Protein stability promotes evolvability.
By Jesse D. Bloom, Sy T Labthavikul, Christopher R. Otey, Frances H. Arnold. 2006
1,153 citations recorded by the source corpus.
Subfields: Genetics, 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 Genetics
- Eugene I. Shakhnovich
- Frances H. Arnold
- Dan S. Tawfik
- Jesse D. Bloom
- Philip A. Romero
- Douglas M. Fowler
- Joseph W. Thornton
- Stanley Fields
In Molecular Biology
- Alexandre M. J. J. Bonvin
- Shengyou Huang
- Xiaoqin Zou
- Brian G. Pierce
- Frances H. Arnold
- Jeffrey J. Gray
- Kevin Kaichuang Yang
- Yang Zhang
Citations in the corpus
- Exploring protein fitness landscapes by directed evolution (2009, background): “For example, the introduction of stabilizing mutations can increase a protein's mutational robustness, opening new routes for further adaptatio”
- Inferring Stabilizing Mutations from Protein Phylogenies: Application to Influenza Hemagglutinin (2009, background): “That mutational tolerance is indeed enhanced by extra stability in this fashion has been experimentally verified for several proteins [56–58].”
- Consensus protein design (2016, background): “However, extra thermodynamic stability is known to increase the robustness of the native structure to random mutations by increasing the fraction of variants that continue to possess the minimal stability required to fold (Nikolova et al., 2000; Bloom et al., 2005, 2006).”
- Robustness and Evolvability (2010, background): “Mutants derived from highly stable variants of a given protein are more likely to retain their fold, and are consequently more likely to develop novel or improved protein functions [59,60].”
- Machine learning-assisted directed protein evolution with combinatorial libraries (2019, background): “Because machine learning-assisted directed evolution makes multiple mutations per iteration, a starting sequence capable of accommodating multiple potentially destabilizing mutations is ideal (27).”
- Stability effects of mutations and protein evolvability. (2009, background): “In the laboratory, downhill divergence was demonstrated with a variant of P450 that was evolved first for higher thermostability, and demonstrating its higher evolvabilty through its ability to accept destabilizing new-function mutations that the wild-type enzyme would not [51 ].”