Author

Trudy F. Ramlall

Regeneron (United States)

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 Neuroscience· 1

Signature Assays, Organisms & Methods

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Assay:cryo-EM· 2 Approach:experimental assay· 2 Research Focus:protein structure prediction· 2 Research Focus:cancer & tumor microenvironment· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Organism:human· 1 Approach:microscopy & imaging analysis· 1

Frequent Co-Authors

Jennifer L. JonesiD· 2 shared Luke L. McGoldrickiD· 2 shared Matthew C. FrankliniD· 2 shared William C. OlsoniD· 2 shared André PinedaiD· 1 shared Annan SI CookiD· 1 shared David EliezeriD· 1 shared Eric SmithiD· 1 shared

Activity by Year

2020-2025 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 22 mutual co-author links

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Curved chords = mutual co-authorship

2 shared papersBiochemistry

Jennifer L. JonesORCID

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Author profile →

3 papers

Recent·Most cited

Structural basis for constitutive activation of oncogenic gp130 mutants in human inflammatory hepatocellular adenomas

Yi Zhou, Jing Cao, Trudy F. Ramlall, Luke L. McGoldrick, Jennifer L. Jones, Annan SI Cook, Raymond Leidich, Mark W. Sleeman, William C. Olson, Panayiotis E. Stevis, Matthew C. Franklin

This study identifies structural mechanisms of gp130 mutant activation in IHCAs using cryo-EM and mutagenesis, revealing two distinct dimer conformations and their activation dependencies.

bioRxiv · Nov 11, 2025 · PreprintBiochemistry

Structural characterization of two full length γδTCR/CD3 complexes

Mohammed Hoque, John Benji Grigg, Trudy F. Ramlall, Jennifer L. Jones, Luke L. McGoldrick, John C. Lin, William C. Olson, Eric Smith, Matthew C. Franklin, Tong Zhang, Kei Saotome

This study reports cryoEM structures of two full-length γδ TCR/CD3 complexes, revealing similarities to β TCRs but with highly mobile extracellular domains and a dimeric assembly in one complex.

Nature Communications · Jan 2, 2025Peer-reviewedBiochemistry

BETA- AND GAMMA-SYNUCLEINS MODULATE SYNAPTIC VESICLE-BINDING OF ALPHA-SYNUCLEIN

Kathryn E. Carnazza, Lauren E. Komer, André Pineda, Yoonmi Na, Trudy F. Ramlall, Vladimir L. Buchman, David Eliezer, Manu Sharma, Jacqueline Burré

This study shows that beta-synuclein and gamma-synuclein modulate alpha-synuclein's membrane binding and synaptic function, but not its downstream roles in vesicle clustering and SNARE-complex assembly.

bioRxiv · Nov 19, 2020 · PreprintNeuroscience