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1Academic Journal
Authors: I. D. Arsyutov, N. M. Kislitsyna, S. V. Novikov, И. Д. Арсютов, Н. М. Кислицына, С. В. Новиков
Source: Ophthalmology in Russia; Том 21, № 2 (2024); 270-275 ; Офтальмология; Том 21, № 2 (2024); 270-275 ; 2500-0845 ; 1816-5095 ; 10.18008/1816-5095-2024-2
Subject Terms: ангиогенез, proteoglycans, vitreomacular pathology, retinal pathology, inflammation, angiogenesis, протеогликаны, витреомакулярные патологии, ретинальные патологии, воспаление
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Relation: https://www.ophthalmojournal.com/opht/article/view/2356/1212; Larsen CS, Johansen M, Harboe E. Sustained‑release prodrugs comprising inflammation inhibitors linked to polysaccharides Eur. Pat. Appl. EP 331471 A1 19890906.; Kubota T, Okabe H, Hisatomi T, Yamakiri K, Sakamoto T, Tawara A. Ultrastructure of the trabecular meshwork in secondary glaucoma eyes after intravitreal triamcinolone acetonide. J Glaucoma. 2006 Apr;15(2):117–119. doi:10.1097/00061198200604000‑00007.; Тульцева C.Н., Астахов Ю.С. Окклюзии вен сетчатки. СПб.: Изд «Н‑Л», 2017. 101 c.; Zarifa R, Shaikh S, Kester E. Peristence of triamcinolone crystals after intravitreal injection: benign crystalline hyaloidopathy. Indian J Ophthalmol. 2013 Apr;61(4):18–23. doi:10.4103/0301‑4738.112166.; Morla S. Glycosaminoglycans and Glycosaminoglycan Mimetics in Cancer and Inflammation. Int J Mol Sci. 2019 Apr 22;20(8):1963. doi:10.3390/ijms20081963.; Bass MD, Humphries MJ. Cytoplasmic interactions of syndecan‑4 orchestrate adhesion receptor and growth factor receptor signalling. Biochem J. 2002 Nov 15;368(Pt 1):1–15. doi:10.1042/BJ20021228.; Moore KL, Patel KD, Bruehl RE, Li F, Johnson DA, Lichenstein HS, Cummings RD, Bainton DF, McEver RP. P‑selectin glycoprotein ligand‑1 mediates rolling of human neutrophils on P‑selectin. J Cell Biol. 1995 Feb;128(4):661–671. doi:10.1083/jcb.128.4.661.; Webb LM, Ehrengruber MU, Clark‑Lewis I, Baggiolini M, Rot A. Binding to heparan sulfate or heparin enhances neutrophil responses to interleukin 8. Proc. Natl. Acad. Sci. USA. 1993;90:7158–7162. doi:10.1073/pnas.90.15.7158.; Götte M. Syndecans in inflammation. FASEB J. 2003 Apr;17(6):575–591. doi:10.1096/fj.02‑0739rev.; Oschatz C, Maas C, Lecher B, Jansen T, Björkqvist J, Tradler T, Sedlmeier R, Burfeind P, Cichon S, Hammerschmidt S, Müller‑Esterl W, Wuillemin WA, Nilsson G, Renné T. Mast cells increase vascular permeability by heparin‑initiated bradykinin formation in vivo. Immunity. 2011 Feb 25;34(2):258–268. doi:10.1016/j.immuni.2011.02.008.; Pretorius D, Richter RP, Anand N, Cardenas JC, Richter JR. Alterations in heparan sulfate proteoglycan synthesis and sulfation and the impact on vascular endothelial function. Published online 2022 Sep 7. doi:10.1016/j.mbplus.2022.100121.; Alexopoulou AN, Multhaupt HA, Couchman JR. Syndecans in wound healing, inflammation and vascular biology. Int J Biochem Cell Biol. 2007;39(3):505–528. doi:10.1016/j.biocel.2006.10.014.; Sezgin E, Levental I, Mayor S, Eggeling C. The mystery of membrane organization: composition, regulation and roles of lipid rafts. Nat Rev Mol Cell Biol. 2017 Jun;18(6):361–374. doi:10.1038/nrm.2017.16.; Schmidt EP, Yang Y, Janssen WJ, Gandjeva A, Perez MJ, Barthel L, Zemans RL, Bowman JC, Koyanagi DE, Yunt ZX, Smith LP, Cheng SS, Overdier KH, Thompson KR, Geraci MW, Douglas IS, Pearse DB, Tuder RM. The pulmonary endothelial glycocalyx regulates neutrophil adhesion and lung injury during experimental sepsis. Nat Med. 2012 Aug;18(8):1217–1223. doi:10.1038/nm.2843.; Гветадзе А.А., Королева И.А. Возрастная макулярная дегенерация. Современный взгляд на проблему (обзор литературы). Клиническая офтальмология. 2015;16(1):125–128.; Gallagher JT. Multiprotein signalling complexes: regional assembly on heparan sulphate. Biochem Soc Trans. 2006 Jun;34(Pt 3):438–441. doi:10.1042/BST0340438.; Buczek‑Thomas JA, Rich CB, Nugent MA. Hypoxia Induced Heparan Sulfate Primes the Extracellular Matrix for Endothelial Cell Recruitment by Facilitating VEGF‑Fibronectin Interactions. Int J Mol Sci. 2019 Oct 12;20(20):5065. doi:10.3390/ijms20205065.; Tkachenko E, Rhodes JM, Simons M. Syndecans: new kids on the signaling block. Circ. Res. 2005;96(5):488–500. doi:10.1161/01.RES.0000159708.71142.c8.; Шацких А.В., Тахчиди Х.П., Тахчиди Е.Х., Горбунова К.С. Перспективность использования естественных регуляторов для профилактики избыточного рубцевания при антиглаукомных операциях. Практическая медицина. 2012;1(40):150–153.; Анисимов С.И. Основные механизмы протекции тканей глаза с применением сульфатированных гликозаминогликанов. Экспериментальные исследования. Глаукома. 2007;2:23–27.; Копаенко А.И., Расин О.Г., Расина О.О. Эффективность применения баларпана у пациентов после трансэпителиальной фоторефракционной кератэктомии, Таврический медико‑биологический вестник, 2016;19(1):123–124.; Канюков В.Н., Стадников А.А., Трубина О.М., Рахматуллин Р.Р., Яхина О.М. Гистоэквивалент биопластического материала в офтальмологии. Оренбург, 2014. 191 с.; Серов В.В., Шехтер А.Б. Соединительная ткань. М., 1981. 321 с. Serov VV, Shehter AB. Connective tissue. Moscow, 1981. 321 p. (In Russ.).; Терещенко А.В., Белый Ю.А., Тахчиди Е.Х., Новиков С.В., Майчук Н.В., Усанова Г.Ю. Экспериментальное обоснование применения раствора сульфатированных гликозаминогликанов (сГАГ) в лечении токсической эрозии роговицы у кроликов. Практическая медицина. 2016;1(2):108–112.; Regatieri CV, Dreyfuss JL, Melo GB, Lavinsky D, Hossaka SK, Rodrigues EB, Farah ME, Maia M, Nader HB. Quantitative evaluation of experimental choroidal neovascularization by confocal scanning laser ophthalmoscopy: fluorescein angiogram parallels heparan sulfate proteoglycan expression. Braz J Med Biol Res. 2010 Jul;43(7):627–633. doi:10.1590/s0100‑879x2010007500043.; Новиков С.В., Кислицына Н.М., Веселкова М.П. Композиция для ингибирования и комплексного лечения интраоперационного макулярного отека. Патент RU 2587779. 20.06.2016.; Веселкова М.П., Новиков С.В., Кислицына Н.М., Петерсен Е.В., Трусова И.А., Дух А.С. Экспериментальное исследование влияния сульфатированных гликозаминогликанов на культуру клеток пигментного эпителия сетчатки человека при воздействии ультразвука (предварительные результаты). Современные технологии в офтальмологии 2015;3; Тахчиди Е.Х., Горбунова К.С. Применение сульфатированных гликозаминогликанов в офтальмологии. Вестник Оренбургского государственного университета. 2012;12(148):201–204.; https://www.ophthalmojournal.com/opht/article/view/2356
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2Academic Journal
Source: Odesa National University Herald. Biology; Vol. 15 No. 17 (2010); 42-48
Вестник Одесского национального университета. Биология; Том 15 № 17 (2010); 42-48
Вісник Одеського національного університету. Біологія; Том 15 № 17 (2010); 42-48Subject Terms: соединительная ткань, синтез, glycosaminoglycans, протеоглікани, сполучна тканина, протеогликаны, proteoglycans, synthesis core proteins', глікозаміноглікани, гликозаминогликаны, коровые белки, корові білки, connective tissue
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Access URL: http://visbio.onu.edu.ua/article/view/258422
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3Academic Journal
Authors: Пономаренко, О. М.
