Reduction of ectopic bone growth in critically-sized rat mandible defects by delivery of rhBMP-2 from kerateine biomaterials
Open accessAbstract
Absorbable collagen sponges (ACS) are used clinically as carriers of recombinant human bone morphogenetic protein 2 (rhBMP-2) to promote bone regeneration. ACS exhibit ectopic bone growth due to delivery of supraphysiological levels of rhBMP-2, which is particularly problematic in craniofacial bone injuries for both functional and esthetic reasons. We hypothesized that hydrogels from the reduced form of keratin proteins (kerateine) would serve as a suitable alternative to ACS carriers of rhBMP-2. The rationale for this hypothesis is that keratin biomaterials degrade slowly in vivo, have modifiable material properties, and have demonstrated capacity to deliver therapeutic agents. We investigated kerateine hydrogels and freeze-dried scaffolds as rhBMP-2 carriers in a critically-sized rat mandibular defect model. ACS, kerateine hydrogels, and kerateine scaffolds loaded with rhBMP-2 achieved bridging in animals by 8 weeks as indicated by micro-computed tomography. Kerateine scaffolds achieved statistically increased bone mineral density compared to ACS and kerateine hydrogels, with levels reaching those of native bone. Importantly, both kerateine hydrogels and kerateine scaffolds had significantly less ectopic bone growth than ACS sponges at both 8 and 16 weeks post-operatively. These studies demonstrate the suitability of keratins as rhBMP-2 carriers due to equal regenerative capacity with reduced ectopic growth compared to ACS.
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Keratin scaffolds lacking rhBMP-2 do not lead to bridging in this critically-sized rat femur defect model.
“We confirmed previous studies showing that keratin scaffolds lacking rhBMP-2 do not lead to bridging in this critically-sized defected model.”
From Keratin Scaffold Formulation Impacts rhBMP-2 Biodistribution and Bone Regeneration in a Rat Femur Defect Model (2025) · cites this paper as [20]
Results §3.4 reports that kerateine scaffolds without rhBMP-2 did not heal the critically sized defect by 16 weeks. However, the studied defects were in rat mandibles, not femurs, so the source does not establish the claim for a femur model. (LLM, conf=0.90)
Experimental — accuracy not yet measuredFormulations with more KOS or KTN with rhBMP-2 showed lower levels of callous outside of the defect site.
“This is likely because formulations with more KOS or KTN with rhBMP-2 showed lower levels of callous outside of the defect site (Figs. 1 and 2), similar to previous observations with KTN in a mandible model [20].”
From Keratin Scaffold Formulation Impacts rhBMP-2 Biodistribution and Bone Regeneration in a Rat Femur Defect Model (2025) · cites this paper as [20]
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Cites
Biomaterials Science: An Introduction to Materials in Medicine
Ratner, B. D., Hoffman, A. S., Schöen, F. J., & Lemons, J. E. (1996) · doi:10.1016/c2009-0-02433-7 · Cited by 5,125 · see citing works
Katagiri, T. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.127.6.1755 · Cited by 1,452 · see citing works
A Review of Keratin-Based Biomaterials for Biomedical Applications
Rouse, J. G., & Dyke, M. E. V. (2010) · Materials · doi:10.3390/ma3020999 · Cited by 662 · see citing works
McKay, W. F., Peckham, S. M., & Badura, J. M. (2007) · International Orthopaedics · doi:10.1007/s00264-007-0418-6 · Cited by 617 · see citing works
Some properties of keratin biomaterials: Kerateines
Hill, P., Brantley, H., & Van Dyke, M. (2010) · Biomaterials · doi:10.1016/j.biomaterials.2009.09.076 · Cited by 349 · cited 1× · see citing works
“, cystine), which results in a stable, crosslinked hydrogel [17].”
