Results 181 to 190 of about 22,588 (217)

OGT as potential novel target: Structure, function and inhibitors

Chemico-Biological Interactions, 2022
O-linked N-acetylglucosamine transferase (OGT), a key protein in O-linked N-acetylglucosamine (O-GlcNAc) post-translational modification, catalyzes O-GlcNAcylation by linking GlcNAc from glycosyl donors to protein Ser/Thr residues to regulate multiple biological processes.
Jiaxin Zhu, Wenyuan Liu, Wei Qu
exaly   +3 more sources

14-3-3ε augments OGT stability by binding with S20-phosphorylated OGT

Journal of Biological Chemistry
The relationship between O-linked N-acetylglucosamine (O-GlcNAc) transferase (OGT) and mitosis is intertwined. Besides the numerous mitotic OGT substrates that have been identified, OGT itself is also a target of the mitotic machinery. Previously, our investigations have shown that Checkpoint kinase 1 (Chk1) phosphorylates OGT at Ser-20 to increase OGT
Jianwei Sun, Jing Li
exaly   +3 more sources

Truncation of the TPR domain of OGT alters substrate and glycosite selection [PDF]

Analytical and Bioanalytical Chemistry, 2021
O-GlcNAc transferase (OGT) is an essential enzyme that installs O-linked N-acetylglucosamine (O-GlcNAc) to thousands of protein substrates. OGT and its isoforms select from these substrates through the tetratricopeptide repeat (TPR) domain, yet the impact of truncations to the TPR domain on substrate and glycosite selection is unresolved.
Daniel H Ramirez, Bo Yang, Alexandria K D'Souza   +2 more
exaly   +3 more sources

Measurement of UDP-N-acetylglucosaminyl transferase (OGT) in brain cytosol and characterization of anti-OGT antibodies

Analytical Biochemistry, 2003
UDP-N-acetylglucosaminyl transferase (OGT) catalyzes O-linked glycosylation of cytosolic and nuclear proteins, but enzyme studies have been hampered by the lack of a rapid, sensitive, and economical OGT assay. Employed assay methods typically involved the use of HPLC, formic acid, and large amounts of expensive radiolabeled [3H]UDP-N-acetylglucosaminyl
Stephen, Marshall, Trung, Duong, Ryan J, Orbus, John M, Rumberger, Ryo, Okuyama   +4 more
openaire   +2 more sources

Inhibition of mTOR affects protein stability of OGT

Biochemical and Biophysical Research Communications, 2014
Autophagy regulates cellular homeostasis through degradation of aged or damaged subcellular organelles and components. Interestingly, autophagy-deficient beta cells, for example Atg7-mutant mice, exhibited hypoinsulinemia and hyperglycemia. Also, autophagy response is diminished in heart of diabetic mice.
S, Park, J, Pak, I, Jang, J W, Cho
openaire   +2 more sources

O-GlcNAc transferase congenital disorder of glycosylation (OGT-CDG): Potential mechanistic targets revealed by evaluating the OGT interactome

Journal of Biological Chemistry
O-GlcNAc transferase (OGT) is the sole enzyme responsible for the post-translational modification of O-GlcNAc on thousands of target nucleocytoplasmic proteins. To date, nine variants of OGT that segregate with OGT Congenital Disorder of Glycosylation (OGT-CDG) have been reported and characterized. Numerous additional variants have been associated with
Johnathan M Mayfield, Naomi L Hitefield, Ignacy Czajewski   +2 more
exaly   +5 more sources

OGT functions as a catalytic chaperone under heat stress response: a unique defense role of OGT in hyperthermia

Biochemical and Biophysical Research Communications, 2004
Protein O-GlcNAcylation is proceeded by O-linked GlcNAc transferase (OGT) in nucleocytoplasm and is involved in many biological processes although its physiological role is not clearly defined. To identify the functional significance of O-GlcNAcylation, we investigated heat stress effects on protein O-GlcNAcylation.
Kyung-Cheol, Sohn, Ki-Young, Lee, Jae Eun, Park, Su-Il, Do   +3 more
openaire   +2 more sources

Global identification of O‐GlcNAc transferase (OGT) interactors by a human proteome microarray and the construction of an OGT interactome

PROTEOMICS, 2014
O‐Linked β‐N‐acetylglucosamine (O‐GlcNAcylation) is an important protein PTM, which is very abundant in mammalian cells. O‐GlcNAcylation is catalyzed by O‐GlcNAc transferase (OGT), whose substrate specificity is believed to be regulated through interactions with other proteins.
Rui-Ping, Deng, Xiang, He, Shu-Juan, Guo, Wei-Feng, Liu, Yong, Tao, Sheng-Ce, Tao   +5 more
openaire   +2 more sources

Essential Role of the Glycosyltransferase Sxc/Ogt in Polycomb Repression

Science, 2009
Putting the Sugar on Polycomb A wide variety of nuclear and cytosolic proteins in human cells carry an O-linked sugar modification, N -acetylglucosamine (GlcNAc), which is added by the highly conserved O-linked GlcNAc transferase, Ogt.
Maria Cristina, Gambetta, Katarzyna, Oktaba, Jürg, Müller   +2 more
openaire   +2 more sources

Ac4GlcNAcF3, an OGT-tolerated but OGA-resistant regulator for O-GlcNAcylation

Bioorganic & Medicinal Chemistry Letters, 2019
O-Linked N-acetylglucosamine (O-GlcNAc) is an abundant posttranslationalmonosaccaride-modification found on Ser or Thr residues of intracellular proteins in most eukaryotes. The dynamic nature of O-GlcNAc has enabled researchers to modulate the stoichiometry of O-GlcNAc on proteins in order to investigate its function.
Haifeng, Wang, Jianshuang, Guo, Nan, Wang, Jiajia, Wang, Qingqing, Xue, Jiyan, Wang, Wenjie, Liu, Kaihui, Liu, Xuefeng, Cao, Wei, Zhao, Rimo, Xi, Youhong, Niu, Peng, Wang, Jing, Li   +13 more
openaire   +2 more sources