Source: Odesa National University Herald. Biology; Vol. 15 No. 17 (2010); 42-48 ; Вестник Одесского национального университета. Биология; Том 15 № 17 (2010); 42-48 ; Вісник Одеського національного університету. Біологія; Том 15 № 17 (2010); 42-48 ; 2415-3125 ; 2077-1746
Subject Terms: соединительная ткань, протеогликаны, гликозаминогликаны, синтез, коровые белки, сполучна тканина, протеоглікани, глікозаміноглікани, корові білки, connective tissue, proteoglycans, glycosaminoglycans, synthesis core proteins’
File Description: application/pdf
Relation: http://visbio.onu.edu.ua/article/view/258422/255206; http://visbio.onu.edu.ua/article/view/258422
Availability: http://visbio.onu.edu.ua/article/view/258422
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4Academic Journal
Authors: D. A. Semenov, I. I. Vashkevich, A. S. Vladyko, O. V. Sviridov, Д. А. Семенов, И. И. Вашкевич, А. С. Владыко, О. В. Свиридов
Source: Doklady of the National Academy of Sciences of Belarus; Том 66, № 4 (2022); 404-413 ; Доклады Национальной академии наук Беларуси; Том 66, № 4 (2022); 404-413 ; 2524-2431 ; 1561-8323 ; 10.29235/1561-8323-2022-66-4
Subject Terms: гепарансульфат протеогликаны, SARS-CoV-2 virus, heparin, heparan sulfate proteoglycans, вирус SARS-CoV-2, гепарин
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Relation: https://doklady.belnauka.by/jour/article/view/1079/1079; Борзенкова, Н. В. Лактоферрин: физико-химические свойства, биологические функции, системы доставки, лекарственные препараты и биологически активные добавки (обзор) / Н. В. Борзенкова, Н. Г. Балабушевич, Н. И. Ларионова // Биофармацевтический журнал. – 2010. – Т. 2, № 3. – С. 3–19.; Mann, D. M. Delineation of the glycosaminoglycan-binding site in the human inflammatory response protein lactoferrin / D. M. Mann, E. Romm, M. Migliorini // J. Biol. Chem. – 1994. – Vol. 269, N 38. – P. 23661–23667. https://doi.org/10.1016/s0021-9258(17)31566-1; Goats producing biosimilar human lactoferrin / D. M. Bogdanovich [et al.] // IOP Conf. Series: Earth and Environmental Science. – 2021. – Vol. 848, N 1. – Art. 012080. https://doi.org/10.1088/1755-1315/848/1/012080; Получение рекомбинантного лактоферрина человека из молока коз-продуцентов и его физиологические эффекты / В. С. Лукашевич [и др.] // Докл. Нац. акад. наук Беларуси. – 2016. – Т. 60, № 1. – С. 72–81.; Антимикробные и антиоксидантные свойства апо-формы рекомбинантного человеческого лактоферрина, выделенного из молока коз-продуцентов / Р. Н. Бирюков [и др.] // Микробные биотехнологии: фундаментальные и прикладные аспекты. – 2017. – Т. 9. – С. 305–317.; Некоторые металлсвязывающие свойства рекомбинантного лактоферрина человека из молока трансгенных коз / Д. А. Семенов [и др.] // Докл. Нац. акад. наук Беларуси. – 2022. – Т. 66, № 1. – С. 43–54. https://doi.org/10.29235/15618323-2022-66-1-43-54; Семенов, Д. А. Новые иммуноаналитические системы на основе рекомбинантного лактоферрина человека / Д. А. Семенов, И. И. Вашкевич, О. В. Свиридов // Докл. Нац. акад. наук Беларуси. – 2021. – Т. 65, № 3. – С. 290–302. https://doi.org/10.29235/1561-8323-2021-65-3-290-302; N-terminal stretch Arg2, Arg3, Arg4 and Arg5 of human lactoferrin is essential for binding to heparin, bacterial lipopolysaccharide, human lysozyme and DNA / P. H. C. van Berkel [et al.] // Biochem. J. – 1997. – Vol. 328, N 1. – P. 145–151. https://doi.org/10.1042/bj3280145; Hermanson, G. T. Bioconjugate techniques / G. T. Hermanson. – 3rd ed. – Academic Press, 2013. – P. 217–218. https://doi.org/10.1016/C2009-0-64240-9; Direct detection of the binding of avidin and lactoferrin fluorescent probes to heparinized surfaces / W. C. Kett [et al.] // Analytical Biochemistry. – 2005. – Vol. 339, N 2. – P. 206–215. https://doi.org/10.1016/j.ab.2005.01.054; Pejler, G. Lactoferrin regulates the activity of heparin proteoglycan-bound mast cell chymase: characterization of the binding of heparin to lactoferrin / G. Pejler // Biochem. J. – 1996. – Vol. 320, N 3. – P. 897–903. https://doi.org/10.1042/bj3200897; Avidin is a heparin-binding protein. Affinity, specificity and structural analysis / W. C. Kett [et al.] // Biochimica et Biophysica Acta. – 2003. – Vol. 1620, N 1–3. – P. 225–234. https://doi.org/10.1016/s0304-4165(02)00539-1; Morphological cell profiling of SARS-CoV-2 infection identifies drug repurposing candidates for COVID-19 / C. Mirabelli [et al.] // PNAS. – 2021. – Vol. 118, N 36. – Art. e2105815118. https://doi.org/10.1073/pnas.2105815118; Inhibition of SARS pseudovirus cell entry by lactoferrin binding to heparan sulfate proteoglycans / J. Lang [et al.] // PLoS ONE. – 2011. – Vol. 6, N 8. – Art. e23710. https://doi.org/10.1371/journal.pone.0023710; https://doklady.belnauka.by/jour/article/view/1079
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5Academic Journal
Authors: Elvira V. Grigorieva, Valentina A. Belyavskaya, Natalya V. Domanitskaya, Nadezhda V. Cherdyntseva, Tatiana Y. Prudnikova, N.V. Litviakov, Vladimir N. Maksimov
Source: Gene. 2017. Vol. 628. P. 224-229
Subject Terms: Adult, Genotype, Сибирь, Gene Expression, Loss of Heterozygosity, Breast Neoplasms, Polymorphism, Single Nucleotide, 03 medical and health sciences, 0302 clinical medicine, Asian People, Meta-Analysis as Topic, Biomarkers, Tumor, Humans, Genetic Predisposition to Disease, Codon, рак молочной железы, Alleles, Aged, Neoplasm Staging, гепарансульфат-протеогликаны, единичные нуклеотидные полиморфизмы, Middle Aged, женщины, 3. Good health, предрасположенность к раку молочной железы, D-глюкуронил С5-эпимераза, Amino Acid Substitution, Case-Control Studies, Female, канцерогенез, Carbohydrate Epimerases, тройной негативный рак молочной железы
Linked Full TextAccess URL: https://pubmed.ncbi.nlm.nih.gov/28734894
https://europepmc.org/abstract/MED/28734894
https://www.sciencedirect.com/science/article/pii/S0378111917305784
https://www.ncbi.nlm.nih.gov/pubmed/28734894
http://vital.lib.tsu.ru/vital/access/manager/Repository/vtls:000645262 -
6Academic Journal
Authors: Yelinska, A. M., Denisenko, S. V., Liashenko, L. I., Kostenko, V. O., Єлінська, Аліна Миколаївна, Денисенко, Софія Валеріївна, Ляшенко, Лілія Іванівна, Костенко, Віталій Олександрович, Елинская, Алина Николаевна, Денисенко, София Валерьевна, Ляшенко, Лилия Ивановна, Костенко, Виталий Александрович
Subject Terms: nuclear factor kappa B, glycoproteins, systemic inflammatory response, connective tissue biopolymers, collagen, proteoglycans, periodontium, ядерний фактор каппа B, системна запальна відповідь, біополімери сполучної тканини, колаген, протеоглікани, глікопротеїни, пародонт, ядерный фактор каппа B, системный воспалительный ответ, биополимеры соединительной ткани, коллаген, протеогликаны, гликопротеины, 616-092:[616.314.17:616-008.9]-599.323.4
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Relation: Influence of inhibitors of transcription factor kappa B on depolimerization of biopolymers in periodontal connective tissue under systemic intlammatory response in rats / A. M. Yelinska, S. V. Denisenko, L. I. Liashenko, V. O. Kostenko // Світ медицини та біології. – 2020. – №1 (71). – С. 180–183.; https://repository.pdmu.edu.ua/handle/123456789/15126
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7Academic Journal
Authors: DEMBITSKAYA Y.V., TYURIKOVA O.V., SEMYANOV A.V.
