The 35 references in paper Т. Тенчурин Х., Л. Истранов П., Е. Истранова В., А. Шепелев Д., В. Мамагулашвили Г., С. Малахов Н., Р. Камышинский А., А. Орехов С., А. Васильев Л., Е. Сытина В., С. Крашенинников В., С. Чвалун Н. (2019) “НАНО- И МИКРОВОЛОКНИСТЫЕ МАТЕРИАЛЫ НА ОСНОВЕ КОЛЛАГЕНА ДЛЯ ТКАНЕВОЙ ИНЖЕНЕРИИ: ПОЛУЧЕНИЕ, СТРУКТУРА И СВОЙСТВА” / spz:neicon:nanorf:y:2018:i:0:p:25-34

1
Ushiki T. Collagen fibers, reticular fibers and elastic fibers. A comprehensive understanding from a morphological viewpoint // Archives Histology Cytol. 2002. V. 65. P. 109–126.
(check this in PDF content)
2
Dyer R.F, Enna C.D. Ultrastructural features of adult human tendon // Cell and Tissue Research. 1976. V. 168. P. 247–259.
(check this in PDF content)
3
Lin Ch., Kao Y., Lin Y., Mab H., Tsay R. A fiber-progressiveengagement model to evaluate the composition, microstructure, and nonlinear pseudoelastic behavior of porcine arteries and decellularized derivatives // Acta Biomater. 2016. V. 46. P. 101–111.
(check this in PDF content)
4
Chen R., Ho H., Tsai Y., Sheu M. Process development of an acellular dermal matrix (ADM) for biomedical applications // Biomat. 2004. V. 25. P. 2679–2686.
(check this in PDF content)
5
Sun F., Jiang Y., Xu Y., Shi H., Zhang S., Liu X., Pan Sh., Ye G., Zhang W., Zhang F. Zhong Ch. Genipin cross-linked decellularized tracheal tubular matrix for tracheal tissue engineering applications // Sci Rep. 2016. V. 6. P. 24429–24441.
(check this in PDF content)
6
Chen Z.G., Wang P.W., Wei B., Mo X.M., Cui F.Z. Electrospun collagen–chitosan nanofiber: A biomimetic extracellular matrix for endothelial cell and smooth muscle cell // Acta Biomater. 2010. V. 6. P. 372–382.
(check this in PDF content)
7
Chen R., Ho H., Tsai Y., Sheu M. Process development of an acellular dermal matrix (ADM) for biomedical applications // Biomater. 2004. V. 25. P. 2679–2686.
(check this in PDF content)
8
Lukanina K.I., Grigor’ev T.E., Tenchurin T.Kh., Shepelev A.D., Chvalun S.N. Nonwoven materials produced by electrospinning for modern medical technologies (review) // Fibre Chem. 2017. V. 49. P. 72–83.
(check this in PDF content)
9
Cao D., Wu Y., Fu Zh., Tian Y., Li C., Gao Ch., Chen Zh., Feng Xi. Cell adhesive and growth behavior on electrospun nanofibrous scaffolds by designed multifunctional composites // Coll Surf B: Biointerfaces. 2011. V. 84. P. 26–34.
(check this in PDF content)
10
Zhang Q., Lv Sh., Lu J., Jiang Sh., Lin L. Characterization of polycaprolactone/collagen fibrous scaffolds by electrospinning and their bioactivity // Int J Biol Macromol. 2015. V. 76. P. 94–101.
(check this in PDF content)
11
Mao Zh., Gao Ch., Wang D., Ma Li., Shen J.G. Controlling biostability of collagen films for fibroblast cytocompatibility // J Bioact Compat Polym. 2004. V. 19. P. 353–364.
(check this in PDF content)
12
Brinkman W.T., Nagapudi K., Thomas B.S., Chaikof E.L. Photocross-linking of type I collagen gels in the presence of smooth muscle cells: mechanical properties cell viability, and function // Biomacromol. 2003. V. 4. P. 890–895.
(check this in PDF content)
13
Miles Ch.A., Avery N.C., Rodin V.V., Bailey A.J. The increase in denaturation temperature following cross-linking of collagen is caused by dehydration of the fibres // J Mol Biol. 2005. V. 346. P. 551–556.
(check this in PDF content)
14
Silva S.S., Oliveira N.M., Oliveira M.B., Soares da Costa D.P., Naskar D., Mano J.F., Kundu S.C., Reis R.L. Fabrication and characterization of Eri silk fibers-based sponges for biomedical application // Acta Biomaterial. 2016. V. 32. P. 178–189.
(check this in PDF content)
15
Madaghiele M., Calo E., Salvatore L., Bonfrate V., Pedone D., Frigione M., Sannino A. Assessment of collagen crosslinking and denaturation for the design of regenerative scaffolds // J Biomed Mater Res A. 2016. V. 104. P. 186–194.
(check this in PDF content)
16
Rioja A.Y., Muniz-Maisonet M., Koob Th.J., Gallant N.D. Effect of nordihydroguaiaretic acid cross-linking on fibrillar collagen: in vitro evaluation of fibroblast adhesion strength and migration // AIMS Bioeng. 2017. V. 4. P. 300–317.
(check this in PDF content)
17
Grover Ch.N., Gwynne J.H., Pugh N., Hamaia S., Farndale R.W., Best S.M., Cameron R.E. Crosslinking and composition influence the surface properties, mechanical stiffness and cell reactivity of collagen-based films // Acta Biomater. 2012. V. 8. P. 3080–3090.
