Results 41 to 50 of about 37,358 (155)

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

Human T cell glycosylation and implications on immune therapy for cancer [PDF]

, 2020
Glycosylation is an important post-translational modification, giving rise to a diverse and abundant repertoire of glycans on the cell surface, collectively known as the glycome.
Callewaert, Nico, De Bousser, Elien, Festjens, Nele, Meuris, Leander   +3 more
core   +1 more source

Protein O-GlcNAc Modification Increases in White Blood Cells After a Single Bout of Physical Exercise

Frontiers in Immunology, 2018
BackgroundProtein O-linked N-acetylglucosamine (O-GlcNAc) is a dynamic posttranslational modification influencing the function of many intracellular proteins.
Tamás Nagy, Tamás Nagy, Emese Kátai, Viktória Fisi, Tamás Tibor Takács, Antal Stréda, István Wittmann, Attila Miseta   +7 more
doaj   +1 more source

O‐GlcNAcylation Mediates Glucose‐Induced Alterations in Endothelial Cell Phenotype in Human Diabetes Mellitus

Journal of the American Heart Association: Cardiovascular and Cerebrovascular Disease, 2020
Background Posttranslational protein modification with O‐linked N‐acetylglucosamine (O‐GlcNAc) is linked to high glucose levels in type 2 diabetes mellitus (T2DM) and may alter cellular function.
Nobuyuki Masaki, Bihua Feng, Rosa Bretón‐Romero, Elica Inagaki, Robert M. Weisbrod, Jessica L. Fetterman, Naomi M. Hamburg   +6 more
doaj   +1 more source

Production of Glycopeptide Derivatives for Exploring Substrate Specificity of Human OGA Toward Sugar Moiety. [PDF]

, 2018
O-GlcNAcase (OGA) is the only enzyme responsible for removing N-acetyl glucosamine (GlcNAc) attached to serine and threonine residues on proteins. This enzyme plays a key role in O-GlcNAc metabolism.
Chen, Xi, Chen, Yi, Guo, Jianshuang, Li, Jing, Li, Shanshan, Li, Yanhong, Wang, Jiajia, Wang, Peng George, Wen, Liuqing, Zang, Lanlan, Zhang, Jiabin, Zhu, Hailiang   +11 more
core  

Nucleocytoplasmic human O-GlcNAc transferase is sufficient for O-GlcNAcylation of mitochondrial proteins [PDF]

, 2016
O-linked N-acetylglucosamine modification (O-GlcNAcylation) is a nutrient-dependent protein post-translational modification (PTM), dynamically and reversibly driven by two enzymes: O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA) that catalyse the ...
Akimoto, Andrew T. Ferenbach, Banerjee, Butkinaree, Cao, Comer, Corrado, Daan M.F. van Aalten, Daniel Mariappa, Dassanayaka, Dias, Dong, Exner, Frezza, Gawlowski, Gu, Haltiwanger, Haltiwanger, Hanover, Hanover, Hart, Hart, Hofer, Housley, Hu, Hube, Iyer, Iyer, Johnsen, Kreppel, Lazarus, Lazarus, Liu, Love, Love, Lozano, Ma, Ma, Nolte, Olichon, Pathak, Pekkurnaz, Riccardo Trapannone, Ruan, Shafi, Shin, Sohn, Tan, Torres, van den Ent, Walgren, Wang, Yang, Yi, Zhao, Zhou, Zhu   +56 more
core   +3 more sources