Crewther, W. G., Fraser, R., Lennox, F. G., & Lindley, H. (1965) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60390-3 · Cited by 306 · see citing works
Zhang, Z., Li, G., & Shi, B. (2006) · Journal of The Society of Leather Technologists and Chemists · Cited by 285 · see citing works
Kempen, D. H. R., Lu, L., Hefferan, T. E., Creemers, L. B., Maran, A., Classic, K. L., Dhert, W. J. A., & Yaszemski, M. J. (2008) · Biomaterials · doi:10.1016/j.biomaterials.2008.04.031 · Cited by 276 · see citing works
Osteoprogenitor cells within skeletal muscle
Bosch, P. P., Musgrave, D. S., Lee, J. Y., Cummins, J., Shuler, F. D., Ghivizzani, S. C., Evans, C., Robbins, P. D., & Huard, J. (2000) · Journal of Orthopaedic Research® · doi:10.1002/jor.1100180613 · Cited by 270 · see citing works
Delivery Systems for BMPs: Factors Contributing to Protein Retention at an Application Site
Uludağ, H., Gao, T., Porter, T. J., Frieß, W., & Wozney, J. M. (2001) · Journal of Bone and Joint Surgery · doi:10.2106/00004623-200100002-00007 · Cited by 208 · see citing works
Mechanical and biological properties of keratose biomaterials
de Guzman, R. C., Merrill, M. R., Richter, J. R., Hamzi, R. I., Greengauz-Roberts, O. K., & Van Dyke, M. E. (2011) · Biomaterials · doi:10.1016/j.biomaterials.2011.07.054 · Cited by 166 · see citing works
Brown, K. V., Li, B., Guda, T., Perrien, D. S., Guelcher, S. A., & Wenke, J. C. (2011) · Tissue Engineering Part A · doi:10.1089/ten.tea.2010.0446 · Cited by 158 · see citing works
Characterization of absorbable collagen sponges as rhBMP-2 carriers
Frieß, W. (1999) · International Journal of Pharmaceutics · doi:10.1016/s0378-5173(99)00174-x · Cited by 149 · see citing works
Lew, T. A., Walker, J. A., Wenke, J. C., Blackbourne, L. H., & Hale, R. G. (2009) · Journal of Oral and Maxillofacial Surgery · doi:10.1016/j.joms.2009.06.006 · Cited by 148 · see citing works
Bone regeneration with BMP-2 delivered from keratose scaffolds
de Guzman, R. C., Saul, J. M., Ellenburg, M. D., Merrill, M. R., Coan, H. B., Smith, T. L., & Van Dyke, M. E. (2013) · Biomaterials · doi:10.1016/j.biomaterials.2012.11.002 · Cited by 147 · see citing works
Self-citationAdverse Events Reported After the Use of Recombinant Human Bone Morphogenetic Protein 2
Woo, E. J. (2011) · Journal of Oral and Maxillofacial Surgery · doi:10.1016/j.joms.2011.09.008 · Cited by 121 · see citing works
Anitha, T. S., & Palanivelu, P. (2013) · Protein Expression and Purification · doi:10.1016/j.pep.2013.01.007 · Cited by 121 · see citing works
Keratin hydrogels support the sustained release of bioactive ciprofloxacin
Saul, J. M., Ellenburg, M. D., de Guzman, R. C., & Dyke, M. V. (2011) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.33147 · Cited by 111 · cited 1× · see citing works
“Furthermore, we have previously observed, and confirmed in this report, a correlation between the rate of hydrogel degradation and the rate of therapeutic agent delivery [21,22].”
