References
- Kohn JC, Lampi MC, Reinhart-King CA, 2015. Age-related vascular stiffening: causes and consequences. Frontiers in Genetics. 6: 112. doi:https://doi.org/10.3389/fgene.2015.00112
- Sharma G, Goodwin J. 2006. Effect of aging on respiratory system physiology and immunology. Clinical Interventions in Aging. 1(3):253–260. doi:https://doi.org/10.2147/ciia.2006.1.3.253.
- Sherratt MJ. 2013. Age-related tissue stiffening: cause and effect. Advances in Wound Care. 2(1):11–17. doi:https://doi.org/10.1089/wound.2011.0328.
- Sayin N, Kara N, Pekel G. 2015. Ocular complications of diabetes mellitus. World Journal of Diabetes. 6(1):92–108. doi:https://doi.org/10.4239/wjd.v6.i1.92.
- Piva SR, Susko AM, Khoja SS, Josbeno DA, Fitzgerald GK, Toledo FGS. 2015. Links between osteoarthritis and diabetes: implications for management from a physical activity perspective. Clinics in Geriatric Medicine. 31(1):67–viii. doi:https://doi.org/10.1016/j.cger.2014.08.019.
- Abate M, Schiavone C, Pelotti P, Salini V. 2010. Limited joint mobility in diabetes and ageing: recent advances in pathogenesis and therapy. International Journal of Immunopathology and Pharmacology. 23(4):997–1003. doi:https://doi.org/10.1177/039463201002300404.
- Gautieri A, Passini FS, Silván U, Guizar-Sicairos M, Carimati G, Volpi P, Moretti M, Schoenhuber H, Redaelli A, Berli M, Snedeker JG, 2017. Advanced glycation end-products: mechanics of aged collagen from molecule to tissue. Matrix Biology. 59: 95–108. https://doi.org/10.1016/j.matbio.2016.09.001
- United States bone and joint initiative: the burden of musculoskeletal diseases in the United States (BMUS). 2018. http://www.boneandjointburden.org
- Snedeker JG, Gautieri A. 2014. The role of collagen crosslinks in ageing and diabetes - the good, the bad, and the ugly. Muscles, Ligaments and Tendons Journal. 4(3):303–308. doi:https://doi.org/10.32098/mltj.03.2014.07.
- Eekhoff JD, Fang F, Lake SP. 2018. Multiscale mechanical effects of native collagen cross-linking in tendon. Connective Tissue Research. 59(5):410–422. doi:https://doi.org/10.1080/03008207.2018.1449837
- Sharma C, Kaur A, Thind SS, Singh B, Raina S. 2015. Advanced glycation end-products (AGEs): an emerging concern for processed food industries. Journal of Food Science and Technology. 52(12):7561–7576. doi:https://doi.org/10.1007/s13197-015-1851-y.
- Uribarri J, Del Castillo MD, de la Maza MP, Filip R, Gugliucci A, Luevano-Contreras C, Macías-Cervantes MH, Markowicz Bastos DH, Medrano A, Menini T, Portero-Otin M, Rojas A, Sampaio GR, Wrobel K, Wrobel K, Garay-Sevilla ME. 2015. Dietary advanced glycation end products and their role in health and disease. Advances in Nutrition (Bethesda, Md.). 6(4):461–473. doi:https://doi.org/10.3945/an.115.008433.
- Nass N, Bartling B, Navarrete Santos A, Scheubel RJ, Börgermann J, Silber RE, Simm A. 2007. Advanced glycation end products, diabetes and ageing. Zeitschrift für Gerontologie und Geriatrie. 40(5):349–356. doi:https://doi.org/10.1007/s00391-007-0484-9
- Singh VP, Bali A, Singh N, Jaggi AS. 2014. Advanced glycation end products and diabetic complications. The Korean Journal of Physiology & Pharmacology : Official Journal of the Korean Physiological Society and the Korean Society of Pharmacology. 18(1):1–14. doi:https://doi.org/10.4196/kjpp.2014.18.1.1.
