Author

Fatima Kamal Zaidi

St. Jude Children's Research HospitalORCID 0000-0002-1986-4015Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Signature Assays, Organisms & Methods

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Assay:proteomics· 2 Approach:experimental assay· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1 Approach:machine learning (classical)· 1 Research Focus:protein folding & dynamics· 1 Approach:statistical model· 1

Frequent Co-Authors

Giulio TeseiiD· 2 shared Kresten Lindorff‐LarseniD· 2 shared Tanja MittagiD· 2 shared Anne BremeriD· 1 shared Anurag SinghiD· 1 shared Bhargavi H. Gindra· 1 shared Davit A. PotoyaniD· 1 shared Joseph L. BasallaiD· 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

Giulio TeseiORCID

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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

Prediction of phase separation propensities of disordered proteins from sequence

Sören von Bülow, Giulio Tesei, Fatima Kamal Zaidi, Tanja Mittag, Kresten Lindorff‐Larsen

The paper develops a machine learning model to predict phase separation propensities of disordered proteins from sequence, identifying 5% of human IDRs likely to undergo homotypic phase separation.

Proceedings of the National Academy of Sciences · Mar 25, 2025Peer-reviewedBiophysics