Results 41 to 50 of about 14,068 (233)

Emerging field: O-GlcNAcylation in ferroptosis

Frontiers in Molecular Biosciences, 2023
In 2012, researchers proposed a non-apoptotic, iron-dependent form of cell death caused by lipid peroxidation called ferroptosis. During the past decade, a comprehensive understanding of ferroptosis has emerged. Ferroptosis is closely associated with the tumor microenvironment, cancer, immunity, aging, and tissue damage.
Hongshuo Zhang, Juan Zhang, Haojie Dong, Ying Kong, Youfei Guan   +4 more
openaire   +3 more sources

Solving the mystery of human sleep schedules one mutation at a time. [PDF]

, 2013
Sleep behavior remains one of the most enigmatic areas of life. The unanswered questions range from "why do we sleep?" to "how we can improve sleep in today's society?" Identification of mutations responsible for altered circadian regulation of human ...
Fu, Ying-Hui, Hallows, William C, Ptáček, Louis J   +2 more
core   +1 more source

O-GlcNAcylation Is Essential for Autophagy in Cardiomyocytes [PDF]

Oxidative Medicine and Cellular Longevity, 2020
Since both O-GlcNAcylation and autophagy sense intracellular nutrient level, the alteration of those two pathways plays substantial roles in the progression of heart failure. Hence, determining the relationship between O-GlcNAcylation and autophagy is imperative to understand, prevent, and treat heart failure.
Houzhi Yu, Li Wen, Yongxin Mu
openaire   +2 more sources

dbOGAP - An Integrated Bioinformatics Resource for Protein O-GlcNAcylation

BMC Bioinformatics, 2011
Background Protein O-GlcNAcylation (or O-GlcNAc-ylation) is an O-linked glycosylation involving the transfer of β-N-acetylglucosamine to the hydroxyl group of serine or threonine residues of proteins.
Hart Gerald W, Liu Hongfang, Torii Manabu, Wang Jinlian, Hu Zhang-Zhi   +4 more
doaj   +1 more source

O-GlcNAcylation Suppresses the Ion Current IClswell by Preventing the Binding of the Protein ICln to α-Integrin

Frontiers in Cell and Developmental Biology, 2020
O-GlcNAcylation is a post-translational modification of proteins that controls a variety of cellular processes, is chronically elevated in diabetes mellitus, and may contribute to the progression of diabetic complications, including diabetic nephropathy.
Roberta Costa, Alessia Remigante, Alessia Remigante, Davide A. Civello, Emanuele Bernardinelli, Zoltán Szabó, Rossana Morabito, Angela Marino, Antonio Sarikas, Wolfgang Patsch, Markus Paulmichl, Tamás Janáky, Attila Miseta, Tamás Nagy, Silvia Dossena   +14 more
doaj   +1 more source

Protein O-GlcNAcylation in multiple immune cells and its therapeutic potential

Frontiers in Immunology, 2023
O-GlcNAcylation is a post-translational modification of proteins that involves the addition of O-GlcNAc to serine or threonine residues of nuclear or cytoplasmic proteins, catalyzed by O-GlcNAc transferase (OGT).
Huanhuan Cai, Huanhuan Cai, Wei Xiong, Wei Xiong, Haoyan Zhu, Haoyan Zhu, Qiongxin Wang, Qiongxin Wang, Shi Liu, Zhibing Lu, Zhibing Lu   +10 more
doaj   +1 more source

O-GlcNAcylation enhances sensitivity to RSL3-induced ferroptosis via the YAP/TFRC pathway in liver cancer

Cell Death Discovery, 2021
Ferroptosis is a form of regulated cell death characterized by iron-dependent accumulation of lipid hydroperoxides to lethal levels. YAP has been reported to play a pivotal role in controlling ferroptotic death, and the expression of YAP is enhanced and ...
Guoqing Zhu, Abduh Murshed, Haojie Li, Ji Ma, Ni Zhen, Miao Ding, Jiabei Zhu, Siwei Mao, Xiaochen Tang, Li Liu, Fenyong Sun, Lei Jin, Qiuhui Pan   +12 more
doaj   +1 more source

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

Chemical approaches to study O-GlcNAcylation [PDF]

Chem. Soc. Rev., 2013
The enzymatic addition of a single β-D-N-acetylglucosamine sugar molecule on serine and/or threonine residues of protein chains is referred to as O-GlcNAcylation. This novel form of post-translational modification, first reported in 1984, is extremely abundant on nuclear and cytoplasmic proteins and has site specific cycling dynamics comparable to that
Partha S, Banerjee, Gerald W, Hart, Jin Won, Cho   +2 more
openaire   +2 more sources

O-Linked β-N-Acetylglucosamine Modification: Linking Hypertension and the Immune System

Frontiers in Immunology, 2022
The O-linked β-N-acetylglucosamine modification (O-GlcNAcylation) of proteins dynamically regulates protein function, localization, stability, and interactions.
Rinaldo Rodrigues dos Passos Junior, Rinaldo Rodrigues dos Passos Junior, Gisele Facholi Bomfim, Fernanda R. Giachini, Fernanda R. Giachini, Rita C. Tostes, Victor Vitorino Lima   +6 more
doaj   +1 more source