Dynamically-driven enhancement of the catalytic machinery of the SARS 3C-like protease by the S284-T285-I286/A mutations on the extra domain
10.1371/journal.pone.0101941
Saved in:
Main Authors: | Lim L., Shi J., Mu Y., Song J. |
---|---|
Other Authors: | BIOLOGY (NU) |
Format: | Article |
Published: |
Public Library of Science
2018
|
Online Access: | http://scholarbank.nus.edu.sg/handle/10635/142460 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Institution: | National University of Singapore |
Similar Items
-
Dynamically-driven enhancement of the catalytic machinery of the SARS 3C-like protease by the S284-T285-I286/A mutations on the extra domain
by: Lim, Liangzhong, et al.
Published: (2014) -
Dynamically-driven inactivation of the catalytic machinery of the sars 3C-like protease by the N214A mutation on the extra domain
by: Shi, J., et al.
Published: (2014) -
The catalysis of the SARS 3C-like protease is under extensive regulation by its extra domain
by: Song, J., et al.
Published: (2011) -
Dissection study on the severe acute respiratory syndrome 3C-like protease reveals the critical role of the extra domain in dimerization of the enzyme. Defining the extra domain as a new target for design of highly specific protease inhibitors
by: Song, J., et al.
Published: (2013) -
Structural study revealing the unique enzymatic mechanism of the severe acute respiratory syndrome (SARS) coronavirus main protease highly mediated by the extra domain
by: SHI JIA-HAI
Published: (2010)