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
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 101–200 of 785
Silk-Based Composite Scaffolds for Tissue Engineering Applications
Tandon, S., Kandasubramanian, B., & Ibrahim, S. M. (2020) · Industrial & Engineering Chemistry Research · doi:10.1021/acs.iecr.0c02195 · Cited by 93
Mobini, S., Hoyer, B., Solati‐Hashjin, M., Lode, A., Nosoudi, N., Samadikuchaksaraei, A., & Gelinsky, M. (2013) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.34537 · Cited by 89
Functional Material Features of Bombyx mori Silk Light versus Heavy Chain Proteins
Zafar, M. S., Belton, D. J., Hanby, B. V. T., Kaplan, D. L., & Perry, C. C. (2015) · Biomacromolecules · doi:10.1021/bm501667j · Cited by 88
Naturally Derived Biomaterials: Preparation and Application
Tran, H. L. B., Minh, T., Nguyen, D., & Minh, D. (2013) · InTech eBooks · doi:10.5772/55668 · Cited by 88
Biological Materials Processing: Time-Tested Tricks for Sustainable Fiber Fabrication
Rising, A., & Harrington, M. J. (2022) · Chemical Reviews · doi:10.1021/acs.chemrev.2c00465 · Cited by 89
Molecular architecture of silk fibroin of Indian golden silkmoth, Antheraea assama
Gupta, A. K., Mita, K., Arunkumar, K. P., & Nagaraju, J. (2015) · Scientific Reports · doi:10.1038/srep12706 · Cited by 87
Silk Fibroin Solution Properties Related to Assembly and Structure
Matsumoto, A., Lindsay, A., Abedian, B., & Kaplan, D. L. (2008) · Macromolecular Bioscience · doi:10.1002/mabi.200800020 · Cited by 87
Tatematsu, K., Kobayashi, I., Uchino, K., Sezutsu, H., Iizuka, T., Yonemura, N., & Tamura, T. (2009) · Transgenic Research · doi:10.1007/s11248-009-9328-2 · Cited by 86
An Insight on Silk Protein Sericin: From Processing to Biomedical Application
Ahsan, F., Ansari, T. M., Usmani, S. A., & Bagga, P. (2017) · Drug Research · doi:10.1055/s-0043-121464 · Cited by 84
Bio-inspired capillary dry spinning of regenerated silk fibroin aqueous solution
Wei, W., Zhang, Y., Zhao, Y., Luo, J., Shao, H., & Hu, X. (2011) · Materials Science and Engineering C · doi:10.1016/j.msec.2011.07.013 · Cited by 84
Silk Fibroin: A Promising Tool for Wound Healing and Skin Regeneration
Vidya, M., & Rajagopal, S. (2021) · International Journal of Polymer Science · doi:10.1155/2021/9069924 · Cited by 82
Dissolution and processing of silk fibroin for materials science
Wang, H., Zhang, Y., & Wei, Z.-G. (2021) · Critical Reviews in Biotechnology · doi:10.1080/07388551.2020.1853030 · Cited by 82
A germline transgenic silkworm that secretes recombinant proteins in the sericin layer of cocoon
Tomita, M., Hino, R., Ogawa, S., Iizuka, M., Adachi, T., Shimizu, K., Sotoshiro, H., & Yoshizato, K. (2007) · Transgenic Research · doi:10.1007/s11248-007-9087-x · Cited by 81
Eliaz, D., Paul, S., Benyamin, D., Cernescu, A., Cohen, S. R., Rosenhek-Goldian, I., Brookstein, O., Miali, M. E., Solomonov, A., Greenblatt, M., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-35505-w · Cited by 71
