The DOI matches its Crossref record; 39 of the 40 references it cites were found in a registry or an index.
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
Open accessAbstract
Silk fibroin produced by the silkworm Bombyx mori consists of a heavy chain, a light chain, and a glycoprotein, P25. The heavy and light chains are linked by a disulfide bond, and P25 associates with disulfide-linked heavy and light chains by noncovalent interactions. Quantitative enzyme-linked immunosorbent assay revealed that molar ratios of the heavy chain, light chain, and P25 were 6:6:1, both in cocoons and in fibroin secreted into the lumen of posterior silk gland. Trace amounts of fibroin produced by three "naked pupa" mutants of B. mori lacked the light chain, but the molar ratio of heavy chain and P25 was also 6:1. Gel filtration chromatography and sedimentation equilibrium analysis demonstrated that a large protein complex of approximately 2.3 MDa, designated an elementary unit of fibroin having 6:6:1 molar ratios of the heavy chain, light chain, and P25, existed in posterior silk gland cells. Inaccessibility of biotinylated concanavalin A to the native elementary unit and partial dissociation of the elementary unit after incubation with excess N-glycosidase F or endoglycosidase H suggest that a single molecule of P25 is located internally and plays an important role in maintaining integrity of the complex.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The cited source says what the claim attributes to it.
In the citing paper
“At present, it is generally believed that silk fibroin is mainly composed of H chain, L chain, and P25 glycoprotein, with the molecular ratio of H:L:P25 = 6:6:1 [21].”
From Recent Advances in Silk Fibroin-Based Composites for Bone Repair Applications: A Review (2025) · cites this paper as [21]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
ASSEMBLY OF ASPARAGINE-LINKED OLIGOSACCHARIDES
Kornfeld, R., & Kornfeld, S. A. (1985) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.54.070185.003215 · Cited by 4,863
Setting the Standards: Quality Control in the Secretory Pathway
Ellgaard, L., Molinari, M., & Helenius, A. (1999) · Science · doi:10.1126/science.286.5446.1882 · Cited by 1,192
Maley, F., Trimble, R. B., Tarentino, A. L., & Plummer, T. H. (1989) · Analytical Biochemistry · doi:10.1016/0003-2697(89)90115-2 · Cited by 798
Molecular mechanisms of male germ cell differentiation
Hecht, N. B. (1998) · BioEssays · doi:10.1002/(sici)1521-1878(199807)20:7 · Cited by 434
Kreis, T. E., & Lodish, H. F. (1986) · Cell · doi:10.1016/0092-8674(86)90075-9 · Cited by 416
Assembly of influenza hemagglutinin trimers and its role in intracellular transport.
Copeland, C. S., Doms, R. W., Bolzau, E., Webster, R. G., & Helenius, A. (1986) · The Journal of Cell Biology · doi:10.1083/jcb.103.4.1179 · Cited by 400
Osawa, T., & Tsuji, T. (1987) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.56.070187.000321 · Cited by 357
[33] One-dimensional gel electrophoresis
Garfin, D. E. (1990) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(90)82035-z · Cited by 354
Copeland, C. S., Zimmer, K., Wagner, K. R., Healey, G. A., Mellman, I., & Helenius, A. (1988) · Cell · doi:10.1016/0092-8674(88)90381-9 · Cited by 274
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
Flagged first, then by citations
1 of the 40 references couldn’t be matched to a known paper.
