Author

L. Swint-Kruse

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 Biophysics· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Research Focus:protein folding & dynamics· 6 Approach:statistical model· 5 Research Focus:cell type annotation· 4 Approach:experimental assay· 4 Organism:human· 4 Assay:proteomics· 4 Research Focus:cell signaling & trafficking· 2 Research Focus:differential expression· 2

Frequent Co-Authors

A. W. Fenton· 6 shared D. J. Parente· 2 shared S. Sreenivasan· 2 shared T. Wu· 2 shared A. Ladokhin· 1 shared B. Hagenbuch· 1 shared C. J. Weeramange· 1 shared C. L. Bird· 1 shared

Activity by Year

2018-2023 · peak 4/yr

Co-Author Collaboration Network

10 top collaborators · 16 mutual co-author links

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6 shared papersBiochemistry

A. W. Fenton

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Author profile →

8 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

Substitutions at Non-Conserved Rheostat Positions Modulate Function by Re-Wiring Long-Range, Dynamic Interactions

P. Campitelli, L. Swint-Kruse, S. B. Ozkan

The paper shows that substitutions at nonconserved positions in the LacI protein alter DNA binding by re-wiring long-range dynamic interactions.

bioRxiv · Jul 2, 2020Biophysics

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

Reconciling in vitro and in vivo activities of engineered, LacI-based repressor proteins: Contributions of DNA looping and operator sequence variation

S. Tungtur, K. M. Schwingen, J. J. Riepe, C. J. Weeramange, L. Swint-Kruse

The paper compares in vitro and in vivo activities of engineered LacI-based repressor proteins, showing that DNA looping and operator sequence variation significantly affect their function.

bioRxiv · Nov 23, 2018 · PreprintBiochemistry