Cassandra M Joiner
Affiliations: | Harvard Medical School, Boston, MA, United States |
Area:
Protein-protein interactions, O-GlcNAc TransferaseGoogle:
"Cassandra Joiner"Mean distance: (not calculated yet)
Parents
Sign in to add mentorAndrew 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 |