Research works printed but not linked: 4
- Chevillard, 1986, Sericologia, 26, 435
- Yamamoto, 1998, Methods Mol. Biol., 76, 35
- Shimura, 1982, J. Seric. Sci. Jpn., 51, 20
- Gamo, 1985, J. Seric. Sci. Jpn., 54, 412
Cited by
Sorted by citations
Items 701–785 of 785
Mandal, B. B., & Kaplan, D. L. (2012) · CRC Press eBooks · doi:10.1201/b13687-8
Systemic Drug Delivery in Gastric Cancer
Li, R., & Yang, M. (2017) · Springer eBooks · doi:10.1007/978-981-10-3978-2_14
김형환 (2017) · Seoul National University Open Repository (Seoul National University)
Nanofibers: Biopolymeric Nanofibers for Tissue Engineering
Krishnamachari, Y. (2015) · Taylor & Francis eBooks · doi:10.1081/e-ebpp-120052539
Chapter 3: Enabling Biologics Combination Products: Device Ability in Protein Therapeutics
Pérez-Ramírez, B. (2020) · AAPS advances in the pharmaceutical sciences series · doi:10.1007/978-3-030-31415-6_3
Silk : a biopolymer for engineering nanoparticles
Wongpinyochit, T. (2019) · STAX · doi:10.48730/ke77-4m21
Bombyx mori silk: From mechanical properties to functionalities
Koh, L. D. (2015)
Collin, M. A. (2010) · eScholarship (California Digital Library)
Guo, K., Zhang, X., Zhao, D., Qin, L., Jiang, W., Hu, W., Liu, X., Xia, Q., Dong, Z., & Zhao, P. (2022) · SSRN Electronic Journal · doi:10.2139/ssrn.4003081
Mulberry silk fabric treatment with natural colorants
Sathish, P., & Jeyakodi Moses, J. (2021) · International Conference on Combinatorial and Optimization (ICCAP) · doi:10.4108/eai.7-12-2021.2314742
Burkinshaw, S. M. (2015) · doi:10.1002/9781118725658.ch12
钟伯雄, 余迎朴, 徐豫松, 俞鸿, 鲁兴萌, 缪云根, 杨君, 徐昊, 胡松年, & 楼程富 (2004) · Science in China Series C-Life Sciences (in Chinese) · doi:10.1360/zc2004-34-5-436
Hakimi, O., Vollrath, F. W., & Carr, A. J. (2019) · Elsevier eBooks · doi:10.1016/b978-0-444-64046-8.00299-8
Silk Fibers as Smart Materials Toward Medical Textiles
Tamada, Y., & Kojima, K. (2015) · Springer eBooks · doi:10.1007/978-981-4451-45-1_11
Breslauer, D. N., & Kaplan, D. L. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-803581-8.01494-6
Functionalization of Silk Fibroin as a Scaffold for Tissue Engineering and Regenerative Medicine
Kambe, Y. (2022) · Sen i Gakkaishi · doi:10.2115/fiber.78.240
RETRACTED: Discovering Intrinsic Magnetism of Silk Fibroins
Ranade, V., Choudhary, R. J., & Singh, K. P. (2024) · Macromolecular Symposia · doi:10.1002/masy.202300059
RetractedMasuoka, Y., Jouraku, A., Tsubota, T., Ono, H., Chiba, H., Sezutsu, H., Bono, H. U., & Yokoi, K. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.03.02.582034
Polvonova, G., Eshchanov, K., & Esomurodova, R. (2024) · International Journal of Advanced Chemistry · doi:10.14419/8ngyt551
Chen, Q., Zhao, H., Wen, M., Li, J., Zhou, H., Wang, J., Zhou, Y., Liu, Y., Du, L., Kang, H., et al. (2020) · Figshare · doi:10.6084/m9.figshare.11999028
Baci, G.-M., Ionascu, A., Rațiu, A. C., & Dezmirean, D. S. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.06.14.598941
Nanotechnology in Vaccine Development to Combat Bacterial Livestock Diseases
Varshney, R., Desai, D. N., Sulabh, S., Varshney, R., & Ghosh, M. (2024) · Livestock diseases and management · doi:10.1007/978-981-16-1610-5_13
Malla, I. A., Sahaf, K. A., Buhroo, Z. I., Bhat, B. A., Rashid, Z., & Masoodi, K. Z. (2024) · Agricultural Research · doi:10.1007/s40003-024-00783-x
Kim, Y. N., Park, J. W., Thi, D., Taghavian, A., Yoon, D., Kang, S.-K., Kim, S., Kim, K., & Koh, Y. H. (2024) · Journal of Asia-Pacific Entomology · doi:10.1016/j.aspen.2024.102358
