Targeted covalent inhibition of O-GlcNAc transferase in cells

Worth, Matthew; Hu, Chia-Wei; Li, Hao; Fan, Dacheng; Estevez, Arielis; Zhu, Dongsheng; Wang, Ao; Jiang, Jiaoyang

doi:10.1039/C9CC04560K

Title: Targeted covalent inhibition of O-GlcNAc transferase in cells

Journal Article · Wed Jan 22 00:00:00 EST 2020 · Chem. Commun.

DOI:https://doi.org/10.1039/C9CC04560K· OSTI ID:1593438

Worth, Matthew; Hu, Chia-Wei; Li, Hao; Fan, Dacheng; Estevez, Arielis; Zhu, Dongsheng; Wang, Ao; Jiang, Jiaoyang ^[1]

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Research Organization:: Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)

Sponsoring Organization:: UNIVERSITYNIH

OSTI ID:: 1593438

Journal Information:: Chem. Commun., Vol. 55, Issue (88) ; 2019

Country of Publication:: United States

Language:: ENGLISH

References (27)

O- GlcNAc Cycling: A Link Between Metabolism and Chronic Disease Bond, Michelle R.; Hanover, John A. Annual Review of Nutrition, Vol. 33, Issue 1 https://doi.org/10.1146/annurev-nutr-071812-161240	journal	July 2013
O-GlcNAc processing enzymes: catalytic mechanisms, substrate specificity, and enzyme regulation Vocadlo, David J. Current Opinion in Chemical Biology, Vol. 16, Issue 5-6 https://doi.org/10.1016/j.cbpa.2012.10.021	journal	December 2012
O-GlcNAcylation at promoters, nutrient sensors, and transcriptional regulation Lewis, Brian A. Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms, Vol. 1829, Issue 11 https://doi.org/10.1016/j.bbagrm.2013.09.003	journal	November 2013
O-GlcNAc occurs cotranslationally to stabilize nascent polypeptide chains Zhu, Yanping; Liu, Ta-Wei; Cecioni, Samy Nature Chemical Biology, Vol. 11, Issue 5 https://doi.org/10.1038/nchembio.1774	journal	March 2015
Nutrient Regulation of Signaling, Transcription, and Cell Physiology by O-GlcNAcylation Hardivillé, Stéphan; Hart, Gerald W. Cell Metabolism, Vol. 20, Issue 2 https://doi.org/10.1016/j.cmet.2014.07.014	journal	August 2014
O-GlcNAcylation in Cancer Biology: Linking Metabolism and Signaling Ferrer, Christina M.; Sodi, Valerie L.; Reginato, Mauricio J. Journal of Molecular Biology, Vol. 428, Issue 16 https://doi.org/10.1016/j.jmb.2016.05.028	journal	August 2016
Discovery of O- GlcNAc Transferase Inhibitors Gross, Benjamin J.; Kraybill, Brian C.; Walker, Suzanne Journal of the American Chemical Society, Vol. 127, Issue 42 https://doi.org/10.1021/ja0555217	journal	October 2005
Hijacking a biosynthetic pathway yields a glycosyltransferase inhibitor within cells Gloster, Tracey M.; Zandberg, Wesley F.; Heinonen, Julia E. Nature Chemical Biology, Vol. 7, Issue 3 https://doi.org/10.1038/nchembio.520	journal	January 2011
A neutral diphosphate mimic crosslinks the active site of human O-GlcNAc transferase Jiang, Jiaoyang; Lazarus, Michael B.; Pasquina, Lincoln Nature Chemical Biology, Vol. 8, Issue 1 https://doi.org/10.1038/nchembio.711	journal	November 2011
Bisubstrate UDP–peptide conjugates as human O-GlcNAc transferase inhibitors Borodkin, Vladimir S.; Schimpl, Marianne; Gundogdu, Mehmet Biochemical Journal, Vol. 457, Issue 3 https://doi.org/10.1042/BJ20131272	journal	January 2014
A Small Molecule That Inhibits OGT Activity in Cells Ortiz-Meoz, Rodrigo F.; Jiang, Jiaoyang; Lazarus, Michael B. ACS Chemical Biology, Vol. 10, Issue 6 https://doi.org/10.1021/acschembio.5b00004	journal	March 2015
Discovery of a Low Toxicity O-GlcNAc Transferase (OGT) Inhibitor by Structure-based Virtual Screening of Natural Products Liu, Yubo; Ren, Yang; Cao, Yu Scientific Reports, Vol. 7, Issue 1 https://doi.org/10.1038/s41598-017-12522-0	journal	September 2017