- Perrone A, Giovino A, Benny J, Martinelli F. 2020. advanced glycation end products (AGEs): biochemistry, signaling, analytical methods, and epigenetic effects hrelia S, editor. Oxidative Medicine and Cellular Longevity. 3818196. doi:https://doi.org/10.1155/2020/3818196.
- Gkogkolou P, Böhm M. 2012. Advanced glycation end products: key players in skin aging? Dermato-endocrinology. 4(3):259–270. doi:https://doi.org/10.4161/derm.22028.
- Nowotny K, Jung T, Höhn A, Weber D, Grune T. 2015. Advanced glycation end products and oxidative stress in type 2 diabetes mellitus. Biomolecules. 5(1):194–222. doi:https://doi.org/10.3390/biom5010194.
- Hegab Z, Gibbons S, Neyses L, Mamas MA. 2012. Role of advanced glycation end products in cardiovascular disease. World Journal of Cardiology. 4(4):90–102. doi:https://doi.org/10.4330/wjc.v4.i4.90.
- Oleniuc M, Secara I, Onofriescu M, Hogas S, Voroneanu L, Siriopol D, Covic A. 2011. Consequences of advanced glycation end products accumulation in chronic kidney disease and clinical usefulness of their assessment using a non-invasive technique - skin autofluorescence. Maedica. 6(4):298–307. https://pubmed.ncbi.nlm.nih.gov/22879845.
- de Groot L, Hinkema H, Westra J, Smit AJ, Kallenberg CGM, Bijl M, Posthumus MD. 2011. Advanced glycation endproducts are increased in rheumatoid arthritis patients with controlled disease. Arthritis Research & Therapy. 13(6):R205–R205. doi:https://doi.org/10.1186/ar3538.
- Rodríguez-García J, Requena JR, Rodríguez-Segade S. 1998. Increased concentrations of serum pentosidine in rheumatoid arthritis. Clinical Chemistry. 44(2):250–255. doi:https://doi.org/10.1093/clinchem/44.2.250
- Miyata T, Ishiguro N, Yasuda Y, Ito T, Nangaku M, Iwata H. Kurokawa K. 1998. increased pentosidine, an advanced glycation end product, in plasma and synovial fluid from patients with rheumatoid arthritis and its relation with inflammatory markers. Biochemical and Biophysical Research Communications. 244(1):45–49. doi:https://doi.org/10.1006/bbrc.1998.8203.
- Sasaki N, Fukatsu R, Tsuzuki K, Hayashi Y, Yoshida T, Fujii N, Koike T, Wakayama I, Yanagihara R, Garruto R, et al. 1998. Advanced glycation end products in alzheimer’s disease and other neurodegenerative diseases. The American Journal of Pathology. 153(4):1149–1155. doi:https://doi.org/10.1016/S0002-9440(10)65659-3
- Karim L, Tang SY, Sroga GE, Vashishth D. 2013. Differences in non-enzymatic glycation and collagen cross-links between human cortical and cancellous bone. Osteoporosis International : A Journal Established as Result of Cooperation between the European Foundation for Osteoporosis and the National Osteoporosis Foundation of the USA. 24(9):2441–2447. doi:https://doi.org/10.1007/s00198-013-2319-4.
- Takahashi M, Kushida K, Ohishi T, Kawana K, Hoshino H, Uchiyama A, Inoue T. 1994. Quantitative analysis of crosslinks pyridinoline and pentosidine in articular cartilage of patients with bone and joint disorders. Arthritis & Rheumatism. 37(5):724–728. doi:https://doi.org/10.1002/art.1780370517
- Takahashi M, Suzuki M, Kushida K, Hoshino H, Inoue T. 1998. The effect of aging and osteoarthritis on the mature and senescent cross-links of collagen in human meniscus. Arthroscopy. 14(4):366–372. doi:https://doi.org/10.1016/S0749-8063(98)70003-9
- Willett TL, Kandel R, JNA DC, Avery NC, Grynpas MD. 2012. Enhanced levels of non-enzymatic glycation and pentosidine crosslinking in spontaneous osteoarthritis progression. Osteoarthritis and Cartilage.20(7):736–744. doi:https://doi.org/10.1016/j.joca.2012.03.012.
