Stability effects of mutations and protein evolvability.
By Nobuhiko Tokuriki, Dan S. Tawfik. 2009
813 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
- Daniel N. A. Bolon
- Frances H. Arnold
- Benjamin P. Roscoe
- Philip A. Romero
- Dan S. Tawfik
- Parul Mishra
- Tyler N. Starr
- G. Diss
In Molecular Biology
- Robin Pearce
- Yang Zhang
- Daniel N. A. Bolon
- Qiang Lv
- Lijun Quan
- Frances H. Arnold
- Luciano A. Abriata
- Sergey Ovchinnikov
Citations in the corpus
- Exploring protein fitness landscapes by directed evolution (2009, positive): “Several studies have revealed a key link between stability and epistasis, where the effect of a mutation can be conditional on the stability of the parent sequenc”
- Systematic exploration of ubiquitin sequence, E1 activation efficiency, and experimental fitness in yeast (2014, methodology): “These structural analyses are consistent with the chemical intuition that the functional sensitivity of a position to mutation is primarily determined by direct binding interfaces 39 as well as structural integrity 40 and dynamics 41 .”
- Toward the solution of the protein structure prediction problem (2021, background): “The key reason for the success of TASSER is its effective combination of multiple templates (20 – 50) and its optimized simulation strategy that combines ef fi cient conformational movements with an effective knowledge and template-based energy function.”
- Selection for Protein Stability Enriches for Epistatic Interactions (2018, background): “But, with some 24 exceptions [7], this view has been largely replaced with a more parsimonious explanation based on 25 the high dimensionality of sequence space: marginal stabilities are observed because, simply, far 26 more sequences are marginally stable than maximally stable [8].”
- Systematic Mapping of Protein Mutational Space by Prolonged Drift Reveals the Deleterious Effects of Seemingly Neutral Mutations (2015, background): “In general, the current state-of-the-art experimental mappings artificially widen the threshold for acceptance of mutations, such that the early accumulating mutations have no apparent effect on the protein’s fitness [73].”
- How Structural and Physicochemical Determinants Shape Sequence Constraints in a Functional Enzyme (2015, result): “for ampicillin hydrolysis by TEM-1 but consistent with several other studies suggesting this is a rather general effect [3,34,35].”
- STRUM: structure-based prediction of protein stability changes upon single-point mutation (2016, background): “Experimental measurements showed that nearly one-third of nsSNP mutations are deleterious to human health (Tokuriki and Tawfik, 2009).”
- Enzyme promiscuity: a mechanistic and evolutionary perspective. (2010, background): “Thus, when drifting in the absence of any selection, loss of all functions (nonfunctionalization) because of (162, 170) is orders of magnitude likely than neofunctionalization (171). www.annualreviews.org • Enzyme Promiscuity 495 utilization parts The above observations prompted a number of…”
- Latent Effects of Hsp90 Mutants Revealed at Reduced Expression Levels (2013, background): “Under these conditions, selection results in stably-folded proteins [19,20], such that modestly destabilizing mutations can be tolerated without dramatic changes to the fraction of natively folded protein molecules and hence function.”
- Epistasis in protein evolution (2016, background): “This kind of epistasis fits a model by which stability maps nonlinearly to function and fitness: in the simplest case, suppose that the biological function of a protein scales linearly with the quantity of folded protein in the cell.(84) Two mutations that independently affect protein stability will”
- The genetic landscape of a physical interaction (2018, background): “Additional non-linearities occur in the folding of individual proteins or RNAs (‘threshold robustness’) (Bershtein et al., 2006; Olson et al., 2014; Tokuriki and Tawfik, 2009), in saturating enzyme flux (Kacser and Burns, 1973; Stiffler et al., 2015), and in regulatory dynamics (Gjuvsland et al.,…”
- Mega-scale experimental analysis of protein folding stability in biology and design (2023, background): “However, the challenge of measuring stability has made it difficult to experimentally distinguish selection for stability from other selective pressures on a global level 36– 38 .”