Self-citationCraniofacial and Skull Base Trauma
Katzen, J. T., Jarrahy, R., Eby, J. B., Mathiasen, R. A., Margulies, D. R., & Shahinian, H. K. (2003) · The Journal of Trauma: Injury, Infection, and Critical Care · doi:10.1097/01.ta.0000066180.14666.8b · Cited by 99 · see citing works
Interleukin-1 induces major phenotypic changes in human skin microvascular endothelial cells
Romero, L. I., Zhang, D.-N., Herron, G. S., & Karasek, M. A. (1997) · Journal of Cellular Physiology · doi:10.1002/(sici)1097-4652(199710)173:1 · Cited by 88 · see citing works
The effects of carrier nature and pH on rhBMP-2-induced ectopic bone formation
Luca, L., Rougemont, A., Walpoth, B. H., Gurny, R., & Jordan, O. (2010) · Journal of Controlled Release · doi:10.1016/j.jconrel.2010.06.011 · Cited by 85 · see citing works
Bone morphogenic protein and its application in trauma cases: A current concept update
Bagaria, V. B., Patil, N., Vikram, S., & Chadda, A. (2007) · Injury · doi:10.1016/j.injury.2006.12.012 · Cited by 73 · see citing works
The proteomics of keratin proteins
Plowman, J. E. (2006) · Journal of Chromatography B · doi:10.1016/j.jchromb.2006.07.055 · Cited by 61 · see citing works
Comparison of BMP‐2 and ‐4 for rat mandibular bone regeneration at various doses1
Arosarena, O. A., & Collins, W. L. (2005) · Orthodontics and Craniofacial Research · doi:10.1111/j.1601-6343.2005.00349.x · Cited by 58 · see citing works
Periosteal BMP2 activity drives bone graft healing
Chappuis, V., Gamer, L. W., Cox, K. A., Lowery, J. W., Bosshardt, D. D., & Rosen, V. (2012) · Bone · doi:10.1016/j.bone.2012.07.017 · Cited by 57 · see citing works
Wegman, F., Geuze, R. E., van der Helm, Y. J. M., Öner, F. C., Dhert, W. J. A., & Alblas, J. (2012) · Journal of Tissue Engineering and Regenerative Medicine · doi:10.1002/term.1571 · Cited by 52 · see citing works
Kumar, R., Balaji, S., Sivagnanam, U. T., Mandal, A. B., & Sehgal, P. K. (2008) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-008-8452-4 · Cited by 51 · see citing works
Wen, B., Karl, M., Pendrys, D. G., Shafer, D. M., Freilich, M., & Kuhn, L. T. (2011) · Journal of Biomedical Materials Research Part B Applied Biomaterials · doi:10.1002/jbm.b.31817 · Cited by 39 · see citing works
Cutter, C. S., & Mehrara, B. J. (2006) · Journal of Long-Term Effects of Medical Implants · doi:10.1615/jlongtermeffmedimplants.v16.i3.50 · Cited by 39 · see citing works
The Proteome of the Wool Cuticle
Koehn, H., Clerens, S., Deb‐Choudhury, S., Morton, J. D., Dyer, J. M., & Plowman, J. E. (2010) · Journal of Proteome Research · doi:10.1021/pr901106m · Cited by 38 · see citing works
The American Society of Plastic Surgeons’ Procedural Statistics: What They Really Mean
Rohrich, R. J. (2003) · Plastic & Reconstructive Surgery · doi:10.1097/01.prs.0000084284.02024.3b · Cited by 35 · see citing works
Cellular invasion and breakdown of three different collagen films in the lumbar muscle of the rat
Gorham, S. D., Hyland, T. P., French, D. A., & Willins, M. J. (1990) · Biomaterials · doi:10.1016/0142-9612(90)90125-a · Cited by 33 · see citing works
Massive Facial Trauma following Improvised Explosive Device Blasts in Operation Iraqi Freedom
Salinas, N. L., Brennan, J. A., & Gibbons, M. D. (2011) · Otolaryngology · doi:10.1177/0194599811400575 · Cited by 17 · see citing works
Flagged first, then by citations
1 of the 34 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Polymeric hydrogel systems as emerging biomaterial platforms to enable hemostasis and wound healing