- Reddy GK. 2004. Cross-linking in collagen by nonenzymatic glycation increases the matrix stiffness in rabbit achilles tendon. Experimental Diabesity Research. 5(2):143–153. doi:https://doi.org/10.1080/15438600490277860.
- Vicens-Zygmunt V, Estany S, Colom A, Montes-Worboys A, Machahua C, Sanabria AJ, Llatjos R, Escobar I, Manresa F, Dorca J, Navajas D, Alcaraz J, Molina-Molina M. 2015. Fibroblast viability and phenotypic changes within glycated stiffened three-dimensional collagen matrices. Respiratory Research. 16(1):82. doi:https://doi.org/10.1186/s12931-015-0237-z
- Aragno M, Mastrocola R. 2017. dietary sugars and endogenous formation of advanced glycation endproducts: emerging mechanisms of disease. Nutrients. 9(4):385. doi:https://doi.org/10.3390/nu9040385.
- Luevano-Contreras C, Garay-Sevilla ME, Chapman-Novakofski K. 2012. Role of dietary advanced glycation end products in diabetes mellitus. Journal of Evidence-Based Complementary & Alternative Medicine. 18(1):50–66. doi:https://doi.org/10.1177/2156587212460054
- Roy R, Boskey AL, Bonassar LJ. 2008. Non-enzymatic glycation of chondrocyte-seeded collagen gels for cartilage tissue engineering. Journal of Orthopaedic Research. 26(11):1434–1439. doi:https://doi.org/10.1002/jor.20662
- Rich H, Odlyha M, Cheema U, Mudera V, Bozec L. 2014. Effects of photochemical riboflavin-mediated crosslinks on the physical properties of collagen constructs and fibrils. Journal of Materials Science. Materials in Medicine. 25(1):11–21. doi:https://doi.org/10.1007/s10856-013-5038-7.
- Uemura R, Miura J, Ishimoto T, Yagi K, Matsuda Y, Shimizu M, Nakano T, Hayashi M. 2019. UVA-activated riboflavin promotes collagen crosslinking to prevent root caries. Scientific Reports. 9(1):1252. doi:https://doi.org/10.1038/s41598-018-38137-7
- Brummer G, Littlechild S, McCall S, Zhang Y, Conrad GW. 2011. The role of nonenzymatic glycation and carbonyls in collagen cross-linking for the treatment of keratoconus. Investigative Ophthalmology & Visual Science. 52(9):6363–6369. doi:https://doi.org/10.1167/iovs.11-7585.
- El-Raggal TM. 2009. Riboflavin-ultraviolet a corneal cross-linking for keratoconus. Middle East African Journal of Ophthalmology. 16(4):256–259. doi:https://doi.org/10.4103/0974-9233.58418.
- Tirella A, Liberto T, Ahluwalia A, 2012. Riboflavin and collagen: new crosslinking methods to tailor the stiffness of hydrogels. Materials Letters. 74: 58–61. https://doi.org/10.1016/j.matlet.2012.01.036
- Ibusuki S, Halbesma GJ, Randolph MA, Redmond RW, Kochevar IE, Gill TJ. 2007. Photochemically cross-linked collagen gels as three-dimensional scaffolds for tissue engineering. Tissue Engineering. 13(8):1995–2001. doi:https://doi.org/10.1089/ten.2006.0153
- Subasinghe SK, Ogbuehi KC, Dias GJ. 2018. Current perspectives on corneal collagen crosslinking (CXL). Graefe’s Archive for Clinical and Experimental Ophthalmology. 256(8):1363–1384. doi:https://doi.org/10.1007/s00417-018-3966-0
- Borde B, Grunert P, Härtl R, Bonassar LJ. 2015. Injectable, high-density collagen gels for annulus fibrosus repair: an in vitro rat tail model. Journal of Biomedical Materials Research Part A. 103(8):2571–2581. doi:https://doi.org/10.1002/jbm.a.35388
- Zhang M, Zou Y, Zhang F, Zhang X, Wang M. 2015. Efficacy of blue-light cross-linking on human scleral reinforcement. Optometry and Vision Science. 92(8):873–878. https://journals.lww.com/optvissci/Fulltext/2015/08000/Efficacy_of_Blue_Light_Cross_linking_on_Human.6.aspx.
