Author

D. W. Anderson

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Evolutionary Biology· 3 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:chromatin & epigenetic regulation· 2 Assay:protein sequence· 2 Assay:protein structure· 2 Approach:statistical model· 2 Research Focus:cell type annotation· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1

Frequent Co-Authors

N. Tokuriki· 3 shared F. Baier· 2 shared G. Yang· 2 shared A. Romero-Rivera· 1 shared C. J. Jackson· 1 shared C. Jackson· 1 shared C. M. Miton· 1 shared E. Bornberg-Bauer· 1 shared

Activity by Year

2018-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 20 mutual co-author links

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3 shared papersEvolutionary Biology

N. Tokuriki

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Author profile →

4 papers

Recent·Most cited

Origin Of Evolutionary Bifurcation In An Enzyme

C. M. Miton, E. C. Campbell, J. A. Kaczmarski, F. Feixas, A. Romero-Rivera, M. Sandhu, D. W. Anderson, N. Shatani, S. Osuna, C. J. Jackson, N. Tokuriki

The paper describes how two distinct enzymes evolved from a common ancestor through different mutational paths, leading to divergent molecular and phenotypic outcomes.

bioRxiv · Nov 25, 2023 · PreprintEvolutionary Biology

Detailed phylogenetic analysis of SARS-CoV-2 reveals latent capacity to bind human ACE2 receptor

E. Brintnell, M. Gupta, D. W. Anderson

The paper uses phylogenetic analysis and simulations to show that the common ancestor of SARS-CoV-2 and RaTG13 had high ACE2 binding affinity, suggesting latent human infectivity potential.

bioRxiv · Jun 22, 2020 · PreprintEvolutionary Biology

Secondary environmental variation creates a shifting evolutionary watershed for the methyl- parathion hydrolase enzyme

D. W. Anderson, F. Baier, G. Yang, N. Tokuriki

The paper shows that secondary environmental factors influence the evolutionary adaptation of an enzyme by shifting the adaptive landscape and altering fitness peaks.

bioRxiv · Nov 7, 2019 · PreprintEvolutionary Biology

Higher-order epistatic networks underlie the evolutionary fitness landscape of a xenobiotic- degrading enzyme

G. Yang, D. W. Anderson, F. Baier, E. Dohmen, N. Hong, P. D. Carr, S. C. L. Kamerlin, C. Jackson, E. Bornberg-Bauer, N. Tokuriki

This study identifies five mutations that enable the evolution of a xenobiotic-degrading enzyme and shows that higher-order epistasis shapes its adaptive landscape and substrate specificity.

bioRxiv · Dec 26, 2018 · PreprintBiochemistry