Source: Sovremennye tehnologii v medicine. 8:260-268
Subject Terms: 0301 basic medicine, 0303 health sciences, 03 medical and health sciences, brain extracellular matrix, synaptic plasticity, brain injuries, spinal cord injuries, chondroitin sulphate proteoglycans, chondroitinase ABC, ВНЕКЛЕТОЧНЫЙ МАТРИКС МОЗГА,СИНАПТИЧЕСКАЯ ПЛАСТИЧНОСТЬ,ТРАВМЫ МОЗГА,СПИННОМОЗГОВАЯ ТРАВМА,ХОНДРОИТИН СУЛЬФАТ ПРОТЕОГЛИКАНЫ,ХОНДРОИТИНАЗА ABC,BRAIN EXTRACELLULAR MATRIX,SYNAPTIC PLASTICITY,BRAIN INJURIES,SPINAL CORD INJURIES,CHONDROITIN SULPHATE PROTEOGLYCANS,CHONDROITINASE ABC
File Description: text/html
Access URL: http://www.stm-journal.ru/en/numbers/2016/4/1304/pdf
https://cyberleninka.ru/article/n/the-role-of-the-brain-extracellular-matrix-in-synaptic-plasticity-after-brain-injuries-review
http://www.stm-journal.ru/en/numbers/2016/4/1304
http://cyberleninka.ru/article/n/the-role-of-the-brain-extracellular-matrix-in-synaptic-plasticity-after-brain-injuries-review
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http://cyberleninka.ru/article/n/the-role-of-the-brain-extracellular-matrix-in-synaptic-plasticity-after-brain-injuries-review-1
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8Academic Journal
Authors: Єлінська, Аліна Миколаївна, Костенко, Віталій Олександрович, Елинская, Алина Николаевна, Костенко, Виталий Александрович, Yelinska, A. М., Kostenko, V. O.
Subject Terms: кверцетин, транскрипційні чинники AP-1 та NF-κB, ліпополісахарид, колагеноліз, протеоглікани, глікопротеїни, пародонт, транскрипционные факторы AP-1 и NF-κB, липополисахарид, коллагенолиз, гликопротеины, протеогликаны, quercetin, transcription factors AP-1 and NF-κB, lipopolysaccharide, collagenolysis, proteoglycans, glycoproteins, periodontium, 616.314.17+611.018.2:599.323.4
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9Academic Journal
Authors: Єлінська, Аліна Миколаївна, Костенко, Віталій Олександрович, Елинская, Алина Николаевна, Yelinska, A. М., Kostenko, V. O., Костенко, Виталий Александрович
Subject Terms: водорозчинна форма кверцетину, системна запальна відповідь, сполучна тканини, колагеноліз, протеоглікани, глікопротеїни, пародонт, водорастворимая форма кверцетина, системный воспалительный ответ, соединительная ткань, коллагенолиз, протеогликаны, гликопротеины, water-soluble form of quercetin, systemic inflammatory response, connective tissue, collagenolysis, proteoglycans, glycoproteins, periodontium, 616.314.17+611.018.2:599.323.4
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Relation: Єлінська А. М. Вплив водорозчинної форми кверцетину на дезінтеграцію органічного матриксу пародонта щурів за умов системного введення ліпополісахариду Salmonella Typhi / А. М. Єлінська, В. О. Костенко // Актуальні проблеми сучасної медицини: Вісник Української медичної стоматологічної академії. – 2019. – Т. 19, вип. 1 (65). – С. 56–60.; https://repository.pdmu.edu.ua/handle/123456789/12499
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10Academic Journal
Authors: Елинская, Алина Николаевна, Денисенко, София Валерьевна, Костенко, Виталий Александрович, Yelinskaya, A. N., Denisenko, S. V., Kostenko, V. A., Єлінська, Аліна Миколаївна, Денисенко, Софія Валеріївна, Костенко, Віталій Олександрович
Subject Terms: системный воспалительный ответ, матриксные металлопротеиназы, коллаген, протеогликаны, гликопротеины, пародонт, systemic inflammatory response, matrix metalloproteinases, collagen, proteoglycans, glycoproteins, periodontium, 616.314.17 : 577.112 : 599.323.4
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Availability: https://repository.pdmu.edu.ua/handle/123456789/15331
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11Academic Journal
Authors: Єлінська, Аліна Миколаївна, Костенко, Віталій Олександрович, Елинская, Алина Николаевна, Костенко, Виталий Александрович, Yelins’ka, A. M., Kostenko, V. O.
Subject Terms: системне запалення, сполучна тканина, колагеноліз, протеоглікани, пародонт, сіалоглікопротеїни, системное воспаление, соединительная ткань, коллагенолиз, протеогликаны, сиалогликопротеины, systemic inflammation, connective tissue, collagenolysis, proteoglycans, sialoglycoproteins, periodontium
File Description: application/pdf
Relation: Єлінська А. М. Механізми дезорганізації сполучної тканини пародонта щурів за умов системного запалення / А. М. Єлінська, В. О. Костенко // Актуальні проблеми сучасної медицини: Вісник Української медичної стоматологічної академії. – 2018. – Т. 18, вип. 1 (61). – С. 175–177.; УДК 616.314.17+611.018.2:599.323.4; https://repository.pdmu.edu.ua/handle/123456789/11328
Availability: https://repository.pdmu.edu.ua/handle/123456789/11328
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12Academic Journal
Authors: Єлінська, Аліна Миколаївна, Костенко, Віталій Олександрович, Елинская, Алина Николаевна, Костенко, Виталий Александрович, Yelinska, A. M., Kostenko, V. O.