- Diamantides N, Wang L, Pruiksma T, Siemiatkoski J, Dugopolski C, Shortkroff S, Kennedy S, Bonassar LJ. 2017. Correlating rheological properties and printability of collagen bioinks: the effects of riboflavin photocrosslinking and pH. Biofabrication. 9(3):34102. doi:https://doi.org/10.1088/1758-5090/aa780f
- Roy R, Boskey A, Bonassar LJ. 2010. Processing of type I collagen gels using nonenzymatic glycation. Journal of Biomedical Materials Research Part A. 93A(3):843–851. doi:https://doi.org/10.1002/jbm.a.32231
- Mason BN, Starchenko A, Williams RM, Bonassar LJ, Reinhart-King CA. 2013. Tuning three-dimensional collagen matrix stiffness independently of collagen concentration modulates endothelial cell behavior. Acta Biomaterialia. 9(1):4635–4644. doi:https://doi.org/10.1016/j.actbio.2012.08.007.
- Puetzer J, Bonassar L. 2016. Physiologically distributed loading patterns drive the formation of zonally organized collagen structures in tissue-engineered meniscus. Tissue Engineering Part A. 22(13–14):907–916. doi:https://doi.org/10.1089/ten.tea.2015.0519
- Puetzer JL, Koo E, Bonassar LJ. 2015. Induction of fiber alignment and mechanical anisotropy in tissue engineered menisci with mechanical anchoring. Journal of Biomechanics. 48(8):1436–1443. doi:https://doi.org/10.1016/j.jbiomech.2015.02.033.
- Cross VL, Zheng Y, Won Choi N, Verbridge SS, Sutermaster BA, Bonassar LJ, Fischbach C, Stroock AD. 2010. Dense type I collagen matrices that support cellular remodeling and microfabrication for studies of tumor angiogenesis and vasculogenesis in vitro. Biomaterials. 31(33):8596–8607. doi:https://doi.org/10.1016/j.biomaterials.2010.07.072.
- Puetzer JL, Ma T, Sallent I, Gelmi A, Stevens MM. 2021. Driving hierarchical collagen fiber formation for functional tendon, ligament, and meniscus replacement. Biomaterials. 269:120527. https://doi.org/10.1016/j.biomaterials.2020.120527
- Tsujii A, Nakamura N, Horibe S. 2017. Age-related changes in the knee meniscus. The Knee. 24(6):1262–1270. doi:https://doi.org/10.1016/j.knee.2017.08.001.
- Puetzer JL, Bonassar LJ. 2013. High density type I collagen gels for tissue engineering of whole menisci. Acta Biomaterialia. 9(8):7787–7795. doi:https://doi.org/10.1016/j.actbio.2013.05.002.
- Bowles RD, Williams RM, Zipfel WR, Bonassar LJ. 2010. Self-assembly of aligned tissue-engineered annulus fibrosus and intervertebral disc composite via collagen gel contraction. Tissue Engineering. Part A. 16(4):1339–1348. doi:https://doi.org/10.1089/ten.TEA.2009.0442.
- Enobakhare BO, Bader DL, Lee DA. 1996. Quantification of sulfated glycosaminoglycans in chondrocyte/alginate cultures, by use of 1,9-dimethylmethylene blue. Analytical Biochemistry. 243(1):189–191. doi:https://doi.org/10.1006/abio.1996.0502.
- Zheng CH, Levenston ME, 2015. Fact versus artifact: avoiding erroneous estimates of sulfated glycosaminoglycan content using the dimethylmethylene blue colorimetric assay for tissue-engineered constructs. European Cells & Materials. 29: 224–236. https://doi.org/10.22203/ecm.v029a17
- Kesava Reddy G, Enwemeka CS. 1996. A simplified method for the analysis of hydroxyproline in biological tissues. Clinical Biochemistry. 29(3):225–229. doi:https://doi.org/10.1016/0009-9120(96)00003-6.