Wang, Z., Song, X., Cui, Y., Cheng, K., Tian, X., Dong, M., & Liu, L. (2021) · Journal of Colloid and Interface Science · doi:10.1016/j.jcis.2021.02.099 · Cited by 78
Advances in Preparation and Properties of Regenerated Silk Fibroin
Huang, L., Shi, J., Zhou, W., & Zhang, Q. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms241713153 · Cited by 86
Biosynthesis and cocoon-export of a recombinant globular protein in transgenic silkworms
Royer, C., Jalabert, A., Rocha, M. D., Grenier, A.-M., Mauchamp, B., Couble, P., & Chavancy, G. (2005) · Transgenic Research · doi:10.1007/s11248-005-4351-4 · Cited by 78
Guo, C., Zhang, J., Wang, X., Nguyen, A. T., Liu, X. Y., & Kaplan, D. L. (2017) · Small · doi:10.1002/smll.201702266 · Cited by 77
High Molecular Weight Silk Fibroin Prepared by Papain Degumming
Feng, Y., Lin, J., Niu, L., Wang, Y., Cheng, Z., Sun, X., & Li, M. (2020) · Polymers · doi:10.3390/polym12092105 · Cited by 77
Self-assembled silk fibroin hydrogels: from preparation to biomedical applications
Önder, Ö. C., Batool, S. R., & Nazeer, M. A. (2022) · Materials Advances · doi:10.1039/d2ma00568a · Cited by 79
CRISPR/Cas9 Initiated Transgenic Silkworms as a Natural Spinner of Spider Silk
Zhang, X., Xia, L., Day, B. A., Harris, T. I., Oliveira, P., Knittel, C., Licon, A. L., Gong, C., Dion, G., Lewis, R. V., et al. (2019) · Biomacromolecules · doi:10.1021/acs.biomac.9b00193 · Cited by 76
Biomaterials for Soft Tissue Repair and Regeneration: A Focus on Italian Research in the Field
Bonferoni, M. C., Caramella, C. M., Catenacci, L., Conti, B., Dorati, R., Ferrari, F., Genta, I., Modena, T., Perteghella, S., Rossi, S., et al. (2021) · Pharmaceutics · doi:10.3390/pharmaceutics13091341 · Cited by 78
Silk Fibroin–Substrate Interactions at Heterogeneous Nanocomposite Interfaces
Grant, A. M., Kim, H. S., Dupnock, T. L., Hu, K., Yingling, Y. G., & Tsukruk, V. V. (2016) · Advanced Functional Materials · doi:10.1002/adfm.201601268 · Cited by 75
Guo, K., Zhang, X., Zhao, D., Qin, L., Jiang, W., Hu, W., Liu, X., Xia, Q., Dong, Z., & Zhao, P. (2022) · Acta Biomaterialia · doi:10.1016/j.actbio.2022.07.021 · Cited by 74
Tough Photocrosslinked Silk Fibroin/Graphene Oxide Nanocomposite Hydrogels
Balu, R., Reeder, S., Knott, R. B., Mata, J. P., de Campo, L., Dutta, N. K., & Choudhury, N. R. (2018) · Langmuir · doi:10.1021/acs.langmuir.8b01141 · Cited by 74
Gandhi, M., Yang, H., Shor, L., & Ko, F. (2009) · Polymer · doi:10.1016/j.polymer.2009.02.022 · Cited by 73
Jo, Y., Kim, S., Kwon, K.-J., Kweon, H., Chae, W., Yang, W., Lee, E.-Y., & Seok, H. K. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18040858 · Cited by 73
Bucciarelli, A., Greco, G. H., Corridori, I., Pugno, N. M., & Motta, A. (2021) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.0c01657 · Cited by 71
Liu, J., Li, W., Jia, J. F., Tang, C., Wang, S., Yu, P., Zhang, Z., Ke, K., Bao, R., Liu, Z., et al. (2022) · Nano Energy · doi:10.1016/j.nanoen.2022.107787 · Cited by 72
Conservation of Silk Genes in Trichoptera and Lepidoptera