Subject Terms: активаторний білок 1, системна запальна відповідь, сполучна тканини, колагеноліз, протеоглікани, активаторный белок 1, системный воспалительный ответ, соединительная ткань, гликопротеины, коллагенолиз, пародонт, протеогликаны, activator protein 1, systemic inflammatory response, connective tissue, collagenolysis, proteoglycans, glycoproteins, periodontium
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Relation: УДК 616.314.17+611.018.2:599.323.4; https://repository.pdmu.edu.ua/handle/123456789/12279
Availability: https://repository.pdmu.edu.ua/handle/123456789/12279
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13Academic Journal
Authors: S. Yu. Petrov, A. A. Antonov, I. A. Novikov, V. S. Reshchikova, N. A. Pahomova, С. Ю. Петров, А. А. Антонов, И. А. Новиков, В. С. Рещикова, Н. А. Пахомова
Source: National Journal glaucoma; Том 14, № 4 (2015); 88-100 ; Национальный журнал Глаукома; Том 14, № 4 (2015); 88-100 ; 2311-6862 ; 2078-4104
Subject Terms: aging, склера, фиброзная оболочка, коллаген, эластин, протеогликаны, соединительная ткань, биомеханика, морфология, старение, cornea, sclera, fibrous tunic, collagen, elastin, proteoglycans, connective tissue, biomechanics, morphology
File Description: application/pdf
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Application of structural analysis to the mechanical behaviour of the cornea. Journal of the Royal Society, Interface / the Royal Society 2004; 1(1):3-15. doi:10.1098/rsif.2004.0002.; Hjortdal J.O. Regional elastic performance of the human cornea. J Biomechanics 1996; 29(7):931-942.; Boote C., Hayes S., Young R.D., Kamma-Lorger C.S. et al. Ultra-structural changes in the retinopathy, globe enlarged (rge) chick cornea. Journal of Structural Biology 2009; 166(2):195-204. doi:10.1016/j.jsb.2009.01.009.; Elsheikh A., Wang D., Brown M., Rama P., Campanelli M., Pye D. Assessment of corneal biomechanical properties and their variation with age. Curr Eye Res 2007; 32(1):11-19. doi:10.1080/02713680601077145.; Myers K.M., Coudrillier B., Boyce B.L., Nguyen T.D. The inflation response of the posterior bovine sclera. Acta biomaterialia 2010; 6(11):4327-4335. doi:10.1016/j.actbio.2010.06.007.; Girard M.J., Suh J.K., Bottlang M., Burgoyne C.F., Downs J.C. 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Using an ultrasound elasticity microscope to map three-dimensional strain in a porcine cornea. Ultrasound in Medicine & Biology 2013; 39(8):1451-1459. doi:10.1016/j.ultrasmedbio.2013.02.465.; Manapuram R.K., Aglyamov S.R., Monediado F.M., Mashiatul-la M. et al. In vivo estimation of elastic wave parameters using phase-stabilized swept source optical coherence elastography. Journal of Biomedical Optics 2012; 17(10):100501. doi:10.1117/1.JB0.17.10.100501.; Nahas A., Bauer M., Roux S., Boccara A.C. 3D static elastography at the micrometer scale using Full Field OCT. Biomedical Optics Express 2013; 4(10):2138-2149. doi:10.1364/B0E.4.002138.; Wang S., Larin K.V. Shear wave imaging optical coherence tomography (SWI-OCT) for ocular tissue biomechanics. Optics letters 2014; 39(1):41-44. doi:10.1364/OL.39.000041.; Albon J., Purslow P.P., Karwatowski W.S., Easty D.L. Age related compliance of the lamina cribrosa in human eyes. 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Availability: https://www.glaucomajournal.ru/jour/article/view/89
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14Academic Journal
Authors: S. Yu. Petrov, A. A. Antonov, I. A. Novikov, V. S. Reshchikova, N. A. Pahomova, С. Ю. Петров, А. А. Антонов, И. А. Новиков, В. С. Рещикова, Н. А. Пахомова
Source: National Journal glaucoma; Том 14, № 3 (2015); 80-86 ; Национальный журнал Глаукома; Том 14, № 3 (2015); 80-86 ; 2311-6862 ; 2078-4104
Subject Terms: aging, склера, фиброзная оболочка, коллаген, эластин, протеогликаны, соединительная ткань, биомеханика, морфология, старение, cornea, sclera, fibrous tunic, collagen, elastin, proteoglycans, connective tissue, biomechanics, morphology
File Description: application/pdf
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Porcine sclera: thickness and surface area. Invest Ophthalmol Vis Sci 2002; 43(8): 2529-2532.; Haider K.M., Mickler C., Oliver D., Moya F.J., Cruz O.A., Davitt B.V. Age and racial variation in central corneal thickness of preschool and school-aged children. J Pediatric Ophthalmology and Strabismus 2008; 45(4): 227-233.; Aghaian E., Choe J.E., Lin S., Stamper R.L. Central corneal thickness of Caucasians, Chinese, Hispanics, Filipinos, African Americans, and Japanese in a glaucoma clinic. Ophthalmology 2004; 111(12): 2211-2219. doi:10.1016/j.ophtha.2004.06.013.; Chen M.J., Liu Y.T., Tsai C.C., Chen Y.C., Chou C.K., Lee S.M. Relationship between central corneal thickness, refractive error, corneal curvature, anterior chamber depth and axial length. J Chinese Medical Association: JCMA 2009; 72(3): 133-137. doi:10.1016/S1726-4901(09)70038-3.; Harper C.L., Boulton M.E., Bennett D., Marcyniuk B. et al. Diurnal variations in human corneal thickness. Br J Ophthalmol 1996; 80(12): 1068-1072.; Dubbelman M., Weeber H.A., van der Heijde R.G., VolkerDieben H.J. Radius and asphericity of the posterior corneal surface determined by corrected Scheimpflug photography. Acta Ophthalmol Scandinavica 2002; 80(4): 379-383.; Olsen T.W., Aaberg S.Y., Geroski D.H., Edelhauser H.F. Human sclera: thickness and surface area. Am J Ophthalmol 1998; 125(2): 237-241.; Doughty M.J., Jonuscheit S. An assessment of regional differences in corneal thickness in normal human eyes, using the Orbscan II or ultrasound pachymetry. Optometry 2007; 78(4): 181-190. doi:10.1016/j.optm.2006.08.018.; Watson P.G., Young R.D. Scleral structure, organisation and disease. A review. Exper Eye Res 2004; 78(3): 609-623.; Brown C.T., Vural M., Johnson M., Trinkaus-Randall V. Agerelated changes of scleral hydration and sulfated glycosaminoglycans. Mechanisms of Ageing and Development 1994; 77(2): 97-107.; Vannas S., Teir H. Observations on structures and age changes in the human sclera. Acta ophthalmologica 1960; 38: 268-279.; Rada J.A., Achen V.R., Penugonda S., Schmidt R.W., Mount B.A. Proteoglycan composition in the human sclera during growth and aging. Invest Ophthalmol Vis Sci 2000; 41(7): 1639-1648.; Kanai A., Kaufman H.E. Electron microscopic studies of corneal stroma: aging changes of collagen fibers. Annals of Ophthalmology 1973; 5(3): 285-287 passim.; Malik N.S., Moss S.J., Ahmed N., Furth A.J., Wall R.S., Meek K.M. Ageing of the human corneal stroma: structural and biochemical changes. Biochimica et biophysica Acta 1992; 1138(3): 222-228.; Scott J.E., Orford C.R., Hughes E.W. Proteoglycan-collagen arrangements in developing rat tail tendon. An electron microscopical