Results 61 to 70 of about 20,888 (214)

‘O-GlcNAc Code’ Mediated Biological Functions of Downstream Proteins

Molecules, 2018
As one of the post-translational modifications, O-linked β-N-acetylglucosamine (O-GlcNAc) modification (O-GlcNAcylation) often occurs on serine (Ser) and threonine (Thr) residues of specific substrate cellular proteins via the addition of O-GlcNAc ...
Linhong Zhao, Junaid Ali Shah, Yong Cai, Jingji Jin   +3 more
doaj   +1 more source

The EGF repeat-specific O-GlcNAc-transferase Eogt interacts with notch signaling and pyrimidine metabolism pathways in Drosophila. [PDF]

PLoS ONE, 2013
The O-GlcNAc transferase Eogt modifies EGF repeats in proteins that transit the secretory pathway, including Dumpy and Notch. In this paper, we show that the Notch ligands Delta and Serrate are also substrates of Eogt, that mutation of a putative UDP ...
Reto Müller, Andreas Jenny, Pamela Stanley   +2 more
doaj   +1 more source

O-GlcNAcylation regulates extracellular signal-regulated kinase (ERK) activation in Alzheimer’s disease

Frontiers in Aging Neuroscience, 2023
IntroductionAberrant activation of Extracellular Signal-Regulated Kinase (ERK) signaling is associated with Alzheimer’s disease (AD) pathogenesis. For example, enhanced ERK signal activation mediated by Apolipoprotein E4 (APOE4), which is a critical ...
Sophiya John Ephrame, Gentry K. Cork, Victoria Marshall, Margaret A. Johnston, Jenna Shawa, Ibtihal Alghusen, Amy Qiang, Aspin R. Denson, Marisa S. Carman, Halyna Fedosyuk, Russell H. Swerdlow, Russell H. Swerdlow, Russell H. Swerdlow, Chad Slawson, Chad Slawson   +14 more
doaj   +1 more source

HCF-1 Is Cleaved in the Active Site of O-GlcNAc Transferase [PDF]

Science, 2013
Dual-Duty Active Site O-linked N-acetylglucosamine transferase (OGT) catalyzes the addition of N-acetylglucosamine (GlcNac) to serine or threonine residues, influencing the localization and function of proteins. Because its activity is sensitive to the nutrient uridine diphosphate (UDP)–GlcNac, OGT has been proposed to regulate ...
Lazarus, M.B., Jiang, J., Kapuria, V., Bhuiyan, T., Janetzko, J., Zandberg, W.F., Vocadlo, D.J., Herr, W., Walker, S.   +8 more
openaire   +4 more sources

Fueling the fire: emerging role of the hexosamine biosynthetic pathway in cancer

BMC Biology, 2019
Altered metabolism and deregulated cellular energetics are now considered a hallmark of all cancers. Glucose, glutamine, fatty acids, and amino acids are the primary drivers of tumor growth and act as substrates for the hexosamine biosynthetic pathway ...
Neha M. Akella, Lorela Ciraku, Mauricio J. Reginato   +2 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

O-GlcNAc transferase regulates transcriptional activity of human Oct4 [PDF]

Glycobiology, 2017
O-linked β-N-acetylglucosamine (O-GlcNAc) is a single sugar modification found on many different classes of nuclear and cytoplasmic proteins. Addition of this modification, by the enzyme O-linked N-acetylglucosamine transferase (OGT), is dynamic and inducible. One major class of proteins modified by O-GlcNAc is transcription factors. O-GlcNAc regulates
Sandii, Constable, Jae-Min, Lim, Krithika, Vaidyanathan, Lance, Wells   +3 more
openaire   +2 more sources

Identification and characterization of O-GlcNAc modifications of a conserved orthopoxvirus core protein

Journal of Virology
O-GlcNAcylation, a post-translational modification consisting of O-linked N-acetylglucosamine attached to serine and threonine residues, occurs in thousands of cytoplasmic, nuclear, and mitochondrial proteins but has been reported for relatively few ...
Yunliang Zhang, Bernard Moss
doaj   +1 more source

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