Cassandra M Joiner

Affiliations: 
Harvard Medical School, Boston, MA, United States 
Area:
Protein-protein interactions, O-GlcNAc Transferase
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"Cassandra Joiner"
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Parents

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Andrew L. Feig research assistant 2011-2012 Wayne State (Microtree)
Anna K. Mapp grad student 2012-2017 University of Michigan
 (Evaluation and utilization of photo-activatable unnatural amino acids for the study of in vivo protein-protein interactions)
Suzanne Walker post-doc 2017- Harvard Medical School
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Publications

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Potter SC, Gibbs BE, Hammel FA, et al. (2024) Dissecting OGT's TPR domain to identify determinants of cellular function. Proceedings of the National Academy of Sciences of the United States of America. 121: e2401729121
Joiner CM, Hammel FA, Janetzko J, et al. (2021) Protein Substrates Engage the Lumen of O-GlcNAc Transferase's Tetratricopeptide Repeat Domain in Different Ways. Biochemistry
Levine ZG, Potter SC, Joiner CM, et al. (2021) Mammalian cell proliferation requires noncatalytic functions of O-GlcNAc transferase. Proceedings of the National Academy of Sciences of the United States of America. 118
Joiner CM, Levine ZG, Aonbangkhen C, et al. (2019) Aspartate residues far from the active site drive O-GlcNAc transferase substrate selection. Journal of the American Chemical Society
Joiner CM, Breen ME, Mapp AK. (2019) Electron-deficient p-benzoyl-L-phenylalanine derivatives increase covalent chemical capture yields for protein-protein interactions. Protein Science : a Publication of the Protein Society
Joiner CM, Li H, Jiang J, et al. (2019) Structural characterization of the O-GlcNAc cycling enzymes: insights into substrate recognition and catalytic mechanisms. Current Opinion in Structural Biology. 56: 97-106
Joiner CM, Breen ME, Clayton J, et al. (2017) A Bifunctional Amino Acid Enables Both Covalent Chemical Capture and Isolation of in Vivo Protein-Protein Interactions. Chembiochem. 18: 181-184
Joiner CM, Breen ME, Clayton J, et al. (2016) A Bifunctional Amino Acid Enables Both Covalent Chemical Capture and Isolation of in Vivo Protein-Protein Interactions. Chembiochem : a European Journal of Chemical Biology
Lancia JK, Nwokoye A, Dugan A, et al. (2014) Sequence context and crosslinking mechanism affect the efficiency of in vivo capture of a protein-protein interaction. Biopolyers. 101: 391-397
Lancia JK, Nwokoye A, Dugan A, et al. (2014) Sequence context and crosslinking mechanism affect the efficiency of in vivo capture of a protein-protein interaction. Biopolymers. 101: 391-7
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