Song, K., Zhang, H., Zhang, X., Li, Y., & Zhu, P. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.03.12.642793
NMR Studies on the Structure of Bombyx mori Silk Fibroin
Asakura, T. (2025) · Springer eBooks · doi:10.1007/978-981-97-6830-1_1
Kambe, Y. (2025) · Sen i Gakkaishi · doi:10.2115/fiber.81.p-216
Divergent and convergent evolution underlie the cocoon-spinning diversity
Cui, Y., Fang, G., Zhong, J. Q., Bai, X.-R., Xue, H., Yi, M., Chen, B.-Z., Zhu, Y.-N., Wang, W., Liu, Y., et al. (2025) · The Innovation Life · doi:10.59717/j.xinn-life.2025.100144
Genetic technologies in silkworm
Sezutsu, H., & Tsubota, T. (2025) · Elsevier eBooks · doi:10.1016/b978-0-323-95424-2.00067-4
Tong, X., Lei, C., Yin, M., Qiu, Q., Hu, X., Zhu, M., & Gong, C. (2025) · Insect Biochemistry and Molecular Biology · doi:10.1016/j.ibmb.2025.104424
Wild-type bacterial silk: a next-gen biomaterial beyond silkworm and spider silks
Abd-El-Haleem, D. A. M. (2025) · Biotechnology for Sustainable Materials · doi:10.1186/s44316-025-00032-3
Silk fibroin as a modulator of the amyloidogenic α-synuclein aggregationPreprint
Miali, M. E., Barak, Y., Fridmann-Sirkis, Y., Rosenhek‐Goldian, I., Brookstein, O., Eliaz, D., & Shimanovich, U. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.10.25.684501
The plasticisation model of dye diffusion: Part 8
Burkinshaw, S. M. (2025) · Coloration Technology · doi:10.1111/cote.70038
Breslauer, D. N. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-24738-5.00029-x
Fusion of silk fibroin light-chain N-terminus with heavy-chain repeats enhances hydrogel formation
Lin, X., Li, D., Xu, Z., Lu, Y., & Ye, Y. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.149652
Production of Silk Fibroin Membrane for Heavy Metal Removal in Water
Sudsandee, S., Dokmaingam, P., Mingkhwan, R., Kiangkoo, N., Worakhunpiset, S., Hu, C., Laohaprapanon, S., & Boonying, P. (2025) · Water Air & Soil Pollution · doi:10.1007/s11270-025-08960-6
Chen, Q., Zhao, H., Wen, M., Li, J., Zhou, H., Wang, J., Zhou, Y., Liu, Y., Du, L., Kang, H., et al. (2020) · Figshare · doi:10.6084/m9.figshare.11999022
Chen, Q., Zhao, H., Wen, M., Li, J., Zhou, H., Wang, J., Zhou, Y., Liu, Y., Du, L., Kang, H., et al. (2020) · Figshare · doi:10.6084/m9.figshare.11999031
Chen, Q., Zhao, H., Wen, M., Li, J., Zhou, H., Wang, J., Zhou, Y., Liu, Y., Du, L., Kang, H., et al. (2020) · Figshare · doi:10.6084/m9.figshare.11999082
Chen, Q., Zhao, H., Wen, M., Li, J., Zhou, H., Wang, J., Zhou, Y., Liu, Y., Du, L., Kang, H., et al. (2020) · Figshare · doi:10.6084/m9.figshare.11999040
Chen, Q., Zhao, H., Wen, M., Li, J., Zhou, H., Wang, J., Zhou, Y., Liu, Y., Du, L., Kang, H., et al. (2020) · Figshare · doi:10.6084/m9.figshare.11999103
Chen, Q., Zhao, H., Wen, M., Li, J., Zhou, H., Wang, J., Zhou, Y., Liu, Y., Du, L., Kang, H., et al. (2020) · Figshare · doi:10.6084/m9.figshare.11999067
Chen, Q., Zhao, H., Wen, M., Li, J., Zhou, H., Wang, J., Zhou, Y., Liu, Y., Du, L., Kang, H., et al. (2020) · Figshare · doi:10.6084/m9.figshare.11999061
Chen, Q., Zhao, H., Wen, M., Li, J., Zhou, H., Wang, J., Zhou, Y., Liu, Y., Du, L., Kang, H., et al. (2020) · Figshare · doi:10.6084/m9.figshare.11999055
Chen, Q., Zhao, H., Wen, M., Li, J., Zhou, H., Wang, J., Zhou, Y., Liu, Y., Du, L., Kang, H., et al. (2020) · Figshare · doi:10.6084/m9.figshare.11999046
Chen, Q., Zhao, H., Wen, M., Li, J., Zhou, H., Wang, J., Zhou, Y., Liu, Y., Du, L., Kang, H., et al. (2020) · Figshare · doi:10.6084/m9.figshare.11999097
