[1] A. Hashimoto, T. Nishikawa, T. Hayashi, N. Fujii, K. Harada, T. Oka, K. Takahashi, The presence of free D-serine in rat brain. FWBS Let. 1992, 296, 33-36, Doi: 10.1016/0014-5793(92)80397-Y.
[2] H. Wolosker, K.N. Sheth, M. Takahashi, J.P. Mothet, R.O.Jr. Brady, C.D. Ferris, S.H. Snyder, Purification of serine racemase: biosynthesis of the neuromodulator D-serine. Proc. Natl. Acad. Sci. U S A.1999b, 96, 721–725.
[3] M.A. Smith, V. Mach, A. Ebneth, O. Moraes, B. Felicetti, M. Wood, D. Schonfeld, O. Mather, A. Cesura, J. Barker, The structure of mammalian serine racemase, Evidence for conformational changes upon inhibitor binding, J. Bio. Chem., 2010, 285, 12873-12881. Doi: 10.1074/jbcM109.050062.
[4] W. Wang, S.W. Barger, Roles of quaternary structure and cysteine residues in the activity of human serine racermase, BMC Biochem. 2011, 12, 63. Doi: 10.1186/1471-2091-12-63.
[5] L. Pollegioni, L. Piubelli, G. Molla, E. Rosini,D-amino acid oxidase-pLG72 interaction and D-serine modulation, Front. Mol. Biosci., 2018, 5, 1-12. Doi: 10.3389/fmolb.2018.00003.
[6] N.R. Kondori, P. Paul, J.P. Robbins, K. Liu, J.C.W. Hilyard, D.J. Wells, J.S. De Belleroche, Focus on the role of D-serine and D-amino acid oxidase in Amyotrophic Lateral Sclerosis/motor neuron disease (ALC), Front. Mol. Biosci., 2018, 5, 1-7. Doi: 10.3389/fmolb.2018.00008.
[7] N. Nitoker, D.T. Major, Understanding the reaction mechanisms and intermediate stabilization in mammalian serine racemase using multiscale quantum-classical simulation, Biochem., 2015, 52(2), 516-527.
[8] T. Hanai, Quantitative in silico analysis of D-amino acid oxidase reactivity and inhibition, Current Bioactive Compounds, 2017, 13, 312-317. Doi:10.2174/1573407212666161014133246
[9] T. Hanai, Basic properties of a molecular mechanics program and the generation of unknown stereo structures of proteins for quantitative analysis of enzyme reactions, In: Watkins, P. (Ed.), Molecular Mechanics and Modeling. Nova Science: New York, 2015, Chapter 2, 25-48. (ISBN: 978-1-63483-388-2)
[10] T. Hanai, Quantitative in silico analysis of enzyme reactions: comparison of D-amino acid oxidase and monoamine oxidase. Am. Biotechnol. Lab.2007, 25, 8-13.
[11] T. Hanai, Quantitative in silico analysis of alanine racemase reactivity, In Watkins, P. (Ed.), Molecular Mechanics and Modeling. Nova Science: New York, 2015, Chapter 3, 49-71. (ISBN: 978-1-63483-388-2)
[12] RCSB, Protein Data Bank, www.rcsb.org/pdb/.
[13]D.L.Nelson, G.A. Applegate, M.L. Beio, D.L. Graham, D.V. Berkowitz, Human serine racemase structure/activity relationship studies provide mechanistic insight and point to position-84 as a hotspot for -elimination function, J. Biol. Chem., published on July 10, 2017, 1-35. Doi:10.1074/jbc.M117.777904.
[14]H. Wu, Y.B. Qi, J. Kong, F. Kou, F. Jia, X.F. Dan, Y. Wang, A seven-coordinate manganese (II) complex formed with the tripodal tetradentate ligand tris(N-methylbenzimidazol-2-ylmethyl)amine,Z.Naturforsch. 2010, 65b, 1097-1100.
[15] D.E. Metzler, E.E. Snell, Deamination of serine: 1. Catalystic deamination of serine and cysteine by pyridoxal and metal salts, J. Biol. Chem., 1952, 198, 353-361.
[16]L. Gorgannezhad, G. Dehghan, S.Y. Ebrahimipour, A. Nasen, J.E.N. Dolatabadi, Complex of manganese (II) with curcumin: Spectroscopic characterization, DFT study, model-based analysis and antiradical activity, J. Mol. Struc.,2016, 1109, 139-145. Doi:org/10.1016/jmoistruc.2015.12.051.
[17]K.Islam, Manganese complex of ethylenediamine-tetraacetic acid (EDTA)-benzothiazole aniline (BTA) conjugate as a potential liver-targeting MRI contrast agent, J. Med. Chem., 2017, 60(7), 2993-3001. Doi: 10.1021/acs.jmedchem.6b01799.
[18]D.W. Gohara, E.D. Cera, Molecular mechanisms of enzyme activation by monovalent cations, J. Biol. Chem. 2016, 291(40),20840-20848.Doi: 10.1074/jbc.R116.737833.