Allysine and α-Aminoadipic Acid as Markers of the Glyco-Oxidative Damage to Human Serum Albumin under Pathological Glucose Concentrations
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C. Luna | M. Estévez | C. Dueñas | A. Arjona
[1] J. Ruiz-Carrascal,et al. Glucose boosts protein oxidation/nitration during simulated gastric digestion of myofibrillar proteins by creating a severe pro-oxidative environment. , 2022, Food chemistry.
[2] F. Peña,et al. Noxious effects of selected food-occurring oxidized amino acids on differentiated CACO-2 intestinal human cells. , 2020, Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association.
[3] M. Estaras,et al. The lysine derivative aminoadipic acid, a biomarker of protein oxidation and diabetes-risk, induces production of reactive oxygen species and impairs trypsin secretion in mouse pancreatic acinar cells. , 2020, Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association.
[4] L. Liang,et al. Lysine pathway metabolites and the risk of type 2 diabetes and cardiovascular disease in the PREDIMED study: results from two case-cohort studies , 2019, Cardiovascular Diabetology.
[5] H. Jang,et al. 2-Aminoadipic acid (2-AAA) as a potential biomarker for insulin resistance in childhood obesity , 2019, Scientific Reports.
[6] K. Davies. Free radicals and redox regulation in ageing. , 2019, Free radical biology & medicine.
[7] C. Luna,et al. Formation of allysine in β-lactoglobulin and myofibrillar proteins by glyoxal and methylglyoxal: Impact on water-holding capacity and in vitro digestibility. , 2019, Food chemistry.
[8] C. Luna,et al. Antioxidant and pro-oxidant actions of resveratrol on human serum albumin in the presence of toxic diabetes metabolites: Glyoxal and methyl-glyoxal. , 2018, Biochimica et biophysica acta. General subjects.
[9] L. Liang,et al. Association of Tryptophan Metabolites with Incident Type 2 Diabetes in the PREDIMED Trial: A Case-Cohort Study. , 2018, Clinical chemistry.
[10] C. Luna,et al. Oxidative damage to food and human serum proteins: Radical-mediated oxidation vs. glyco-oxidation. , 2017, Food chemistry.
[11] M. Hecker,et al. Role of protein carbonylation in diabetes , 2018, Journal of Inherited Metabolic Disease.
[12] L. Lago,et al. Generation of Advanced Glycation End-Products (AGEs) by glycoxidation mediated by copper and ROS in a human serum albumin (HSA) model peptide: reaction mechanism and damage in motor neuron cells. , 2017, Mutation research.
[13] P. Njølstad,et al. The kynurenine:tryptophan ratio as a predictor of incident type 2 diabetes mellitus in individuals with coronary artery disease , 2017, Diabetologia.
[14] S. Hazen,et al. Myeloperoxidase‐mediated protein lysine oxidation generates 2‐aminoadipic acid and lysine nitrile in vivo , 2017, Free radical biology & medicine.
[15] J. Masuda,et al. Concentrations of various tryptophan metabolites are higher in patients with diabetes mellitus than in healthy aged male adults , 2017, Diabetology International.
[16] I. Sadowska-Bartosz,et al. Effect of glycation inhibitors on aging and age-related diseases , 2016, Mechanisms of Ageing and Development.
[17] S. De Smet,et al. Apple phenolics as inhibitors of the carbonylation pathway during in vitro metal-catalyzed oxidation of myofibrillar proteins. , 2016, Food chemistry.
[18] Rohan V. Tikekar,et al. Generation of reactive oxidative species from thermal treatment of sugar solutions. , 2016, Food chemistry.
[19] Michael J. Davies,et al. Protein oxidation and peroxidation , 2016, The Biochemical journal.
[20] C. Luna,et al. Redox chemistry of the molecular interactions between tea catechins and human serum proteins under simulated hyperglycemic conditions. , 2016, Food & function.
[21] M. Blüher,et al. Carbonylated plasma proteins as potential biomarkers of obesity induced type 2 diabetes mellitus. , 2014, Journal of proteome research.
[22] D. Bernlohr,et al. Oxidative stress and protein carbonylation in adipose tissue - implications for insulin resistance and diabetes mellitus. , 2013, Journal of proteomics.
[23] R. Vasan,et al. 2-Aminoadipic acid is a biomarker for diabetes risk. , 2013, The Journal of clinical investigation.
[24] M. Estévez,et al. Oxidative damage to poultry, pork, and beef during frozen storage through the analysis of novel protein oxidation markers. , 2013, Journal of agricultural and food chemistry.
[25] M. Estévez,et al. Oxidation of myofibrillar proteins and impaired functionality: underlying mechanisms of the carbonylation pathway. , 2012, Journal of agricultural and food chemistry.
[26] M. Estévez,et al. Fluorescent HPLC for the detection of specific protein oxidation carbonyls - α-aminoadipic and γ-glutamic semialdehydes - in meat systems. , 2011, Meat science.
[27] V. Monnier,et al. Mechanism of Lysine Oxidation in Human Lens Crystallins during Aging and in Diabetes* , 2009, The Journal of Biological Chemistry.
[28] V. Monnier,et al. 2-aminoadipic acid is a marker of protein carbonyl oxidation in the aging human skin: effects of diabetes, renal failure and sepsis. , 2007, The Biochemical journal.
[29] R. Ali,et al. Biochemical, biophysical, and thermodynamic analysis of in vitro glycated human serum albumin , 2007, Biochemistry (Moscow).
[30] J. Ruiz,et al. Phospholipid oxidation, non-enzymatic browning development and volatile compounds generation in model systems containing liposomes from porcine Longissimus dorsi and selected amino acids , 2007 .
[31] M. Akagawa,et al. Formation of α‐Aminoadipic and γ‐Glutamic Semialdehydes in Proteins by the Maillard Reaction , 2005 .
[32] A. Booth,et al. Unusual susceptibility of heme proteins to damage by glucose during non-enzymatic glycation. , 2003, Biophysical chemistry.
[33] Takeshi Sasaki,et al. Oxidative deamination of lysine residue in plasma protein from diabetic rat: α-dicarbonyl-mediated mechanism , 2002 .
[34] M. Akagawa,et al. Oxidative Deamination by Hydrogen Peroxide in the Presence of Metals , 2002, Free radical research.
[35] E. Stadtman,et al. Glutamic and aminoadipic semialdehydes are the main carbonyl products of metal-catalyzed oxidation of proteins. , 2001, Proceedings of the National Academy of Sciences of the United States of America.
[36] N. C. Price,et al. Glucose modification of human serum albumin: a structural study. , 1997, Free radical biology & medicine.
[37] G. L. Miller. Use of Dinitrosalicylic Acid Reagent for Determination of Reducing Sugar , 1959 .