Author

J. M. Reimer

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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Approach:experimental assay· 4 Organism:human· 3 Research Focus:protein structure prediction· 3 Assay:cryo-EM· 2 Assay:structural biology· 2 Organism:yeast· 2 Research Focus:chromatin & epigenetic regulation· 1

Frequent Co-Authors

A. E. Leschziner· 4 shared S. L. Reck-Peterson· 4 shared E. P. Karasmanis· 2 shared I. Lahiri· 2 shared A. A. Kendrick· 1 shared A. M. Dickey· 1 shared D. Chatterjee· 1 shared E. J. Fay· 1 shared

Activity by Year

2021-2022 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 30 mutual co-author links

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4 shared papersCell Biology

A. E. Leschziner

Mutual co-authors in cluster

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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

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

Structures of human cytoplasmic dynein in complex with the lissencephaly 1 protein, LIS1

J. M. Reimer, M. E. DeSantis, S. L. Reck-Peterson, A. E. Leschziner

The paper reports cryo-EM structures of human dynein-LIS1 complexes, revealing differences from yeast and mapping disease mutations.

bioRxiv · Oct 8, 2022Cell 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