Author

Y. X. Lin

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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Biochemistry· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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Assay:cryo-EM· 2 Approach:experimental assay· 2 Organism:human· 2 Research Focus:protein structure prediction· 2 Research Focus:cell signaling & trafficking· 1 Approach:microscopy & imaging analysis· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

A. E. Leschziner· 2 shared A. M. Dickey· 2 shared S. L. Reck-Peterson· 2 shared D. Chatterjee· 1 shared D. M. Snead· 1 shared E. J. Fay· 1 shared J. M. Reimer· 1 shared M. D. Daugherty· 1 shared

Activity by Year

2022-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 35 mutual co-author links

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2 shared papersBiochemistry

A. E. Leschziner

Mutual co-authors in cluster

Author profile →

2 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