Results 61 to 70 of about 37,468 (260)

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

X-inactivation normalizes O-GlcNAc transferase levels and generates an O-GlcNAc-depleted Barr body [PDF]

Frontiers in Genetics, 2014
O-GlcNAc Transferase (OGT) catalyzes protein O-GlcNAcylation, an abundant and dynamic nuclear and cytosolic modification linked to epigenetic regulation of gene expression. The steady-state levels of O-GlcNAc are influenced by extracellular glucose concentrations suggesting that O-GlcNAcylation may serve as a metabolic sensor.
Olivier-Van Stichelen, Stéphanie, Hanover, John A.   +1 more
openaire   +3 more sources

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

Dammarenediol II enhances etoposide‐induced apoptosis by targeting O‐GlcNAc transferase and Akt/GSK3β/mTOR signaling in liver cancer

Molecular Oncology, EarlyView.
Etoposide induces DNA damage, activating p53‐dependent apoptosis via caspase‐3/7, which cleaves PARP1. Dammarenediol II enhances this apoptotic pathway by suppressing O‐GlcNAc transferase activity, further decreasing O‐GlcNAcylation. The reduction in O‐GlcNAc levels boosts p53‐driven apoptosis and influences the Akt/GSK3β/mTOR signaling pathway ...
Jaehoon Lee, Byung‐Cheol Han, Gi‐Bang Koo, Jihye Park, Mijin Kwon, Young Bin Park, Jae‐Mun Choi, Seung‐Ho Lee, Sangho Roh   +8 more
wiley   +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

Molecular dynamics simulations of positively selected codons in FcγRI reveal novel biochemical binding properties

FEBS Open Bio, EarlyView.
Evolutionary analysis across 32 placental mammals identified positive selection at residues H148 and W149 in the immune receptor FcγR1. Ancestral reconstruction combined with molecular dynamics simulations reveals how these mutations may influence receptor structure and dynamics, providing insight into the evolution of antibody recognition and immune ...
David A. Young, Omar Arias‐Gaguancela, Fiona Gibson, Morgan Grainger, Jodie Score, Amit Nathubhai, Mauricio Cafiero, Lee Richard Machado   +7 more
wiley   +1 more source

O-GlcNAc: A Sweetheart of the Cell Cycle and DNA Damage Response

Frontiers in Endocrinology, 2018
The addition and removal of O-linked N-acetylglucosamine (O-GlcNAc) to and from the Ser and Thr residues of proteins is an emerging post-translational modification.
Caifei Liu, Jing Li
doaj   +1 more source

Increasing brain protein O-GlcNAc-ylation mitigates breathing defects and mortality of Tau.P301L mice. [PDF]

PLoS ONE, 2013
The microtubule associated protein tau causes primary and secondary tauopathies by unknown molecular mechanisms. Post-translational O-GlcNAc-ylation of brain proteins was demonstrated here to be beneficial for Tau.P301L mice by pharmacological inhibition
Peter Borghgraef, Clément Menuet, Clara Theunis, Justin V Louis, Herman Devijver, Hervé Maurin, Caroline Smet-Nocca, Guy Lippens, Gerard Hilaire, Harrie Gijsen, Dieder Moechars, Fred Van Leuven   +11 more
doaj   +1 more source