Silk Fibroin of Bombyx mori Is Secreted, Assembling a High Molecular Mass Elementary Unit Consisting of H-chain, L-chain, and P25, with a 6:6:1 Molar Ratio

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Mechanism of the growth and development of the posterior silk gland and silk secretion revealed by mutation of the fibroin light chain in silkworm

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Nanopatterned silk fibroin films with high transparency and high haze for optical applications

Malinowski, C. B., He, F., Zhao, Y., Chang, I., Hatchett, D. W., Zhai, S., & Zhao, H. J. (2019) · RSC Advances · doi:10.1039/c9ra07391d · Cited by 28

A Comparison of Co-expression Networks in Silk Gland Reveals the Causes of Silk Yield Increase During Silkworm Domestication

Zhou, Q., Fu, P., Li, S.-S., Zhang, C.-J., Yu, Q., Qiu, C.-Z., Zhang, H., & Zhang, Z. (2020) · Frontiers in Genetics · doi:10.3389/fgene.2020.00225 · Cited by 29

Chain-folded lamellar structure and dynamics of the crystalline fraction of Bombyx mori silk fibroin and of (Ala-Gly-Ser-Gly-Ala-Gly)n model peptides

Asakura, T., Ogawa, T., Naito, A., & Williamson, M. P. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.08.220 · Cited by 28

Genetic hybridization of highly active exogenous functional proteins into silk-based materials using “light-clothing” strategy

Long, D., Cheng, X., Hao, Z., Sun, J., Diane, U., Liu, Y., Chen, L., Xiang, Z., Yang, F., & Zhao, A. (2021) · Matter · doi:10.1016/j.matt.2021.03.020 · Cited by 28

Recent progress in silk-based biosensors

Ru, M., Hai, A. M., Wang, L., Yan, S., & Zhang, Q. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.10.134 · Cited by 28

Decoding silkworm spinning programmed by pH and metal ions

Song, K., Wang, Y., Dong, W., Li, Z., Xia, Q., Zhu, P., & He, H. (2023) · 中国科学通报：英文版 · doi:10.1016/j.scib.2023.12.050 · Cited by 28

Prospects of the practical use of silk sericins

Sehnal, F. (2008) · Entomological Research · doi:10.1111/j.1748-5967.2008.00168.x · Cited by 28

Dimerization of Terminal Domains in Spiders Silk Proteins Is Controlled by Electrostatic Anisotropy and Modulated by Hydrophobic Patches

Kurut, A., Dicko, C., & Lund, M. (2015) · ACS Biomaterials Science & Engineering · doi:10.1021/ab500039q · Cited by 27

Nuclear hormone receptor BmFTZ-F1 is involved in regulating the fibroin heavy chain gene in the silkworm, Bombyx mori

Zhou, C., Zha, X., Shi, P., Zhao, P., He, W., Zheng, R., & Xia, Q. (2016) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2016.07.025 · Cited by 27

Identification and comparison of long non‐coding RNAs in the silk gland between domestic and wild silkworms

Zhou, Q., Fang, S., Zhang, Q., Yu, Q., & Zhang, Z. (2017) · Insect Science · doi:10.1111/1744-7917.12443 · Cited by 27

Hybrid fibroin-nanocellulose composites for the consolidation of aged and historical silk

Cianci, C., Chelazzi, D., Poggi, G., Modi, F., Giorgi, R., & Laurati, M. (2021) · Colloids and Surfaces A Physicochemical and Engineering Aspects · doi:10.1016/j.colsurfa.2021.127944 · Cited by 27

High Performance Marine and Terrestrial Bioadhesives and the Biomedical Applications They Have Inspired

Melrose, J. (2022) · Molecules · doi:10.3390/molecules27248982 · Cited by 27

A New Silkworm Race for Sericin Production, “Sericin Hope” and its Product, “Virgin Sericin”

Mase, K., Iizuka, T., Okada, E., Miyajima, T., & Yamamoto, T. (2006) · Journal of insect biotechnology and sericology · doi:10.11416/jibs.75.85 · Cited by 27

Silk Gland Development and Regulation of Silk Protein Genes

Julien, E., Coulon-Bublex, M., Garel, A., Royer, C., Chavancy, G., Prudhomme, J. C., & Couble, P. (2005) · Elsevier eBooks · doi:10.1016/b0-44-451924-6/00022-3 · Cited by 27

Effect of different cocoon stifling methods on the properties of silk fibroin biomaterials

Aznar‐Cervantes, S. D., Pagán, A., Santesteban, B. M., & Cenís, J. L. (2019) · Scientific Reports · doi:10.1038/s41598-019-43134-5 · Cited by 27

Structure and function of 5′-flanking regions of Bombyx mori fibroin heavy chain gene: Identification of a novel transcription enhancing element with a homeodomain protein-binding motif

Shimizu, K., Ogawa, S., Hino, R., Adachi, T., Tomita, M., & Yoshizato, K. (2007) · Insect Biochemistry and Molecular Biology · doi:10.1016/j.ibmb.2007.03.016 · Cited by 27

Silk Fibroin Bombyx mori is Secreted Assembling a High Molecular-Mass Elementary Unit Consisting of H-chain, L-chain and P25, with 6:6:1 Molar Ratios

有坂, 文., & Arisaka, F. (2000) · Institutional Repositories DataBase (IRDB)

Assembly of the silk fibroin elementary unit in endoplasmic reticulum and a role of L‐chain for protection of α1,2‐mannose residues in N‐linked oligosaccharide chains of fibrohexamerin/P25

Inoue, S., Tanaka, K., Tanaka, H., Ohtomo, K., Kanda, T., Imamura, M., Quan, G.-X., Kojima, K., Yamashita, T., Nakajima, T., et al. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03934.x · Cited by 55

Hydrophobic interaction of P25, containing Asn-linked oligosaccharide chains, with the H-L complex of silk fibroin produced by Bombyx mori.

Tanaka, K., Inoue, S., & Mizuno, S. (1999) · Insect Biochemistry and Molecular Biology · doi:10.1016/s0965-1748(98)00135-0 · Cited by 212

Determination of the site of disulfide linkage between heavy and light chains of silk fibroin produced by Bombyx mori

Tanaka, K., Kajiyama, N., Ishikura, K., Waga, S., Kikuchi, A., Ohtomo, K., Takagi, T., & Mizuno, S. (1999) · Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology · doi:10.1016/s0167-4838(99)00088-6 · Cited by 259

Homologues of fibroin L-chain and P25 of Bombyx mori are present in Dendrolimus spectabilis and Papilio xuthus but not detectable in Antheraea yamamai.

Tanaka, K., & Mizuno, S. (2001) · Insect Biochemistry and Molecular Biology · doi:10.1016/s0965-1748(00)00173-9 · Cited by 68