Structure-Based Evolution of Low Nanomolar O-GlcNAc Transferase Inhibitors Martin, Sara E. S.; Tan, Zhi-Wei; Itkonen, Harri M. Journal of the American Chemical Society, Vol. 140, Issue 42 https://doi.org/10.1021/jacs.8b07328	journal	September 2018
The resurgence of covalent drugs Singh, Juswinder; Petter, Russell C.; Baillie, Thomas A. Nature Reviews Drug Discovery, Vol. 10, Issue 4 https://doi.org/10.1038/nrd3410	journal	April 2011
Electrophilic probes for deciphering substrate recognition by O-GlcNAc transferase Hu, Chia-Wei; Worth, Matthew; Fan, Dacheng Nature Chemical Biology, Vol. 13, Issue 12 https://doi.org/10.1038/nchembio.2494	journal	October 2017
Structural snapshots of the reaction coordinate for O-GlcNAc transferase Lazarus, Michael B.; Jiang, Jiaoyang; Gloster, Tracey M. Nature Chemical Biology, Vol. 8, Issue 12 https://doi.org/10.1038/nchembio.1109	journal	October 2012
Disparate proteome reactivity profiles of carbon electrophiles Weerapana, Eranthie; Simon, Gabriel M.; Cravatt, Benjamin F. Nature Chemical Biology, Vol. 4, Issue 7 https://doi.org/10.1038/nchembio.91	journal	May 2008
Promiscuity and Selectivity in Covalent Enzyme Inhibition: A Systematic Study of Electrophilic Fragments Jöst, Christian; Nitsche, Christoph; Scholz, Therese Journal of Medicinal Chemistry, Vol. 57, Issue 18 https://doi.org/10.1021/jm5006918	journal	September 2014
Using Protein-Confined Proximity To Determine Chemical Reactivity Kobayashi, Tomonori; Hoppmann, Christian; Yang, Bing Journal of the American Chemical Society, Vol. 138, Issue 45 https://doi.org/10.1021/jacs.6b08656	journal	November 2016
A chemical approach for identifying O-GlcNAc-modified proteins in cells Vocadlo, D. J.; Hang, H. C.; Kim, E. -J. Proceedings of the National Academy of Sciences, Vol. 100, Issue 16 https://doi.org/10.1073/pnas.1632821100	journal	July 2003
Changes in Metabolic Chemical Reporter Structure Yield a Selective Probe of O -GlcNAc Modification Chuh, Kelly N.; Zaro, Balyn W.; Piller, Friedrich Journal of the American Chemical Society, Vol. 136, Issue 35 https://doi.org/10.1021/ja504063c	journal	August 2014
One-pot three-enzyme synthesis of UDP-GlcNAc derivatives Chen, Yi; Thon, Vireak; Li, Yanhong Chemical Communications, Vol. 47, Issue 38 https://doi.org/10.1039/c1cc14034e	journal	January 2011
Highly Efficient Synthesis of UDP-GalNAc/GlcNAc Analogues with Promiscuous Recombinant Human UDP-GalNAc Pyrophosphorylase AGX1 Guan, Wanyi; Cai, Li; Wang, Peng George Chemistry - A European Journal, Vol. 16, Issue 45 https://doi.org/10.1002/chem.201002315	journal	October 2010
Analysis of nuclear pore protein p62 glycosylation Lubas, W. A.; Smith, M.; Starr, C. M. Biochemistry, Vol. 34, Issue 5 https://doi.org/10.1021/bi00005a025	journal	February 1995
Comparative Proteomic Analysis of Eleven Common Cell Lines Reveals Ubiquitous but Varying Expression of Most Proteins Geiger, Tamar; Wehner, Anja; Schaab, Christoph Molecular & Cellular Proteomics, Vol. 11, Issue 3 https://doi.org/10.1074/mcp.M111.014050	journal	January 2012
A variant of yellow fluorescent protein with fast and efficient maturation for cell-biological applications Nagai, Takeharu; Ibata, Keiji; Park, Eun Sun Nature Biotechnology, Vol. 20, Issue 1 https://doi.org/10.1038/nbt0102-87	journal	January 2002
Structure and function of extracellular O-GlcNAc Ogawa, Mitsutaka; Okajima, Tetsuya Current Opinion in Structural Biology, Vol. 56 https://doi.org/10.1016/j.sbi.2018.12.002	journal	June 2019

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