Author

S. Sreenivasan

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 Microbiology· 1

Signature Assays, Organisms & Methods

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Research Focus:cell type annotation· 2 Approach:experimental assay· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:differential expression· 1 Organism:E. coli· 1 Organism:human· 1 Research Focus:metabolism & bioenergetics· 1 Research Focus:protein folding & dynamics· 1

Frequent Co-Authors

A. W. Fenton· 2 shared L. Swint-Kruse· 2 shared A. Ladokhin· 1 shared C. L. Bird· 1 shared C. Menjivar· 1 shared C. Weeramange· 1 shared E. Kosa· 1 shared J. D. Fontes· 1 shared

Activity by Year

2023-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 30 mutual co-author links

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2 shared papersMicrobiology

A. W. Fenton

Mutual co-authors in cluster

Author profile →

2 papers

Recent·Most cited

Fructose-1-kinase has pleiotropic roles in Escherichia coli

C. Weeramange, C. Menjivar, P. T. O'Neil, S. El Qaidi, K. S. Harrison, S. Meinhardt, C. L. Bird, S. Sreenivasan, A. W. Fenton, P. S. Hefty, P. R. Hardwidge, J. L. Bose, L. Swint-Kruse

This study shows that fructose-1-kinase in E. coli can reverse its reaction to generate F-1-P from F-1,6-BP, binds Cra, and influences metabolism and biofilm formation beyond fructose catabolism.

bioRxiv · Dec 14, 2023 · PreprintMicrobiology

The intrinsically disordered transcriptional activation domain of CIITA is functionally tuneable by single substitutions: An exception or a new paradigm?

S. Sreenivasan, P. Heffren, K.-S. Suh, M. V. Rodnin, E. Kosa, A. W. Fenton, A. Ladokhin, P. E. Smith, J. D. Fontes, L. Swint-Kruse

The study shows that the intrinsically disordered activation domain of CIITA is tuneable by single amino acid substitutions, challenging the acidic exposure model and suggesting variability in IDR tuneability.

bioRxiv · Nov 2, 2023Biochemistry