- Heveran CM, Schurman CA, Acevedo C, Livingston EW, Howe D, Schaible EG, Hunt HB, Rauff A, Donnelly E, Carpenter RD, Levi M, Lau AG, Bateman TA, Alliston T, King KB, Ferguson VL, 2019. Chronic kidney disease and aging differentially diminish bone material and microarchitecture in C57Bl/6 mice. Bone. 127: 91–103. https://doi.org/10.1016/j.bone.2019.04.019
- Girton TS, Oegema TR, Tranquillo RT. 1999. Exploiting glycation to stiffen and strengthen tissue equivalents for tissue engineering. Journal of Biomedical Materials Research. 46(1):87–92. doi:https://doi.org/10.1002/(SICI)1097-4636(199907)
- Francis-Sedlak ME, Uriel S, Larson JC, Greisler HP, Venerus DC, Brey EM. 2009. Characterization of type I collagen gels modified by glycation. Biomaterials. 30(9):1851–1856. doi:https://doi.org/10.1016/j.biomaterials.2008.12.014.
- Monnier VM, Kohn RR, Cerami A. 1984. Accelerated age-related browning of human collagen in diabetes mellitus. Proceedings of the National Academy of Sciences. 81(2): 583LP – 587. doi:https://doi.org/10.1073/pnas.81.2.583.
- Trębacz H, Szczęsna A, Arczewska M. 2018. Thermal stability of collagen in naturally ageing and in vitro glycated rabbit tissues. Journal of Thermal Analysis and Calorimetry. 134(3):1903–1911. doi:https://doi.org/10.1007/s10973-018-7375-8
- Fessel G, Li Y, Diederich V, Guizar-Sicairos M, Schneider P, Sell DR, Monnier VM, Snedeker JG. 2014. Advanced glycation end-products reduce collagen molecular sliding to affect collagen fibril damage mechanisms but not stiffness. PloS One. 9(11):e110948–e110948. doi:https://doi.org/10.1371/journal.pone.0110948.
- Tang SY, Zeenath U, Vashishth D. 2007. Effects of non-enzymatic glycation on cancellous bone fragility. Bone. 40(4):1144–1151. doi:https://doi.org/10.1016/j.bone.2006.12.056.
- Sell DR, Monnier VM. 1989. Structure elucidation of a senescence cross-link from human extracellular matrix: implication of pentoses in the aging process *. Journal of Biological Chemistry. 264(36):21597–21602. doi:https://doi.org/10.1016/S0021-9258(20)88225-8
- Guex AG, Puetzer JL, Armgarth A, Littmann E, Stavrinidou E, Giannelis EP, Malliaras GG, Stevens MM, 2017. Highly porous scaffolds of PEDOT:PSS for bone tissue engineering. Acta Biomaterialia. 62: 91–101. https://doi.org/10.1016/j.actbio.2017.08.045
- Antoine EE, Vlachos PP, Rylander MN. 2014. Review of collagen I hydrogels for bioengineered tissue microenvironments: characterization of mechanics, structure, and transport. Tissue Engineering Part B: Reviews. 20(6):683–696. doi:https://doi.org/10.1089/ten.teb.2014.0086
- Bailey JL, Critser PJ, Whittington C, Kuske JL, Yoder MC, Voytik-Harbin SL. 2011. Collagen oligomers modulate physical and biological properties of three-dimensional self-assembled matrices. Biopolymers. 95(2):77–93. doi:https://doi.org/10.1002/bip.21537
- Ramtani S, Takahashi-Iñiguez Y, Helary O, Geiger C, Didier Guille MMG. 2010. Mechanical behavior under unconfined compressoin loadings of dense fibrillar collagen matrices mimetic of living tissues. Journal of Mechanics in Medicine and Biology. 10(1):35–55. doi:https://doi.org/10.1142/S0219519410003290
- Monnier VM, Sell DR, Nagaraj RH, Miyata S, Grandhee S, Odetti P, Ibrahim SA. 1992. Maillard reaction-mediated molecular damage to extracellular matrix and other tissue proteins in diabetes, aging, and uremia. Diabetes. 41(Supplement2): 36LP – 41. doi:https://doi.org/10.2337/diab.41.2.S36.