Pourshahrestani, S., Zeimaran, E., Kadri, N. A., Mutlu, N., & Boccaccini, A. R. (2020) · Advanced Healthcare Materials · doi:10.1002/adhm.202000905 · Cited by 448 · see citing works
Silk as a potential candidate for bone tissue engineering
Mottaghitalab, F., Hosseinkhani, H., Shokrgozar, M. A., Mao, C., Yang, M., & Farokhi, M. (2015) · Journal of Controlled Release · doi:10.1016/j.jconrel.2015.07.031 · Cited by 191 · see citing works
Ju, W., Hao, S., Luo, T., Cheng, Z., Li, W., Gao, F., Guo, T., Gong, Y., & Wang, B. (2016) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2016.10.038 · Cited by 184 · see citing works
Kowalczewski, C. J., & Saul, J. M. (2018) · Frontiers in Pharmacology · doi:10.3389/fphar.2018.00513 · Cited by 170 · see citing works
Self-citationA review on carrier systems for bone morphogenetic protein‐2
Agrawal, V., & Sinha, M. (2016) · Journal of Biomedical Materials Research Part B Applied Biomaterials · doi:10.1002/jbm.b.33599 · Cited by 136 · see citing works
Keratinous materials: Structures and functions in biomedical applications
Rajabi, M., Ali, A., McConnell, M. A., & Cabral, J. D. (2020) · Materials Science and Engineering C · doi:10.1016/j.msec.2019.110612 · Cited by 134 · see citing works
Tunable Keratin Hydrogels for Controlled Erosion and Growth Factor Delivery
Ham, T. R., Lee, R. T., Han, S., Haque, S., Vodovotz, Y., Gu, J., Burnett, L. R., Tomblyn, S., & Saul, J. M. (2016) · Biomacromolecules · doi:10.1021/acs.biomac.5b01328 · Cited by 111 · see citing works
Self-citationKeratin Hydrogel Enhances In Vivo Skeletal Muscle Function in a Rat Model of Volumetric Muscle Loss
Passipieri, J. A., Baker, H. B., Siriwardane, M. L., Ellenburg, M. D., Vadhavkar, M., Saul, J. M., Tomblyn, S., Burnett, L., & Christ, G. J. (2017) · Tissue Engineering Part A · doi:10.1089/ten.tea.2016.0458 · Cited by 93 · see citing works
Self-citationComparative study of keratin extraction from human hair
Agarwal, V., Panicker, A. G., Indrakumar, S., & Chatterjee, K. (2019) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2019.04.098 · Cited by 94 · see citing works
Han, S., Ham, T. R., Haque, S., Sparks, J. L., & Saul, J. M. (2015) · Acta Biomaterialia · doi:10.1016/j.actbio.2015.05.013 · Cited by 91 · see citing works
Self-citationTomblyn, S., Kneller, E. L. P., Walker, S. J., Ellenburg, M. D., Kowalczewski, C. J., Dyke, M. E. V., Burnett, L., & Saul, J. M. (2015) · Journal of Biomedical Materials Research Part B Applied Biomaterials · doi:10.1002/jbm.b.33438 · Cited by 78 · see citing works
Self-citationCellulose/keratin–catechin nanocomposite hydrogel for wound hemostasis
Sun, Z., Chen, X., Ma, X., Cui, X., Zeng, Y., & Li, X. (2018) · Journal of Materials Chemistry B · doi:10.1039/c8tb01109e · Cited by 77 · see citing works
Natural polymers in wound healing: From academic studies to commercial products
Tavakoli, M., Labbaf, S., Mirhaj, M., Salehi, S., Seifalian, A. M., & Firuzeh, M. (2023) · Journal of Applied Polymer Science · doi:10.1002/app.53910 · Cited by 74 · see citing works
Development and assessment of kerateine nanoparticles for use as a hemostatic agent
Luo, T., Hao, S., Chen, X., Wang, J., Yang, Q., Wang, Y., Weng, Y., Wei, H., Zhou, J., & Wang, B. (2016) · Materials Science and Engineering C · doi:10.1016/j.msec.2016.03.007 · Cited by 68 · see citing works
