Structural determinants of protein evolution are context-sensitive at the residue level.

By Eric A. Franzosa, Yu Xia. 2009

179 citations recorded by the source corpus.

Subfields: Materials Chemistry, Molecular Biology

How researchers see this paper

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

In Materials Chemistry

1. Claus O. Wilke
2. Claudio Mirabello
3. Björn Wallner

In Molecular Biology

1. Claus O. Wilke
2. Stephanie J. Spielman
3. Jesse D. Bloom
4. Claudio Mirabello
5. Björn Wallner

Citations in the corpus

• Highly accurate sequence-based prediction of half-sphere exposures of amino acid residues in proteins (2016, unknown): “HSE has also been found useful in many other applications (Franzosa and Xia, 2009; Kringelum et al., 2012; Sweredoski and Baldi, 2008).”
• Maximum Allowed Solvent Accessibilites of Residues in Proteins (2012, background): “protein evolutionary rates and has been incorporated as a parameter into models which determine these rates [6–13].”