acetylglucosamine has been researched along with Diabetes Mellitus in 33 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 1 (3.03) | 18.7374 |
| 1990's | 3 (9.09) | 18.2507 |
| 2000's | 7 (21.21) | 29.6817 |
| 2010's | 13 (39.39) | 24.3611 |
| 2020's | 9 (27.27) | 2.80 |
| Authors | Studies |
|---|---|
| Aplin, JD; Graham, R; Palin, V; Russell, M; Westwood, M | 1 |
| Bai, X; Liang, T; Lu, Q; Zhang, X | 1 |
| Liu, J; Xiao, X; Xie, T; Xie, Z; Zhang, Q | 1 |
| Packer, M | 1 |
| Chen, Y; Wu, H; Zhao, X | 1 |
| Fisi, V; Frank, D; Kátai, E; Miseta, A; Nagy, T; Nagy, Z | 1 |
| Maegawa, H; Morino, K | 1 |
| Hart, GW; Zhu, Y | 1 |
| Chatham, JC; Young, ME; Zhang, J | 1 |
| Gomeshtapeh, FI; Tian, JL | 1 |
| Fields, PE; Qiang, A; Slawson, C | 1 |
| Hart, GW; Ma, J | 1 |
| Amo, K; Ebina, Y; Hashida, S; Ishikura, S; Nagaya, H; Uchiyama, K; Yuasa, T | 1 |
| Bailey, SM; Udoh, US; Young, ME | 1 |
| Hardivillé, S; Hart, GW | 1 |
| Caon, I; D'Angelo, ML; De Luca, G; Karousou, E; Moretto, P; Passi, A; Vigetti, D; Viola, M | 1 |
| Banerjee, PS; Hart, GW; Lagerlöf, O | 1 |
| Comer, F; Hart, GW; Hsieh-Wilson, LC; Park, K; Saudek, CD; Wang, Z | 1 |
| Dillmann, WH; Fricovsky, E; Han, W; Hu, Y; Oyeleye, MO; Scott, BT; Suarez, J; Trauger, SA; Wang, H | 1 |
| Butkinaree, C; Hart, GW; Park, K | 1 |
| Cho, JW; Choe, KM; Ji, S; Kang, JG; Kim, JE; Mook-Jung, I; Park, SY; Song, H; Yang, WH | 1 |
| Copeland, RJ; Hart, GW; Slawson, C | 1 |
| Facundo, HT; Jones, SP; Ngoh, GA; Zafir, A | 1 |
| Hart, GW; Lagerlof, O; Ramirez-Correa, G; Slawson, C | 1 |
| GAULDEN, EC; KEATING, WC | 1 |
| Akimoto, Y; Hart, GW; Hirano, H; Kawakami, H | 1 |
| Akimoto, Y; Hart, GW; Hirano, H; Kawakami, H; Munetomo, E; Nagamatsu, S; Nishiwaki, C; Ohara-Imaizumi, M; Vosseller, K; Wells, L; Yamamoto, K | 1 |
| Andrali, SS; Ozcan, S; Qian, Q | 1 |
| Dias, WB; Hart, GW | 1 |
| Akimoto, Y; Hart, GW; Hirano, H; Kreppel, LK | 1 |
| Hart, GW; Zachara, NE | 1 |
| Aamlid, KH; Pócsi, I; Price, RG; Richardson, AC; Smith, BV; Taylor, SA | 1 |
| Harakawa, K; Kanayama, M; Makise, J; Obuchi, M; Saito, E; Yoshida, K | 1 |
22 review(s) available for acetylglucosamine and Diabetes Mellitus
| Article | Year |
|---|---|
O-GlcNAcylation: an important post-translational modification and a potential therapeutic target for cancer therapy.
Topics: Acetylglucosamine; Animals; Diabetes Mellitus; Humans; Neoplasms; Neovascularization, Pathologic; Protein Processing, Post-Translational; Proteins | 2022 |
Emerging Role of Protein O-GlcNAcylation in Liver Metabolism: Implications for Diabetes and NAFLD.