and biochemical investigation. Biochemical J 1981; 195(3): 573-581.; Chakravarti S., Zhang G., Chervoneva I., Roberts L., Birk D.E. Collagen fibril assembly during postnatal development and dysfunctional regulation in the lumican-deficient murine cornea. Developmental dynamics: an official publication of the American Association of Anatomists 2006; 235(9): 2493-2506. doi:10.1002/dvdy.20868.; Koga T., Inatani M., Hirata A., Inomata Y. et al. Expression of a chondroitin sulfate proteoglycan, versican (PG-M), during development of rat cornea. Curr Eye Res 2005; 30(6): 455-463. doi:10.1080/02713680590959376.; Keeley F.W., Morin J.D., Vesely S. Characterization of collagen from normal human sclera. Exper Eye Res 1984; 39(5): 533-542.; Lee P.P., Walt J.W., Rosenblatt L.C., Siegartel L.R., Stern L.S., Glaucoma Care Study G. Association between intraocular pressure variation and glaucoma progression: data from a United States chart review. Am J Ophthalmol 2007; 144(6): 901-907. doi:10.1016/j.ajo.2007.07.040.; Lee R.E., Davison P.F. The collagens of the developing bovine cornea. Exper Eye Res 1984; 39(5): 639-652.; Ben-Zvi A., Rodrigues M.M., Krachmer J.H., Fujikawa L.S. Immunohistochemical characterization of extracellular matrix in the developing human cornea. Curr Eye Res 1986; 5(2): 105-117.; Drubaix I., Legeais J.M., Malek-Chehire N., Savoldelli M. et al. Collagen synthesized in fluorocarbon polymer implant in the rabbit cornea. Exper Eye Res 1996; 62(4): 367-376. doi:10.1006/exer.1996.0042.; Rucklidge G.J., Milne G., McGaw B.A., Milne E., Robins S.P. Turnover rates of different collagen types measured by isotope ratio mass spectrometry. Biochimica et Biophysica Acta 1992; 1156(1): 57-61.; Ihanamaki T., Salminen H., Saamanen A.M., Pelliniemi L.J. et al. Age-dependent changes in the expression of matrix components in the mouse eye. Exper Eye Res 2001; 72(4): 423-431. doi:10.1006/exer.2000.0972.; Sorsby A., Wilcox K., Ham D. The calcium content of the sclerotic and its variation with age. Brit J Ophthalmol 1935; 19(6): 327-337.; Manschot W.A. Senile scleral plaques and senile scleromalacia. Brit J Ophthalmol 1978; 62(6): 376-380.; Hogan M.J., Alvarado J. Ultrastructure of the deep corneolimbal region. Documenta Ophthalmologica Advances in Ophthalmology 1969; 26: 9-30.; Hirano K., Nakamura M., Kobayashi M., Kobayashi K., Hoshino T., Awaya S. Long-spacing collagen in the human corneal stroma. Japan J Ophthalmol 1993; 37(2): 148-155.; Yan D., McPheeters S., Johnson G., Utzinger U., Vande Geest J.P. Microstructural differences in the human posterior sclera as a function of age and race. Invest Ophthalmol Vis Sci 2011; 52(2): 821-829. doi:10.1167/iovs.09-4651.; Girard M.J., Suh J.K., Bottlang M., Burgoyne C.F., Downs J.C. Scleral biomechanics in the aging monkey eye. Invest Ophthalmol Vis Sci 2009; 50(11): 5226-5237. doi:10.1167/iovs.08-3363.; Sheppard J., Hayes S., Boote C., Votruba M., Meek K.M. Changes in corneal collagen architecture during mouse postnatal development. Invest Ophthalmol Vis Sci 2010; 51(6): 2936-2942. doi:10.1167/iovs.09-4612.; Boote C., Hayes S., Young R.D., Kamma-Lorger C.S. et al. Ultrastructural changes in the retinopathy, globe enlarged (rge) chick cornea. J Structural Biol 2009; 166(2): 195-204. doi:10.1016/j.jsb.2009.01.009.; McBrien N.A., Cornell L.M., Gentle A. Structural and ultra-structural changes to the sclera in a mammalian model of high myopia. Invest Ophthalmol Vis Sci 2001; 42(10): 2179-2187.; McBrien N.A., Gentle A. Role of the sclera in the development and pathological complications of myopia. Progress in Retinal and Eye Research 2003; 22(3): 307-338.; Daxer A., Misof K., Grabner B., Ettl A., Fratzl P. Collagen fibrils in the human corneal stroma: structure and aging. Invest Ophthalmol Vis Sci 1998; 39(3): 644-648.; Bailey A.J. Structure, function and ageing of the collagens of the eye. Eye 1987; 1(Pt 2): 175-183. doi:10.1038/eye.1987.34.; Tanaka S., Avigad G., Brodsky B., Eikenberry E.F. Glyca-tion induces expansion of the molecular packing of collagen. J Molecular Biol 1988; 203(2): 495-505.; https://www.glaucomajournal.ru/jour/article/view/76
Availability: https://www.glaucomajournal.ru/jour/article/view/76
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15Academic Journal
Contributors: Казанский (Приволжский) федеральный университет
Subject Terms: травма спинного мозга, хондроитинсульфат протеогликаны, соматосенсорная кора, перинейрональные сети, внеклеточный матрикс
Access URL: https://openrepository.ru/article?id=190847
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16Academic Journal
Contributors: Российский фонд фундаментальных исследований, д.б.н. В.И. Кашуба, к.б.н. Л.А. Мостович
Source: Advances in Molecular Oncology; Том 3, № 1 (2016); 53-60 ; Успехи молекулярной онкологии; Том 3, № 1 (2016); 53-60 ; 2413-3787 ; 2313-805X ; 10.17650/2313-805X.2016.3.1
Subject Terms: рак предстательной железы, tumour microenvironment, proteoglycan, expression pattern, tissue-specificity, lung cancer, breast cancer, prostate cancer, микроокружение опухоли, протеогликаны, паттерн экспрессии, тканеспецифичность, рак легкого, рак молочной железы
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Relation: https://umo.abvpress.ru/jour/article/view/55/56; Sarrazin S., Lamanna W.C., Esko J.D. Heparan sulfate proteoglycans. Cold Spring Harb Perspect Biol 2011;3(7):pii:a004952.; Theocharis A.D., Skandalis S.S., Tzanakakis G.N., Karamanos N.K. Proteoglycans in health and disease: novel roles for proteoglycans in malignancy and their pharmacological targeting. FEBS J 2010;277:3904–23.; Dietrich C.P., Nader H.B., Straus A.H. Structural differences of heparan sulfates according to the tissue and species of origin. Biochem Biophys Res Commun 1983;111(3):865–71.; Gharbaran R. Advances in the molecular functions of syndecan-1 (SDC1/CD138) in the pathogenesis of malignancies. Crit Rev Oncol Hematol 2015;94(1):1–17.; Liu W., Litwack E.D., Stanley M.J. et al. Heparan sulfate proteoglycans as adhesive and anti-invasive molecules. Syndecans and glypican have distinct functions. J Biol Chem 1998;273:22825–32.; Beauvais D.M., Burbach B.J., Rapraeger A.C. The syndecan-1 ectodomain regulates alphavbeta3 integrin activity in human mammary carcinoma cells. J Cell Biol 2004;167:171–81.; Shi X., Liang W., Yang W., et al. Decorin is responsible for progression of non-smallcell lung cancer by promoting cell proliferation and metastasis. Tumour Biol 2015;36(5):3345–54.; Iozzo R.V., Sanderson R.D. Proteoglycans in cancer biology, tumour microenvironment and angiogenesis. J Cell Mol Med 2011;15(5):1013–31.; Gotte M., Kersting C., Ruggiero M. et al. Predictive value of syndecan-1 expression for the response to neoadjuvant