Author

Hanlin Wang

University of TorontoORCID 0000-0002-7823-4259Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Signature Assays, Organisms & Methods

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Assay:cryo-EM· 2 Approach:experimental assay· 2 Research Focus:protein structure prediction· 2 Organism:Arabidopsis· 1 Approach:biophysical modeling· 1 Organism:human· 1 Approach:microscopy & imaging analysis· 1 Organism:mouse· 1

Frequent Co-Authors

John L. RubinsteiniD· 3 shared Alexander I. M. SeveriD· 1 shared Fabian Fink· 1 shared Huaying ZhaoiD· 1 shared James M. AraminiiD· 1 shared Jeffrey P. BoniniD· 1 shared Karin SchumacheriD· 1 shared Lewis E. KayiD· 1 shared

Activity by Year

2024-2026 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 22 mutual co-author links

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3 shared papersBiochemistry

John L. RubinsteinORCID

Mutual co-authors in cluster

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3 papers

Recent·Most cited

Cryo-EM structure of the Arabidopsis thaliana V-type ATPase

Mariia Khamina, Nadja Wunsch, Upendo Lupanga, Fabian Fink, Hanlin Wang, Piers A. Hemsley, Waltraud X. Schulze, Karin Schumacher, John L. Rubinstein

The paper determines the Cryo-EM structure of the Arabidopsis thaliana V-type ATPase, revealing its catalytic cycle and organelle-specific interactions with TLDc proteins.

Structure · Oct 1, 2026Peer-reviewedBiochemistry

The dynamic and heterogeneous structure of the non-canonical inflammasome

Alexander I. M. Sever, James M. Aramini, Jeffrey P. Bonin, Huaying Zhao, Hanlin Wang, John L. Rubinstein, Peter Schuck, Lewis E. Kay

This paper determines the structure and dynamics of the non-canonical inflammasome using biophysical methods, showing it is heterogeneous and primed for rapid substrate cleavage.

Proceedings of the National Academy of Sciences · Aug 3, 2026Peer-reviewedBiophysics

Structure of yeast RAVE bound to a partial V1 complex

Hanlin Wang, Maureen Tarsio, Patricia M. Kane, John L. Rubinstein

The paper determines the structure of yeast RAVE bound to a partial V1 complex using cryo-EM, revealing its role in facilitating V1-VO reassociation.

Proceedings of the National Academy of Sciences · Dec 3, 2024Peer-reviewedBiochemistry