Three-dimensional domain swapping as a mechanism to lock the active conformation in a super-active octamer of SARS-CoV main protease

Liberation of SARS-CoV main protease from the viral polyprotein: N-terminal autocleavage does not depend on the mature dimerization mode

(2010) Shuai Chen et al.   Protein & Cell

Protein acrobatics in pairs—dimerization via domain swapping

(2009) Angela M Gronenborn   CURRENT OPINION IN STRUCTURAL BIOLOGY

Two adjacent mutations on the dimer interface of SARS coronavirus 3C-like protease cause different conformational changes in crystal structure

(2009) Tiancen Hu et al.   VIROLOGY

Correlation between dissociation and catalysis of SARS-CoV main protease

(2008) Pei-Ying Lin et al.   ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS

A Structural View of the Inactivation of the SARS Coronavirus Main Proteinase by Benzotriazole Esters

(2008) Koen H.G. Verschueren et al.   CHEMISTRY & BIOLOGY

A Novel Biological Actions Acquired by Ribonuclease Through Oligomerization

(2008) M. Libonati et al.   CURRENT PHARMACEUTICAL BIOTECHNOLOGY

Mechanism for Controlling the Dimer-Monomer Switch and Coupling Dimerization to Catalysis of the Severe Acute Respiratory Syndrome Coronavirus 3C-Like Protease

(2008) J. Shi et al.   JOURNAL OF VIROLOGY

Without Its N-Finger, the Main Protease of Severe Acute Respiratory Syndrome Coronavirus Can Form a Novel Dimer through Its C-Terminal Domain

(2008) N. Zhong et al.   JOURNAL OF VIROLOGY

Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization

(2008) Masayuki Yamasaki et al.   NATURE