Author

S. C. Garman

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· 4

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:protein folding & dynamics· 2 Assay:structural biology· 2 Research Focus:cell type annotation· 1 Organism:human· 1 Approach:mechanistic / dynamical model· 1 Assay:protein structure· 1 Approach:statistical model· 1

Frequent Co-Authors

C. Ozden· 2 shared M. Stratton· 2 shared A. P. Torres-Ocampo· 1 shared A. Samkutty· 1 shared A. T. Ocampo· 1 shared B. A. Kelch· 1 shared C. E. Bobst· 1 shared C. Gaubitz· 1 shared

Activity by Year

2020-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 15 mutual co-author links

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2 shared papersBiochemistry

C. Ozden

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4 papers

Recent·Most cited

Human Saposin B Ligand Binding and Presentation to α-Galactosidase A

T. K. Sawyer, E. Aral, J. V. Staros, C. E. Bobst, S. C. Garman

This study investigates how saposin B presents Gb3 to α-galactosidase A using biochemical assays, crystal structures, and cross-linking to reveal molecular recognition mechanisms.

bioRxiv · Apr 4, 2024 · PreprintBiochemistry

A domain-swapped CaMKII conformation facilitates linker-mediated allosteric regulation

V. C. B. Nguyen, C. Özden, K. Dong, O. Koc, A. P. Torres-Ocampo, N. Dziedzic, D. Flaherty, J. Huang, S. Sankura, N. L. Abromson, D. R. Tomchick, R. A. Fissore, J. Chen, S. C. Garman, M. Stratton

This study identifies a domain-swapped conformation in CaMKII that enables linker-mediated allosteric regulation, demonstrated through structural, computational, and live-cell analyses.

bioRxiv · Mar 24, 2024Biochemistry

CaMKIIalpha and CaMKIIbeta hub domains adopt distinct oligomeric states and stabilities

C. Ozden, S. MacManus, R. Adafia, A. Samkutty, A. T. Ocampo, S. C. Garman, M. M. Stratton

This study investigates the oligomeric states and stability of CaMKIIalpha and CaMKIIbeta hub domains, revealing differences in their stoichiometry and stability in solution.

bioRxiv · Oct 9, 2023 · PreprintBiochemistry

CaMKII binds both substrates and activators at the active site

C. Ozden, R. Sloutsky, T. Mitsugi, N. Santos, E. Agnello, C. Gaubitz, J. Foster, E. Lapinskas, E. A. Esposito, T. Saneyoshi, B. A. Kelch, S. C. Garman, Y. Hayashi, M. Stratton

This study challenges a longstanding model of CaMKII activation by showing that activators and substrates bind to a single site rather than distinct S- and T-sites.

bioRxiv · Oct 25, 2020Biochemistry