References
- Aramwit P, Kanokpanont S, De-Eknamkul W, Kamei K, Srichana T (2009) The effect of sericin with variable amino-acd content from different silk strains on the production of collagen and nitric oxide, J Biomater Sci Polym Ed 20, 1295-1306. https://doi.org/10.1163/156856209X453006
- Aramwit P, Sangcakul A (2007) The effects of sericin cream on wound healing in rats, Biosci Biotechnol Biochem 71, 2473-2477. https://doi.org/10.1271/bbb.70243
- Fan JB, Wu LP, Chen LS, Mao XY, Ren FZ (2009) Antioxidant activities of silk sericin from silkworm Bombyx mori, J Food Biochem 33, 74-88. https://doi.org/10.1111/j.1745-4514.2008.00204.x
- Garel A, Deleage G, Prudhomme JC (1997) Structure and organization of the Bombyx mori sericin 1 gene and of the sericins 1 deduced from the sequence of the Ser 1B cDNA, Insect Biochem Mol Biol 27, 469-477. https://doi.org/10.1016/S0965-1748(97)00022-2
- Ha Y, Park Y, Kweon HY, Jo YY, Kim SG (2014) Comparison of the physical properties and in vivo bioactivities of silkworm-cocoon-derived silk membrane, collagen membrane, and polytetrafluoroethylene membrane for guided bone regeneration, Macromol Res 22, 1018-1023. https://doi.org/10.1007/s13233-014-2138-2
- Horan RL, Antle K, Collette AL, Wang Y, Huang J, Moreau JE, Volloch V, Kaplan DL, Altman GH (2005) In vitro degradation of silk fibroin, Biomaterials 26, 3385-3393. https://doi.org/10.1016/j.biomaterials.2004.09.020
- Ju WT, Kim KY, Sung GB, Kim YS (2014) Quantitative analysis of 1-Deoxynojirimycin content using silkworm genetic resources. Int J Indust Entomol 29(2), 162-168. https://doi.org/10.7852/ijie.2014.29.2.162
- Kaewkorn W, Limpeanchob N, Tiyaboonchai W, Pongcharoen S, Sutheerawattananonda M (2012) Effects of silk sericin on the proliferation and apoptosis of colon cancer cells, Biol. Res., 45, 45-50. https://doi.org/10.4067/S0716-97602012000100006
- Kato N, Sato S, Yamanaka A, Yamada H, Fuwa N, Nomura M (1998) Silk protein, sericin, inhibits lipid peroxidation and tyrosinase activity, Biosci Biotechnol Biochem 62, 145-147. https://doi.org/10.1271/bbb.62.145
- Kim J, Kim CH, Park CH, Seo JN, Kweon HY, Kang SW, Lee KG (2000) Comparison of methods for the repair of acute tympanic membrane perforations: Silk patch vs. Paper patch. Wound Rep Regen 18, 132-138.
- Kundu B, Rajkhowa R, Kundu SC, Wang X. (2013) Silk fibroin biomaterials for tissue regenerations, Adv Drug Deliv Rev 65, 457-470. https://doi.org/10.1016/j.addr.2012.09.043
- Meinel L, Hofmann S, Karageorgiou V, Kirker-Head C, McCool J, Gronowicz G, Zichner L, Langer R, Vunjak-Novakovic G, Kaplan DL (2005) The inflammatory responses to silk films in vitro and in vivo, Biomaterials 26, 147-155. https://doi.org/10.1016/j.biomaterials.2004.02.047
- Mo C, Holland C, Porter D, Shao Z, Vollrath F (2009) Concentration state dependence of the rheological and structural properties of reconstituted silk, Biomacromol 10, 2724-2728. https://doi.org/10.1021/bm900452u
- Terada S, Nishimura T, Sasaki M, Yamada H, Miki M (2002) Sericin, a protein derived from silkworms, accelerates the proliferation of several mammalian cell lines including a hybridoma, Cytotechnol 40, 3-12. https://doi.org/10.1023/A:1023993400608
- Teramoto H, Kameda T, Tamada Y (2008) Preparation of gel film from Bombyx mori silk sericin and its characterization as a wound dressing, Biosci Biotechnol Biochem 72, 3189-3196. https://doi.org/10.1271/bbb.80375
- Teramoto H, Miyazawa M (2005) Molecular orientation behavior of silk sericin film as revealed by ATR infrared spectroscopy. Biomacromol 6, 2049-2057. https://doi.org/10.1021/bm0500547
- Vepari C, Kaplan DL (2007) Silk as a biomaterial, Prog Polym Sci 32, 991-1007. https://doi.org/10.1016/j.progpolymsci.2007.05.013
- Zhaorigetu S, Yanaka N, Sasaki M, Watanabe H, Kato N (2003) Silk protein, sericin, suppresses DMBA-TPA-induced mouse skin tumorigenesis by reducing oxidative stress, inflammatory responses and endogenous tumor promoter TNF-alpha, Oncol Rep 10, 537-543.
- Zhou CZ, Confalonieri F, Jacquet M, Perasso R, Li ZG, Janin J. (2001) Silk fibroin: Structural implications of a remarkable amino acid sequence, Proteins 44, 119-122. https://doi.org/10.1002/prot.1078
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