Author

S. E. Kane

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Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1 Assay:proteomics· 1

Frequent Co-Authors

A. Celis· 1 shared D. Jiang· 1 shared E. Denny· 1 shared E. Monterroso· 1 shared E. Parga· 1 shared F. Zhou· 1 shared J. Momand· 1 shared M. L. Phillips· 1 shared

Activity by Year

2017-2017 · peak 1/yr

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10 top collaborators · 45 mutual co-author links

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1 shared paperBiochemistry

A. Celis

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1 paper

Recent·Most cited

t-Darpp is an elongated monomer that binds to calcium and is phosphorylated by cyclin-dependent kinases 1 and 5

J. Momand, P. Magdziarz, Y. Feng, D. Jiang, E. Parga, A. Celis, E. Denny, X. Wang, M. L. Phillips, E. Monterroso, S. E. Kane, F. Zhou

This study characterizes t-Darpp's structure, metal-binding, and phosphorylation by CDK1 and CDK5, revealing its monomeric form and calcium-binding properties.

bioRxiv · Jun 19, 2017Biochemistry