Topics: Acetylglucosamine; Acylation; Diabetes Mellitus; Humans; N-Acetylglucosaminyltransferases; Non-alcoholic Fatty Liver Disease; Protein Processing, Post-Translational; Signal Transduction | 2023 |
Metabolic Stress and Cardiovascular Disease in Diabetes Mellitus: The Role of Protein
Topics: Acetylglucosamine; Animals; Diabetes Mellitus; Diabetic Cardiomyopathies; Humans; Mice; N-Acetylglucosaminyltransferases; Prognosis; Protein Processing, Post-Translational; Role; Signal Transduction; Stress, Physiological | 2019 |
Hyperglycemia-Induced Aberrant Cell Proliferation; A Metabolic Challenge Mediated by Protein O-GlcNAc Modification.
Topics: Acetylglucosamine; Animals; Cell Cycle; Cell Proliferation; Cells, Cultured; Diabetes Mellitus; Glycosylation; Humans; Hyperglycemia; Mice; Protein Processing, Post-Translational; Proteins; Rats | 2019 |
Role of O-linked N-acetylglucosamine in the homeostasis of metabolic organs, and its potential links with diabetes and its complications.
Topics: Acetylglucosamine; Animals; Diabetes Complications; Diabetes Mellitus; Glucose; Homeostasis; Humans; Multiple Organ Failure; Protein Processing, Post-Translational | 2021 |
Targeting O-GlcNAcylation to develop novel therapeutics.
Topics: Acetylglucosamine; Diabetes Mellitus; Humans; N-Acetylglucosaminyltransferases; Phosphorylation; Protein Processing, Post-Translational | 2021 |
Role of O-linked N-acetylglucosamine (O-GlcNAc) modification of proteins in diabetic cardiovascular complications.
Topics: Acetylglucosamine; Cardiovascular System; Diabetes Complications; Diabetes Mellitus; Hexosamines; Humans; Protein Processing, Post-Translational | 2021 |
Potential Roles of O-GlcNAcylation in Primary Cilia- Mediated Energy Metabolism.
Topics: Acetylglucosamine; Cilia; Diabetes Mellitus; Energy Metabolism; Homeostasis; Humans; Insulin-Secreting Cells; Obesity; Signal Transduction | 2020 |
The Role of O-GlcNAcylation in Immune Cell Activation.
Topics: Acetylglucosamine; Animals; Diabetes Mellitus; Humans; Immune System; N-Acetylglucosaminyltransferases; Obesity | 2021 |
Protein O-GlcNAcylation in diabetes and diabetic complications.
Topics: Acetylation; Acetylglucosamine; Diabetes Mellitus; Humans; Proteome | 2013 |
Circadian regulation of metabolism.
Topics: Acetylglucosamine; Adenosine Diphosphate Ribose; Alcohol Drinking; Amino Acids; AMP-Activated Protein Kinases; Animals; Carbohydrate Metabolism; Circadian Clocks; Circadian Rhythm; Diabetes Mellitus; Energy Metabolism; Heme; Homeostasis; Humans; Light; Lipid Metabolism; Mitochondria; NAD; Obesity; Proteins; Sleep; Sleep Disorders, Circadian Rhythm; Suprachiasmatic Nucleus; Wakefulness | 2014 |
Nutrient regulation of signaling, transcription, and cell physiology by O-GlcNAcylation.
Topics: Acetylglucosamine; AMP-Activated Protein Kinases; Diabetes Mellitus; Epigenomics; Glycosylation; Humans; Neoplasms; Signal Transduction; Transcription, Genetic | 2014 |
Regulation of hyaluronan synthesis in vascular diseases and diabetes.
Topics: Acetylglucosamine; Acylation; Adenylate Kinase; Animals; Cardiovascular Diseases; Cell Adhesion; Cell Differentiation; Diabetes Mellitus; Gene Expression Regulation, Enzymologic; Humans; Hyaluronic Acid; Inflammation; Microcirculation; Myocytes, Smooth Muscle; Vascular Diseases | 2015 |
Roles of O-GlcNAc in chronic diseases of aging.