Baker, H. B., Passipieri, J. A., Siriwardane, M. L., Ellenburg, M. D., Vadhavkar, M., Bergman, C. R., Saul, J. M., Tomblyn, S., Burnett, L., & Christ, G. J. (2017) · Tissue Engineering Part A · doi:10.1089/ten.tea.2016.0457 · Cited by 67 · see citing works
Self-citationLi, Y., Wang, Y., Ye, J., Yuan, J., & Xiao, Y. (2016) · Materials Science and Engineering C · doi:10.1016/j.msec.2016.05.117 · Cited by 57 · see citing works
An overview of de novo bone generation in animal models
Taguchi, T., & Lopez, M. J. (2020) · Journal of Orthopaedic Research® · doi:10.1002/jor.24852 · Cited by 55 · see citing works
The Hair Follicle: An Underutilized Source of Cells and Materials for Regenerative Medicine
Kiani, M. T., Higgins, C. A., & Almquist, B. D. (2017) · ACS Biomaterials Science & Engineering · doi:10.1021/acsbiomaterials.7b00072 · Cited by 51 · see citing works
A standardized rat burr hole defect model to study maxillofacial bone regeneration
Liu, G., Guo, Y., Zhang, L., Wang, X., Liu, R., Huang, P., Xiao, Y., Chen, Z., & Chen, Z. (2018) · Acta Biomaterialia · doi:10.1016/j.actbio.2018.12.049 · Cited by 47 · see citing works
Gao, H., Li, X., Wang, C., Ji, P., & Wang, C. (2019) · Materials Science and Engineering C · doi:10.1016/j.msec.2019.109934 · Cited by 47 · see citing works
Surface active complexes formed between keratin polypeptides and ionic surfactants
Pan, F., Lu, Z., Tucker, I., Hosking, S., Petkov, J. T., & Lu, J. R. (2016) · Journal of Colloid and Interface Science · doi:10.1016/j.jcis.2016.08.082 · Cited by 46 · see citing works
Zhi, X., Wang, Y., Li, P., Yuan, J., & Shen, J. (2015) · RSC Advances · doi:10.1039/c5ra16253j · Cited by 43 · see citing works
Navarro, J., Clohessy, R. M., Holder, R. C., Gabard, A. R., Herendeen, G. J., Christy, R. J., Burnett, L., & Fisher, J. P. (2019) · Tissue Engineering Part A · doi:10.1089/ten.tea.2019.0181 · Cited by 39 · see citing works
Self-citationThree-dimensional macroporous materials for tissue engineering of craniofacial bone
Shakya, A. K., & Kandalam, U. (2017) · British Journal of Oral and Maxillofacial Surgery · doi:10.1016/j.bjoms.2017.09.007 · Cited by 38 · see citing works
Zhang, S., Feng, Z., Hu, Y. Y., Zhao, D., Guo, X., Du, F., Wang, N., Sun, C., Liu, C., & Liu, H. (2021) · Small · doi:10.1002/smll.202105589 · Cited by 37 · see citing works
Keratin-containing scaffolds for tissue engineering applications: a review
Bakhtiari, S. S. E., & Karbasi, S. (2024) · Journal of Biomaterials Science Polymer Edition · doi:10.1080/09205063.2024.2311450 · Cited by 35 · see citing works
Kowalczewski, C. J., & Saul, J. M. (2015) · Acta Biomaterialia · doi:10.1016/j.actbio.2015.07.045 · Cited by 35 · see citing works
Self-citationKelly, R. (2016) · Elsevier eBooks · doi:10.1016/b978-1-78242-456-7.00017-9 · Cited by 29 · see citing works
Lang, A., Kirchner, M., Stefanowski, J., Durst, M. S., Weber, M.-C., Pfeiffenberger, M., Damerau, A., Hauser, A. E., Hoff, P., Duda, G. N., et al. (2019) · Acta Biomaterialia · doi:10.1016/j.actbio.2018.12.043 · Cited by 27 · see citing works
Berkmann, J. C., Herrera, A., Pontremoli, C., Zheng, K., Bucher, C. H., Ellinghaus, A., Boccaccini, A. R., Fiorilli, S., Vitale‐Brovarone, C., Duda, G. N., et al. (2020) · Pharmaceutics · doi:10.3390/pharmaceutics12090823 · Cited by 26 · see citing works
Lang, A., Helfmeier, S., Stefanowski, J., Kuppe, A., Sunkara, V., Pfeiffenberger, M., Wolter, A., Damerau, A., Hemmati‐Sadeghi, S., Ringe, J., et al. (2021) · Bone · doi:10.1016/j.bone.2021.116247 · Cited by 24 · see citing works
