Cargando…
Correlation between dissociation and catalysis of SARS-CoV main protease
The dimeric interface of severe acute respiratory syndrome coronavirus main protease is a potential target for the anti-SARS drug development. We have generated C-terminal truncated mutants by serial truncations. The quaternary structure of the enzyme was analyzed using both sedimentation velocity a...
Autores principales: | Lin, Pei-Ying, Chou, Chi-Yuan, Chang, Hui-Chuan, Hsu, Wen-Chi, Chang, Gu-Gang |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier Inc.
2008
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7094404/ https://www.ncbi.nlm.nih.gov/pubmed/18275836 http://dx.doi.org/10.1016/j.abb.2008.01.023 |
Ejemplares similares
-
Critical Assessment of Important Regions in the Subunit Association and Catalytic Action of the Severe Acute Respiratory Syndrome Coronavirus Main Protease
por: Hsu, Wen-Chi, et al.
Publicado: (2005) -
Mutation of Glu-166 Blocks the Substrate-Induced Dimerization of SARS Coronavirus Main Protease
por: Cheng, Shu-Chun, et al.
Publicado: (2010) -
Reversible Unfolding of the Severe Acute Respiratory Syndrome Coronavirus Main Protease in Guanidinium Chloride
por: Chang, Hui-Ping, et al.
Publicado: (2007) -
Quaternary Structure of the SARS Coronavirus Main Protease
por: Chang, Gu-Gang
Publicado: (2009) -
Critical Assessment of the Important Residues Involved in the Dimerization and Catalysis of MERS Coronavirus Main Protease
por: Ho, Bo-Lin, et al.
Publicado: (2015)