Mutants of Micromonospora viridifaciens sialidase have highly variable activities on natural and non-natural substrates
Author:
Publisher
Oxford University Press (OUP)
Subject
Molecular Biology,Biochemistry,Bioengineering,Biotechnology
Link
http://academic.oup.com/peds/article-pdf/28/2/37/17495064/gzu054.pdf
Reference37 articles.
1. Bacterial and Viral Sialidases: Contribution of the Conserved Active Site Glutamate to Catalysis
2. Crystal structure of a bacterial sialidase (from Salmonella typhimurium LT2) shows the same fold as an influenza virus neuraminidase.
3. PoPMuSiC 2.1: a web server for the estimation of protein stability changes upon mutation and sequence optimality
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