References
- Bunn HF, Gabbay KH, Gallop PM. The glycosylation of hemoglobin: relevance to diabetes mellitus. Science. 1978;200(4337):21–27.
- Stevens VJ, Vlassara H, Abati A, et al. Nonenzymatic glycosylation of hemoglobin. J Biol Chem. 1977;252(9):2998–3002.
- Watkins NG, Neglia-Fisher CI, Dyer DG, et al. Effect of phosphate on kinetics and specificity of glycation of protein. J Biol Chem. 1987;262(15):7207–7212.
- Clark SLD, Santin AE, Bryant PA, et al. The initial noncovalent binding of glucose to human hemoglobin in nonenzymatic glycation. Glycobiology. 2013;23(11):1250–1259.
- Bookchin RM, Gallop PM. Structure of hemoglobin A1c: nature of the N-terminal β chain blocking group. Biochem Biophys Res Commun. 1968;32(1):86–93.
- Little RR, Sacks DB. HbA1c: how do we measure it and what does it mean? Curr Opin Endocrinol. 2009;16(2):113–118.
- Bunn HF. Evaluation of glycosylated hemoglobin in diabetic patients. Diabetes. 1981;30(7):613–617.
- Gould BJ, Davie SJ, Yudkin JS. Investigation of the mechanism underlying the variability of glycated haemoglobin in non-diabetic subjects not related to glycaemia. Clin Chim Acta. 1997;260(1):49–64.
- Brownlee M. Advanced protein glycosylation in diabetes and aging. Ann Rev Med. 1995;46(1):223–234.
- Rondeau P, Bourdon E. The glycation of albumin: structural and functional impacts. Biochimie. 2011;93(4):645–658.
- Forbes JM, Cooper ME. Mechanisms of diabetic complications. Physiol Rev. 2013;93(1):137–188.
- Smith RJ, Koening RJ, Binnerts A, et al. Regulation of Hemoglobin A1c formation in human erythrocytes in vitro. Effects of physiological factors other than glucose. J Clin Invest. 1982;69(5):1164–1168.
- Furth AJ. Methods of assaying nonenzymatic glycation. Anal Biochem. 1988;175(2):347–360.
- Hempe JM, McGehee AM, Hsia D, et al. Characterization of unstable Hemoglobin A1c complexes by dynamic capillary isoelectric focusing. Anal Biochem. 2012;424(2):149–155.
- Rodnick KJ, Holman RW, Ropski PS, et al. A perspective on reagent diversity and non-covalent binding of reactive carbonyl species (RCS) and effector reagents in non-enzymatic glycation (NEG): mechanistic considerations and implications for future research. Front Chem. 2017;5(article 39):1–8.
- Bishop C, Surgenor DM. The Red Blood Cell: A Comprehensive Treatise. New York (NY, USA): Academic Press; 1964.
- Richard V, Dodson GG, Mauguen M. Human deoxyhaemoglobin-2,3-diphosphoglycerate complex low salt structure at 2.5 Å resolution. J Mol Biol. 1993;233(2):270–274.
- Hobish MK, Powers DA. The binding of physiologically significant protons to 2,3-diphosphoglycerate. Biophys Chem. 1983;18(4):407–411.
- Bobadilla L, Nino F, Narasimhan G. Predicting and characterizing metal-binding sites using support vector machines. Proc ICBA. 2005;8(1):307–318.
- Ito S, Nakahari T, Yamamoto D. The structural feature surrounding glycated lysine residues in human hemoglobin. Biomed Res. 2011;32(3):217–223.
- Higgins PJ, Bunn HF. Kinetic analysis of the non-enzymatic glycosylation of hemoglobin. J Biol Chem. 1981;256(10):5204–5208.
- Lowrey CH, Lyness SJ, Soeldner JS. The effect of hemoglobin ligands on the kinetics of HbA1c formation. J Biol Chem. 1985;260(21):16111–16118.
- Park B, Holman RW, Slade T, et al. A biochemistry question-guided derivation of a potential mechanism for HbA1c formation in diabetes mellitus leading to a data-driven clinical diagnosis. J Chem Ed. 2016;93(4):795–797.
- Gil H, Peña M, Vásquez B, et al. Catalysis by organic phosphates of the glycation of human hemoglobin. J Phys Org Chem. 2002;15(12):820–825.
- Kunika K, Itakura M, Yamashita K. Inorganic phosphate accelerates hemoglobin A1c synthesis. Life Sci. 1989;45(7):623–630.
- Smith BA, Mottishaw CR, Hendricks AJ, et al. Potential roles of inorganic phosphate on the progression of initially bound glucopyranose toward the nonenzymatic glycation of human hemoglobin: Mechanistic diversity and impacts on site selectivity. Cogent Biol. 2018;4(1):1–18.
- Bevington A, Mundy KI, Yates AJP, et al. A study of intracellular orthophosphate concentration in human muscle and erythrocytes by 31P nuclear magnetic resonance spectroscopy and selective chemical assay. Clin Sci. 1986;71(6):729–735.
- Gupta RK, Benovic JL, Rose ZB. The determination of free magnesium level in the human red blood cell by 31P NMR. J Biol Chem. 1978;253(17):6172–6176.
- Goldstein DE, Little RR, Lorenz RA, et al. Tests of glycemia in diabetes. Diabetes Care. 1995;18(6):896–909.
- De Heer J. The principle of Le Chatelier and Braun. J Chem Ed. 1957;34(8):375–380.
- Nakashima K, Hattori Y, Yamazaki K, et al. Immediate elimination of labile Hb A1c with allosteric effectors of hemoglobin. Diabetes. 1990;39(1):17–21.