Author

S. M. Terrell

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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Microbiology· 2 Biochemistry· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:drug response / drug discovery· 2 Approach:biophysical modeling· 1 Research Focus:cell type annotation· 1 Organism:human· 1 Assay:metabolomics· 1 Organism:mouse· 1 Assay:proteomics· 1

Frequent Co-Authors

J. Z. Long· 4 shared M. Bogyo· 3 shared B. M. Babin· 2 shared I. T. Foe· 2 shared O. Onguka· 2 shared P. Cieplak· 2 shared V. L. Li· 2 shared A. C. Yang· 1 shared

Activity by Year

2019-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 29 mutual co-author links

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4 shared papersMicrobiology

J. Z. Long

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

A screen of covalent inhibitors in Mycobacterium tuberculosis identifies serine hydrolases involved in lipid metabolism as potential therapeutic targets

B. M. Babin, L. J. Keller, Y. Pinto, V. L. Li, A. Eneim, S. E. Vance, S. M. Terrell, A. S. Bhatt, J. Z. Long, M. Bogyo

bioRxiv · Jun 7, 2021 · PreprintMicrobiology

Toxoplasma gondii serine hydrolases regulate parasite lipid mobilization during growth and replication within the host

O. Onguka, B. M. Babin, M. Lakemeyer, I. T. Foe, N. Amara, S. M. Terrell, K. M. Lum, P. Cieplak, M. J. Niphakis, J. Z. Long, M. Bogyo

This study identifies serine hydrolases in Toxoplasma gondii that hydrolyze lipid esters, showing their role in lipid metabolism and potential as therapeutic targets.

bioRxiv · Nov 24, 2020Microbiology

Cell type-selective secretome profiling in vivo

W. Wei, N. M. Riley, A. C. Yang, J. T. Kim, S. M. Terrell, V. L. Li, M. Garcia-Contreras, C. R. Bertozzi, J. Z. Long

The paper introduces a method to profile cell-type-specific secretomes in vivo and identifies novel secreted proteins and dynamic changes in hepatocyte secretomes.

bioRxiv · Sep 18, 2020Biochemistry

The antimalarial natural product salinipostin A identifies essential α/β serine hydrolases involved in lipid metabolism in P. falciparum parasites

E. Yoo, C. J. Schulze, B. H. Stokes, O. Onguka, T. Yeo, S. Mok, N. F. Gnadig, Y. Zhou, K. Kurita, I. T. Foe, S. M. Terrell, M. J. Boucher, P. Cieplak, R. G. Linington, J. Z. Long, , M. Bogyo

The study identifies essential α/β serine hydrolases in P. falciparum as targets of the antimalarial Salinipostin A, which disrupt lipid metabolism and inhibit parasite growth.

bioRxiv · Nov 1, 2019Cell Biology