Author

W. Dylan Hale

Johns Hopkins UniversityORCID 0000-0002-1492-0735Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Neuroscience· 2 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:cell signaling & trafficking· 1 Research Focus:cell-cell communication· 1 Assay:cryo-EM· 1 Research Focus:drug response / drug discovery· 1 Assay:electrophysiology· 1 Approach:microscopy & imaging analysis· 1 Organism:mouse· 1

Frequent Co-Authors

Richard L. HuganiriD· 3 shared Akhilesh PandeyiD· 1 shared Alexei M. BygraveiD· 1 shared Casey N. BarberiD· 1 shared David J. MeyersiD· 1 shared Edward C. TwomeyiD· 1 shared Hana L. GoldschmidtiD· 1 shared Jevon A. CutleriD· 1 shared

Activity by Year

2023-2025 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 37 mutual co-author links

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3 shared papersNeuroscience

Richard L. HuganirORCID

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Author profile →

3 papers

Recent·Most cited

Dynamic extracellular interactions with AMPA receptors

Hana L. Goldschmidt, Casey N. Barber, Santosh Renuse, Jevon A. Cutler, Simion D. Kreimer, Alexei M. Bygrave, David J. Meyers, W. Dylan Hale, Akhilesh Pandey, Richard L. Huganir

The paper identifies 70 extracellular proteins interacting with AMPARs during synaptic plasticity, showing OBCAM and NTM regulate AMPAR mobility.

Proceedings of the National Academy of Sciences · Nov 17, 2025Peer-reviewedNeuroscience

Architecture, Activation, and Conformational Plasticity in the GluA4 AMPA Receptor

W. Dylan Hale, Richard L. Huganir, Edward C. Twomey

This study investigates the structural features of GluA4 AMPA receptors, revealing their unique architecture and conformational plasticity that influence ion channel function and disease relevance.

bioRxiv · Jun 12, 2025 · PreprintBiophysics

Engineered Adhesion Molecules Drive Synapse Organization

W. Dylan Hale, Thomas Christian Südhof, Richard L. Huganir

This study engineers novel adhesion molecules that drive synapse formation in cultured neurons by combining domains from bacterial proteins and synaptic cell-adhesion molecules.

Proceedings of the National Academy of Sciences · Jan 13, 2023Peer-reviewedNeuroscience