Author

A. W. Fenton

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· 6 Microbiology· 1

Signature Assays, Organisms & Methods

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Organism:human· 5 Research Focus:protein folding & dynamics· 5 Research Focus:cell type annotation· 4 Approach:experimental assay· 4 Assay:proteomics· 4 Approach:statistical model· 4 Research Focus:cell signaling & trafficking· 2 Research Focus:differential expression· 2

Frequent Co-Authors

L. Swint-Kruse· 6 shared D. J. Parente· 2 shared Q. Tang· 2 shared S. Sreenivasan· 2 shared T. Wu· 2 shared A. Artigues· 1 shared A. Ladokhin· 1 shared B. Hagenbuch· 1 shared

Activity by Year

2019-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 16 mutual co-author links

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6 shared papersBiochemistry

L. Swint-Kruse

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Author profile →

7 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

"Multiplex" rheostat positions cluster around allosterically critical regions of the lactose repressor protein

L. E. Bantis, D. J. Parente, A. W. Fenton, L. Swint-Kruse

The paper identifies multiplex rheostat positions in LacI that modulate multiple functional parameters and shows they overlap with allosteric regions, suggesting complex biophysical effects.

bioRxiv · Nov 17, 2020 · PreprintBiochemistry

A clinically-relevant polymorphism in the Na+/taurocholate cotransporting polypeptide (NTCP) occurs at a rheostat position

M. J. Ruggiero, S. Malhotra, A. W. Fenton, L. Swint-Kruse, J. Karanicolas, B. Hagenbuch

The paper identifies a rheostat position in NTCP where substitutions produce varied functional effects, showing substrate-dependent transport changes and structural stability variations.

bioRxiv · Jul 2, 2020Biochemistry

Identification of biochemically neutral positions in liver pyruvate kinase

T. A. Martin, T. Wu, Q. Tang, L. L. Dougherty, D. J. Parente, L. Swint-Kruse, A. W. Fenton

The paper identifies biochemically neutral positions in human liver pyruvate kinase by analyzing evolutionary patterns and functional outcomes of amino acid substitutions.

bioRxiv · May 12, 2020Biochemistry

Functional tunability from a distance: Rheostat positions influence allosteric coupling between two distant binding sites

T. Wu, L. Swint-Kruse, A. W. Fenton

The paper evaluates how distant mutations affect allosteric coupling between effector binding sites in pyruvate kinase, finding that distant positions can fully tune allosteric coupling.

bioRxiv · May 9, 2019Biochemistry

Mutational mimics of allosteric effectors: a genome editing design to validate allosteric drug targets

Q. Tang, M. T. Villar, A. Artigues, J. P. Thyfault, U. Apte, H. Zhu, K. R. Peterson, A. W. Fenton

The paper identifies point mutations that mimic allosteric effectors in human liver pyruvate kinase to validate potential drug targets for treating diabetes.

bioRxiv · May 9, 2019Biochemistry