(check this in PDF content)
18
Sung H., Chang Y., Liang I., Chang W., Chen Yi. Fixation of biological tissues with a naturally occurring crosslinking agent: fixation rate and effects of pH, temperature, and initial fixative concentration // J Biomed Mater Res. 2000. V. 52. P. 77–87.
(check this in PDF content)
19
i F., Shyu Sh., Peng Ch. Characterization of ring-opening polymerization of genipin and pH-dependent cross-linking reactions between chitosan and genipin // J Polym Sci: Part A: Polym Chem. 2005. V. 43. P. 1985–2000.
(check this in PDF content)
20
Tokareva M.I., Ivantsova M.N., Mironov M.A. Heterocycles of natural origin as non-toxic reagents for cross-linking of proteins and polysaccharides // Chem Heterocycl Comp. 2017. V. 53. P. 21–35.
(check this in PDF content)
21
Torres-Giner S., Gimeno-Alcaniz J.V., Ocio M.J., Lagaron J.M. Comparative performance of electrospun collagen nanofibers сross-linked by means of different methods // ACS Appl Mater Interfaces. 2009. V. 1. P. 218–223.
(check this in PDF content)
22
Orekhov A.S., Klechkovskaya V.V., Kononova S.V. Low-voltage scanning electron microscopy of multilayer polymer systems // Crystallogr Rep. 2017. V. 62. P. 735–740.
(check this in PDF content)
23
Schindelin J., Arganda-Carreras I., Frise E., Kaynig V., Longair M., Pietzsch T., Preibisch S., Rueden C., Saalfeld S., Schmid B., Tinevez J., James White D., Hartenstein V., Eliceiri K., Tomancak P., Cardona A. Fiji: an open-source platform for biological-image analysis // Nat Methods. 2012. V. 9. P. 676–682.
(check this in PDF content)
24
Arutyunyan I.V., Tenchurin T.Kh., Kananykhina E.Y., Chernikov V.P., Vasyukova O.A., Elchaninov A.V., Makarov A.V., Korshunov A.A., Burov A.A., Podurovskaya Y.L., Chuprynin V.D., Uvarova E.V., Degtyarev D.N., Shepelev A.D., Mamagulashvili V.G., Kamyshinskiy R.A., Krasheninnikov S.V., Chvalun S.N., Fatkhudinov T.Kh. Nonwoven polycaprolactone scaffolds for tissue engineering: the choice of the structure and the method of cell seeding // Genes Cells. 2017. V. 12. P. 62–71.
(check this in PDF content)
25
Aasen T., Izpisúa Belmonte J.C. Isolation and cultivation of human keratinocytes from skin or plucked hair for the generation of induced pluripotent stem cells // Nat Protoc. 2010. V. 5. P. 371–382.
(check this in PDF content)
26
Tenchurin T., Belousov S., Kiryukhin Y., Istranov L., Istranova E., Shepelev A., Mamagulashvili V., Kamyshinsky R., Chvalun S. Control on rheological behavior of collagen 1 dispersions for efficient electrospinning // J Biomed Mater Res Part A. 2018. Accepted Author Manuscript. DOI: 10.1002/jbm.a.36459
(check this in PDF content)
27
Yang H., Xu S., Shen L., Liu W., Li G. Changes in aggregation behavior of collagen molecules in solution with varying concentrations of acetic acid // Int J Biol Macromol. 2016. V. 92. P. 581–586.
(check this in PDF content)
28
Fiorani A., Gualandi Ch., Panseri S., Montesi M., Marcacci M., Focarete M. L., Bigi A. Comparative performance of collagen nanofibers electrospun from different solvents and stabilized by different crosslinkers // J Mater Sci: Mater Med. 2014. V. 25. P. 2313–2321.
(check this in PDF content)
29
Bürck J., Heissler S., Geckle U., Ardakani M.F., Schneider R., Ulrich A.S., Kazanci M. Resemblance of electrospun collagen nanofibers to their native structure // Langmuir. 2013. V. 29. P. 1562–1572.
(check this in PDF content)
30
Mu Ch., Li D., Lin W., Ding Y., Zhang G. Temperature induced denaturation of collagen in acidic solution // Biopolym. 2007. V. 86. P. 282–287.
(check this in PDF content)
31
Schek R.M., Michalek A.J., Iatridis J.C. Genipin-crosslinked fibrin hydrogels as a potential adhesive to augment intervertebral disc annulus repair // European Cells Mater. 2011. V. 21. P. 373–383.
(check this in PDF content)
32
Yoo J.S., Kim Y.J., Kim S.H., Choi S.H. Study on genipin: a new alternative natural crosslinking agent for fixing heterograft tissue // Korean J Thorac Cardiovasc Surg. 2011. V. 44. No 3. P. 197–207.
(check this in PDF content)
33
Sung H., Chang W., Ma Ch., Lee M. Crosslinking of biological tissues using genipin and/or carbodiimide // J Biomed Mater Res Part A. 2003. V. 64A. P. 427–438.
(check this in PDF content)
34
Mu Ch., Liu F., Cheng Q., Li H., Wu B., Zhang G., Lin. W. Collagen cryogel cross‐linked by dialdehyde starch // Macromol Mater Engin. 2010. V. 295. P. 100–107.
(check this in PDF content)
35
Liu D., Lianga L., Regenstein J.M., Zhou P. Extraction and characterisation of pepsin-solubilised collagen from fins, scales, skins, bones and swim bladders of bighead carp (hypophthalmichthys nobilis) // Food Chem. 2012. V. 133. P. 1441–1448.
(check this in PDF content)