John Janetzko

Affiliations: 
Stanford University School of Medicine, Palo Alto, CA, United States 
Area:
GPCRs, biochemistry, biophysics, GRK, post-translational modifications, mass spectrometry
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"John Janetzko"
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Parents

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Datong Song research assistant 2007-2007 University of Toronto
Robert A. Batey research assistant 2008-2011 University of Toronto
Daniel E. Kahne grad student 2012-2017 Harvard
Suzanne Walker grad student 2012-2017 Harvard Medical School
Brian K. Kobilka post-doc 2017- Stanford 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
Janetzko J, Kise R, Barsi-Rhyne B, et al. (2022) Membrane phosphoinositides regulate GPCR-β-arrestin complex assembly and dynamics. Cell
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
Huang W, Masureel M, Qianhui Q, et al. (2020) Structure of the neurotensin receptor 1 in complex with β-arrestin 1. Nature
Martin SES, Tan ZW, Itkonen HM, et al. (2018) Structure-Based Evolution of Low Nanomolar O-GlcNAc Transferase Inhibitors. Journal of the American Chemical Society
Janetzko J, Walker S. (2017) Aspartate glycosylation triggers isomerization to isoaspartate. Journal of the American Chemical Society
Janetzko J, Trauger SA, Lazarus MB, et al. (2016) How the glycosyltransferase OGT catalyzes amide bond cleavage. Nature Chemical Biology
Goodreid JD, Janetzko J, Santa Maria JP, et al. (2016) Development and Characterization of Potent Cyclic Acyldepsipeptide Analogues with Increased Antimicrobial Activity. Journal of Medicinal Chemistry. 59: 624-46
Ortiz-Meoz RF, Jiang J, Lazarus MB, et al. (2015) A small molecule that inhibits OGT activity in cells. Acs Chemical Biology. 10: 1392-7
Janetzko J, Walker S. (2014) The making of a sweet modification: structure and function of O-GlcNAc transferase. The Journal of Biological Chemistry. 289: 34424-32
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