Yonemura, N., Mita, K., Tamura, T., & Sehnal, F. (2009) · Journal of Molecular Evolution · doi:10.1007/s00239-009-9234-5 · Cited by 80
Ion electrodiffusion governs silk electrogelation
Kojić, N., Panzer, M. J., Leisk, G. G., Raja, W. K., Kojić, M., & Kaplan, D. L. (2012) · Soft Matter · doi:10.1039/c2sm25783a · Cited by 72
A New Method for the Modification of Fibroin Heavy Chain Protein in the Transgenic Silkworm
Kojima, K., Kuwana, Y., Sezutsu, H., Kobayashi, I., Uchino, K., Tamura, T., & Tamada, Y. (2007) · Bioscience Biotechnology and Biochemistry · doi:10.1271/bbb.70353 · Cited by 72
Chirilă, T. V., Suzuki, S., Bray, L. J., Barnett, N. L., & Harkin, D. G. (2013) · Progress in Biomaterials · doi:10.1186/2194-0517-2-14 · Cited by 72
Identification of Bombyx mori sericin 4 protein as a new biological adhesive
Dong, Z., Guo, K., Zhang, X., Zhang, T., Zhang, Y., Ma, S., Chang, H., Tang, M., An, L., Xia, Q., et al. (2019) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2019.03.166 · Cited by 71
Hossain, K. S., Ochi, A., Ooyama, E., Magoshi, J., & Nemoto, N. (2003) · Biomacromolecules · doi:10.1021/bm020109u · Cited by 71
Kurihara, H., Sezutsu, H., Tamura, T., & Yamada, K. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.02.055 · Cited by 70
Ma, S., Shi, R., Wang, X., Liu, Y., Chang, J., Gao, J., Lü, W., Zhang, J., Zhao, P., & Xia, Q. (2014) · Scientific Reports · doi:10.1038/srep06867 · Cited by 70
Wang, F., Xu, H., Yuan, L., Ma, S., Wang, Y., Duan, X., Duan, J., Xiang, Z., & Xia, Q. (2013) · Transgenic Research · doi:10.1007/s11248-013-9695-6 · Cited by 70
Tubular lipid binding proteins (TULIPs) growing everywhere
Wong, L. H., & Levine, T. P. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.05.019 · Cited by 65
Tanaka, K., & Mizuno, S. (2001) · Insect Biochemistry and Molecular Biology · doi:10.1016/s0965-1748(00)00173-9 · Cited by 68
Hou, Y., Xia, Q., Zhao, P., Zou, Y., Liu, H., Guan, J., Gong, J., & Xiang, Z. (2007) · Insect Biochemistry and Molecular Biology · doi:10.1016/j.ibmb.2007.02.011 · Cited by 68
Potential use of natural silk for bio-dental applications
Zafar, M. S., & Al-Samadani, K. H. (2014) · Journal of Taibah University Medical Sciences · doi:10.1016/j.jtumed.2014.01.003 · Cited by 68
Kostag, M., Jedvert, K., & Seoud, O. A. E. (2020) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2020.11.151 · Cited by 66
Percot, A., Colomban, P., Paris, C., Dinh, H. M., Wojcieszak, M., & Mauchamp, B. (2014) · Vibrational Spectroscopy · doi:10.1016/j.vibspec.2014.05.004 · Cited by 65
Zhao, A., Zhao, T., Zhang, Y., Xia, Q., Lu, C., Zhou, Z., Xiang, Z., & Nakagaki, M. (2009) · Transgenic Research · doi:10.1007/s11248-009-9295-7 · Cited by 65
High-strength and ultra-tough whole spider silk fibers spun from transgenic silkworms
Mi, J., Zhou, Y., Ma, S., Zhou, X., Xu, S., Yang, Y.-C., Sun, Y., Xia, Q.-Y., Zhu, H.-N., Wang, S., et al. (2023) · Matter · doi:10.1016/j.matt.2023.08.013 · Cited by 59
Sadeghianmaryan, A., Ahmadian, N., Wheatley, S., Sardroud, H. A., Nasrollah, S. A. S., Naseri, E., & Ahmadi, A. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.131207 · Cited by 64
