Диссертация (Молекулярные и клеточные механизмы ультрафиолетового сшивания роговицы), страница 43
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Файл "Диссертация" внутри архива находится в папке "Молекулярные и клеточные механизмы ультрафиолетового сшивания роговицы". PDF-файл из архива "Молекулярные и клеточные механизмы ультрафиолетового сшивания роговицы", который расположен в категории "". Всё это находится в предмете "биология" из Аспирантура и докторантура, которые можно найти в файловом архиве РНИМУ им. Пирогова. Не смотря на прямую связь этого архива с РНИМУ им. Пирогова, его также можно найти и в других разделах. , а ещё этот архив представляет собой докторскую диссертацию, поэтому ещё представлен в разделе всех диссертаций на соискание учёной степени доктора биологических наук.
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Paladini, R. Mencucci // Mol. Vis. –2013. – Vol. 19, № 19. – P. 1526-1537.279. Keratoconus: matrix metalloproteinase-2 activation and TIMP modulation / V.A.Smith, F.J. Matthews, M.A. Majid, S.D. Cook // Biochim. Biophys. Acta. –2006.
–Vol. 1762, № 4. – P. 431-439.280. Keratocyte apoptosis after corneal collagen cross-linking using riboflavin/UVAtreatment / G. Wollensak, E. Spoerl, M. Wilsch, T. Seiler // Cornea. – 2004а. – Vol.23, № 1. – P. 43-49.263281. Keratocyte Apoptosis after Corneal Surgery / M.C.
Helena, F. Baerveldt, W.J. Kim,S.E. Wilson // Invest. Ophthalmol. Vis. Sci. – 1998. – Vol. 39, № 2. – P. 276-283.282. Keratocyte apoptosis associated with keratoconus / W.J. Kim, Y.S. Rabinowitz, D.M.Meisler, S.E. Wilson // Exp. Eye Res. – 1999. – Vol. 69, № 5. – P. 475-481.283. Keratocyte cytotoxicity of riboflavin/UVA-treatment in vitro / G.
Wollensak, E.Spoerl, F. Reber, T. Seiler // Eye. – 2004в. – Vol. 18, № 7. – P. 718-722.284. Kernacki, K.A. Evidence for TIMP-1 protection against P. aeruginosa-induced cornealulceration and perforation / K.A. Kernacki, R. Barrett, L.D. Hazlett // Invest.Ophthalmol. Vis. Sci.
– 1999. – Vol. 40, № 13. – P. 3168-3176.285. Klyce, S.D. Numerical solution of coupled transport equations applied to cornealhydration dynamics / S.D. Klyce, S.R. Russell // J. Physiol. – 1979. – Vol. 292. – P.107-118.286. Knox Cartwright, N.E. Age-related differences in the elasticity of the human cornea /N.E. Knox Cartwright, J.R. Tyrer, J. Marshall // Invest. Ophthalmol. Vis. Sci. – 2011.– Vol. 52, № 7. – P. 4324-4329.287. Knox Cartwright, N.E. In vitro quantification of the stiffening effect of corneal crosslinking in the human cornea using radial shearing speckle pattern interferometry / N.E.Knox Cartwright, J.R. Tyrer, J. Marshall // J.
Refract. Surg. – 2012. – Vol. 28, № 7. –P. 503-508.288. Kohlhaas, M. Collagen crosslinking with riboflavin and UVA-light in keratoconus /M. Kohlhaas // Ophthalmologe. – 2008. – Bd. 105, № 8. – S. 785-793.289. Kohlhaas, M. Complications and postoperative therapeutic strategies in cross-linking /M. Kohlhaas // Ophthalmologe. – 2017. – doi: 10.1007/s00347-017-0511-1.290. Koller, T. Therapeutic cross-linking of the cornea using riboflavin/UVA / T. Koller, T.Seiler // Klin. Monbl.
Augenheilkd. – 2007. – Bd. 224, № 9. – S. 700-706.291. Kolli, S. Safety and efficacy of collagen crosslinking for the treatment of keratoconus/ S. Kolli, I.M. Aslanides // Exp. Opin. Drug Saf. – 2010. – Vol. 9, № 6. – P. 949-957.264292. Komai, Y. The three-dimensional organisation of collagen fibrils in the humancornea and sclera / Y. Komai, T. Ushiki // Invest. Ophthalmol. Vis.
