Author

A. M. Dickey

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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Cell Biology· 3 Biochemistry· 1

Signature Assays, Organisms & Methods

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Organism:human· 4 Research Focus:cell signaling & trafficking· 3 Approach:microscopy & imaging analysis· 3 Assay:cryo-EM· 2 Approach:experimental assay· 2 Research Focus:protein structure prediction· 2 Assay:fluorescence / live-cell microscopy· 1 Assay:imaging· 1

Frequent Co-Authors

A. E. Leschziner· 2 shared J. W. Taraska· 2 shared K. A. Sochacki· 2 shared S. L. Reck-Peterson· 2 shared Y. X. Lin· 2 shared A. D. Hoppe· 1 shared A. D. Roberts· 1 shared A. Hor· 1 shared

Activity by Year

2017-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 18 mutual co-author links

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2 shared papersBiochemistry

A. E. Leschziner

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Structure of LRRK1 and mechanisms of autoinhibition and activation

J. M. Reimer, A. M. Dickey, Y. X. Lin, R. G. Abrisch, S. Mathea, D. Chatterjee, E. J. Fay, M. D. Daugherty, S. L. Reck-Peterson, A. E. Leschziner

This study solves cryo-EM structures of LRRK1 in monomeric and dimeric forms, revealing distinct autoinhibition mechanisms compared to LRRK2 and their evolutionary context.

bioRxiv · Nov 22, 2022Biochemistry

Structural basis for Parkinson's Disease-linked LRRK2's binding to microtubules

D. M. Snead, M. Matyszewski, A. M. Dickey, Y. X. Lin, A. E. Leschziner, S. L. Reck-Peterson

This study determines the structural basis of LRRK2's microtubule binding, identifies key residues involved, and shows their disruption affects binding without impacting kinase activity.

bioRxiv · Jan 21, 2022Cell Biology

Structurally distinct endocytic pathways for B cell receptors in B lymphocytes

A. D. Roberts, T. M. Davenport, A. M. Dickey, R. Ahn, K. A. Sochacki, J. W. Taraska

This study shows that B cells use different endocytic mechanisms depending on BCR cluster size, switching from clathrin-mediated endocytosis to large membrane invaginations with actin and FCHSD2 recruitment.

bioRxiv · Jul 24, 2020Cell Biology

Membrane bending begins at any stage of clathrin-coat assembly and defines endocytic dynamics

B. L. Scott, K. A. Sochacki, S. T. Low-Nam, E. M. Bailey, Q. Luu, A. Hor, A. M. Dickey, S. Smith, J. G. Kerkvliet, J. W. Taraska, A. D. Hoppe

The paper uses advanced imaging techniques to study membrane bending during clathrin-coat assembly and finds that bending occurs at different stages of the process, challenging existing models.

bioRxiv · Jul 13, 2017Cell Biology