Author

Aidan M. Jessop

Columbia University Irving Medical Center

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· 1 Genetics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:chromatin & epigenetic regulation· 1 Assay:cryo-EM· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1 Research Focus:protein structure prediction· 1 Organism:yeast· 1

Frequent Co-Authors

Eric C. GreeneiD· 2 shared Katherine Morse· 2 shared Michael T. PetassiiD· 2 shared Razvan Matei· 2 shared Stefan Y. KimiD· 2 shared Vivek B. RainaiD· 2 shared Yeonoh ShiniD· 2 shared Sahiti KuppaiD· 1 shared

Activity by Year

2025-2025 · peak 2/yr

Co-Author Collaboration Network

9 top collaborators · 35 mutual co-author links

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2 shared papersGenetics

Eric C. GreeneORCID

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2 papers

Recent·Most cited

Lineage-specific amino acids define functional attributes of the protomer-protomer interfaces for the Rad51 and Dmc1 recombinases

Michael T. Petassi, Yeonoh Shin, Aidan M. Jessop, Katherine Morse, Stefan Y. Kim, Sahiti Kuppa, Razvan Matei, Vivek B. Raina, Eric C. Greene

The paper compares Rad51 and Dmc1 recombinases using structural and functional analyses to show differences in their interfacial amino acids and evolutionary trajectories.

Journal of Biological Chemistry · Dec 8, 2025Peer-reviewedGenetics

Structural basis for Rad54- and Hed1-mediated regulation of Rad51 during the transition from mitotic to meiotic recombination

Yeonoh Shin, Michael T. Petassi, Aidan M. Jessop, Stefan Y. Kim, Razvan Matei, Katherine Morse, Vivek B. Raina, Upasana Roy, Eric C. Greene

The paper identifies Rad51 interaction motifs in Rad54 and Hed1, and solves their CryoEM structures to explain their roles in regulating Rad51 activity during mitosis and meiosis.

Proceedings of the National Academy of Sciences · Sep 11, 2025Peer-reviewedBiochemistry