Conserved amino acid networks modulate discrete functional properties in an enzyme superfamily
Author:
Publisher
Springer Science and Business Media LLC
Subject
Multidisciplinary
Link
http://www.nature.com/articles/s41598-017-03298-4.pdf
Reference40 articles.
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2. Sorrentino, S. The eight human “canonical” ribonucleases: Molecular diversity, catalytic properties, and special biological actions of the enzyme proteins. FEBS Letters 584, 2194–2200 (2010).
3. Kelemen, B. R. et al. Hypersensitive substrate for ribonucleases. Nucleic Acids Res 27, 3696–701 (1999).
4. Cole, R. & Loria, J. P. Evidence for flexibility in the function of ribonuclease A. Biochemistry 41, 6072–81 (2002).
5. Doucet, N., Watt, E. D. & Loria, J. P. The flexibility of a distant loop modulates active site motion and product release in ribonuclease A. Biochemistry 48, 7160–8 (2009).
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