Age-related loss of neural stem cell O-GlcNAc promotes a glial fate switch through STAT3 activation von White, Charles W., Fan, Xuelai, Maynard, Jason C., Wheatley, Elizabeth G., Bieri, Gregor, Couthouis, Julien, Burlingame, Alma L., Villeda, Saul A.

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The lineage stability and suppressive program of regulatory T cells require protein O-GlcNAcylation von Liu, Bing, Salgado, Oscar C., Singh, Sangya, Hippen, Keli L., Maynard, Jason C., Burlingame, Alma L., Ball, Lauren E., Blazar, Bruce R., Farrar, Michael A., Hogquist, Kristin A., Ruan, Hai-Bin

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SPINDLY mediates O-fucosylation of hundreds of proteins and sugar-dependent growth in Arabidopsis von Bi, Yang, Shrestha, Ruben, Zhang, Zhenzhen, Hsu, Chuan-Chih, Reyes, Andres V, Karunadasa, Sumudu, Baker, Peter R, Maynard, Jason C, Liu, Yang, Hakimi, Amirmansoor, Lopez-Ferrer, Daniel, Hassan, Tahmid, Chalkley, Robert J, Xu, Shou-Ling, Wang, Zhi-Yong

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Schwann Cell O-GlcNAc Glycosylation Is Required for Myelin Maintenance and Axon Integrity von Kim, Sungsu, Maynard, Jason C, Sasaki, Yo, Strickland, Amy, Sherman, Diane L, Brophy, Peter J, Burlingame, Alma L, Milbrandt, Jeffrey

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O-GlcNAc glycosylation orchestrates fate decision and niche function of bone marrow stromal progenitors von Zhang, Zengdi, Huang, Zan, Awad, Mohamed, Elsalanty, Mohammed, Cray, James, Ball, Lauren E, Maynard, Jason C, Burlingame, Alma L, Zeng, Hu, Mansky, Kim C, Ruan, Hai-Bin

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Processing of progranulin into granulins involves multiple lysosomal proteases and is affected in frontotemporal lobar degeneration von Mohan, Swetha, Sampognaro, Paul J, Argouarch, Andrea R, Maynard, Jason C, Welch, Mackenzie, Patwardhan, Anand, Courtney, Emma C, Zhang, Jiasheng, Mason, Amanda, Li, Kathy H, Huang, Eric J, Seeley, William W, Miller, Bruce L, Burlingame, Alma, Jacobson, Mathew P, Kao, Aimee W

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Methods for Enrichment and Assignment of N-Acetylglucosamine Modification Sites von Maynard, Jason C., Chalkley, Robert J.

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Gp93, the Drosophila GRP94 ortholog, is required for gut epithelial homeostasis and nutrient assimilation-coupled growth control von Maynard, Jason C., Pham, Trang, Zheng, Tianli, Jockheck-Clark, Angela, Rankin, Helen B., Newgard, Christopher B., Spana, Eric P., Nicchitta, Christopher V.

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Schwann cell O-GlcNAcylation promotes peripheral nerve remyelination via attenuation of the AP-1 transcription factor JUN von Kim, Sungsu, Maynard, Jason C., Strickland, Amy, Burlingame, Alma L., Milbrandt, Jeffrey

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Cysteine S-linked N-acetylglucosamine (S-GlcNAcylation), A New Post-translational Modification in Mammals von Maynard, Jason C., Burlingame, Alma L., Medzihradszky, Katalin F.

