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Quantitative Description of a Protein Fitness Landscape Based on Molecular Features.

Quantitative Description of a Protein Fitness Landscape Based on Molecular Features.

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Enzyme Efficiency but Not Thermostability Drives Cefotaxime Resistance Evolution in TEM-1 β-Lactamase.Triton Hodge Test: Improved Protocol for Modified Hodge Test for Enhanced Detection of NDM and Other Carbapenemase Producers.Membrane anchoring stabilizes and favors secretion of New Delhi metallo-β-lactamase Local fitness landscape of the green fluorescent protein.Insights into an evolutionary strategy leading to antibiotic resistance.A general reaction mechanism for carbapenem hydrolysis by mononuclear and binuclear metallo-β-lactamases.Structural Insights into TMB-1 and the Role of Residues 119 and 228 in Substrate and Inhibitor Binding.How mutational epistasis impairs predictability in protein evolution and design Using cellular fitness to map the structure and function of a major facilitator superfamily effluxer.Selecting among three basic fitness landscape models: Additive, multiplicative and stickbreaking.Clinical Evolution of New Delhi Metallo-β-Lactamase (NDM) Optimizes Resistance under Zn(II) Deprivation.Optimization of Conformational Dynamics in an Epistatic Evolutionary Trajectory.The Influence of Higher-Order Epistasis on Biological Fitness Landscape Topography.

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Quantitative Description of a Protein Fitness Landscape Based on Molecular Features.

http://www.wikidata.org/entity/Q35765112

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2015 nî lūn-bûn

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年论文

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2015年论文

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2015年论文

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Quantitative Description of a Protein Fitness Landscape Based on Molecular Features.

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Quantitative Description of a Protein Fitness Landscape Based on Molecular Features.

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Quantitative Description of a Protein Fitness Landscape Based on Molecular Features.

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Quantitative Description of a Protein Fitness Landscape Based on Molecular Features.

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Molecular Biology and Evolution

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Quantitative Description of a Protein Fitness Landscape Based on Molecular Features.

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Alejandro J Vila

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Daniel M Weinreich

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Pablo E Tomatis

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P2860

Stability-mediated epistasis constrains the evolution of an influenza protein

Exploring protein fitness landscapes by directed evolution

Quantitative exploration of the catalytic landscape separating divergent plant sesquiterpene synthases

The causes of epistasis

Predicting the emergence of antibiotic resistance by directed evolution and structural analysis

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

Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity

Adaptive protein evolution grants organismal fitness by improving catalysis and flexibility

Metallo-β-lactamases withstand low Zn(II) conditions by tuning metal-ligand interactions

Resurrecting ancestral alcohol dehydrogenases from yeast

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1774-1787

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scholarly article

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10.1093/MOLBEV/MSV059

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7

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32

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María-Rocío Meini

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2015-03-12T00:00:00Z

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25767204

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4476158

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