Results 71 to 80 of about 20,888 (214)

Chemical biology tools to interrogate the roles of O-GlcNAc in immunity

Frontiers in Immunology, 2023
The O-linked β-N-acetylglucosamine (O-GlcNAc) glycosylation of proteins is an essential and dynamic post-translational modification in mammalian cells that is regulated by the action of two enzymes.
Abhijit Saha, Alberto Fernández-Tejada, Alberto Fernández-Tejada   +2 more
doaj   +1 more source

Glycosylation in the thyroid gland : vital aspects of glycoprotein function in thyrocyte physiology and thyroid disorders [PDF]

, 2018
The key proteins responsible for hormone synthesis in the thyroid are glycosylated. Oligosaccharides strongly affect the function of glycosylated proteins.
Ewa Pocheć, Kamila Kozłowska, Marta Ząbczyńska   +2 more
core   +1 more source

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

Synergistische Entwicklungsstrategien von Inhibitoren gegen humane UDP‐Galactose‐4‐Epimerase

Angewandte Chemie, EarlyView.
Die Epimerase GalE ist essenziell für die Biosynthese von krebsrelevanten O‐GalNAc Glykanen. Wir verwenden orthogonales, strukturbasiertes Screening niedermolekularer Fragmente an, um kovalente und nichtkovalente Inhibitoren gegen GalE mit nicht mehr als 22 optimierten Verbindungen zu erhalten.
William M. Browne, Jonathan Pettinger, Teresa Weckwerth, Andrew Purkiss, Sing Hei Lok, Louisa Penicaut, Roksana Ogrodowicz, Raveena Prema, Simone Kunzelmann, Chloe Roustan, Ganka Bineva‐Todd, Saskia Pieters, Francesca Zappacosta, Alfred E. Doherty, Isobel Oram, Christelle Soudy, Robert Quinlan, Joanna Redmond, Svend Kjaer, David House, Stephane Mouilleron, Jacob T. Bush, Benjamin Schumann   +22 more
wiley   +1 more source

Structural Divergence in O-GlcNAc Glycans Displayed on Epidermal Growth Factor-like Repeats of Mammalian Notch1

Molecules, 2018
Extracellular O-GlcNAc is a novel class of modification catalyzed by epidermal growth factor-like (EGF)-domain specific O-GlcNAc transferase (EOGT). In mammals, EOGT is required for ligand-mediated Notch signaling for vascular development.
Mitsutaka Ogawa, Yuya Senoo, Kazutaka Ikeda, Hideyuki Takeuchi, Tetsuya Okajima   +4 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  

Biochemical evidence for an alternate pathway in N-linked glycoprotein biosynthesis [PDF]

, 2012
Asparagine-linked glycosylation is a complex protein modification conserved among all three domains of life. Herein we report the in vitro analysis of N-linked glycosylation from the methanogenic archaeon Methanococcus voltae.
A Herscovics, A Krogh, A Larkin, A Larkin, Angelyn Larkin, B Chaban, B Chaban, B Imperiali, B Imperiali, Barbara Imperiali, C Kuntz, C Lizak, CB Sharma, CL Branch, CM Szymanski, D Calo, DJ VanDyke, E Świeżewska, F Ramirez, G Ferrante, Garrett E Whitworth, H Magidovich, H Nothaft, H Shams-Eldin, J Eichler, J Flint, J Folch, J Kelly, J Lechner, JM Troutman, JS Tkacz, JV O'Connor, KJ Glover, L Kaminski, LL Lairson, M Abu-Qarn, M Igura, MB Jaffee, MB Jones, MD Hartley, MF Mescher, MF Mescher, Michelle M Chang, MM Sim, NH Behrens, P Burda, PM Coutinho, R Wu, S Heesen, S Matsumoto, S Naparstek, S Suzuki, S Voisin, S Yurist-Doutsch, SJ Charnock, VWF Tai, Z Guan, Z Guan   +57 more
core   +1 more source

Structural Insights into O‐GlcNAc Transferase

The FASEB Journal, 2013
O‐GlcNAc Transferase (OGT) is an essential glycosyltransferase that catalyzes the attachment of N‐acetylglucosamine (GlcNAc) to serines and threonines of numerous nuclear and cytoplasmic proteins. Global O‐GlcNAcylation levels increase with increased flux through the hexosamine biosynthetic pathway, which produces OGT's donor substrate, UDP‐GlcNAc ...
openaire   +1 more source

A Synergistic Inhibitor Development Strategy Against Human UDP‐Galactose‐4‐Epimerase

Angewandte Chemie International Edition, EarlyView.
The epimerase GalE is crucial for the biosynthesis of cancer‐relevant O‐GalNAc glycans. Here, we employ orthogonal, structurally enabled small molecule fragment screens to yield both covalent and non‐covalent inhibitors against GalE within no more than 22 elaborated compounds.
William M. Browne, Jonathan Pettinger, Teresa Weckwerth, Andrew Purkiss, Sing Hei Lok, Louisa Penicaut, Roksana Ogrodowicz, Raveena Prema, Simone Kunzelmann, Chloe Roustan, Ganka Bineva‐Todd, Saskia Pieters, Francesca Zappacosta, Alfred E. Doherty, Isobel Oram, Christelle Soudy, Robert Quinlan, Joanna Redmond, Svend Kjaer, David House, Stephane Mouilleron, Jacob T. Bush, Benjamin Schumann   +22 more
wiley   +1 more source

Disruption of O-GlcNAc cycling by deletion of O-GlcNAcase (Oga/Mgea5) changed gene expression pattern in mouse embryonic fibroblast (MEF) cells

Genomics Data, 2015
Adding a single O-GlcNAc moiety to a Ser/Thr molecule of a protein by O-GlcNAc transferase and transiently removing it by O-GlcNAcase is referred to as O-GlcNAc cycling (or O-GlcNAcylation).
Chithra Keembiyehetty
doaj   +1 more source