chemotherapy of primary breast cancer. Anticancer Res 2006;26:621–7.; Juuti A., Nordling S., Lundin J. et al. Syndecan-1 expression – a novel prognostic marker in pancreatic cancer. Oncology 2005;68(2–3):97–106.; Wiksten J.P., Lundin J., Nordling S. et al. Epithelial and stromal syndecan-1 expression as predictor of outcome in patients with gastric cancer. Int J Cancer 2001;95:1–6.; Hasengaowa, Kodama J., Kusumoto T. et al. Prognostic significance of syndecan-1 expression in human endometrial cancer. Ann Oncol 2005;16(7):1109–15.; Kusumoto T., Kodama J., Seki N. et al. Clinical significance of syndecan-1 and versican expression in human epithelial ovarian cancer. Oncol Rep 2010;23:917–25.; Ibrahim S.A., Hassan H., Vilardo L. et al. Syndecan-1 (CD138) modulates triple-negative breast cancer stem cell properties via regulation of LRP-6 and IL-6-mediated STAT3 signaling. PloS One 2013;8(12):e85737.; Kim S.Y., Choi E.J., Yun J.A. et al. Syndecan-1 Expression Is Associated with Tumor Size and EGFR Expression in Colorectal Carcinoma: a Clinicopathological Study of 230 Cases. Int J Med Sci 2015;12(2):92–9.; Shimada K., Anai S., Fujii T. et al. Syndecan-1 (CD138) contributes to prostate cancer progression by stabilizing tumourinitiating cells. J Pathol 2013;231(4): 495–504.; Zellweger T., Ninck C., Mirlacher M. et al. Tissue microarray analysis reveals prognostic significance of syndecan-1 expression in prostate cancer. Prostate 2003;55(1):20–9.; Xu Y., Yuan J., Zhang Z. et al. Syndecan-1 expression inhuman glioma is correlated with advanced tumor progression and poor prognosis. Mol Biol Rep 2012;39(9):8979–85.; Theocharis A.D., Skandalis S.S., Tzanakakis G., Karamanos N.K. Proteoglycans in health and disease: novel roles for proteoglycans in malignancy and their pharmacological targeting. FEBS J 2010;277(19):3904–23.; Iozzo R.V., Moscatello D.K., McQuillan D.J., Eichstetter I. Decorin is a biological ligand for the epidermal growth factor receptor. J Biol Chem 1999;274(8): 4489–92.; Merline R., Moreth K., Beckmann J. et al. Signaling by the matrix proteoglycan decorin controls inflammation and Cancer through PD CD4 and microRNA-21. Sci Signal 2011;4(199):ra75.; Albig A.R., Roy T., Becenti D.J., Schiemann W.P. Transcriptome analysis of endothelialcell gene expression induced by growth on matrigel matrices: identificationand characterization of MAGP-2 and lumican as novel regulators of angiogenesis. Angiogenesis 2007;10(3):197–216.; Matsuda Y., Yamamoto T., Kudo M. et al. Expression and roles of lumican in lung adenocarcinoma and squamous cell carcinoma. Int J Oncol 2008;33:1177–85.; Ishiwata T., Cho K., Kawahara K. et al. Role of lumican in cancer cells and adjacent stromal tissues in human pancreatic cancer. Onc Rep 2007;18(3):537–43.; Eshchenko T.Y., Rykova V.I., Chernakov A.E. et al. Expression of different proteoglycans in human breast tumors. Biochemistry (Mosc) 2007;72(9):1016–20.; Suhovskih A.V., Mostovich L.A., Kunin I.S. et al. Proteoglycan expression in normal human prostate tissue and prostate cancer. ISRN Oncol 2013;2013:680136.; Suhovskih A.V., Aidagulova S.V., Kashuba V.I., Grigorieva E.V. Proteoglycans as potential microenvironmental biomarkers for colon cancer. Cell Tissue Res 2015;361(3):833–44.; Skandalis S.S., Theocharis A.D., Theocharis D.A. et al. Matrix proteoglycans are markedly affected in advanced laryngeal squamous cell carcinoma. Biochim Biophys Acta 2004;1689(2):152–61.; Gulyás M., Hjerpe A. Proteoglycans and WT1 as markers for distinguishing adenocarcinoma, epithelioid mesothelioma, and benign mesothelium. J Pathol 2003;199(4):479–87.; García-Suárez O., García B., FernándezVega I. et al. Neuroendocrine tumors show altered expression of chondroitin sulfate, glypican 1, glypican 5, and syndecan 2 depending on their differentiation grade. Front Oncol 2014;4:15.; Nackaerts K., Verbeken E., Deneffe G. et al. Heparan sulfate proteoglycan expression in human lung-cancer cells. Int J Cancer 1997;74(3):335–45.; Kokenyesi R. Ovarian carcinoma cells synthesize both chondroitin sulfate and heparan sulfate cell surface proteoglycans that mediate cell adhesion to interstitial matrix. J Cell Biochem 2001;83(2):259–70.; https://umo.abvpress.ru/jour/article/view/55
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17Academic Journal
Authors: E. N. Iomdina, S. Yu. Petrov, A. A. Аntonov, I. A. Novikov, I. A. Pahomova, Е. Н. Иомдина, С. Ю. Петров, А. А. Антонов, И. А. Новиков, И. А. Пахомова
Source: Ophthalmology in Russia; Том 13, № 1 (2016); 10-19 ; Офтальмология; Том 13, № 1 (2016); 10-19 ; 2500-0845 ; 1816-5095 ; 10.18008/1816-5095-2016-1
Subject Terms: старение, sclera, fibrous tunic, collagen, elastin, proteoglycans, connective tissue, biomechanics, morphology, aging, склера, фиброзная оболочка, коллаген, эластин, протеогликаны, соединительная ткань, биомеханика
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Relation: https://www.ophthalmojournal.com/opht/article/view/292/302; Иомдина Е. Н., Бауэр С. М., Котляр К. Е. Биомеханика глаза: теоретические аспекты и клинические приложения. Москва: Реальное время; 2015.; Eysteinsson T., Jonasson F., Sasaki H., Arnarsson A., et al. Central corneal thickness, radius of the corneal curvature and intraocular pressure in normal subjects using non-contact techniques: Reykjavik Eye Study. Acta Ophthalmol Scand. 2002;80 (1):11‑15.; Kaufmann C., Bachmann L. M., Robert Y. C., Thiel M. A. Ocular pulse amplitude in healthy subjects as measured by dynamic contour tonometry. Arch Ophthalmol. 2006;124 (8):1104‑1108.; Liu J. H., Kripke D. F., Twa M. D., Hoffman R. E., et al. Twenty-four-hour pattern of intraocular pressure in the aging population. Invest Ophthalmol Vis Sci. 1999;40 (12):2912‑2917.; Buzard K. A. Introduction to biomechanics of the cornea. Refract Corneal Surg. 1992;8 (2): 127‑138.; D. M. M. The cornea and the sclera. In: Davson Y, ed The Eye: Vegetative Physiology and Biochemistry. Orlando, Florida: AcademicPress; 1984. p. 1‑58.; Boote C., Dennis S., Huang Y., Quantock A. J., Meek K. M. Lamellar orientation in human cornea in relation to mechanical properties. J Struct Biol. 2005;149 (1):1‑6.; Borcherding M. S., Blacik L. J., Sittig R. A., Bizzell J. W., Breen M., Weinstein H. G. Proteoglycans and collagen fibre organization in human corneoscleral tissue. Exp Eye Res. 1975;21 (1):59‑70.; Komai Y., Ushiki T. The three-dimensional organization of collagen fibrils in the human cornea and sclera. Invest Ophthalmol Vis Sci. 1991;32 (8):2244‑2258.; Olsen T. On the calculation of power from curvature of the cornea. Br J Ophthalmol. 1986;70 (2):152‑154.; Shimmyo M., Orloff P. N. Corneal thickness and axial length. Am J Ophthalmol. 