Author

J. I. Boucher

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· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Assay:protein structure· 2 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:host-pathogen & immune response· 1 Organism:mouse· 1 Organism:plant (other)· 1

Frequent Co-Authors

J. D. Wirth· 2 shared S. Classen· 2 shared A. Dauphin· 1 shared C. A. Schiffer· 1 shared C. Xu· 1 shared D. L. Theobald· 1 shared D. N. A. Bolon· 1 shared D. Theobald· 1 shared

Activity by Year

2018-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

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2 shared papersEvolutionary Biology

J. D. Wirth

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3 papers

Recent·Most cited

Strong epistasis constrains the evolution of strict substrate specificity in apicomplexan lactate dehydrogenases

J. D. Wirth, J. I. Boucher, C. Xu, S. Classen, D. L. Theobald

This study investigates the evolution of substrate specificity in apicomplexan lactate dehydrogenases, revealing strong epistasis that constrains evolutionary changes and limits reversion to ancestral phenotypes.

bioRxiv · Jun 21, 2023 · PreprintEvolutionary Biology

Constrained mutational sampling of amino acids in HIV-1 protease evolution

J. I. Boucher, T. W. Whitfield, A. Dauphin, G. Nauchum, K. B. Zeldovich, R. Swanstrom, C. A. Schiffer, J. Luban, D. N. A. Bolon

The paper investigates HIV-1 protease evolution by comparing experimental fitness landscapes with sequenced isolate data, showing mutational sampling influences multiple mutations.

bioRxiv · Jan 28, 2019Evolutionary Biology

Functional and structural resilience of the active site loop in the evolution of Plasmodium lactate dehydrogenase.

J. D. Wirth, J. I. Boucher, J. R. Jacobowitz, S. Classen, D. Theobald

The study shows PfLDH activity remains resilient to loop perturbations, suggesting alternative insertions could evolve LDH specificity as long as they contain a tryptophan in the correct position.

bioRxiv · Aug 7, 2018Biochemistry