Author

S. C. Otto

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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Biophysics· 2 Physiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Research Focus:cell signaling & trafficking· 1 Assay:fluorescence / live-cell microscopy· 1 Approach:genetic perturbation / CRISPR· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1 Assay:proteomics· 1 Research Focus:synaptic & neural circuits· 1

Frequent Co-Authors

S. E. Gordon· 2 shared A. Nhim· 1 shared A. Stratiievska· 1 shared C. J. Kuykendall· 1 shared C. P. Johnson· 1 shared D.-S. Koh· 1 shared E. G. Evans· 1 shared E. N. Senning· 1 shared

Activity by Year

2021-2024 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 17 mutual co-author links

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2 shared papersPhysiology

S. E. Gordon

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3 papers

Recent·Most cited

Genetic code expansion, click chemistry, and light-activated PI3K reveal details of membrane protein trafficking downstream of receptor tyrosine kinases

D.-S. Koh, A. Stratiievska, S. Jana, S. C. Otto, T. M. Swanson, A. Nhim, S. Carlson, M. Raza, L. A. Naves, E. N. Senning, R. A. Mehl, S. E. Gordon

The paper uses optogenetic PI3K activation and genetic code expansion to study RTK signaling, showing PI3K alone can traffic TRPV1 and insulin receptors to the plasma membrane.

eLife · Aug 20, 2024Peer-reviewedPhysiology

Long-distance tmFRET using bipyridyl- and phenanthroline-based ligands

S. E. Gordon, E. G. Evans, S. C. Otto, M. Tessmer, K. D. Shaffer, M. T. Gordon, J. Petersson, S. Stoll, W. N. Zagotta

This paper expands the working distance of tmFRET to 50 Å using new ligands, enabling precise measurement of conformational changes in maltose binding protein under physiological conditions.

bioRxiv · Oct 9, 2023Biophysics

Calcium Sensitive Allostery Regulates the PI(4,5)P2 Binding Site of the Dysferlin C2A Domain

S. C. Otto, P. N. Reardon, T. M. Kumar, C. J. Kuykendall, C. P. Johnson

The paper identifies how calcium binding affects the dynamics of the dysferlin C2A domain's phosphoinositide binding site, revealing a mechanism for calcium-dependent membrane targeting.

bioRxiv · Feb 10, 2021 · PreprintBiophysics