Cargando…
A High Capacity Microbial Screen for Inhibitors of Human Rhinovirus Protease 3C
We have developed a high capacity screen for compounds that inhibit the 3C protease of human rhinovirus–1b. The assay uses a recombinant strain of Escherichia coli expressing both the protease and a tetracycline resistance–conferring protein modified to contain the minimal protease cleavage site. Cu...
Autores principales: | McCall, J. Owen, Kadam, Sunil, Katz, Leonard |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group US
1994
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7097487/ https://www.ncbi.nlm.nih.gov/pubmed/7765405 http://dx.doi.org/10.1038/nbt1094-1012 |
Ejemplares similares
-
Structure–activity relationships of heteroaromatic esters as human rhinovirus 3C protease inhibitors
por: Im, Isak, et al.
Publicado: (2009) -
An efficient and tunable route to AG7088, a rhinovirus protease inhibitor
por: Ma, Dawei, et al.
Publicado: (2004) -
Dual inhibition of SARS-CoV-2 and human rhinovirus with protease inhibitors in clinical development
por: Liu, Cheng, et al.
Publicado: (2021) -
Rhinovirus 3C protease suppresses apoptosis and triggers caspase-independent cell death
por: Lötzerich, Mark, et al.
Publicado: (2018) -
Design of a Human Rhinovirus-14 3C Protease-Inducible Caspase-3
por: Wagner, Hanna J., et al.
Publicado: (2019)