Results 71 to 80 of about 14,068 (233)

Demystifying O-GlcNAcylation: hints from peptide substrates [PDF]

Glycobiology, 2018
O-GlcNAcylation, analogous to phosphorylation, is an essential post-translational modification of proteins at Ser/Thr residues with a single β-N-acetylglucosamine moiety. This dynamic protein modification regulates many fundamental cellular processes and its deregulation has been linked to chronic diseases such as cancer, diabetes and neurodegenerative
Jie Shi, Rob Ruijtenbeek, Roland J Pieters   +2 more
openaire   +3 more sources

O-GlcNAcylation of nuclear proteins in the mouse liver exhibit daily oscillations that are influenced by meal timing.

PLoS Biology
The liver circadian clock and hepatic transcriptome are highly responsive to metabolic signals generated from feeding-fasting rhythm. Previous studies have identified a number of nutrient-sensitive signaling pathways that could interpret metabolic input ...
Xianhui Liu, Yao D Cai, Chunyan Hou, Xu Liu, Youcheng Luo, Aron Judd P Mendiola, Xuehan Xu, Yige Luo, Haiyan Zheng, Caifeng Zhao, Ching-Hsuan Chen, Yong Zhang, Yang K Xiang, Junfeng Ma, Joanna C Chiu   +14 more
doaj   +1 more source

Control of lipid metabolism by the dynamic and nutrient‐dependent post‐translational modification O‐GlcNAcylation

Natural Sciences, 2023
O‐GlcNAcylation is a post‐translational modification belonging to the large group of glycosylations. It consists of the modification of cytoplasmic, nuclear, and mitochondrial proteins with a single N‐acetylglucosamine residue by O‐GlcNAc transferase ...
Céline Schulz, Quentin Lemaire, Alexandre Berthier, Amandine Descat, Mostafa Kouach, Anne‐Sophie Vercoutter‐Edouart, Ikram El Yazidi‐Belkoura, Stéphan Hardivillé, Jean‐François Goossens, Philippe Lefebvre, Tony Lefebvre   +10 more
doaj   +1 more source

O-GlcNAcylation and Activity of Succinate Dehydrogenase [PDF]

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

Oncogenic KRAS Rewires Stress Granule Dynamics: Mechanisms and Therapeutic Opportunities

The Kaohsiung Journal of Medical Sciences, EarlyView.
ABSTRACT Stress granules (SGs) are dynamic, membrane‐less structures that form in response to various cellular stresses, including metabolic, oxidative, and therapeutic challenges. They function as adaptive hubs and reorganize protein synthesis and signaling networks to help cells survive under stress. In cancer, these condensates are often hijacked to
Msimisi Ndzinisa, Birhanetensay Masresha Altaye, Yuh‐Pyng Sher   +2 more
wiley   +1 more source

Multi‐Targeting Ligands as Prospective Therapeutics for Alzheimer's Disease, a Prevalent Neurodegenerative Disorder: Mechanistic Insights, Emerging Targets and Drug Discovery Campaigns

Medicinal Research Reviews, EarlyView.
ABSTRACT Alzheimer's disease (AD) is a debilitating neurodegenerative condition characterized by progressive cognitive impairment, memory deterioration, and neuronal dysfunction. Its complex pathophysiology involves multiple interlinked processes, including amyloid‐β (Aβ) aggregation, tau hyperphosphorylation, oxidative stress, neuroinflammation ...
Amandeep Thakur, Mandeep Rana, Sakshi Vanjani, Kei‐Chi Liou, Rajeev Taliyan, Kunal Nepali, Chih‐Hao Yang   +6 more
wiley   +1 more source

O-GlcNAcylation and Inflammation: A Vast Territory to Explore [PDF]

Frontiers in Endocrinology, 2015
O-GlcNAcylation is a reversible post-translational modification that regulates the activities of cytosolic and nuclear proteins according to glucose availability. This modification appears to participate in several hyperglycemia-associated complications.
Baudoin, Léa, Issad, Tarik
openaire   +4 more sources

A mutant O-GlcNAcase enriches Drosophila developmental regulators [PDF]

, 2017
YesProtein O-GlcNAcylation is a reversible post-translational modification of serines/threonines on nucleocytoplasmic proteins. It is cycled by the enzymes O-GlcNAc transferase (OGT) and O-GlcNAc hydrolase (O-GlcNAcase or OGA).
A Erkner, A Nandi, AC Diernfellner, Andrew T Ferenbach, B Charroux, B Guo, B Li, CF Teo, D Mariappa, D Mariappa, DA Sinclair, Daan M F van Aalten, Daniel Mariappa, David G Campbell, DM Webster, DY Chen, FV Rao, GI Miura, GW Hart, H Hahne, H Zhang, HR Huang, Iva Hopkins-Navratilova, J Ma, JC Trinidad, JE Rexach, JF Alfaro, K Sakabe, L Wang, M Ogawa, Matthias Trost, MB Lazarus, MC Gambetta, MC Gambetta, MC Gambetta, MM Gilbert, NE Zachara, Nithya Selvan, O Sekine, P Ramakrishnan, PT Radermacher, PW Ingham, PW Ingham, R Sprung, Ritchie Williamson, Robert Gourlay, S Kenwrick, S Park, S Pathak, S Zhang, SA Myers, SA Yuzwa, SY Cong, T Pradhan-Sundd, T Pradhan-Sundd, Tonia Aristotelous, TW Liu, Z Wang, Z Zhang   +58 more
core   +3 more sources

Interplay of Ser273 Phosphorylation and K268 and K293 Acetylation in PPARγ: Implications for PPARγ Activation

Proteins: Structure, Function, and Bioinformatics, EarlyView.
ABSTRACT Post‐translational modifications (PTMs) play a critical role in regulating the transcriptional activity of PPARγ, a nuclear receptor central to glucose and lipid homeostasis. Among these, lysine acetylation at K268 and K293 and phosphorylation at S273 are particularly relevant to insulin sensitivity.
Caique Camargo Malospirito, Marieli Mariano Gonçalves Dias, Gabriel Ernesto Jara, Thayná Mendonça Avelino, Giovanna Blazutti Elias, Paulo Sergio Lopes de Oliveira, Ana Carolina Migliorini Figueira   +6 more
wiley   +1 more source

O-GlcNAc regulation of autophagy and α-synuclein homeostasis; implications for Parkinson’s disease

Molecular Brain, 2017
Post-translational modification on protein Ser/Thr residues by O-linked attachment of ß-N-acetyl-glucosamine (O-GlcNAcylation) is a key mechanism integrating redox signaling, metabolism and stress responses.
Willayat Y. Wani, Xiaosen Ouyang, Gloria A. Benavides, Matthew Redmann, Stacey S. Cofield, John J. Shacka, John C. Chatham, Victor Darley-Usmar, Jianhua Zhang   +8 more
doaj   +1 more source