Results 131 to 140 of about 20,888 (214)

Regulation of senescence-associated secretory phenotypes in osteoarthritis by cytosolic UDP-GlcNAc retention and O-GlcNAcylation

Nature Communications
UDP-GlcNAc serves as a building block for glycosaminoglycan (GAG) chains in cartilage proteoglycans and simultaneously acts as a substrate for O-GlcNAcylation. Here, we show that transporters for UDP-GlcNAc to the endoplasmic reticulum (ER) and Golgi are
Donghyun Kang, Jeeyeon Lee, Geunho Yook, Sehan Jeong, Jungkwon Shin, Mi-Sung Kim, Yi-Jun Kim, Hyeryeon Jung, Jinsung Ahn, Tae Woo Kim, Moon Jong Chang, Chong Bum Chang, Seung-Baik Kang, Won Ho Yang, Yong-ho Lee, Jin Won Cho, Eugene C. Yi, Chanhee Kang, Jin-Hong Kim   +18 more
doaj   +1 more source

Polη O-GlcNAcylation governs genome integrity during translesion DNA synthesis

Nature Communications, 2017
Polη is a key player in translesion DNA synthesis. Here, the authors uncover that, in response to DNA damage, Polη undergoes O-GlcNAcylation at threonine 457 by O-GlcNAc transferase to facilitate the timely disassembly of Polη after DNA lesion bypass.
Xiaolu Ma, Hongmei Liu, Jing Li, Yihao Wang, Yue-He Ding, Hongyan Shen, Yeran Yang, Chenyi Sun, Min Huang, Yingfeng Tu, Yang Liu, Yongliang Zhao, Meng-Qiu Dong, Ping Xu, Tie-Shan Tang, Caixia Guo   +15 more
doaj   +1 more source

O-GlcNAcylation: roles and potential therapeutic target for bone pathophysiology

Cell Communication and Signaling
O-linked N-acetylglucosamine (O-GlcNAc) protein modification (O-GlcNAcylation) is a critical post-translational modification (PTM) of cytoplasmic and nuclear proteins.
Xiaohan Yan, Jingjing Zheng, Wenhao Ren, Shaoming Li, Shuying Yang, Keqian Zhi, Ling Gao   +6 more
doaj   +1 more source

Genetic Locus and Structural Characterization of the Biochemical Defect in the O-Antigenic Polysaccharide of the Symbiotically Deficient \u3cem\u3eRhizobium etli\u3c/em\u3e Mutant, CE166 [PDF]

, 2003
The O-antigen polysaccharide (OPS) of Rhizobium etli CE3 lipopolysaccharide (LPS) is linked to the core oligosaccharide via an N-acetylquinovosaminosyl (QuiNAc) residue.
Box, Jodie M., Carlson, Russell W, Forsberg, Lennart Scott, Noel, K. Dale   +3 more
core   +1 more source

Genetic gradual reduction of OGT activity unveils the essential role of O-GlcNAc in the mouse embryo.

PLoS Genetics
The reversible glycosylation of nuclear and cytoplasmic proteins (O-GlcNAcylation) is catalyzed by a single enzyme, namely O-GlcNAc transferase (OGT). The mammalian Ogt gene is X-linked, and it is essential for embryonic development and for the viability
Sara Formichetti, Agnieszka Sadowska, Michela Ascolani, Julia Hansen, Kerstin Ganter, Christophe Lancrin, Neil Humphreys, Mathieu Boulard   +7 more
doaj   +1 more source

Regulation of a Cytosolic and Nuclear O-GlcNAc Transferase [PDF]

Journal of Biological Chemistry, 1999
Lisa K. Kreppel, Gerald W. Hart
openaire   +1 more source

FpOGT is required for fungal growth, stress response, and virulence of Fusarium proliferatum by affecting the expression of glucokinase and other glucose metabolism-related genes

Phytopathology Research
O-GlcNAcylation, an important post-translational modification catalyzed by O-GlcNAc transferase (OGT), plays critical roles in several biological processes.
Yizhou Gao, Yitong Wang, Siming He, Haibo Li, Yuqing Wang, Zhihong Wu   +5 more
doaj   +1 more source

Modulation of synaptic transmission through O-GlcNAcylation

Molecular Brain
O-GlcNAcylation is a posttranslational modification where N-acetylglucosamine (O-GlcNAc) is attached and detached from a serine/threonine position by two enzymes: O-GlcNAc transferase and O-GlcNAcase.
Seunghyo Han, Jun-Nyeong Kim, Chan Ho Park, Jin-Seok Byun, Do-Yeon Kim, Hyoung-Gon Ko   +5 more
doaj   +1 more source

O-GlcNAcylation and Activity of Succinate Dehydrogenase [PDF]

, 2019
Undergraduate ...
Truong, Nhat Quang, Vickers, Abigail
core   +1 more source

Deciphering the functions of O-GlcNAc glycosylation in the brain: The role of site-specific quantitative O-GlcNAcomics [PDF]

, 2018
The dynamic posttranslational modification O-linked β-N-acetylglucosamine glycosylation (O-GlcNAcylation) is present on thousands of intracellular proteins in the brain.
Hsieh-Wilson, Linda C., Sorum, Alexander W., Thompson, John W.   +2 more
core