Cargando…
The N-terminal octapeptide acts as a dimerization inhibitor of SARS coronavirus 3C-like proteinase()
The 3C-like proteinase of severe acute respiratory syndrome (SARS) coronavirus has been proposed to be a key target for structural-based drug design against SARS. Accurate determination of the dimer dissociation constant and the role of the N-finger (residues 1–7) will provide more insights into the...
Autores principales: | Wei, Ping, Fan, Keqiang, Chen, Hao, Ma, Liang, Huang, Changkang, Tan, Lei, Xi, Dong, Li, Chunmei, Liu, Ying, Cao, Aoneng, Lai, Luhua |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier Inc.
2006
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7092940/ https://www.ncbi.nlm.nih.gov/pubmed/16329994 http://dx.doi.org/10.1016/j.bbrc.2005.11.102 |
Ejemplares similares
-
Only One Protomer Is Active in the Dimer of SARS 3C-like Proteinase
por: Chen, Hao, et al.
Publicado: (2006) -
The interaction between severe acute respiratory syndrome coronavirus 3C-like proteinase and a dimeric inhibitor by capillary electrophoresis
por: Ding, Li, et al.
Publicado: (2005) -
Synthesis and activity of an octapeptide inhibitor designed for SARS coronavirus main proteinase
por: Gan, Yi-Ru, et al.
Publicado: (2006) -
Biosynthesis, Purification, and Substrate Specificity of Severe Acute Respiratory Syndrome Coronavirus 3C-like Proteinase
por: Fan, Keqiang, et al.
Publicado: (2004) -
The substrate specificity of SARS coronavirus 3C-like proteinase
por: Fan, Keqiang, et al.
Publicado: (2005)