- He W, Goodkind D, Kowal P.2016. An aging world: 2015. Washington D.C: U.S Government Publishing Office. doi:https://doi.org/10.13140/RG.2.1.1088.9362.
- Grote C, Reinhardt D, Zhang M, Wang J. 2019. Regulatory mechanisms and clinical manifestations of musculoskeletal aging. Journal of Orthopaedic Research. 37(7):1475–1488. doi:https://doi.org/10.1002/jor.24292
- Li Y, Fessel G, Georgiadis M, Snedeker JG. 2013. Advanced glycation end-products diminish tendon collagen fiber sliding. Matrix Biology. 32(3–4):169–177. accessed 2019 Jun 24. doi:https://doi.org/10.1016/J.MATBIO.2013.01.003
- Lee JM, Veres SP. 2019. Advanced glycation end-product cross-linking inhibits biomechanical plasticity and characteristic failure morphology of native tendon. Journal of Applied Physiology (Bethesda, Md. : 1985). 126(4):832–841. doi:https://doi.org/10.1152/japplphysiol.00430.2018.
- Goh S-Y, Cooper ME. 2008. The role of advanced glycation end products in progression and complications of diabetes. The Journal of Clinical Endocrinology & Metabolism. 93(4):1143–1152. doi:https://doi.org/10.1210/jc.2007-1817
- Ahmed N. 2005. Advanced glycation endproducts—role in pathology of diabetic complications. Diabetes Research and Clinical Practice. 67(1):3–21. doi:https://doi.org/10.1016/j.diabres.2004.09.004.
- Morales Santana S, García-Salcedo J, Muñoz-Torres M. 2010. Pentosidine: a new biomarker in diabetes mellitus complications. Medicina clínica. 136(7):298–302. doi:https://doi.org/10.1016/j.medcli.2009.12.001
- Koyama Y, Takeishi Y, Arimoto T, Niizeki T, Shishido T, Takahashi H, Nozaki N, Hirono O, Tsunoda Y, Nitobe J, Watanabe T, Kubota I. 2007. High serum level of pentosidine, an advanced glycation end product (AGE), is a risk factor of patients with heart failure. Journal of Cardiac Failure. 13(3):199–206. doi:https://doi.org/10.1016/j.cardfail.2006.11.009.
- Kadler KE, Holmes DF, Trotter JA, Chapman JA. 1996. Collagen fibril formation. The Biochemical Journal. 316(Pt 1 (Pt1):1–11. doi:https://doi.org/10.1042/bj3160001.
- Sarrigiannidis SO, Rey JM, Dobre O, González-García C, Dalby MJ, Salmeron-Sanchez M, 2021. A tough act to follow: collagen hydrogel modifications to improve mechanical and growth factor loading capabilities. Materials Today Bio. 10: 100098. https://doi.org/10.1016/j.mtbio.2021.100098
- Wollensak G, Wilsch M, Spoerl E, Seiler T. 2004. Collagen fiber diameter in the rabbit cornea after collagen crosslinking by riboflavin/UVA. Cornea. 23(5):503–507. https://journals.lww.com/corneajrnl/Fulltext/2004/07000/Collagen_Fiber_Diameter_in_the_Rabbit_Cornea_After.14.aspx.
- Bai P, Phua K, Hardt T, Cernadas M, Brodsky B. 1992. Glycation alters collagen fibril organization. Connective Tissue Research. 28(1–2):1–12. doi:https://doi.org/10.3109/03008209209014224
- Panwar P, Lamour G, Mackenzie NCW, Yang H, Ko F, Li H, Brömme D. 2015. Changes in structural-mechanical properties and degradability of collagen during aging-associated modifications. The Journal of Biological Chemistry. 290(38):23291–23306. doi:https://doi.org/10.1074/jbc.M115.644310.
