Author

Cassandra M. Joiner

Observed names: Cassandra Joiner, Cassandra M Joiner

Observed institutions: Harvard University, St. Olaf College, University of Michigan

ORCID: 0000-0003-0476-9418

Observed ORCID: 0000-0003-0476-9418

OpenAlex ID: A5033965684

Structural characterization of the O-GlcNAc cycling enzymes: insights into substrate recognition and catalytic mechanisms

2019 · Cassandra M Joiner, Hao Li, et al. · Current Opinion in Structural Biology · 91

Mammalian cell proliferation requires noncatalytic functions of O-GlcNAc transferase

2021 · Zebulon G. Levine, Sarah C. Potter, et al. · Proceedings of the National Academy of Sciences · 82

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Aspartate Residues Far from the Active Site Drive O-GlcNAc Transferase Substrate Selection

2019 · Cassandra M. Joiner, Zebulon G. Levine, et al. · Journal of the American Chemical Society · 65

A Bifunctional Amino Acid Enables Both Covalent Chemical Capture and Isolation of in Vivo Protein–Protein Interactions

2016 · Cassandra M. Joiner, Meghan E. Breen, et al. · ChemBioChem · 40

Protein Substrates Engage the Lumen of O-GlcNAc Transferase’s Tetratricopeptide Repeat Domain in Different Ways

2021 · Cassandra M. Joiner, Forrest A. Hammel, et al. · Biochemistry · 33

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Sequence context and crosslinking mechanism affect the efficiency of in vivo capture of a protein–protein interaction

2013 · Jody K. Lancia, Adaora Nwokoye, et al. · Biopolymers · 18

Dissecting OGT’s TPR domain to identify determinants of cellular function

2024 · Sarah C. Potter, Bettine E. Gibbs, et al. · Proceedings of the National Academy of Sciences · 15

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Electron‐deficient p‐benzoyl‐ l ‐phenylalanine derivatives increase covalent chemical capture yields for protein–protein interactions

2019 · Cassandra M. Joiner, Meghan E. Breen, et al. · Protein Science · 12

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Photoactivatable O‐GlcNAc Transferase Library Enables Covalent Chemical Capture of Solvent‐Exposed TPR Domain Interactions

2024 · Cassandra M. Joiner, Tiarra J. Glogowski, et al. · ChemBioChem · 3

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Using Open-Source Bioinformatics and Visualization Tools to Explore the Structure and Function of SARS-CoV-2 Spike Protein

2022 · Laura L. Listenberger, Cassandra M. Joiner, et al. · CourseSource · 1

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Abstract 1062 Photoactivatable O-GlcNAc transferase library enables covalent chemical capture of solvent-exposed TPR domain interactions

2025 · Cassandra Joiner, Tiarra Glogowski, et al. · Journal of Biological Chemistry

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Abstract 1257 Mapping an adaptor protein interaction on O-GlcNAc transferase's tetratricopeptide (TPR) domain using photocrosslinking

2025 · Huy Huynh, Peter Leach, et al. · Journal of Biological Chemistry

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Control of glycosyltransferase activity by nucleotide‐binding active site residues in SECRET AGENT

2022 · Kaylee Philbrick, Dana Nelson, et al. · The FASEB Journal

Selection of GDP‐fucose by active site residues in Arabidopsis thaliana SPY

2022 · Jenelle Rolli, Kate Desrochers, et al. · The FASEB Journal

Mechanistic study of nucleotide‐sugar binding and catalysis in SECRET AGENT O‐GlcNAc Transferase

2022 · Dana Nelson, Kaylee Philbrick, et al. · The FASEB Journal

Evaluation and Utilization of Photo-Activatable Unnatural Amino Acids for The Study of Protein-Protein Interactions

2017 · Cassandra M. Joiner · Deep Blue (University of Michigan)

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Works count: 16

Citation count: 360

H-index: 8

I10-index: 8