참고문헌
-
Candia PD, Minopoli G, Verga V, Gargiulo A, Vanoni M, Alberghina L (2011) Nutritional Limitation Sensitizes Mammalian Cells to GSK-
$3{\beta}$ Inhibitors and Leads to Growth Impairment. Am J Pathol 178, 1814-1823. https://doi.org/10.1016/j.ajpath.2010.12.047 - Cao Y, Wang B (2009) Biodegradation of silk biomaterials. Int J Mol Sci 10, 1514-1524. https://doi.org/10.3390/ijms10041514
- Capelli R, Amsden JJ, Generali G, Toffanin S, Benfenati V, Muccini M, Kaplan DL (2011) Integration of silk protein in organic and lightemitting transistors. Org Electron 12, 1146-1151. https://doi.org/10.1016/j.orgel.2011.04.005
- Foo CWP, Bini E, Hensman J, Knight DP, Lewis RV, Kaplan DL (2006) Role of pH and charge on silk protein assembly in insects and spiders. Appl Phys A 82, 223-233. https://doi.org/10.1007/s00339-005-3426-7
-
Hu X, Kaplan D, Cebe P (2008) Dynamic protein-water relationships during
${\beta}$ -sheet formation. Macromolecules 41, 3939-3948. https://doi.org/10.1021/ma071551d - Hu Y, Zhang Q, You R, Wang L, Li M (2012) The relationship between secondary structure and biodegradation behavior of silk fibroin scaffolds. Adv Mater Sci Eng, Article ID: 185905
- Kang GD, Nahm JH, Park JS, Moon JY, Cho CS, Yeo JH (2000) Effects of poloxamer on the gelation of silk fibroin. Marcromol Rapid Commun 21, 788-791. https://doi.org/10.1002/1521-3927(20000701)21:11<788::AID-MARC788>3.0.CO;2-X
- Ki CS, Park YH, Jin, HJ (2009) Silk protein as a fascinating biomedical polymer: structural fundamentals and applications. Macromol Res 17, 935-942. https://doi.org/10.1007/BF03218639
- Lawrence BD, Marchant JK, Pindrus MA, Omenetto FG, Kaplan DL (2009) Silk film biomaterials for cornea tissue engineering. Biomaterials 30, 1299-1308. https://doi.org/10.1016/j.biomaterials.2008.11.018
- Mao CD, Hoang P, DiCorleto PE (2001) Lithium inhibits cell cycle progression and induces stabilization of p53 in bovine aortic endothelial cells. J Biol Chem 276, 26180-26188. https://doi.org/10.1074/jbc.M101188200
- Rockwood DN, Preda RC, Yucel T, Wang X, Lovett ML, Kaplan DL (2011) Materials fabrication from Bombyx mori silk fibroin, Nat Protoc 6, 1612-1631. https://doi.org/10.1038/nprot.2011.379
- Zhang H, Deng L, Yang M, Min S, Yang L, Zhu L (2011) Enhancing Effect of Glycerol on the Tensile Properties of Bombyx mori Cocoon Sericin Films. Int J Mol Sci 12, 3170-3181. https://doi.org/10.3390/ijms12053170
- Zhou L, Chen X, Shao Z, Huang Y, Knight DP (2005) Effect of Metallic Ions on Silk Formation in the Mulberry Silkworm, Bombyx mori. J Phys Chem B 109, 16937-16945. https://doi.org/10.1021/jp050883m
- Zong XH, Zhou P, Shao ZZ, Chen SM, Chen X, Ju BW, Deng F, Yao WH (2004) Effect of pH and Copper(II) on the conformation transitions of silk fibroin based on EPR, NMR, and raman spectroscopy. Biochemistry 43, 11932-11941. https://doi.org/10.1021/bi049455h
피인용 문헌
- Fabrication and characterization of fibroin solution and nanoparticle from silk fibers of Bombyx mori vol.35, pp.3, 2017, https://doi.org/10.1080/02726351.2016.1154908
- Effect of Microwave Irradiation on the Microstructural Properties of Bivoltine Silk Fibroin Films vol.141, 2016, https://doi.org/10.1016/j.proeng.2015.08.1110
- Progress and Trends in Artificial Silk Spinning: A Systematic Review vol.3, pp.3, 2017, https://doi.org/10.1021/acsbiomaterials.6b00669
- Phase Behaviour and Miscibility Studies of Collagen/Silk Fibroin Macromolecular System in Dilute Solutions and Solid State vol.22, pp.8, 2017, https://doi.org/10.3390/molecules22081368