Author

M. Ostermeier

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· 4 Research Focus:cell signaling & trafficking· 2 Approach:deep learning· 2 Organism:E. coli· 2 Research Focus:protein folding & dynamics· 2 Assay:proteomics· 2 Research Focus:drug response / drug discovery· 1 Research Focus:gene regulatory network inference· 1

Frequent Co-Authors

J. D. Mehlhoff· 2 shared A. F. Rubin· 1 shared B. M. Moerschbacher· 1 shared B. Wang· 1 shared C. E. Gonzalez· 1 shared D. Rohm· 1 shared E.-Y. Tsou· 1 shared F. M. Goycoolea· 1 shared

Activity by Year

2019-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 24 mutual co-author links

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2 shared papersEvolutionary Biology

J. D. Mehlhoff

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4 papers

Recent·Most cited

Genes vary greatly in their propensity for collateral fitness effects of mutations

J. D. Mehlhoff, M. Ostermeier

The paper uses deep mutational scanning to show that different genes have varying propensities for mutations causing collateral fitness effects, with TEM-1 showing the highest rate.

Molecular Biology and Evolution · Mar 4, 2023Peer-reviewedEvolutionary Biology

Fitness and functional landscapes of the E. coli RNase III gene rnc

R. Weeks, M. Ostermeier

The paper examines the fitness and functional effects of ~4,500 missense mutations in the E. coli rnc gene, finding that RNase III's dsRNA cleavage ability is the main determinant of mutation fitness effects.

bioRxiv · Nov 1, 2022 · PreprintEvolutionary Biology

Collateral fitness effects of mutations

J. D. Mehlhoff, F. W. Stearns, D. Rohm, B. Wang, E.-Y. Tsou, N. Dutta, M.-H. Hsiao, C. E. Gonzalez, A. F. Rubin, M. Ostermeier

This study identifies collateral fitness effects of mutations in E. coli, showing that 42% of missense mutations in TEM-1 β-lactamase are deleterious through mechanisms unrelated to protein function.

bioRxiv · Mar 4, 2020Evolutionary Biology

Protein-surfactant-polysaccharide nanoparticles increase the catalytic activity of an engineered β-lactamase maltose-activated switch enzyme

J. P. Fuenzalida Werner, T. xiong, B. M. Moerschbacher, M. Ostermeier, F. M. Goycoolea

The paper describes protein-surfactant-polysaccharide nanoparticles that enhance the catalytic activity of an engineered β-lactamase switch enzyme by specific interactions with alginate on nanoparticle surfaces.

bioRxiv · Aug 24, 2019 · PreprintBiochemistry