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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Non-equilibrium silk fibroin adhesives

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Identification of four small molecular mass proteins in the silk of Bombyx mori

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Revealing the Influence of the Degumming Process in the Properties of Silk Fibroin Nanoparticles

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Proteome analysis of silk gland proteins from the silkworm, Bombyx mori

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A fibroin secretion-deficient silkworm mutant, Nd-s, provides an efficient system for producing recombinant proteins

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Analytical markers for silk degradation: comparing historic silk and silk artificially aged in different environments

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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

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

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

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

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