Author

Eric O. Long

National Institutes of HealthORCID 0000-0002-7793-3728Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Assay:proteomics· 3 Research Focus:cell type annotation· 2 Organism:human· 2 Research Focus:cell signaling & trafficking· 1 Organism:mouse· 1

Frequent Co-Authors

Jinghua LuiD· 2 shared Malcolm J. W. SimiD· 2 shared Beining Li· 1 shared Emery HoosiD· 1 shared Erin J. AdamsiD· 1 shared George M Mastorakos· 1 shared Geraldine M. GillespieiD· 1 shared James C. Yang· 1 shared

Activity by Year

2024-2026 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 19 mutual co-author links

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2 shared papersImmunology

Jinghua LuORCID

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3 papers

Recent·Most cited

Allosteric disulfide control of ligand binding and endocytosis of KIR2DL4, the natural killer cell receptor for HLA-G

Sumati Rajagopalan, Joyce Chiu, Priyanka Chaurasia, Jinghua Lu, George M Mastorakos, Saurav Majumder, Kristof Nolan, Jan Petersen, Erin J. Adams, Peter D Sun, Jamie Rossjohn, Philip J. Hogg, Eric O. Long

This study identifies an allosteric disulfide bond in KIR2DL4 that regulates HLA-G binding and endocytosis, influencing NK cell function during pregnancy.

eLife · Oct 13, 2026Peer-reviewedImmunology

Using peptide-exchange systems to interrogate peptide-specific KIR binding to HLA Class -I

Tanusya Murali Murali, Beining Li, Emery Hoos, Lucy Collinson, Eric O. Long, Omer Dushek, Tim J Elliott, Malcolm J. W. Sim

This study develops a peptide-exchange system to efficiently study KIR binding to HLA-I molecules with peptide specificity.

Discovery Immunology · Jan 1, 2026Peer-reviewedImmunology

Identification and Structural Characterization of a mutant KRAS-G12V specific TCR restricted by HLA-A3

Malcolm J. W. Sim, Ken‐ichi Hanada, Zachary Stotz, Zhiya Yu, Jinghua Lu, Paul Brennan, Max Quastel, Geraldine M. Gillespie, Eric O. Long, James C. Yang, Peter D. Sun

The paper identifies a TCR specific to KRAS-G12V neoantigen and characterizes its structural interaction with HLA-A3, revealing challenges in targeting this mutation.

bioRxiv · Feb 1, 2024Immunology