Author

E. P. Karasmanis

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

Click to filter author papers

Cell Biology· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 3 Organism:human· 2 Assay:structural biology· 2 Organism:yeast· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:drug response / drug discovery· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

A. E. Leschziner· 3 shared S. L. Reck-Peterson· 3 shared I. Lahiri· 2 shared J. M. Reimer· 2 shared A. A. Kendrick· 1 shared A. Pluckthun· 1 shared B. Dreier· 1 shared C. Galicia· 1 shared

Activity by Year

2021-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 30 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

3 shared papersCell Biology

A. E. Leschziner

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Development of LRRK2 designed ankyrin-repeat proteins

V. Dederer, M. Sanz Murillo, E. P. Karasmanis, K. S. Hatch, D. Chatterjee, F. Preuss, K. R. Abdul Azeez, L. V. Nguyen, C. Galicia, B. Dreier, A. Pluckthun, W. Versees, S. Mathea, A. E. Leschziner, S. L. Reck-Peterson, S. Knapp

This study develops a high-affinity DARPin that binds to LRRK2's WD40 domain, improving structural analysis and revealing its role in disrupting LRRK2 filaments and Rab8A phosphorylation.

bioRxiv · Nov 14, 2023Biochemistry

Lis1 relieves cytoplasmic dynein-1 auto-inhibition by acting as a molecular wedge

E. P. Karasmanis, J. M. Reimer, A. A. Kendrick, J. A. Rodriguez, J. B. Truong, I. Lahiri, S. L. Reck-Peterson, A. E. Leschziner

The paper presents a structure showing Lis1 relieves dynein-1 auto-inhibition by acting as a molecular wedge, revealing its role in dynein activation.

bioRxiv · Oct 10, 2022 · PreprintCell Biology

Structural Basis for Cytoplasmic Dynein-1 Regulation by Lis1

J. P. Gillies, J. M. Reimer, E. P. Karasmanis, I. Lahiri, Z. M. Htet, A. E. Leschziner, S. L. Reck-Peterson

This study presents the first high-resolution structure of the yeast dynein-Lis1 complex, revealing molecular interactions essential for Lis1's regulation of dynein function across species.

bioRxiv · Jun 11, 2021Cell Biology