Evolution favors protein mutational robustness in sufficiently large populations - sprookjes - yvandenbroek - TriplyDB

Evolution favors protein mutational robustness in sufficiently large populations

Evolution favors protein mutational robustness in sufficiently large populations

http://www.wikidata.org/entity/Q21245352

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In the light of directed evolution: pathways of adaptive protein evolution Weak selection and protein evolution Exploring protein fitness landscapes by directed evolution Congruent evolution of genetic and environmental robustness in micro-RNA Does mutational robustness inhibit extinction by lethal mutagenesis in viral populations?DNA polymerases engineered by directed evolution to incorporate non-standard nucleotides Protein engineering in designing tailored enzymes and microorganisms for biofuels production A nonadaptive origin of a beneficial trait: in silico selection for free energy of folding leads to the neutral emergence of mutational robustness in single domain proteins.Neutral genetic drift can alter promiscuous protein functions, potentially aiding functional evolution.Visualizing time-related data in biology, a review Defining an essence of structure determining residue contacts in proteins.Directed enzyme evolution via small and effective neutral drift libraries.Inferring stabilizing mutations from protein phylogenies: application to influenza hemagglutinin.Mutation bias favors protein folding stability in the evolution of small populations Determining the factors driving selective effects of new nonsynonymous mutations.An improved kinetic model for the acetone-butanol-ethanol pathway of Clostridium acetobutylicum and model-based perturbation analysis.Experimental evolution of adenylate kinase reveals contrasting strategies toward protein thermostability.Random field model reveals structure of the protein recombinational landscape.Critical mutation rate has an exponential dependence on population size in haploid and diploid populations Mutagenic Organized Recombination Process by Homologous IN vivo Grouping (MORPHING) for directed enzyme evolution.Comparative laboratory evolution of ordered and disordered enzymes.On the Nature and Evolutionary Impact of Phenotypic Robustness Mechanisms.Dissecting enzyme function with microfluidic-based deep mutational scanning Level of gene expression is a major determinant of protein evolution in the viral order Mononegavirales.Functional Trade-Offs in Promiscuous Enzymes Cannot Be Explained by Intrinsic Mutational Robustness of the Native Activity Overdispersion of the molecular clock varies between yeast, Drosophila and mammals Integration of new genes into cellular networks, and their structural maturation.P450(BM3) (CYP102A1): connecting the dots.Adaptive laboratory evolution -- principles and applications for biotechnology.A tractable genotype-phenotype map modelling the self-assembly of protein quaternary structure.Antigenic diversification is correlated with increased thermostability in a mammalian virus.Limits of neutral drift: lessons from the in vitro evolution of two ribozymes.Effects of knot type in the folding of topologically complex lattice proteins.Directed -in vitro- evolution of Precambrian and extant Rubiscos.Engineering the product profile of a polysialyltransferase.Shuffling the neutral drift of unspecific peroxygenase in

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Evolution favors protein mutational robustness in sufficiently large populations

http://www.wikidata.org/entity/Q21245352

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2007 nî lūn-bûn

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2007 թուականին հրատարակուած գիտական յօդուած

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2007年の論文

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2007年學術文章

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Evolution favors protein mutational robustness in sufficiently large populations

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Evolution favors protein mutational robustness in sufficiently large populations

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Evolution favors protein mutational robustness in sufficiently large populations

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Evolution favors protein mutational robustness in sufficiently large populations

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Evolution favors protein mutational robustness in sufficiently large populations

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Evolution favors protein mutational robustness in sufficiently large populations

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Evolution favors protein mutational robustness in sufficiently large populations

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Evolution favors protein mutational robustness in sufficiently large populations

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Evolution favors protein mutational robustness in sufficiently large populations

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Evolution favors protein mutational robustness in sufficiently large populations

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Evolution favors protein mutational robustness in sufficiently large populations

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Evolution favors protein mutational robustness in sufficiently large populations

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Evolution favors protein mutational robustness in sufficiently large populations

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Alpan Raval

http://www.w3.org/2001/XMLSchema#string

David Chen

http://www.w3.org/2001/XMLSchema#string

Ophelia S Venturelli

http://www.w3.org/2001/XMLSchema#string

Zhongyi Lu

http://www.w3.org/2001/XMLSchema#string

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Balancing robustness and evolvability

Evolution of mutational robustness in an RNA virus

Protein stability promotes evolvability

Thermodynamic prediction of protein neutrality

Neutral evolution of mutational robustness

Evolution of an antibiotic resistance enzyme constrained by stability and activity trade-offs

Enhancement of protein stability by the combination of point mutations in T4 lysozyme is additive

Evolution of digital organisms at high mutation rates leads to survival of the flattest

ProTherm, version 4.0: thermodynamic database for proteins and mutants

Protein tolerance to random amino acid change

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10.1186/1741-7007-5-29

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1039403477

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17640347

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0704.1885

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protein evolution

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1995189

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