2005;139 (3):553‑554.; Olsen T. W., Aaberg S. Y., Geroski D. H., Edelhauser H. F. Human sclera: thickness and surface area. Am J Ophthalmol. 1998;125 (2):237‑241.; Haider K. M., Mickler C., Oliver D., Moya F. J., Cruz O. A., Davitt B. V. Age and racial variation in central corneal thickness of preschool and school-aged children. J Pediatr Ophthalmol Strabismus. 2008;45 (4):227‑233.; Aghaian E., Choe J. E., Lin S., Stamper R. L. Central corneal thickness of Caucasians, Chinese, Hispanics, Filipinos, African Americans, and Japanese in a glaucoma clinic. Ophthalmology. 2004;111 (12):2211‑2219.; Chen M. J., Liu Y. T., Tsai C. C., Chen Y. C., Chou C. K., Lee S. M. Relationship between central corneal thickness, refractive error, corneal curvature, anterior chamber depth and axial length. J Chin Med Assoc. 2009;72 (3):133‑137.; Harper C. L., Boulton M. E., Bennett D., Marcyniuk B., et al. Diurnal variations in human corneal thickness. Br J Ophthalmol. 1996;80 (12):1068‑1072.; Dubbelman M., Weeber H. A., van der Heijde R. G., Volker-Dieben H. J. Radius and asphericity of the posterior corneal surface determined by corrected Scheimpflug photography. Acta Ophthalmol Scand. 2002;80 (4):379‑383.; Katsube N., Wang R., Okuma E., Roberts C. Biomechanical response of the cornea to phototherapeutic keratectomy when treated as a fluid-filled porous material. J Refract Surg. 2002;18 (5):593‑597.; Roberts C. Biomechanics of the cornea and wavefront-guided laser refractive surgery. J Refract Surg. 2002;18 (5):589‑592.; Аветисов Э. С. Близорукость. Москва: Медицина; 1999.; Doughty M. J., Jonuscheit S. An assessment of regional differences in corneal thickness in normal human eyes, using the Orbscan II or ultrasound pachymetry. Optometry. 2007;78 (4):181‑190.; Olsen T. W., Sanderson S., Feng X., Hubbard W. C. Porcine sclera: thickness and surface area. Invest Ophthalmol Vis Sci. 2002;43 (8):2529‑2532.; Vurgese S., Panda-Jonas S., Jonas J. B. Scleral thickness in human eyes. PLoS One. 2012;7 (1):e29692.; Нестеров А. П., Бунин А. Я., Кацнельсон Л. А. Внутриглазное давление. Физиология и патология. Москва: Наука; 1974.; Страхов В. В., Алексеев В. В. Динамическая ригидометрия. Вестник Офтальмологии. 1995;1:18‑20.; Pallikaris I. G., Kymionis G. D., Ginis H. S., Kounis G. A., Tsilimbaris M. K. Ocular rigidity in living human eyes. Invest Ophthalmol Vis Sci. 2005;46 (2):409‑414.; Friedman E., Ivry M., Ebert E., Glynn R., Gragoudas E., Seddon J. Increased scleral rigidity and age-related macular degeneration. Ophthalmology. 1989;96 (1):104‑108.; Акпатров А. И., Кустов В. Н. О зависимости между коэффи¬циентом ригидности и объемом глаза. Вестник офтальмологии. 1978;6:15‑17.; Пинтер Л. А. Активный и пассивный компоненты ригидности глаза. Вестник Офтальмологии. 1978;3:9‑10.; Faragher R. G., Mulholland B., Tuft S. J., Sandeman S., Khaw P. T. Aging and the cornea. Br J Ophthalmol. 1997;81 (10):814‑817.; Сарвазян А. П., Лырчиков А. Г. Связь объемно-упругих свойств мягких биологических тканей с содержанием воды, белка и жира. В кн: Медицинская биомеханика. Рига. p. 75‑77.; Dische Z. Biochemistry of connective tissue of the vertebrate eye. Int Rev Connect Tissue Res. 1970;5:209‑279.; Vo T. D., Blumenfeld O. O., Coleman D. J. The biochemical composition of the human sclera and its relationship to the pathogenesis of degenerative myopia. Proc of 3rd Intern Conference on Myopia. 1987. p. 206‑214.; Иомдина Е. Н. Биомеханические и биохимические нарушения склеры при прогрессирующей близорукости и методы их коррекции. В кн: С. Э. Аветисов, Т. П. Кащенко, А. М. Шамшинова «Зрительные функции и их коррекция у детей». Москва: Медицина; 2006. p. 163‑183.; Brown C. T., Vural M., Johnson M., Trinkaus-Randall V. Age-related changes of scleral hydration and sulfated glycosaminoglycans. Mech Ageing Dev. 1994;77 (2):97‑107.; Watson P. G., Young R. D. Scleral structure, organisation and disease. A review. Exp Eye Res. 2004;78 (3):609‑623.; Rada J. A., Achen V. R., Penugonda S., Schmidt R. W., Mount B. A. Proteoglycan composition in the human sclera during growth and aging. Invest Ophthalmol Vis Sci. 2000;41 (7):1639‑1648.; Kanai A., Kaufman H. E. Electron microscopic studies of corneal stroma: aging changes of collagen fibers. Ann Ophthalmol. 1973;5 (3):285‑287 passim.; Malik N. S., Moss S. J., Ahmed N., Furth A. J., Wall R. S., Meek K. M. Ageing of the human corneal stroma: structural and biochemical changes. Biochim Biophys Acta. 1992;1138 (3):222‑228.; Scott J. E., Orford C. R., Hughes E. W. Proteoglycan-collagen arrangements in developing rat tail tendon. An electron microscopical and biochemical investigation. Biochem J. 1981;195 (3): 573‑581.; Chakravarti S., Zhang G., Chervoneva I., Roberts L., Birk D. E. Collagen fibril assembly during postnatal development and dysfunctional regulation in the lumican-deficient murine cornea. Dev Dyn. 2006;235 (9):2493‑2506.; Koga T., Inatani M., Hirata A., Inomata Y., et al. Expression of a chondroitin sulfate proteoglycan, versican (PG-M), during development of rat cornea. Curr Eye Res. 2005;30 (6):455‑463.; Затулина Н. И., Сеннова Л. Г. Об эластических волокнах дренажной системы глаза человека. Офтальмологический журнал. 1983;8:497‑499.; Marshall G. E. Human scleral elastic system: an immunoelectron microscopic study. Br J Ophthalmol. 1995;79 (1):57‑64.; Moses R. A., Grodzki W. J., Jr., Starcher B. C., Galione M. J. Elastin content of the scleral spur, trabecular mesh, and sclera. Invest Ophthalmol Vis Sci. 1978;17 (8):817‑818.; Weale R. A. A biography of the eye. Development, growth, age. London: H. K. Lewis Co. LTD; 1982.; Hassan A. U., Hassan G., Rasool Z., Hassan S. Clinical outcomes of elastin fibre defects. Journal of Cytology and Histology 2013;4 (1):166‑169.; Иомдина Е. Н., Игнатьева Н. Ю., Арутюнян Л. Л., Шехтер А. Б. и др. Изучение коллагеновых и эластических структур склеры глаз при глаукоме с помощью нелинейно-оптической (мультифотонной) микроскопии и гистологии (предварительное сообщение). Российский офтальмологический журнал. 2015;8 (1):50‑58.; Keeley F. W., Morin J. D., Vesely S. Characterization of collagen from normal human sclera. Exp Eye Res. 1984;39 (5):533‑542.; Серов В. В., Пауков В. С. Ультраструктурная патология. Москва: Медицина; 1975.; Серов В. В., Шехтер А. Б. Соединительная ткань: функциональная морфология и общая патология. Москва: Медицина; 1981.; Аветисов Э. С., Хорошилова-Маслова И. П., Андреева Л. Д. Ультраструктурные изменения склеры при миопии. Вестник Офтальмологии. 1980;6:36‑42.; Bailey A. J. Structure, function and ageing of the collagens of the eye. Eye (Lond). 1987;1 (Pt 2):175‑183.; Fung Y. C. Biomechanics. Mechanical Properties of Living Tissues. NewYork: Springer-Verlag; 1990.; Lee P. P., Walt J. W., Rosenblatt L. C., Siegartel L. R., Stern L. S., Glaucoma Care Study G. Association between intraocular pressure variation and glaucoma progression: data from a United States chart review. Am J Ophthalmol. 