Sci. – 1991. –Vol. 32, № 8. – P. 2244-2258.293. Kurpakus Wheater, M. Corneal cell proteins and ocular surface pathology / M.Kurpakus Wheater, K.A. Kernacki, L.D. Hazlett // Biotech. Histochem. – 1999. – Vol.74, № 3. – P. 146-159.294. Kurpakus-Wheater, M. Maintaining corneal integrity how the "window" stays clear /M. Kurpakus-Wheater, K.A. Kernacki, L.D. Hazlett // Prog. Histochem. Cytochem.
–2001. – Vol. 36, № 3. – P. 185-259.295. Lane, D.P. Cancer. p53, guardian of the genome / D.P. Lane // Nature. – 1992. – Vol.358, № 6381. – P. 15-16.296. Laser scanning in vivo confocal microscopy reveals reduced innervation and reductionin cell density in all layers of the keratoconic cornea / R.L. Niederer, D. Perumal, T.Sherwin, C.N.
McGhee // Invest. Ophthalmol. Vis. Sci. – 2008. – Vol. 49, № 7. – P.2964-2970.297. Leccisotti, A. Transepithelial corneal collagen cross-linking in keratoconus / A.Leccisotti, T. Islam // J. Refract. Surg. – 2010. – Vol. 26, № 12. – P. 942-948.298. Lema, I. Inflammatory molecules in the tears of patients with keratoconus / I.
Lema,J.A. Durаn // Ophthalmology. – 2005. – Vol. 112, № 4. – P. 654-659.299. Levels of collagen degradation products (telopeptides) in the tear film of patients withkeratoconus / J.H. Abalain, H. Dossou, J. Colin, H.H. Floch // Cornea. – 2000. – Vol.19, № 4. – P. 474-476.300. Li, D.Q. Differential expression and regulation of TGF-beta1, TGF-beta2, TGF-beta3,TGF-betaRI, TGF-betaRII and TGF-betaRIII in cultured human corneal, limbal, andconjunctival fibroblasts / D.Q. Li, S.B. Lee, S.C.
Tseng // Curr. Eye Res. – 1999. –Vol. 19, № 2. – P. 154-161.301. Li, D.Q. Matrix metalloproteinases in corneal inflammation / D.Q. Li, S.C. Pflugfelder// Ocul. Surf. – 2005. – Vol. 3, № 4. – P. 198-202.265302. Lin, J. Efficacy S-formula and kinetics of non-oxygen-mediated (Type-I) and oxygenmediated (Type-II) corneal cross-linking / J. Lin // Ophthalmol. Res. – 2018. – Vol. 8,№ 1.
– P. 1-11.303. Lobacheva, G.V. State of the organ of vision and behavior of rats after action on theeye of increased doses of UV-irradiation / G.V. Lobacheva, G.V. Galaktionova //Kosm. Biol. Aviakosm. Med. – 1990. – Vol. 24, № 5. – P. 48-51.304. Localization of TIMP-1, TIMP-2, TIMP-3, gelatinase A and gelatinase B inpathological human corneas / M.C. Kenney, M. Chwa, A. Alba [et al.] // Curr. EyeRes.
– 1998. – Vol. 17, № 3. – P. 238-246.305. Long-term changes in backscattered light measurements in keratoconus corneastreated with collagen cross-linking / G. Nemeth, J. Hassan, L. Modis, Z. Hassan //Curr. Eye Res. – 2018. – Vol. 43, № 1. – P. 18-26.306. Low levels of hydrogen peroxide stimulate corneal epithelial cell adhesion, migration,and wound healing / Q. Pan, W.Y. Qiu, Y.N. Huo [et al.] // Invest. Ophthalmol. Vis.Sci.
– 2011. – Vol. 52, № 3. – P. 1723-1734.307. Luce, D.A. Determining in vivo biomechanical properties of the cornea with an ocularresponse analyzer / D.A. Luce // J. Cataract Refract. Surg. – 2005. – Vol. 31, № 1. – P.156-162.308. Magnusson, B. The identification of contact allergens by animal assay. The guinea pigmaximization test / B. Magnusson, A.M. Kligman // J. Invest. Dermatol. – 1969.