Chen, X., Weng, H., Wang, J., Qu, Z., Wu, X., He, R., Cao, J., Zhou, W., & Ye, A. (2026) · Journal of Economic Entomology · doi:10.1093/jee/toag018
Tian, H., (23863), W. C., Liu, X., Lei, J., Guo, Y., Cheng, T., & Liu, C. (2026) · Journal of Resource Insects · doi:10.1016/j.jori.2026.100010
Xiang, Z., Guo, K., Xi, J., Xu, S., Duan, J., Wen, S., Liu, Z., Wang, X., Zhao, P., & Zhang, X. (2026) · Journal of Insect Physiology · doi:10.1016/j.jinsphys.2026.104962
Design and development of materials with controlled biodegradability for regenerative medicine
Goczkowski, M. (2017) · theses.fr (ABES) · doi:10.70675/ba057218za419z42a9z9062z063097b58717
Climate Resilience in Non-mulberry Sericulture: A Genomic Perspective
Prabhu, I. G., Sukhija, N., Kumar, V., Gadad, H. S., & Chowdary, N. B. (2026) · Springer eBooks · doi:10.1007/978-3-032-13890-3_17
Indian Silk: Origin, Properties, and Notable Handicrafts
Debnath, S., Kamble, M., Goutam, P., & Roychowdhury, R. (2026) · Textile science and clothing technology · doi:10.1007/978-3-032-16230-4_2
Puerta-González, A., Soto-Ospina, A., Montoya, Y., Bustamante, J., & Peláez, L. M. S. (2026) · Journal of Genetic Engineering and Biotechnology · doi:10.1016/j.jgeb.2026.100692
Tian, H., Chen, W., Li, J., Zhang, Y., Cheng, T., Zhang, W., & Liu, C. (2026) · Insect Biochemistry and Molecular Biology · doi:10.1016/j.ibmb.2026.104564
Majumder, S., & Sinha, S. N. (2026) · Smart nanomaterials technology · doi:10.1007/978-981-95-1135-8_7
Physicochemical Properties of Silk Proteins
Fasna, P. K., Navya, V. B., Krishnan, R., Anju, M., & Kumar, R. (2026) · Smart nanomaterials technology · doi:10.1007/978-981-95-1135-8_3
Silk Protein-Based Nano Carriers for Drug Delivery
Kallimani, C. S., Garai, I., Shravanilakshmi, V., & Satish, L. (2026) · Smart nanomaterials technology · doi:10.1007/978-981-95-1135-8_8
Extraction and Purification of Silk Proteins
Shruthi, D. G., Gowda, M., & NARAYANASWAMY, K. C. (2026) · Smart nanomaterials technology · doi:10.1007/978-981-95-1135-8_2
Takahashi, Y., Koyano, W., Fuji, T., Kozono, T., Sato, M., Yokoyama, T., & Ito, K. (2026) · SSRN Electronic Journal · doi:10.2139/ssrn.6827668
Application of Transgenic Silk Fibroin to Biomaterials
Asakura, T., Tanaka, T., 謙一郎, 立., & Sezutsu, H. (2026) · Biotechnology and Bioengineering · doi:10.1002/bit.70249
Eccles, L. E., Liwang, R. K., Orozco, A. A., Aikman, E. L., & Stoppel, W. L. (2026) · Biomacromolecules · doi:10.1021/acs.biomac.6c00328
Marchi, S. C., Dionísio, J. F., da Silva, S. A., Lopes, T. B. F., Aguiar, R. C. M., Pezenti, L. F., Semprebon, S. C., Mantovani, M. S., de Santana, H., Nascimento, C. C., et al. (2026) · Physiological Entomology · doi:10.1111/phen.70056
Baci, G.-M., Ionascu, A., Rațiu, A. C., & Dezmirean, D. S. (2026) · Insects · doi:10.3390/insects17070665
Application of silk fibroin-based drug delivery strategies in bone tissue engineering
Yao, Q., He, L., Zou, H., Tan, X., Bao, C., Xiang, S., Tang, F., & Ao, J. (2026) · Materials Today Chemistry · doi:10.1016/j.mtchem.2026.103773
Ou, Y., Zhang, P., Sheng, Y., YiXin, S. U. N., & Zhang, R. (2026) · Journal of Applied Polymer Science · doi:10.1002/app.71148
Deep Mutational Scanning for the Study and Engineering of Protein Assemblies
Wolfanger, J., Banerjee, S., & Mills, C. E. (2026) · Chemistry - Methods · doi:10.1002/cmtd.70144
Utilization of Silk in the Field of Medicine and Biotechnology
Paavana, O. S. K., Sruthi, S. P., & Nadar, M. S. A. M. (2026) · Textile science and clothing technology · doi:10.1007/978-3-032-26880-8_4