Rajabi, M., Firouzi, M., Hassannejad, Z., Haririan, I., & Zahedi, P. (2017) · Journal of Biomedical Materials Research Part B Applied Biomaterials · doi:10.1002/jbm.b.33968 · Cited by 64
On the Routines of Wild-Type Silk Fibroin Processing Toward Silk-Inspired Materials: A Review
Volkov, V., Ferreira, A. V., & Cavaco-Paulo, A. M. (2015) · Macromolecular Materials and Engineering · doi:10.1002/mame.201500179 · Cited by 63
You, R., Xu, Y., Liu, Y., Li, X., & Li, M. (2014) · Biomedical Materials · doi:10.1088/1748-6041/10/1/015003 · Cited by 63
Aznar‐Cervantes, S. D., Vicente-Cervantes, D., Meseguer‐Olmo, L., Cenís, J. L., & Pérez, A. A. L. (2013) · Materials Science and Engineering C · doi:10.1016/j.msec.2013.01.001 · Cited by 63
Fedič, R. (2003) · OpenGrey (Institut de l'Information Scientifique et Technique) · Cited by 63
Biodegradation behavior of silk fibroin membranes in repairing tympanic membrane perforations
Lee, O. J., Lee, J. M., Kim, J. H., Kim, J., Kweon, H., Jo, Y., & Park, C. H. (2012) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.33308 · Cited by 62
Aerogels and their applications
Montes, S., & Maleki, H. H. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-813357-6.00015-2 · Cited by 64
Zhao, X., Liu, C., Li, Q., Hu, W., Zhou, M., Nie, H., Zhang, Y., Peng, Z., Zhao, P., & Xia, Q. (2014) · PLoS ONE · doi:10.1371/journal.pone.0094091 · Cited by 61
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
NMR study of the structures of repeated sequences, GAGXGA (X = S, Y, V), in Bombyx mori liquid silk.
Suzuki, Y., Yamazaki, T., Aoki, A., Shindo, H., & Asakura, T. (2014) · Biomacromolecules · doi:10.1021/bm401346h · Cited by 55
Artificial superstrong silkworm silk surpasses natural spider silks
Wang, J., Fan, T., Li, X., Hu, X., Huang, W., Yuan, W., & Lin, Z. (2022) · Matter · doi:10.1016/j.matt.2022.08.028 · Cited by 60
A review of silk fibroin-based drug delivery systems and their applications
Yadav, R. H., Kenchegowda, M., Angolkar, M., Meghana, T. S., Osmani, R. A. M., Palaksha, S., & Gangadharappa, H. V. (2024) · European Polymer Journal · doi:10.1016/j.eurpolymj.2024.113286 · Cited by 60
Novel Molecular and Mechanical Properties of Egg Case Silk from Wasp Spider, Argiope bruennichi
Zhao, A., Zhao, T., Nakagaki, K., Zhang, Y., Sima, Y., Miao, Y., Shiomi, K., Kajiura, Z., Nagata, Y., Takadera, M., et al. (2006) · Biochemistry · doi:10.1021/bi052414g · Cited by 60
Zhu, Z., Kikuchi, Y., Kojima, K., Tamura, T., Kuwabara, N., Nakamura, T., & Asakura, T. (2010) · Journal of Biomaterials Science Polymer Edition · doi:10.1163/156856209x423126 · Cited by 60
Silk fibroin‐based films in food packaging applications: A review
Low, J. T., Yusoff, N. I. S. M., Othman, N., Wong, T., & Wahit, M. U. (2022) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.12939 · Cited by 58
Analysis of proteome dynamics inside the silk gland lumen of Bombyx mori
