Year |
Citation |
Score |
2021 |
Maynard JC, Chalkley RJ. Methods for Enrichment and Assignment of N-Acetylglucosamine Modification Sites. Molecular & Cellular Proteomics : McP. 20: 100031. PMID 33583772 DOI: 10.1074/Mcp.R120.002206 |
0.302 |
|
2020 |
Maynard JC, Fujihira H, Dolgonos GE, Suzuki T, Burlingame AL. Cytosolic N-GlcNAc proteins are formed by the action of endo-β-N-acetylglucosaminidase. Biochemical and Biophysical Research Communications. 530: 719-724. PMID 32782141 DOI: 10.1016/J.Bbrc.2020.06.127 |
0.374 |
|
2019 |
Liu B, Salgado OC, Singh S, Hippen KL, Maynard JC, Burlingame AL, Ball LE, Blazar BR, Farrar MA, Hogquist KA, Ruan HB. The lineage stability and suppressive program of regulatory T cells require protein O-GlcNAcylation. Nature Communications. 10: 354. PMID 30664665 DOI: 10.1038/S41467-019-08300-3 |
0.424 |
|
2017 |
Xu SL, Chalkley RJ, Maynard JC, Wang W, Ni W, Jiang X, Shin K, Cheng L, Savage D, Hühmer AF, Burlingame AL, Wang ZY. Proteomic analysis reveals O-GlcNAc modification on proteins with key regulatory functions in Arabidopsis. Proceedings of the National Academy of Sciences of the United States of America. PMID 28154133 DOI: 10.1073/Pnas.1610452114 |
0.365 |
|
2016 |
Maynard JC, Burlingame AL, Medzihradszky KF. Cysteine S-linked N-acetylglucosamine (S-GlcNAcylation), a new post-translational modification in mammals. Molecular & Cellular Proteomics : McP. PMID 27558639 DOI: 10.1074/Mcp.M116.061549 |
0.366 |
|
2016 |
Myers SA, Peddada S, Chatterjee N, Freidreich T, Tomoda K, Krings G, Thomas S, Broeker M, Maynard J, Thomson M, Pollard K, Yamanaka S, Burlingame AL, Panning B. SOX2 O-GlcNAcylation alters its protein-protein interactions and genomic occupancy to modulate gene expression in pluripotent cells. Elife. 5. PMID 26949256 DOI: 10.7554/Elife.10647 |
0.338 |
|
2016 |
Myers SA, Peddada S, Chatterjee N, Friedrich T, Tomoda K, Krings G, Thomas S, Maynard J, Broeker M, Thomson M, Pollard K, Yamanaka S, Burlingame AL, Panning B. Author response: SOX2 O-GlcNAcylation alters its protein-protein interactions and genomic occupancy to modulate gene expression in pluripotent cells Elife. DOI: 10.7554/Elife.10647.033 |
0.383 |
|
2012 |
Duerfeldt AS, Peterson LB, Maynard JC, Ng CL, Eletto D, Ostrovsky O, Shinogle HE, Moore DS, Argon Y, Nicchitta CV, Blagg BS. Development of a Grp94 inhibitor. Journal of the American Chemical Society. 134: 9796-804. PMID 22642269 DOI: 10.1021/Ja303477G |
0.56 |
|
2010 |
Maynard JC, Pham T, Zheng T, Jockheck-Clark A, Rankin HB, Newgard CB, Spana EP, Nicchitta CV. Gp93, the Drosophila GRP94 ortholog, is required for gut epithelial homeostasis and nutrient assimilation-coupled growth control. Developmental Biology. 339: 295-306. PMID 20044986 DOI: 10.1016/J.Ydbio.2009.12.023 |
0.57 |
|
2010 |
Lev A, Dimberu P, Das SR, Maynard JC, Nicchitta CV, Bennink JR, Yewdell JW. Efficient cross-priming of antiviral CD8+ T cells by antigen donor cells is GRP94 independent (Journal of Immunology (2009) 183, (4205-4210)) Journal of Immunology. 185: 770. DOI: 10.4049/Jimmunol.1090046 |
0.612 |
|
2009 |
Lev A, Dimberu P, Das SR, Maynard JC, Nicchitta CV, Bennink JR, Yewdell JW. Efficient cross-priming of antiviral CD8+ T cells by antigen donor cells is GRP94 independent. Journal of Immunology (Baltimore, Md. : 1950). 183: 4205-10. PMID 19752220 DOI: 10.4049/Jimmunol.0901828 |
0.649 |
|
2008 |
Lev A, Takeda K, Zanker D, Maynard JC, Dimberu P, Waffarn E, Gibbs J, Netzer N, Princiotta MF, Neckers L, Picard D, Nicchitta CV, Chen W, Reiter Y, Bennink JR, et al. The exception that reinforces the rule: crosspriming by cytosolic peptides that escape degradation. Immunity. 28: 787-98. PMID 18549799 DOI: 10.1016/J.Immuni.2008.04.015 |
0.643 |
|
2008 |
Tewalt EF, Maynard JC, Walters JJ, Schell AM, Berwin BL, Nicchitta CV, Norbury CC. Redundancy renders the glycoprotein 96 receptor scavenger receptor A dispensable for cross priming in vivo. Immunology. 125: 480-91. PMID 18489571 DOI: 10.1111/J.1365-2567.2008.02861.X |
0.675 |
|
2006 |
Chu F, Maynard JC, Chiosis G, Nicchitta CV, Burlingame AL. Identification of novel quaternary domain interactions in the Hsp90 chaperone, GRP94. Protein Science : a Publication of the Protein Society. 15: 1260-9. PMID 16731965 DOI: 10.1110/Ps.052065106 |
0.55 |
|
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