Topics: Acetylglucosamine; Aging; Chronic Disease; Diabetes Mellitus; Heart Diseases; Humans; Hyperglycemia; Inflammation; N-Acetylglucosaminyltransferases; Neoplasms; Neurodegenerative Diseases | 2016 |
O-linked beta-N-acetylglucosamine (O-GlcNAc): Extensive crosstalk with phosphorylation to regulate signaling and transcription in response to nutrients and stress.
Topics: Acetylglucosamine; Acetylglucosaminidase; Animals; Diabetes Mellitus; Food; Gene Expression Regulation, Enzymologic; Hexosamines; Humans; N-Acetylglucosaminyltransferases; Neurons; Phosphorylation; Proteasome Endopeptidase Complex; Protein Processing, Post-Translational; Signal Transduction; Stress, Physiological; Ubiquitination | 2010 |
O-GlcNAc signaling: a metabolic link between diabetes and cancer?
Topics: Acetylglucosamine; Animals; Diabetes Mellitus; Hexosamines; Humans; Insulin; Neoplasms; Signal Transduction | 2010 |
O-GlcNAc signaling in the cardiovascular system.
Topics: Acetylglucosamine; Acylation; Animals; Cardiovascular Diseases; Cardiovascular System; Cell Cycle; Cell Survival; Diabetes Mellitus; Glycosylation; Humans; Insulin; Myocytes, Cardiac; Phosphorylation; Protein Processing, Post-Translational; Signal Transduction; Stress, Physiological; Transcription, Genetic | 2010 |
Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease.
Topics: Acetylglucosamine; Animals; Chronic Disease; Diabetes Mellitus; Glycosylation; Humans; Models, Molecular; Molecular Structure; N-Acetylglucosaminyltransferases; Neoplasms; Neurodegenerative Diseases; Phosphorylation; Protein Conformation; Signal Transduction; Transcription, Genetic | 2011 |
O-GlcNAc modification of nucleocytoplasmic proteins and diabetes.
Topics: Acetylglucosamine; Animals; Aorta; Cytoplasm; Diabetes Mellitus; Glycosylation; Hexosamines; Humans; Insulin Resistance; Nuclear Proteins; Pancreas | 2005 |
O-GlcNAc modification in diabetes and Alzheimer's disease.
Topics: Acetylglucosamine; Acylation; Alzheimer Disease; Diabetes Mellitus; Humans; Models, Biological; Protein Processing, Post-Translational | 2007 |
[O-GlcNAc and its function].
Topics: Acetylglucosamine; Animals; Cell Nucleus; Cloning, Molecular; Diabetes Mellitus; Glycosylation; Hexosamines; Humans; N-Acetylglucosaminyltransferases; Nuclear Proteins; Phosphorylation; Serine; Signal Transduction; Threonine | 1998 |
The emerging significance of O-GlcNAc in cellular regulation.
Topics: Acetylglucosamine; Animals; Cell Physiological Phenomena; Diabetes Mellitus; Glycosylation; Humans; Neurodegenerative Diseases; Phosphorylation; Proteins | 2002 |
11 other study(ies) available for acetylglucosamine and Diabetes Mellitus
| Article | Year |
|---|---|
Altered protein O-GlcNAcylation in placentas from mothers with diabetes causes aberrant endocytosis in placental trophoblast cells.
Topics: Acetylglucosamine; Acylation; Adult; Clathrin; Diabetes Mellitus; Endocytosis; Female; Glycosylation; Hexosamines; Humans; Mothers; N-Acetylglucosaminyltransferases; Placenta; Pregnancy; Protein Processing, Post-Translational; Trophoblasts; Young Adult | 2021 |
Fetal Reprogramming of Nutrient Surplus Signaling, O-GlcNAcylation, and the Evolution of CKD.
Topics: Acetylglucosamine; Adenosine Triphosphate; Diabetes Mellitus; Glucose; Humans; Nutrients; Protein Processing, Post-Translational; Renal Insufficiency, Chronic; TOR Serine-Threonine Kinases; Uridine Diphosphate | 2023 |
Development of in vitro model of insulin receptor cleavage induced by high glucose in HepG2 cells.