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Epithelial STAT6 O-GlcNAcylation drives a concerted anti-helminth alarmin response dependent on tuft cell hyperplasia and Gasdermin C von Zhao, Ming, Ren, Kaiqun, Xiong, Xiwen, Xin, Yue, Zou, Yujie, Maynard, Jason C., Kim, Angela, Battist, Alexander P., Koneripalli, Navya, Wang, Yusu, Chen, Qianyue, Xin, Ruyue, Yang, Chenyan, Huang, Rong, Yu, Jiahui, Huang, Zan, Zhang, Zengdi, Wang, Haiguang, Wang, Daoyuan, Xiao, Yihui, Salgado, Oscar C., Jarjour, Nicholas N., Hogquist, Kristin A., Revelo, Xavier S., Burlingame, Alma L., Gao, Xiang, von Moltke, Jakob, Lin, Zhaoyu, Ruan, Hai-Bin

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Proteomic analysis reveals O-GlcNAc modification on proteins with key regulatory functions in Arabidopsis von Xu, Shou-Ling, Chalkley, Robert J., Maynard, Jason C., Wang, Wenfei, Ni, Weimin, Jiang, Xiaoyue, Shin, Kihye, Cheng, Ling, Savage, Dasha, Hühmer, Andreas F. R., Burlingame, Alma L., Wang, Zhi-Yong

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Cytosolic N-GlcNAc proteins are formed by the action of endo-β-N-acetylglucosaminidase von Maynard, Jason C., Fujihira, Haruhiko, Dolgonos, Gabby E., Suzuki, Tadashi, Burlingame, Alma L.

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Development of a Grp94 inhibitor von Duerfeldt, Adam S, Peterson, Laura B, Maynard, Jason C, Ng, Chun Leung, Eletto, Davide, Ostrovsky, Olga, Shinogle, Heather E, Moore, David S, Argon, Yair, Nicchitta, Christopher V, Blagg, Brian S. J

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Epithelial STAT6 O-GlcNAcylation drives a concerted anti-helminth alarmin response dependent on tuft cell hyperplasia and Gasdermin C von Zhao, Ming, Ren, Kaiqun, Xiong, Xiwen, Xin, Yue, Zou, Yujie, Maynard, Jason C., Kim, Angela, Battist, Alexander P., Koneripalli, Navya, Wang, Yusu, Chen, Qianyue, Xin, Ruyue, Yang, Chenyan, Huang, Rong, Yu, Jiahui, Huang, Zan, Zhang, Zengdi, Wang, Haiguang, Wang, Daoyuan, Xiao, Yihui, Salgado, Oscar C., Jarjour, Nicholas N., Hogquist, Kristin A., Revelo, Xavier S., Burlingame, Alma L., Gao, Xiang, von Moltke, Jakob, Lin, Zhaoyu, Ruan, Hai-Bin

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Redundancy renders the glycoprotein 96 receptor scavenger receptor A dispensable for cross priming in vivo von Tewalt, Eric F., Maynard, Jason C., Walters, Julie Jo, Schell, Amanda M., Berwin, Brent L., Nicchitta, Christopher V., Norbury, Christopher C.

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The Exception that Reinforces the Rule: Crosspriming by Cytosolic Peptides that Escape Degradation von Lev, Avital, Takeda, Kazuyo, Zanker, Damien, Maynard, Jason C., Dimberu, Peniel, Waffarn, Elizabeth, Gibbs, James, Netzer, Nir, Princiotta, Michael F., Neckers, Len, Picard, Didier, Nicchitta, Christopher V., Chen, Weisan, Reiter, Yoram, Bennink, Jack R., Yewdell, Jonathan W.

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Efficient Cross-Priming of Antiviral CD8+ T Cells by Antigen Donor Cells Is GRP94 Independent von Lev, Avital, Dimberu, Peniel, Das, Suman R, Maynard, Jason C, Nicchitta, Christopher V, Bennink, Jack R, Yewdell, Jonathan W

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Identification of novel quaternary domain interactions in the Hsp90 chaperone, GRP94 von Chu, Feixia, Maynard, Jason C., Chiosis, Gabriela, Nicchitta, Christopher V., Burlingame, Alma L.

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Methods for Enrichment and Assignment of N-Acetylglucosamine Modification Sites von Maynard, Jason C, Chalkley, Robert J

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