Brief introduction of keratin and its biological application, especially in drug delivery
Zhang, H., Su, F., Ma, X., & Zhao, G. (2021) · Emergent Materials · doi:10.1007/s42247-021-00216-3 · Cited by 23 · see citing works
Zuniga, K., Isaac, A., Christy, S., Wrice, N. L., Mangum, L. H., Natesan, S., Burnett, L., Christy, R. J., & Kowalczewski, C. J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23084100 · Cited by 23 · see citing works
Self-citationKeratin-based matrices from wool fibers and human hair
Patrucco, A., Visai, L., Fassina, L., Magenes, G., & Tonin, C. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-816872-1.00013-3 · Cited by 21 · see citing works
Chernysheva, M., Ruchko, E. S., & Валерьевич, Е. А. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262110723 · Cited by 20 · see citing works
Keratose hydrogel for tissue regeneration and drug delivery
Ledford, B. T., Barron, C., Dyke, M. E. V., & He, J. (2021) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2021.06.017 · Cited by 19 · see citing works
Sow, W. T., Wang, Y., Chen, L., Lai, Q., Chen, Q., Chen, L., Zhang, C., & Li, H. (2023) · Advanced Healthcare Materials · doi:10.1002/adhm.202201886 · Cited by 18 · see citing works
Qi, L., Wang, J., Yan, J., Jiang, W., Ge, W., Fang, X., Wang, X., Shen, S. G., Liu, L., & Zhang, L. (2025) · Journal of Nanobiotechnology · doi:10.1186/s12951-025-03168-6 · Cited by 18 · see citing works
Insight into the Regulatory Function of Human Hair Keratins in Wound Healing Using Proteomics
Gao, F., Li, W., Kan, J., Ding, Y., Wang, Y., Deng, J., Qing, R., Wang, B., & Hao, S. (2020) · Advanced Biosystems · doi:10.1002/adbi.201900235 · Cited by 17 · see citing works
BMP delivery systems for bone regeneration: Healthy vs osteoporotic population. Review
Segredo-Morales, E., García‐García, P., Évora, C., & Delgado, A. (2017) · Journal of Drug Delivery Science and Technology · doi:10.1016/j.jddst.2017.05.014 · Cited by 17 · see citing works
Design of nanoconstructs that exhibit enhanced hemostatic efficiency and bioabsorbability
Eissa, R. A., Saafan, H. A., Ali, A. A., Ibrahim, K. M., Eissa, N. G., Hamad, M. A., Pang, C., Guo, H., Gao, H., Elsabahy, M., et al. (2022) · Nanoscale · doi:10.1039/d2nr02043b · Cited by 16 · see citing works
Diwan, H., & Sah, M. K. (2023) · Emergent Materials · doi:10.1007/s42247-023-00545-5 · Cited by 16 · see citing works
Cohen, D. J., Hyzy, S. L., Haque, S., Olson, L. C., Boyan, B. D., Saul, J. M., & Schwartz, Z. (2018) · Tissue Engineering Part A · doi:10.1089/ten.tea.2017.0471 · Cited by 15 · see citing works
Self-citationExtrusion 3D printing of keratin protein hydrogels free of exogenous chemical agents
Brodin, E., Boehmer, M., Prentice, A., Neff, E., McCoy, K., Mueller, J., Saul, J. M., & Sparks, J. L. (2022) · Biomedical Materials · doi:10.1088/1748-605x/ac7f15 · Cited by 14 · see citing works
Self-citationA keratin-based microparticle for cell delivery
Thompson, M. A., Giuffre, A., McClenny, C., & Dyke, M. E. V. (2020) · Journal of Biomaterials Applications · doi:10.1177/0885328220951892 · Cited by 14 · see citing works
Miguez, P. A., Gonçalves, V. D. P., Musskopf, M. L., Rivera-Concepcion, A., McGaughey, S., Yu, C., Lee, D. J., Tuin, S. A., & Ali, A. (2024) · Scientific Reports · doi:10.1038/s41598-024-52566-7 · Cited by 12 · see citing works
Parker, R. N., Trent, A., Roth, K. L., Dyke, M. E. V., & Grove, T. Ž. (2020) · Biomedical Materials · doi:10.1088/1748-605x/ab98e8 · Cited by 10 · see citing works
