhibitors [Homo sapiens]
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No pathways have been reviewed or authored by Severe acute respiratory syndrome coronavirus 3C-like proteinase N terminus is indispensable for proteolytic activity but not for enzyme dimerization. Biochemical and thermodynamic investigation in conjunction with molecular dynamics simulations (9686168)