2007;144 (6):901‑907.; Lee R. E., Davison P. F. The collagens of the developing bovine cornea. Exp Eye Res. 1984;39 (5):639‑652.; Vannas S., Teir H. Observations on structures and age changes in the human sclera. Acta Ophthalmol (Copenh). 1960;38:268‑279.; Ben-Zvi A., Rodrigues M. M., Krachmer J. H., Fujikawa L. S. Immunohistochemical characterization of extracellular matrix in the developing human cornea. Curr Eye Res. 1986;5 (2):105‑117.; Rucklidge G. J., Milne G., McGaw B. A., Milne E., Robins S. P. Turnover rates of different collagen types measured by isotope ratio mass spectrometry. Biochim Biophys Acta. 1992;1156 (1):57‑61.; Ihanamaki T., Salminen H., Saamanen A. M., Pelliniemi L. J., et al. Age-dependent changes in the expression of matrix components in the mouse eye. Exp Eye Res. 2001;72 (4):423‑431.; Manschot W. A. Senile scleral plaques and senile scleromalacia. Br J Ophthalmol. 1978;62 (6):376‑380.; Sorsby A., Wilcox K., Ham D. The Calcium Content of the Sclerotic and Its Variation with Age. Br J Ophthalmol. 1935;19 (6):327‑337.; Hogan M. J., Alvarado J. Ultrastructure of the deep corneolimbal region. Doc Ophthalmol. 1969;26:9‑30.; Hirano K., Nakamura M., Kobayashi M., Kobayashi K., Hoshino T., Awaya S. Longspacing collagen in the human corneal stroma. Jpn J Ophthalmol. 1993;37 (2):148‑155.; Yan D., McPheeters S., Johnson G., Utzinger U., Vande Geest J. P. Microstructural differences in the human posterior sclera as a function of age and race. Invest Ophthalmol Vis Sci. 2011;52 (2):821‑829.; Girard M. J., Suh J. K., Bottlang M., Burgoyne C. F., Downs J. C. Scleral biomechanics in the aging monkey eye. Invest Ophthalmol Vis Sci. 2009;50 (11):5226‑5237.; Sheppard J., Hayes S., Boote C., Votruba M., Meek K. M. Changes in corneal collagen architecture during mouse postnatal development. Invest Ophthalmol Vis Sci. 2010;51 (6):2936‑2942.; Boote C., Hayes S., Young R. D., Kamma-Lorger C. S., et al. Ultrastructural changes in the retinopathy, globe enlarged (rge) chick cornea. J Struct Biol. 2009;166 (2):195‑204.; McBrien N. A., Cornell L. M., Gentle A. Structural and ultrastructural changes to the sclera in a mammalian model of high myopia. Invest Ophthalmol Vis Sci. 2001;42 (10):2179‑2187.; McBrien N. A., Gentle A. Role of the sclera in the development and pathological complications of myopia. Prog Retin Eye Res. 2003;22 (3):307‑338.; Daxer A., Misof K., Grabner B., Ettl A., Fratzl P. Collagen fibrils in the human corneal stroma: structure and aging. Invest Ophthalmol Vis Sci. 1998;39 (3):644‑648.; Fratzl P. Collagen. Potsdam: Springer; 2008.; Malik N. S., Meek K. M. Vitamins and analgesics in the prevention of collagen ageing. Age Ageing. 1996;25 (4):279‑284.; https://www.ophthalmojournal.com/opht/article/view/292
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18Academic Journal
Authors: L. A. Bardonova, E. G. Belykh, V. A. Byvaltsev, Л. А. Бардонова, Е. Г. Белых, В. А. Бывальцев
Source: Acta Biomedica Scientifica; Том 1, № 4 (2016); 99-103 ; 2587-9596 ; 2541-9420
Subject Terms: протеогликаны, degeneration, bone morphogenetic protein, proteoglycans, дегенерация, костный морфогенетический белок
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Relation: https://www.actabiomedica.ru/jour/article/view/250/251; Булатов А.А., Савельев В.И., Калинин А.В. Применение костных морфогенетических белков в эксперименте и клинике // Травматология и ортопедия России. - 2005. - № 1 (34). - С. 46-54; Бывальцев В.А., Степанов И.А., Белых Е.Г., Гиерс М., Прул М. Цитокиновые механизмы дегенерации межпозвонкового диска // Сибирский медицинский журнал. - 2015. - № 5. - С. 17-21; Belykh E, Giers M, Bardonova L, Theodore N, Preul M, Byvaltsev V (2015). The role of bone morphogenetic proteins 2, 7, and 14 in approaches for intervertebral disk restoration. World Neurosurg., 84 (4), 870-877.; Coulson-Thomas V, Gesteira TF (2014). Dimeth-ylmethylene Blue Assay (DMMB). Bio-protocol, 4 (18), e1236. Available at: http://www.bio-protocol.org/e1236.; Farndale RW, Buttle DJ, Barrett AJ (1986). Improved quantitation and discrimination of sulphated glycosaminoglycans by use of dimethylmethylene blue. Biochim. Biophys. Acta., (883), 173-177.; Gantenbein B, Illien-Jünger S, Chan SC, Walser J, Haglund L, Ferguson SJ, Iatridis JC, Grad S (2015). Organ culture bioreactors - platforms to study human intervertebral disc degeneration and regenerative therapy. Curr. Stem. Cell Res. Ther, 10 (4), 339-352.; Haschtmann D, Ferguson SJ, Stoyanov JV (2012). BMP-2 and TGF-ß3 do not prevent spontaneous degeneration in rabbit disc explants but induce ossification of the annulus fibrosus. Eur. Spine J., 21 (9), 1724-1733.; Huang YC, Urban JP, Luk KD (2014). Intervertebral disc regeneration: do nutrients lead the way? Nat. Rev. Rheumatol., 10 (9), 561-566.; Kraemer J (2009). Intervertebral disk diseases: causes, diagnosis, treatment, prophylaxis, 368.; Le Maitre CL, Richardson SM, Baird P, Freemont AJ, Hoyland JA (2005). Expression of receptors for putative anabolic growth factors in human intervertebral disc: implications for repair and regeneration of the disc. J. Pathol, 207 (4), 445-452.; Lo KW, Ulery BD, Ashe KM, Laurencin CT (2012). Studies of bone morphogenetic protein-based surgical repair. Adv. Drug. Deliv. Rev., 64 (12), 1277-1291.; Louis KS, Siegel AC (2011). Cell viability analysis using trypan blue: manual and automated methods. Methods Mol. Biol., (740), 7-12.; Nolan JS, Packer L (1974). Monolayer culture techniques for normal human diploid fibroblasts. Meth. Enzymol., 32 (B), 561-568.; Raj PP (2008). Intervertebral disc: anatomyphysiology-pathophysiology-treatment, Pain Pract., (8), 18-44.; Tomaszewski KA, Walocha JA, Mizia E, Gla-dysz T, Glowacki R, Tomaszewska R (2015). Age- and degeneration-related variations in cell density and glycosaminoglycan content in the human cervical intervertebral disc and its endplates. Pol. J. Pathol., 66 (3), 296-309.; Urban JP, Smith S, Fairbank JC (2004). Nutrition of the intervertebral disc, Spine (Phila Pa 1976), (29), 2700-2709.; https://www.actabiomedica.ru/jour/article/view/250
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19Academic Journal
Authors: ЦЫДЫПОВ Р.Ц.
Subject Terms: ПРИДАТОК СЕМЕННИКА, ХРЯКИ, БЕЛОК, ЭПИТЕЛИЙ, СИАЛОГЛИКОПРОТЕИНЫ, ПРОТЕОГЛИКАНЫ, ГЛИКОГЕН, ГИАЛУРОНАТЫ
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20Academic Journal
Authors: Ветошкин, Р., Николаев, А.
Subject Terms: ПРОТЕОГЛИКАНЫ,СЕМЕННАЯ ПЛАЗМА,СПЕРМАТОЗОИДЫ,КАПАЦИТАЦИЯ,PROTEOGLYCANS,SEMINAL PLASMA,SPERM,CAPACITATE
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