Silk Protein-Based Composite Materials for Biomedical Applications
Yumatov, E. N., Григорьевна, Е. Е., Leinveber, E. F., Финк, М. А., Raguzina, D. V., Закопайко, Б. А., Д., П. Э., & Викторович, Т. Д. (2026) · Nanobiotechnology Reports · doi:10.1134/s2635167626602500
Miao, B., Zhu, Z., & Liu, Y. (2026) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2026.154427
Silk fibroin as a biomaterial for drug delivery: From gland to clinic
Cheng, Q., Yan, C., Lu, L., Xu, L., Wu, Y., Miao, Y., Zhang, Q., Yang, T., Wei, T., Jiang, H., et al. (2026) · Progress in Materials Science · doi:10.1016/j.pmatsci.2026.101841 · Cited by 1
Wang, N., Wang, Y., Liu, N., Liu, W., Wang, Y., Li, X., Luo, Q., Zhang, X., Guo, P., Zhang, Y., et al. (2026) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.6c14733
Engineering silkworm–spider composite silk via the fibroin light chain fusion system in Bombyx mori
Yu, S., Cui, X., Jiang, N., Dai, X., Ye, X., Dai, X., Zhang, G., & Zhong, B. (2026) · Insect Science · doi:10.1111/1744-7917.70362
Applications of Biomaterials in Separators for Secondary Batteries
Choi, J., Mun, S. C., Choi, Y., & Won, J. H. (2026) · Carbon Energy · doi:10.1002/cey2.70337
Malki, J., Chalek, K. R., Ulloa, N. M., Tran, B. N. Q., & Holland, G. P. (2026) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.6c01363
Atmospheric degradation of historic cotton and silk textiles in museums: a review
Mouats, C. E., Chabas, A., & Petitmangin, A. (2026) · The European Physical Journal Plus · doi:10.1140/epjp/s13360-026-08371-4
Evidence of a Calcium-Chelating Protein Involved in Silkworm Silk Fiber Spinning
Allardyce, B. J., Linton, S. M., Wijesekara, D., Zaki, M., Holland, C., Faulder, H., & Rajkhowa, R. (2026) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.6c01458
Kumara, S. S. P., Nirala, N. S., Giri, S., & Kachroo, U. (2026) · International Journal of Polymeric Materials · doi:10.1080/00914037.2026.2742464
Mishra, P., & Singh, B. N. (2026) · Elsevier eBooks · doi:10.1016/b978-0-443-34207-3.00015-0
Metadata
- Authors
- Inoue, S., Tanaka, K., Arisaka, F., Kimura, S., Ohtomo, K., & Mizuno, S.
- Affiliations
- Tohoku University (JP)
- Tokyo Institute of Technology (JP)
- Chiba University (JP)
- Corresponding author
- Mizuno, Shigeki
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2000-12
- Volume
- 275
- Issue
- 51
- Pages
- 40517-40528
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2120240537
- Cited by
- 784
- References
- 40
- Citations by year
- 2026: 46 · 2025: 49 · 2024: 69 · 2023: 43 · 2022: 57 · 2021: 53 · 2020: 62 · 2019: 39 · 2018: 36 · 2017: 28 · 2016: 32 · 2015: 45 · 2014: 41 · 2013: 25 · 2012: 24
- FWCI
- 3.98
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Physical Sciences › Materials Science › Biomaterials › Silk-based biomaterials and applications
- Life Sciences › Agricultural and Biological Sciences › Insect Science › Silkworms and Sericulture Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein purification and stability
- Keywords
- silk fibroin, Bombyx mori, heavy chain, light chain, molar ratio, posterior silk gland, disulfide bonds, non-covalent interactions, protein complexes, N-glycosidase F, endoglycosidase H, concanavalin A, glycosylation
- MeSH terms
- Amino Acid Sequence, Animals, Base Sequence, Disulfides, DNA, Electrophoresis, Polyacrylamide Gel, Fibroins, Glycoproteins, Molecular Sequence Data, Molecular Weight, Oligosaccharides, Protein Conformation, Bombyx, Insect Proteins, Silk
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review