Dong, Z., Zhao, P., Zhang, Y., Song, Q., Zhang, X., Guo, P., Wang, D., & Xia, Q. (2016) · Scientific Reports · doi:10.1038/srep21158 · Cited by 59
Patel, M., Dubey, D. K., & Singh, S. P. (2019) · Materials Science and Engineering C · doi:10.1016/j.msec.2019.110414 · Cited by 59
Unique Molecular Architecture of Silk Fibroin in the Waxmoth,Galleria mellonella *
Žurovec, M., & Sehnal, F. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201622200 · Cited by 58
Wöltje, M., Kölbel, A., Aibibu, D., & Cherif, C. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221910565 · Cited by 58
Chirilă, T. V., Suzuki, S., & McKirdy, N. C. (2016) · Progress in Biomaterials · doi:10.1007/s40204-016-0052-8 · Cited by 58
Silk‐Based Biomaterials for Cardiac Tissue Engineering
Song, Y., Wang, H., Yue, F., Lv, Q., Cai, B., Dong, N., Wang, Z., & Wang, L. (2020) · Advanced Healthcare Materials · doi:10.1002/adhm.202000735 · Cited by 57
Zhao, X., Liu, C., Jiang, L., Li, Q., Zhou, M., Cheng, T., Mita, K., & Xia, Q. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.606921 · Cited by 57
The Design of Silk Fiber Composition in Moths Has Been Conserved for More Than 150 Million Years
Yonemura, N., & Sehnal, F. (2006) · Journal of Molecular Evolution · doi:10.1007/s00239-005-0119-y · Cited by 57
Mimicking biopolymers on a molecular scale: nano(bio)technology based on engineered proteins
Grunwald, I., Rischka, K., Kast, S. M., Scheibel, T., & Bargel, H. (2009) · Philosophical Transactions of the Royal Society A Mathematical Physical and Engineering Sciences · doi:10.1098/rsta.2009.0012 · Cited by 57
A single-cell transcriptomic atlas characterizes the silk-producing organ in the silkworm
Ma, Y., Zeng, W., Ba, Y., Luo, Q., Ou, Y., Liu, R., Ma, J., Tang, Y., Hu, J. H., Wang, H., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31003-1 · Cited by 56
Silk as a leading-edge biological macromolecule for improved drug delivery
Pandey, V., Haider, T., Jain, P., Gupta, P. N., & Soni, V. (2019) · Journal of Drug Delivery Science and Technology · doi:10.1016/j.jddst.2019.101294 · Cited by 56
Chen, W., Priewalder, H., John, J. P. P., & Lübec, G. (2009) · PROTEOMICS · doi:10.1002/pmic.200900624 · Cited by 55
Wang, F., Xu, H., Wang, Y., Wang, R., Yuan, L., Ding, H., Song, C., Ma, S., Peng, Z., Peng, Z., et al. (2014) · Acta Biomaterialia · doi:10.1016/j.actbio.2014.06.031 · Cited by 55
The Fractal Network Structure of Silk Fibroin Molecules and Its Effect on Spinning of Silkworm Silk.
Yang, S., Zhao, C., Yang, Y.-H., Ren, J., & Ling, S.-J. (2023) · ACS Nano · doi:10.1021/acsnano.3c00105 · Cited by 51
Improving the properties of natural fibres by chemical treatments
Rippon, J. A., & Evans, D. J. (2012) · Elsevier eBooks · doi:10.1533/9780857095510.1.63 · Cited by 54
Mao, M., Ahrens, L., Luka, J., Contreras, F., Kurkina, T., Bienstein, M., Sárria, M. P., Schirinzi, G. F., Méhn, D., Valsesia, A., et al. (2024) · Chemical Society Reviews · doi:10.1039/d2cs00991a · Cited by 53
Primary low grade B-cell lymphoma of the dura in an immunocompetent patient.
