** Joiner lab members are bolded.

Listenberger, L.L., Joiner, C.M., Terrell, C.R. Using open-source bioinformatics and visualization tools to explore the structure and function of SARS-CoV-2 spike protein. CourseSource, 2022.

Postdoctoral Work:

Joiner, C.M., Hammel, F.A., Janetzko, J., Walker, S. Protein substrates engage the lumen of O-GlcNAc transferase’s tetratricopeptide repeat domain in different ways. Biochemistry 2021, 60, 11, 847-853.

Levine, Z.M., Potter, S.C., Joiner, C.M., Fei, G.Q., Nabet, B., Sonnett, M., Zachara, N.E., Gray, N.S., Paulo, J.A., Walker, S. Mammalian cell proliferation requires noncatalytic functions of O-GlcNAc transferase. Proc. Natl. Aca. Sci. USA. 2021, 118, 4, e2016778118

Joiner, C.M.*, Levine, Z.M.*, Aonbangkhen, C., Woo, C.M., Walker, S. Aspartate residues far from active site drive O-GlcNAc transferase substrate selection. Journal of American Chemical Society 2019, 141, 33, 12974-12978. *denotes co-first authors

Joiner, C.M., Li, H., Jiang, J., Walker, S. Structural characterization of the O-GlcNAc cycling enzymes: insights into substrate recognition and catalytic mechanisms. Current Opinions in Structural Biology 2019, 56, 97-106.

Graduate Work:

Joiner, C.M.*, Breen, M.E.*, Mapp, A.K. Electron-deficient p-benzoyl-L-phenylalanine derivatives increase covalent chemical capture yields for protein-protein interactions. Protein Science 2019, 28(6), 1163-1170. *denotes co-first authors

Joiner, C.M.*, Breen, M.E.*, Clayton, J., Mapp, A.K. A bifunctional amino acid enables both covalent chemical capture and isolation of in vivo protein-protein interactions. ChemBioChem 2017, 18(2), 181-184. *denotes co-first authors

Lancia, J., Nwokoye, A., Dugan, A., Joiner, C., Pricer, R., Mapp, A. Sequence context and crosslinking mechanism affect the efficiency of in vivo capture of protein-protein interactions. Biopolymers 2014, 101(4), 391-397.