Author

Renjith Viswanathan

Brown UniversityORCID 0000-0002-2875-2090Unclaimed ORCID profile · follow to get notified of new preprints

Biology Disciplines

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Biochemistry· 2 Genomics· 1

Signature Assays, Organisms & Methods

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Organism:human· 2 Research Focus:protein folding & dynamics· 2 Assay:proteomics· 2 Approach:biophysical modeling· 1 Research Focus:cell type annotation· 1 Research Focus:cell-cell communication· 1 Approach:deep learning· 1 Research Focus:differential expression· 1

Frequent Co-Authors

Nicolas Lux FawziiD· 3 shared Jayakrishna ShenoyiD· 2 shared Jeetain MittaliD· 2 shared Priyesh MohantyiD· 2 shared Ryan Z PuterbaughiD· 2 shared Szu‐Huan WangiD· 2 shared Victoria Johnson· 2 shared Alexander E. ConicellaiD· 1 shared

Activity by Year

2024-2025 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 36 mutual co-author links

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3 shared papersBiochemistry

Nicolas Lux FawziORCID

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3 papers

Recent·Most cited

Site-specific methionine oxidation alters structure and phase separation of TDP-43 C-terminal domain

Busra Ozguney, Ryan Z Puterbaugh, Renjith Viswanathan, Jayakrishna Shenoy, Priyesh Mohanty, Jeetain Mittal, Nicolas Lux Fawzi

This study shows methionine oxidation in TDP-43's C-terminal domain disrupts structure and phase separation through region-specific mechanisms.

bioRxiv · Dec 16, 2025 · PreprintBiochemistry

Structural details of helix-mediated TDP-43 C-terminal domain multimerization

Azamat Rizuan, Jayakrishna Shenoy, Priyesh Mohanty, Patricia M. dos Passos, José F. Mercado Ortiz, Leanna Bai, Renjith Viswanathan, Julia Zaborowksy, Szu‐Huan Wang, Victoria Johnson, Lohany Dias Mamede, Amanda R. Titus, Yuna M. Ayala, Rodolfo Ghirlando, Jeetain Mittal, Nicolas Lux Fawzi

This study investigates the structural basis of TDP-43 C-terminal domain multimerization using biophysical experiments, AlphaFold2-Multimer, and simulations, revealing helical oligomerization and the role of specific residues in phase separation and disease.

Nature Communications · Nov 26, 2025Peer-reviewedBiochemistry

A dual DNA/RNA-binding factor regulates co-transcriptional splicing through target RNA interaction and modulates splicing factor dynamics

Mukulika Ray, Julia Zaborowsky, Pranav Mahableshwarkar, Smriti Vaidyanathan, Jasmine Shum, Annie Huang, Renjith Viswanathan, Isabelle Pilo, Victoria Chen, Kaitlyn Cortez, Ashley Mae Conard, Szu‐Huan Wang, Victoria Johnson, Noah Wake, Alexander E. Conicella, , Erica Larschan

The paper shows CLAMP, a DNA-binding factor, regulates sex-specific splicing by interacting with RNA and modulating RBP dynamics.

bioRxiv · Jan 11, 2024 · PreprintGenomics