Results 21 to 30 of about 20,888 (214)

O-GlcNAcase contributes to cognitive function in Drosophila [PDF]

, 2020
Contains fulltext : 219183.pdf (publisher's version ) (Open ...
Catinozzi, Marica, Eidhof, Ilse, Fenckova, Michaela, Ferenbach, Andrew, Muha, Villo, Schenck, Annette, Storkebaum, Erik, van Aalten, Daan   +7 more
core   +3 more sources

Structural snapshots of the reaction coordinate for O-GlcNAc transferase [PDF]

Nature Chemical Biology, 2012
Visualization of the reaction coordinate undertaken by glycosyltransferases has remained elusive but is critical for understanding this important class of enzyme. Using substrates and substrate mimics, we describe structural snapshots of all species along the kinetic pathway for human O-linked β-N-acetylglucosamine transferase (O-GlcNAc transferase ...
Lazarus, Michael B., Jiang, Jiaoyang, Gloster, Tracey M., Zandberg, Wesley F., Whitworth, Garrett E., Vocadlo, David J., Kahne, Suzanne   +6 more
openaire   +3 more sources

Structural insights into mechanism and specificity of O-GlcNAc transferase [PDF]

The EMBO Journal, 2008
Post-translational modification of protein serines/threonines with N-acetylglucosamine (O-GlcNAc) is dynamic, inducible and abundant, regulating many cellular processes by interfering with protein phosphorylation. O-GlcNAcylation is regulated by O-GlcNAc transferase (OGT) and O-GlcNAcase, both encoded by single, essential, genes in metazoan genomes. It
Clarke, Andrew J., Hurtado-Guerrero, Ramon, Pathak, Shalini, Schuettelkopf, Alexander, Borodkin, Vladimir, Shepherd, Sharon M., Ibrahim, Adel F. M., van Aalten, Daan M. F.   +7 more
openaire   +3 more sources

Interaction between O-GlcNAc modification and tyrosine phosphorylation of prohibitin: implication for a novel binary switch. [PDF]

PLoS ONE, 2009
Prohibitin (PHB or PHB1) is an evolutionarily conserved, multifunctional protein which is present in various cellular compartments including the plasma membrane. However, mechanisms involved in various functions of PHB are not fully explored yet. Here we
Sudharsana R Ande, Saby Moulik, Suresh Mishra   +2 more
doaj   +1 more source

O-GlcNAc transferase suppresses necroptosis and liver fibrosis [PDF]

JCI Insight, 2019
Abstract Over a billion people suffer from chronic liver diseases worldwide, which often leads to fibrosis and then cirrhosis. Treatments for fibrosis remain experimental, in part because no unifying mechanism has been identified that initiates liver fibrosis.
Bichen Zhang, Min-Dian Li, Ruonan Yin, Yuyang Liu, Yunfan Yang, Kisha A. Mitchell-Richards, Jin Hyun Nam, Rui Li, Li Wang, Yasuko Iwakiri, Dongjun Chung, Marie E. Robert, Barbara E. Ehrlich, Anton M. Bennett, Jun Yu, Michael H. Nathanson, Xiaoyong Yang   +16 more
openaire   +2 more sources

O-GlcNAc Transferase Regulates Mitotic Chromatin Dynamics [PDF]

Journal of Biological Chemistry, 2010
Mitosis must faithfully divide the genome such that each progeny inherits the same genetic material. DNA condensation is crucial in ensuring that chromosomes are correctly attached to the mitotic spindle for segregation, preventing DNA breaks or constrictions from the contractile ring.
Kaoru, Sakabe, Gerald W, Hart
openaire   +2 more sources

Substrate specificity provides insights into the sugar donor recognition mechanism of O-GlcNAc transferase (OGT). [PDF]

, 2013
O-Linked β-N-acetylglucosaminyl transferase (OGT) plays an important role in the glycosylation of proteins, which is involved in various cellular events.
Chen, Xi, Chen, Yi, Li, Lei, Liu, Pi, Liu, Xiaoyan, Ma, Xiaofeng, Muthana, Musleh M, Sun, Hong, Wang, Peng G, Yan, Hui, Zhang, Lianwen, Zhou, Feng   +11 more
core   +2 more sources

O-GlcNAcase:promiscuous hexosaminidase or key regulator of O-GlcNAc signalling? [PDF]

, 2014
O-GlcNAc signaling is regulated by an opposing pair of enzymes: O-GlcNAc transferase installs and O-GlcNAcase (OGA) removes the modification from proteins.
Banerjee, Butkinaree, Cantarel, Cecioni, Cetinba, Comtesse, Copeland, Dennis, Dong, Dorfmueller, Dorfmueller, Drougat, Forsythe, Francisco, Gao, Gong, Graham, Guinez, Hanover, Hart, Hayakawa, He, He, Heckel, Hilgers, Housley, Howerton, Hu, Itkonen, Keembiyehetty, Knapp, Laczy, Lefebvre, Lepage, Libina, Liu, Macauley, Macauley, Macauley, Macauley, Macauley, Mahuran, Martin, Minami, Müller, Nagel, Olszewski, Ostrowski, Pathak, Penton, Radermacher, Rahman, Rao, Rao, Robinson, Ruan, Ruan, Schimpl, Schimpl, Schultz, Sekine, Shen, Slawson, Speakman, Stryke, Swallow, Tews, Toleman, Toleman, Torres, Wang, Wang, Webster, Wells, Whisenhunt, Whitworth, Yang, Yu, Yuzwa, Yuzwa, Zachara, Zachara, Zhu   +82 more
core   +3 more sources

O-GlcNAc transferase inhibits visceral fat lipolysis and promotes diet-induced obesity

Nature Communications, 2020
Post-translational O-linked β-N acetylglucosamine (O-GlcNAc) modification acts as a nutrient-sensing mechanism. Here the authors report that O-GlcNAc transferase inhibits adipose tissue lipolysis via O-GlcNAcylation of the lipid droplet protein perilipin
Yunfan Yang, Minnie Fu, Min-Dian Li, Kaisi Zhang, Bichen Zhang, Simeng Wang, Yuyang Liu, Weiming Ni, Qunxiang Ong, Jia Mi, Xiaoyong Yang   +10 more
doaj   +1 more source

Hypertonic stress modulates eNOS function through O-GlcNAc modification at Thr-866

Scientific Reports, 2021
O-GlcNAcylation, an energy-sensitive posttranslational modification, can regulate the activity of endothelial nitric oxide synthase (eNOS). Previous studies found that Thr866 is the key site for low-glucose-mediated regulation of eNOS O-GlcNAc.
Chang Li, An He, Yongzheng Guo, Xiyang Yang, Minghao Luo, Zhe Cheng, Longxiang Huang, Yong Xia, Suxin Luo   +8 more
doaj   +1 more source