Results 31 to 40 of about 8,190 (170)

O‐GlcNAcylation regulates lysophosphatidic acid‐induced cell migration by regulating ERM family proteins

FEBS Open Bio, 2022
O‐GlcNAcylation of intracellular proteins (O‐GlcNAc) is a post‐translational modification that often competes with phosphorylation in diverse cellular signaling pathways.
Minseok Song, Pann‐Ghill Suh
doaj   +1 more source

Parallel identification of O-GlcNAc-modified proteins from cell lysates [PDF]

, 2004
We report a new strategy for the parallel identification of O-GlcNAc-glycosylated proteins from cell lysates. The approach permits specific proteins of interest to be rapidly interrogated for the modification in any tissue or cell type and can be ...
Ficarro, Scott B., Hsieh-Wilson, Linda C., Khidekel, Nelly, Peters, Eric C., Tai, Hwan-Ching   +4 more
core   +1 more source

The glycosyltransferase EOGT regulates adropin expression in decidualizing human endometrium [PDF]

, 2017
In pregnancy, resistance of endometrial decidual cells to stress signals is critical for the integrity of the feto-maternal interface and, by extension, survival of the conceptus. O-GlcNAcylation is an essential post-translational modification that links
Alam, Mohammad T., Aplin, John D., Barros, Flavio S. V., Brosens, Jan J., Ewington, Lauren J., Muter, Joanne, Ruane, Peter T., Vrljicak, Pavle, Westwood, Melissa   +8 more
core   +2 more sources

Nutrient-Driven O-GlcNAcylation at Promoters Impacts Genome-Wide RNA Pol II Distribution

Frontiers in Endocrinology, 2018
Nutrient-driven O-GlcNAcylation has been linked to epigenetic regulation of gene expression in metazoans. In C. elegans, O-GlcNAc marks the promoters of over 800 developmental, metabolic, and stress-related genes; these O-GlcNAc marked genes show a ...
Michael W. Krause, Dona C. Love, Salil K. Ghosh, Peng Wang, Sijung Yun, Tetsunari Fukushige, John A. Hanover   +6 more
doaj   +1 more source

Drosophila O-GlcNAcase Mutants Reveal an Expanded Glycoproteome and Novel Growth and Longevity Phenotypes

Cells, 2021
The reversible posttranslational O-GlcNAc modification of serine or threonine residues of intracellular proteins is involved in many cellular events from signaling cascades to epigenetic and transcriptional regulation.
Ilhan Akan, Adnan Halim, Sergey Y. Vakhrushev, Henrik Clausen, John A. Hanover   +4 more
doaj   +1 more source

A mutant O-GlcNAcase enriches Drosophila developmental regulators [PDF]

, 2017
YesProtein O-GlcNAcylation is a reversible post-translational modification of serines/threonines on nucleocytoplasmic proteins. It is cycled by the enzymes O-GlcNAc transferase (OGT) and O-GlcNAc hydrolase (O-GlcNAcase or OGA).
A Erkner, A Nandi, AC Diernfellner, Andrew T Ferenbach, B Charroux, B Guo, B Li, CF Teo, D Mariappa, D Mariappa, DA Sinclair, Daan M F van Aalten, Daniel Mariappa, David G Campbell, DM Webster, DY Chen, FV Rao, GI Miura, GW Hart, H Hahne, H Zhang, HR Huang, Iva Hopkins-Navratilova, J Ma, JC Trinidad, JE Rexach, JF Alfaro, K Sakabe, L Wang, M Ogawa, Matthias Trost, MB Lazarus, MC Gambetta, MC Gambetta, MC Gambetta, MM Gilbert, NE Zachara, Nithya Selvan, O Sekine, P Ramakrishnan, PT Radermacher, PW Ingham, PW Ingham, R Sprung, Ritchie Williamson, Robert Gourlay, S Kenwrick, S Park, S Pathak, S Zhang, SA Myers, SA Yuzwa, SY Cong, T Pradhan-Sundd, T Pradhan-Sundd, Tonia Aristotelous, TW Liu, Z Wang, Z Zhang   +58 more
core   +3 more sources

First comprehensive identification of cardiac proteins with putative increased O-GlcNAc levels during pressure overload hypertrophy.

PLoS ONE, 2022
Protein posttranslational modifications (PTMs) by O-GlcNAc globally rise during pressure-overload hypertrophy (POH). However, a major knowledge gap exists on the specific proteins undergoing changes in O-GlcNAc levels during POH primarily because this ...
Wei Zhong Zhu, Teresa Palazzo, Mowei Zhou, Dolena Ledee, Heather M Olson, Ljiljana Paša-Tolić, Aaron K Olson   +6 more
doaj   +1 more source

Liver X receptor regulates hepatic nuclear O-GlcNAc signaling and carbohydrate responsive element-binding protein activity [PDF]

, 2015
Liver X receptor (LXR)α and LXRβ play key roles in hepatic de novo lipogenesis through their regulation of lipogenic genes, including sterol regulatory element-binding protein (SREBP)-1c and carbohydrate responsive element-binding protein (ChREBP).
Bindesbøll, Christian, Fan, Qiong, Grønning-Wang, Line M, MacPherson, Laura, Mandrup, Susanne, Matthews, Jason, Nebb, Hilde I, Nørgaard, Rikke C, Pedersen, Thomas Å, Ruan, Hai-Bin, Steffensen, Knut R, Wu, Jing, Yang, Xiaoyong   +12 more
core   +2 more sources

Comprehensive mapping of O-GlcNAc modification sites using a chemically cleavable tag [PDF]

, 2016
The post-translational modification of serine or threonine residues of proteins with a single N-acetylglucosamine monosaccharide (O-GlcNAcylation) is essential for cell survival and function.
Griffin, Matthew E., Hsieh-Wilson, Linda C., Jenkins, Courtney L., Jensen, Elizabeth H., Mason, Daniel E., Peters, Eric C., Stone, Shannon E.   +6 more
core   +3 more sources

Incorporation of Novel Synthetic Glycolipids in Liposomal Nanoparticles Affects Opsonization and In Vivo Clearance

Angewandte Chemie, EarlyView.
We prepared five glycosylated liposomal nanoparticles (G‐LNPs) to investigate the role of glycosylation and protein corona in modulating the in vivo behavior of G‐LNPs. We show that IgG and complement C3 adsorption enhanced liposomal nanoparticle clearance, with IgG promoting subsequent C3 binding.
Yingjie Yu, Xuehan Li, Yu Gao, Shijia Tao, Xiaofei Li, Lemei Zhao, Wenshuai Han, Hao Fan, Ying Qiu, Man Wang, Luying Zhou, Xiaoyan Fang, Wenhua Yang, Haiyang Zhang, Volker Mailänder, Daniel Crespy, Katharina Landfester, Shuai Jiang, Xiangzhao Mao   +18 more
wiley   +2 more sources