Author

I. Lahiri

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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Biophysics· 2 Cell Biology· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Organism:human· 2 Assay:structural biology· 2 Organism:yeast· 2 Research Focus:chromatin & epigenetic regulation· 1 Assay:cryo-EM· 1 Research Focus:host-pathogen & immune response· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

A. E. Leschziner· 4 shared S. L. Reck-Peterson· 3 shared E. P. Karasmanis· 2 shared J. M. Reimer· 2 shared A. A. Kendrick· 1 shared A. K. Shiau· 1 shared C. K. Deniston· 1 shared D. M. Snead· 1 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

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4 shared papersBiophysics

A. E. Leschziner

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4 papers

Recent·Most cited

Elf1 promotes Rad26 interaction with lesion-arrested Pol II for transcription-coupled repair

R. Sarsam, J. Xu, I. Lahiri, W. Gong, J. Oh, Z. Zhou, J. Chong, N. Hao, S. Li, D. Wang, A. E. Leschziner

The paper investigates how Rad26 interacts with lesion-arrested Pol II and identifies Elf1's role in enhancing this interaction for transcription-coupled repair.

bioRxiv · Sep 8, 2023Biophysics

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

Parkinson's Disease-linked LRRK2 structure and model for microtubule interaction

C. K. Deniston, J. Salogiannis, S. Mathea, D. M. Snead, I. Lahiri, O. Donosa, R. Watanabe, J. Böhning, A. K. Shiau, S. Knapp, E. Villa, S. L. Reck-Peterson, A. E. Leschziner

This study reports the structure of LRRK2 and its interaction with microtubules, showing that its conformation regulates binding and affects motor protein function.

bioRxiv · Jan 6, 2020Biophysics