Topics: Acetylglucosamine; Acylation; Blood Glucose; Blotting, Western; Calcium; Cell Line, Tumor; Diabetes Mellitus; Dose-Response Relationship, Drug; Enzyme-Linked Immunosorbent Assay; Glucose; HEK293 Cells; HeLa Cells; Hep G2 Cells; Humans; Models, Biological; N-Acetylglucosaminyltransferases; Peptide Hydrolases; Proteolysis; Receptor, Insulin; RNA Interference; Time Factors | 2014 |
Site-specific GlcNAcylation of human erythrocyte proteins: potential biomarker(s) for diabetes.
Topics: Acetylglucosamine; Biomarkers; Diabetes Mellitus; Erythrocytes; Humans; Immunoblotting; Immunoprecipitation; Mass Spectrometry; Models, Biological; Proteins | 2009 |
Increased enzymatic O-GlcNAcylation of mitochondrial proteins impairs mitochondrial function in cardiac myocytes exposed to high glucose.
Topics: Acetylglucosamine; Animals; Cyclooxygenase 1; Diabetes Mellitus; Gene Expression Regulation, Enzymologic; Glucose; Glucosyltransferases; Glycosylation; Membrane Proteins; Mice; Mitochondria, Heart; Mitochondrial Proteins; Myocytes, Cardiac; NADH Dehydrogenase; Protein Processing, Post-Translational; Rats; Sweetening Agents | 2009 |
O-GlcNAcylation regulates hyperglycemia-induced GPX1 activation.
Topics: Acetylglucosamine; Acylation; Animals; Cell Line; Diabetes Mellitus; Enzyme Activation; Female; Glutathione Peroxidase; Glutathione Peroxidase GPX1; Humans; Hyperglycemia; Mice; Mice, Inbred C3H; Mice, Inbred C57BL; Rats | 2010 |
THE EFFECT OF INTRAVENOUS N-ACETYL-D-GLUCOSAMINE ON THE BLOOD AND URINE SUGAR CONCENTRATIONS OF NORMAL SUBJECTS.
Topics: Acetylglucosamine; Biomedical Research; Blood Glucose; Carbohydrate Metabolism; Diabetes Mellitus; Glucosamine; Glucose Tolerance Test; Glycosuria; Humans; Injections, Intravenous; Liver Diseases; Liver Glycogen; Pharmacology; Postoperative Care | 1964 |
Elevation of the post-translational modification of proteins by O-linked N-acetylglucosamine leads to deterioration of the glucose-stimulated insulin secretion in the pancreas of diabetic Goto-Kakizaki rats.
Topics: Acetylglucosamine; Animals; Diabetes Mellitus; Glucose; Homeodomain Proteins; Insulin; Insulin Secretion; Islets of Langerhans; N-Acetylglucosaminyltransferases; Pancreas; Protein Processing, Post-Translational; Rats; Rats, Wistar; RNA Interference; Trans-Activators | 2007 |
Glucose mediates the translocation of NeuroD1 by O-linked glycosylation.
Topics: Acetylglucosamine; Active Transport, Cell Nucleus; Animals; Basic Helix-Loop-Helix Transcription Factors; Cell Line, Tumor; Cell Nucleus; Chronic Disease; Diabetes Mellitus; Gene Expression Regulation; Glucose; Glycosylation; Hyperglycemia; Insulin; Insulin-Secreting Cells; Mice; Protein Processing, Post-Translational; Sweetening Agents | 2007 |
"VRA-GlcNAc": novel substrate for N-acetyl-beta-D-glucosaminidase applied to assay of this enzyme in urine.
Topics: Acetylglucosamine; Acetylglucosaminidase; Diabetes Mellitus; Humans; Hydrogen-Ion Concentration; Kinetics; Substrate Specificity; Temperature; Thiazoles | 1990 |
Improved kinetic rate assay of urinary N-acetyl-beta-D-glucosaminidase with 2-chloro-4-nitrophenyl-N-acetyl-beta-D-glucosaminide as substrate.
Topics: Acetylglucosamine; Acetylglucosaminidase; Adolescent; Adult; Aged; Child; Child, Preschool; Diabetes Mellitus; Female; Glucosamine; Health Status; Hexosaminidases; Humans; Infant; Infant, Newborn; Kinetics; Male; Middle Aged; Placenta; Reference Values | 1990 |