Engineering of protease variants exhibiting high catalytic activity and exquisite substrate selectivity.

By N. Varadarajan, J. Gam, Mark J. Olsen, G. Georgiou, B. Iverson. 2005

161 citations recorded by the source corpus.

Subfields: Molecular Biology, Oncology, Radiology, Nuclear Medicine and Imaging

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

1. O. Khersonsky
2. Dan S. Tawfik
3. Andreas Wagner

In Oncology

1. Dan S. Tawfik

Citations in the corpus

• Engineering of TEV protease variants by yeast ER sequestration screening (YESS) of combinatorial libraries (2013, background): “Studies from our laboratory and others have highlighted the importance of incorporating simultaneous counterselection substrates during the directed evolution of proteases to avoid isolating variants with relaxed specificity (14, 20, 36, 37).”
• Enzyme promiscuity: a mechanistic and evolutionary perspective. (2010, background): “In few cases, a single amino acid exchange can completely switch the specificity of an enzyme (152).”
• Highly active and selective endopeptidases with programmed substrate specificities. (2008, methodology): “The cells were harvested and resuspended in 1% sucrose as described previously 15 .”