–Vol. 52, № 3. – P. 268-276.309. Makdoumi, K. Infectious Keratitis Treated With Corneal Crosslinking / K. Makdoumi,J. Mortensen, S. Crafoord // Cornea. – 2010. – Vol. 29, № 12. – P. 1353-1358.310. Marshall, G.E. Immunogold fine structural localization of extracellular matrixcomponents in aged human cornea. II. Collagen types V and VI / G.E. Marshall, A.G.Konstas, W.R. Lee // Graefes Arch. Clin. Exp. Ophthalmol.
– 1991. – Bd. 229, № 2. –S. 164-171.266311. Marshall, G.E. Immunogold localization of type IV collagen and laminin in the aginghuman outflow system / G.E. Marshall, A.G. Konstas, W.R. Lee // Exp. Eye Res. –1990. – Vol. 51, № 6. – P. 691-699.312. Mastropasqua, L. Collagen cross-linking: when and how? A review of the state of theart of the technique and new perspectives / L. Mastropasqua // Eye Vis. (Lond). –2015. – № 2. – P. 19.313. Matrix metalloproteinase-2 and myocardial oxidative stress injury: beyond the matrix /A.D. Kandasamy, A.K.
Chow, M.A. Ali, R. Schulz // Cardiovasc. Res. – 2010. – Vol.85, № 3. – P. 413-423.314. Maurice, D.M. Cohesive strength of corneal lamellae / D.M. Maurice, F. Monroe //Exp. Eye Res. – 1990. – Vol. 50, № 1. – P. 59-63.315. McQuaid, R. The theory and art of corneal cross-linking / R. McQuaid, A.B.Cummings, M. Mrochen // Indian J. Ophthalmol. – 2013. – Vol. 61, № 8. – P. 416419.316. Mechanisms of corneal tissue CXL in response to treatment with topical riboflavinand long-wavelength ultraviolet radiation (UVA) / A.S. McCall, S. Kraft, H.F.Edelhauser [et al.] // Invest.
Ophthalmol. Vis. Sci. – 2010. – Vol. 51, № 1. – P. 129138.317. Microbial keratitis after accelerated corneal collagen cross-linking in keratoconus /P.K. Maharana, P. Sahay, M. Sujeeth [et al.] // Cornea. – 2018. – Vol. 37, № 2. – P.162-167.318. Microbial keratitis after corneal collagen crosslinking / J.J. Perez-Santonja, A. Artola,J.
Javaloy [et al.] // J. Cataract Refract. Surg. – 2009. – Vol. 35. – P. 1138-1140.319. Millin, J.A. Human basement membrane components of keratoconus and normalcorneas / J.A. Millin, B.M. Golub, C.S. Foster // Invest. Ophthalmol. Vis. Sci. – 1986.– Vol. 27, № 4. – P. 604-607.267320. Mita, M. High-irradiance accelerated collagen crosslinking for the treatment ofkeratoconus: six-month results / M. Mita, G.O. Waring, M. Tomita // J. CataractRefract. Surg. – 2014. – Vol. 40, № 6.
– P. 1032-1040.321. Modulation of autoimmune diseases by nitric oxide / V.K. Singh, S. Mehrotra, P.Narayan [et al.] // Immunol. Res. – 2000. – Vol. 22, № 1. – P. 1-19.322. Molecular definitions of cell death subroutines: recommendations of theNomenclature Committee on Cell Death 2012 / L. Galluzzi, I. Vitale, J.M. Abrams [etal.] // Cell Death Differ. – 2012.
– Vol. 19, № 1. – P. 107-120.323. Molecular mechanisms of necroptosis: an ordered cellular explosion / P.Vandenabeele, L. Galluzzi, T. Vanden Berghe, G. Kroemer // Nat. Rev. Mol. CellBiol. – 2010. – Vol. 11, № 10. – P. 700-714.324. Moller-Pedersen, T. Keratocyte reflectivity and corneal haze / T. Moller-Pedersen //Exp.
Eye Res. – 2004. – Vol. 78, № 3. – P. 553-560.325. Monboisse, J.C. Oxidative damage to collagen / J.C. Monboisse, J.P. Borel // EXS. –1992. – Vol. 62. – P. 323-327.326. Morphological and functional correlations in riboflavin UV A corneal collagen crosslinking for keratoconus / C. Mazzotta, T. Caporossi, R. Denaro [et al.] // ActaOphthalmol. – 2012. – Vol. 90, № 3. – P. 259-265.327. Morphological and immunohistochemical changes after corneal cross-linking / E.M.Messmer, P. Meyer, M.C. Herwig [et al.] // Cornea.