Zhou, T., Yang, H., Tian, Z., Wang, Y., Tang, X., & Hu, J. (2017) · Journal of Oral and Maxillofacial Surgery · doi:10.1016/j.joms.2017.05.031 · Cited by 9 · see citing works
Valorization of Human Hair and Its Derivatives in Tissue Engineering: A Review
Vitus, V., Ibrahim, F., & Zaman, W. S. W. K. (2022) · Tissue Engineering Part C Methods · doi:10.1089/ten.tec.2021.022333 · Cited by 5 · see citing works
The Use of Keratin as Potential Biomaterial for Bio-Dental Applications
Sharma, A. (2020) · Open Access Journal of Biomedical Science · doi:10.38125/oajbs.000204 · Cited by 4 · see citing works
Saul, J. M., Bohnert, J. S., O’Brien, M., Alnuaimi, S., Carnwath, T. P., Dunivan, Q., Coffin, D. W., & Smith, T. L. (2025) · Tissue Engineering and Regenerative Medicine · doi:10.1007/s13770-025-00747-4 · Cited by 3 · see citing works
“1 and 2, respectively), consistent with prior studies with KOS[16] and KTN[20] derived from human hair showing minimal bone formation in the absence of rhBMP-2.”
Self-citationDevelopment of a Rat Model of Mandibular Irradiation Sequelae for Preclinical Studies of Bone Repair
Dréno, M., Bléry, P., Guicheux, J., Weiss, P., Malard, O., & Espitalier, F. (2020) · Tissue Engineering Part C Methods · doi:10.1089/ten.tec.2020.0109 · Cited by 3 · see citing works
Review article Silk as a potential candidate for bone tissue engineering
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Effective Mitigation of BMP-Induced Inflammation and Improvement of Bone Parameters by HesperidinPreprint
Miguez, P. A., Gonçalves, V. D. P., Musskopf, M. L., Rivera-Concepcion, A., McGaughey, S., Yu, C., Lee, D. J., & Tuin, S. A. (2023) · SSRN Electronic Journal · doi:10.2139/ssrn.4463348
- Authors
- Kowalczewski, C. J., Tombyln, S., Wasnick, D. C., Hughes, M. R., Ellenburg, M. D., Callahan, M. F., Smith, T. L., Van Dyke, M. E., Burnett, L. R., & Saul, J. M.
- Affiliations
- Virginia Tech - Wake Forest University School of Biomedical Engineering & Sciences (US)
- KeraNetics (United States) (US)
- Miami University (US)
- Wake Forest University Health Sciences (US)
- Corresponding author
- Saul, Justin M.
- Venue
- Biomaterials
- Publisher
- Elsevier BV
- Published
- 2014-03
- Volume
- 35
- Issue
- 10
- Pages
- 3220-3228
- ISSN
- 0142-9612 (ISSN-L)
- PMC
- PMC4321825
- OpenAlex
- W1973282714
- Cited by
- 58
- References
- 34
- Citations by year
- 2026: 1 · 2025: 3 · 2024: 2 · 2023: 3 · 2022: 5 · 2021: 4 · 2020: 9 · 2019: 6 · 2018: 4 · 2017: 7 · 2016: 7 · 2015: 7
- FWCI
- 3.63
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Biomaterials (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- KeraNetics LLC
- National Institutes of Health (R01AR061391)
- US Army Medical Research and Materiel Command
- Topics
- Physical Sciences › Engineering › Biomedical Engineering › Bone Tissue Engineering Materials
- Physical Sciences › Materials Science › Biomaterials › Silk-based biomaterials and applications
- Physical Sciences › Materials Science › Biomaterials › Collagen: Extraction and Characterization
- Keywords
- rhBMP-2, absorbable collagen sponge, bone regeneration, mandibular defects, biomaterial carriers, bone mineral density
- MeSH terms
- Animals, Biocompatible Materials, Bone Development, Bone Regeneration, Keratins, Male, Mandible, Recombinant Proteins, Rheology, Rats, Sprague-Dawley, Rats, Tissue Scaffolds, Bone Morphogenetic Protein 2
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 ›
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