Author

Tapojyoti Das

St. Jude Children's Research HospitalORCID 0000-0002-4644-1499Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Approach:statistical model· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:host-pathogen & immune response· 1 Research Focus:protein folding & dynamics· 1 Assay:protein sequence· 1 Assay:proteomics· 1

Frequent Co-Authors

Anurag SinghiD· 2 shared Fatima Kamal ZaidiiD· 2 shared Priya R. BanerjeeiD· 2 shared Tanja MittagiD· 2 shared Tharun Selvam MahendraniD· 2 shared Xinrui GuiiD· 2 shared Anne BremeriD· 1 shared Bhargavi H. Gindra· 1 shared

Activity by Year

2025-2026 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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2 shared papersBiophysics

Anurag SinghORCID

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2 papers

Recent·Most cited

Viscoelasticity and interface properties of multi-component condensates govern protein sequestration and suppression of amyloid formation

Tharun Selvam Mahendran, Xinrui Gui, Anne Bremer, Anurag Singh, Fatima Kamal Zaidi, Giulio Tesei, Joseph L. Basalla, Sagar Chittori, Melissa R. Marzahn, Bhargavi H. Gindra, Richoo B. Davis, Tapojyoti Das, Kresten Lindorff‐Larsen, Davit A. Potoyan, Tanja Mittag, Priya R. Banerjee

This study shows multi-component biomolecular condensates suppress amyloid formation by sequestering proteins, limiting their availability for fibril formation.

bioRxiv · Jul 9, 2026 · PreprintBiophysics

Tunable metastability of condensates reconciles their dual roles in amyloid fibril formation

Tapojyoti Das, Fatima Kamal Zaidi, Mina Farag, Kiersten M. Ruff, Tharun Selvam Mahendran, Anurag Singh, Xinrui Gui, James Messing, J. Paul Taylor, Priya R. Banerjee, Rohit V. Pappu, Tanja Mittag

The paper shows that separable interactions in A1-LCD allow tunable metastability of condensates, which can suppress amyloid fibril formation even with ALS mutations.

Molecular Cell · May 28, 2025Peer-reviewedBiophysics