Altundag, M. K., Ozişik, Y., Yalçın, S. S., Akyol, F. H., & Uner, A. (2000) · PubMed · Cited by 50
Emerging trends in silk fibroin based nanofibers for impaired wound healing
Sabarees, G., Tamilarasi, G. P., Velmurugan, V., Alagarsamy, V., Sibuh, B. Z., Sikarwar, M., Taneja, P., Kumar, A., & Gupta, P. K. (2022) · Journal of Drug Delivery Science and Technology · doi:10.1016/j.jddst.2022.103994 · Cited by 52
Ma, L., Sun, Y., Cheng, Q., Yang, Z., Wang, J., Xu, Z., Yang, M., & Shuai, Y. (2023) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.3c04067 · Cited by 51
Chung, T., & Chang, Y. L. (2010) · Journal of Materials Science Materials in Medicine · doi:10.1007/s10856-009-3876-0 · Cited by 51
Maerten, C., Jierry, L., Schaaf, P., & Boulmedais, F. (2017) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.7b06319 · Cited by 51
Composite silk fibroin hydrogel scaffolds for cartilage tissue regeneration
Montaseri, Z., Abolmaali, S. S., Tamaddon, A. M., & Farvadi, F. (2022) · Journal of Drug Delivery Science and Technology · doi:10.1016/j.jddst.2022.104018 · Cited by 50
Autonomous Bioelectronic Devices Based on Silk Fibroin
Wang, Y., Feng, X., & Chen, X. (2025) · Advanced Materials · doi:10.1002/adma.202500073 · Cited by 50
Ohno, K., Sawada, J.-I., Takiya, S., Kimoto, M., Matsumoto, A., Tsubota, T., Uchino, K., Hui, C., Sezutsu, H., Handa, H., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.514471 · Cited by 50
Chang, H., Cheng, T., Wu, Y., Hu, W., Long, R., Liu, C., Zhao, P., & Xia, Q. (2015) · PLoS ONE · doi:10.1371/journal.pone.0139424 · Cited by 50
Badillo-Sanchez, D. A., Chelazzi, D., Giorgi, R., Cincinelli, A., & Baglioni, P. (2018) · Polymer Degradation and Stability · doi:10.1016/j.polymdegradstab.2018.09.022 · Cited by 50
Antimicrobial components in the cocoon silk of silkworm, Bombyx mori
Dong, Z., Xia, Q., & Zhao, P. (2022) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2022.10.103 · Cited by 49
Walker, A., Holland, C., & Sutherland, T. (2015) · Proceedings of the Royal Society of London. Biological Sciences · doi:10.1098/rspb.2015.0259 · Cited by 51
Zuluaga‐Vélez, A., Cómbita-Merchán, D. F., Buitrago‐Sierra, R., Santa, J. F., Aguilar-Fernández, E., & Arias, J. C. (2019) · PLoS ONE · doi:10.1371/journal.pone.0213303 · Cited by 49
Porous 3‐D scaffolds from regenerated Antheraea pernyi silk fibroin
Li, M., Tao, W., Lu, S., & Zhao, C. (2007) · Polymers for Advanced Technologies · doi:10.1002/pat.998 · Cited by 49
Solomun, J. I., Totten, J. D., Wongpinyochit, T., Florence, A. J., & Seib, F. (2020) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.0c00202 · Cited by 43
Challenges and opportunities of silk protein hydrogels in biomedical applications
Liu, J., Ge, X., Liu, L., Xu, W., & Shao, R. (2022) · Materials Advances · doi:10.1039/d1ma00960e · Cited by 48
Zhong, T., Jiang, Z., Wang, P., Bie, S., Zhang, F., & Zuo, B. (2015) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2015.08.035 · Cited by 48
Lai, Y., Xiao, X., Huang, Z., Duan, H., Yang, L., Yang, Y.-C., Li, C., & Feng, L. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms252312567 · Cited by 58
Moriya, M., Roschzttardtz, F., Nakahara, Y., Saitô, H., Masubuchi, Y., & Asakura, T. (2009) · Biomacromolecules · doi:10.1021/bm801442g · Cited by 47
Production of Bombyx mori Silk Fibroin Incorporated with Unnatural Amino Acids
Teramoto, H., & Kojima, K. (2014) · Biomacromolecules · doi:10.1021/bm5005349 · Cited by 47
Chakraborty, J., & Ghosh, S. (2020) · ACS Applied Bio Materials · doi:10.1021/acsabm.0c01252 · Cited by 48
β‐Silks: Enhancing and Controlling Aggregation
Dicko, C., Kenney, J. M., & Vollrath, F. W. (2006) · Advances in protein chemistry · doi:10.1016/s0065-3233(06)73002-9 · Cited by 47
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