- Daxer A, Misof K, Grabner B, Ettl A, Fratzl P, 1998. Collagen fibrils in the human corneal stroma: structure and aging. Investigative Ophthalmology & Visual Science. 39(3):644–648.
- Ahearne M, Yang Y, Then KY, Liu -K-K. 2008. Non-destructive mechanical characterisation of UVA/riboflavin crosslinked collagen hydrogels. British Journal of Ophthalmology. 92(2): 268LP – 271. doi:https://doi.org/10.1136/bjo.2007.130104.
- Chandran PL, Barocas VH. 2004. Microstructural mechanics of collagen gels in confined compression: poroelasticity, viscoelasticity, and collapse. Journal of Biomechanical Engineering. 126(2):152–166. doi:https://doi.org/10.1115/1.1688774
- Van PL, De SS, Moortgat P. 2016. The effects of advanced glycation end products (AGEs) on dermal wound healing and scar formation: a systematic review. Scars, Burns & Healing. 2:2059513116676828. https://doi.org/10.1177/2059513116676828.
- Flurkey K, Currer J M, Harrison DE.2007. Chapter 20 - mouse models in aging research. In: Fox JG, Davisson MT, editors. Quimby FW, barthold sw, newcomer CE, smith ALBT-TM in BR (Second E, editors. American college of laboratory animal medicine. Burlington:Academic Press. 637–672. http://www.sciencedirect.com/science/article/pii/B9780123694546500741. doi:https://doi.org/10.1016/B978-012369454-6/50074-1
- McKay TB, Priyadarsini S, Karamichos D. 2019. Mechanisms of collagen crosslinking in diabetes and keratoconus. Cells. 8(10):1239. doi:https://doi.org/10.3390/cells8101239.
- Hudson DM, Archer M, King KB, Eyre DR. 2018. Glycation of type I collagen selectively targets the same helical domain lysine sites as lysyl oxidase–mediated cross-linking. Journal of Biological Chemistry. 293(40):15620–15627. doi:https://doi.org/10.1074/jbc.RA118.004829
- Grandhee SK, Monnier VM. 1991. Mechanism of formation of the maillard protein cross-link pentosidine. glucose, fructose, and ascorbate as pentosidine precursors. Journal of Biological Chemistry. 266(18):11649–11653. doi:https://doi.org/10.1016/S0021-9258(18)99006-X
- McCall AS, Kraft S, Edelhauser HF, Kidder GW, Lundquist RR, Bradshaw HE, Dedeic Z, Dionne MJC, Clement EM, Conrad GW. 2010. Mechanisms of corneal tissue cross-linking in response to treatment with topical riboflavin and long-wavelength ultraviolet radiation (UVA). Investigative Ophthalmology & Visual Science. 51(1):129–138. doi:https://doi.org/10.1167/iovs.09-3738.
- Dyer DG, Blackledge JA, Thorpe SR, Baynes JW. 1991. Formation of pentosidine during nonenzymatic browning of proteins by glucose. Identification of glucose and other carbohydrates as possible precursors of pentosidine in vivo. Journal of Biological Chemistry. 266(18):11654–11660. doi:https://doi.org/10.1016/s0021-9258(18)99007-1.
- Liang J-Y, Yuann J-MP, Hsie Z-J, Huang S-T, Chen -C-C, 2017. Blue light induced free radicals from riboflavin in degradation of crystal violet by microbial viability evaluation. Journal of Photochemistry and Photobiology B: Biology. 174: 355–363. https://doi.org/10.1016/j.jphotobiol.2017.08.018
- Youn H-Y, Chou BR, Cullen AP, Sivak JG. 2009. Effects of 400nm, 420nm, and 435.8nm radiations on cultured human retinal pigment epithelial cells. Journal of Photochemistry and Photobiology B: Biology. 95(1):64–70. doi:https://doi.org/10.1016/j.jphotobiol.2009.01.001.