High-resolution structural validation of the computational redesign of human U1A protein.
By Neil Dobson, G. Dantas, David Baker, Gabriele Varani. 2006
23 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
- David Baker
- Jeffrey J. Gray
- Tanja Kortemme
- Brian Kuhlman
- Andrew Leaver-Fay
- Yuedong Yang
- Yaoqi Zhou
- Ron Jacak
In Molecular Biology
- David Baker
- Tanja Kortemme
- Jeffrey J. Gray
- Brian Kuhlman
- Andrew Leaver-Fay
- Yaoqi Zhou
- Yuedong Yang
- Sergey Lyskov
Citations in the corpus
- Scientific Benchmarks for Guiding Macromolecular Energy Function Improvement (2013, background): “…(Liang & Grishin, 2002; Petrella, Lazaridis, & Karplus, 1998), including extensive use to evaluate the Rosetta energy function (Dantas et al., 2007; Dobson, Dantas, Baker, & Varani, 2006; Jacak et al., 2012; Kortemme et al., 2003), the ORBIT energy function (Sharabi, Yanover, Dekel, & Shifman,…”
- High-resolution Structural and Thermodynamic Analysis of Extreme Stabilization of Human Procarboxypeptidase by Computational Protein Design (2007, background): “18,19 While structural validation in a few cases has confirmed the high-resolution accuracy of the designs, 12,15,16,18 – 20 the total repertoire of high-resolution structures of computationally designed proteins remains small.”
- The highly cooperative folding of small naturally occurring proteins is likely the result of natural selection. (2007, background): “, 1997), while computational protein design has allowed for the complete redesign of sequences capable of folding to naturally occurring structures (Dahiyat and Mayo, 1997; Dantas et al., 2003; Dobson et al., 2006; Gillespie et al., 2003).”
- Direct prediction of profiles of sequences compatible with a protein structure by neural networks with fragment‐based local and energy‐based nonlocal profiles (2014, unknown): “Proteins: Structure, Function and Genetics, 82(10), pp.”
- Energy functions in de novo protein design: current challenges and future prospects. (2013, background): “Currently, on the other hand, specific structures of de novo designed proteins are routinely validated by NMR or X-ray structure determination (5, 9, 17, 21, 27, 41, 56, 60, 82, 104, 115).”