[1] Smith, G.J. (1999) The Fluorescence of Dihydroxyphenylalanine; The Effects of Protonation-Deprotonation. Journal of Studies in Dynamics and Change, 115, 346-349.
http://dx.doi.org/10.1111/j.1478-4408.1999.tb00351.x
[2] Gross, A.J. and Sizer, I.W. (1959) The Oxidation of Tyramine, Tyrosine, and Related Compounds by Peroxidase. Journal of Biological Chemistry, 234, 1611-1614.
[3] Guilivi, C., Traaseth, N.J. and Davies, K.J.A. (2003) Tyrosine Oxidation Products: Analysis and Biological Relevance. Amino Acids, 25, 227-232.
http://dx.doi.org/10.1007/s00726-003-0013-0
[4] Nagaraj, R.H. and Monnier, V.M. (1992) Isolation and Characterization of a Blue Fluorophore from Human Lens Eye Crystallins: In Vitro Formation from Maillard Reaction with Ascorbate and Ribose. Biochimica et Biophysica Acta, 1116, 34-42.
http://dx.doi.org/10.1016/0304-4165(92)90125-E
[5] Sell, D.R. and Monnier, V.M. (1989) Structure Elucidation of a Senescence Cross-Link from Human Extracellular Matrix. Journal of Biological Chemistry, 264, 21597-21602.
[6] Sell, D.R., Ramanakoppa, H., Grandhee, S.K., Odetti, P., Lapolla, A., Fogarty, J. and Monnier, V.M. (1991) Pentosidine: A Molecular Marker for the Cumulative Damage to Proteins in Diabetes, Aging and Uremia. Diabetes/Metabolism Reviews, 7, 239-251.
http://dx.doi.org/10.1002/dmr.5610070404
[7] Verzijl, N., DeGroot, J., Oldehinkel, E., Bank, R.A., Thorpe, S.R., Baynes, J.W., Bayliss, M.T., Bijlsma, J.W.J., Lafeber, F.P.G. and TeKoppele, J.M. (2000) Age-Related Accumulation of Maillard Reaction Products in Human Articular Cartilage Collagen. Biochemical Journal, 350, 381-387.
http://dx.doi.org/10.1042/0264-6021:3500381
[8] Lamore, S.D., Azimian, S., Horn, D., Anglin, B.L., Uchida, K., Cabello, C.M. and Wondrak, G.T. (2010) The Malondialdehyde-Derived Fluorophore DHP-Lysine Is a Potent Photosensitizer of UVA-Induced Photosensitized Oxidative Stress in Human Skin Cells. Journal of Photochemistry and Photobiology, 101, 261-264.
http://dx.doi.org/10.1016/j.jphotobiol.2010.07.010
[9] Shimizu, O. (1973) Excited States in Photodimerization of Aqueous Tyrosine at Room Temperature. Photochemistry and Photobiology, 18, 125-133.
http://dx.doi.org/10.1111/j.1751-1097.1973.tb06402.x
[10] Lehrer, S.S. and Fasman, G.D. (1967) Ultraviolet Irradiation Effects in Poly-L-Tyrosine and Model Compounds. Identification of Bityrosine as a Photoproduct. Biochemistry, 6, 757-767.
http://dx.doi.org/10.1021/bi00855a017
[11] Menter, J.M., Williams, G.D., Carlyle, K., Moore, C.L. and Willis, I. (1995) Photochemistry of Type I Acid-Soluble Calf Skin Collagen: Dependence on Excitation Wavelength. Photochemistry and Photobiology, 62, 402-408.
http://dx.doi.org/10.1111/j.1751-1097.1995.tb02360.x
[12] Menter, J.M., Chu, E.G. and Martin, N.V. (2009) Temperature-Dependence of Photochemical Fluorescence Fading in Skh-1 Hairless Mouse Collagen. Photodermatology, Photoimmunology & Photomedicine, 25, 128-131.
http://dx.doi.org/10.1111/j.1600-0781.2009.00421.x
[13] Menter, J.M., Abukhalaf, I.K., Patta, A.M., Silvestrov, N.A. and Willis, I. (2007) Fluorescence of Putative Chromophores in Skh-1 and Citrate-Soluble Calf Skin Collagens. Photodermatology, Photoimmunology & Photomedicine, 23, 222-228.
http://dx.doi.org/10.1111/j.1600-0781.2007.00312.x
[14] Permyakov, E.A. (1993) Luminescent Spectroscopy of Proteins. CRC Press, Inc., Boca Raton, 38.
[15] Tomaselli, V.P. and Shamos, M.H. (1974) Electrical Properties of Hydrated Collagen II. Biopolymers, 13, 2423-2434.
http://dx.doi.org/10.1002/bip.1974.360131203
[16] Barry, B.A., Chen, J., Keough, J., Jenson, D., Offenbacher, A. and Paqba, C. (2012) Proton-Coupled Electron Transfer and Redox-Active Tyrosines: Structure and Function of the Tyrosyl Radicals in Ribonucleotide Reductase and Photosystem II. The Journal of Physical Chemistry Letters, 3, 543-554.
http://dx.doi.org/10.1021/jz2014117
[17] Chen, Z., Concepcion, J.A., Hu, X., Yang, W., Hoertz, P.G. and Meyer, T.J. (2010) Proton Transfer in the Excited State-Concerted O Atom-Proton Transfer in the O-O Bond Forming Step in Water Oxidation. Proceedings of the National Academy of Sciences, 107, 7225-7229.
http://dx.doi.org/10.1073/pnas.1001132107