Expression and Purification of Recombinant Rhinovirus 14 3CD Proteinase and Its Comparison to the 3C Proteinase
- 1 October 1997
- journal article
- research article
- Published by Elsevier in Archives of Biochemistry and Biophysics
- Vol. 346 (1) , 125-130
- https://doi.org/10.1006/abbi.1997.0291
Abstract
No abstract availableKeywords
This publication has 9 references indexed in Scilit:
- Development of a Continuous Fluorescence Assay for Rhinovirus 14 3C Protease Using Synthetic PeptidesAntiviral Chemistry and Chemotherapy, 1997
- Small peptidic aldehyde inhibitors of human rhinovirus 3C proteaseBioorganic & Medicinal Chemistry Letters, 1996
- Mutations in the Poliovirus 3CD Proteinase S1-Specificity Pocket Affect Substrate Recognition and RNA BindingVirology, 1996
- Purification of Recombinant Human Rhinovirus 14 3C Protease Expressed in Escherichia coliProtein Expression and Purification, 1995
- Structure of human rhinovirus 3C protease reveals a trypsin-like polypeptide fold, RNA-binding site, and means for cleaving precursor polyproteinCell, 1994
- PROTEOLYTIC PROCESSING OF PICORNAVIRAL POLYPROTEINAnnual Review of Microbiology, 1990
- Hydrolysis of a Series of Synthetic Peptide Substrates by the Human Rhinovirus 14 3C Proteinase, Cloned and Expressed in Escherichia coliJournal of General Virology, 1989
- Protein 3CD is the major poliovirus proteinase responsible for cleavage of the p1 capsid precursorVirology, 1988
- Poliovirus Protein 3CD Is the Active Protease for Processing of the Precursor Protein P1 in vitroJournal of General Virology, 1988