Author

Jennifer Ramirez

University of Pennsylvania

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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Biochemistry· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Assay:proteomics· 2 Research Focus:cell signaling & trafficking· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

David EliezeriD· 2 shared E. James PeterssoniD· 2 shared Elizabeth R. RhoadesiD· 2 shared Marie ShimogawaiD· 2 shared Minghao LiiD· 2 shared Benjamin A. Garcia· 1 shared Bernard AbakahiD· 1 shared Chao PengiD· 1 shared

Activity by Year

2025-2025 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 39 mutual co-author links

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2 shared papersBiochemistry

David EliezerORCID

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2 papers

Recent·Most cited

Genetic Code Expansion and Enzymatic Modifications as Accessible Methods for Studying Site-Specific Post-Translational Modifications of Alpha-Synuclein and Tau

Ibrahim G. Saleh, Marie Shimogawa, Jennifer Ramirez, Bernard Abakah, Yarra Venkatesh, Honey Priya James, Minghao Li, Sarah A. Louie, Marshall G. Lougee, Wai‐Kit Chia, Christopher R. Brue, Richard B. Cooley, Ryan A. Mehl, Tobias Baumgart, Robert H. Mach, , E. James Petersson

The paper provides methods for site-specific post-translational modification of alpha-synuclein and tau using genetic code expansion and enzymatic approaches, enabling studies of their structural dynamics and aggregation.

Protein Science · Sep 13, 2025Peer-reviewedBiochemistry

Investigation of Disease-Relevant Lysine Acetylation Sites in α-Synuclein Enabled by Non-canonical Amino Acid Mutagenesis

Marie Shimogawa, Minghao Li, Grace Shin Hye Park, Jennifer Ramirez, Hudson Lee, Paris R. Watson, Swati Sharma, Zongtao Lin, Chao Peng, Virginia M.-Y. Lee, Benjamin A. Garcia, David W. Christianson, Elizabeth R. Rhoades, David Eliezer, E. James Petersson

This study investigates how acetylation of specific lysine sites in α-synuclein affects aggregation and function, identifying K80 acetylation as a potential therapeutic target.

bioRxiv · Jan 21, 2025 · PreprintBiochemistry