Tunable Keratin Hydrogels for Controlled Erosion and Growth Factor Delivery
Open accessAbstract
Tunable erosion of polymeric materials is an important aspect of tissue engineering for reasons that include cell infiltration, controlled release of therapeutic agents, and ultimately to tissue healing. In general, the biological response to proteinaceous polymeric hydrogels is favorable (e.g., minimal inflammatory response). However, unlike synthetic polymers, achieving tunable erosion with natural materials is a challenge. Keratins are a class of intermediate filament proteins that can be obtained from several sources, including human hair, and have gained increasing levels of use in tissue engineering applications. An important characteristic of keratin proteins is the presence of a large number of cysteine residues. Two classes of keratins with different chemical properties can be obtained by varying the extraction techniques: (1) keratose by oxidative extraction and (2) kerateine by reductive extraction. Cysteine residues of keratose are "capped" by sulfonic acid and are unable to form covalent cross-links upon hydration, whereas cysteine residues of kerateine remain as sulfhydryl groups and spontaneously form covalent disulfide cross-links. Here, we describe a straightforward approach to fabricate keratin hydrogels with tunable rates of erosion by mixing keratose and kerateine. SEM imaging and mechanical testing of freeze-dried materials showed similar pore diameters and compressive moduli, respectively, for each keratose-kerateine mixture formulation (∼1200 kPa for freeze-dried materials and ∼1.5 kPa for hydrogels). However, the elastic modulus (G') determined by rheology varied in proportion with the keratose-kerateine ratios, as did the rate of hydrogel erosion and the release rate of thiol from the hydrogels. The variation in keratose-kerateine ratios also led to tunable control over release rates of recombinant human insulin-like growth factor 1.
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
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?
By varying the ratios of KOS and KTN in keratin materials, the rates of degradation of materials composed of keratin can be controlled.
“By varying the ratios of KOS and KTN in keratin materials, the rates of degradation of materials composed of keratin can be controlled in a manner reminiscent of synthetic polymers.”
From Keratin Scaffold Formulation Impacts rhBMP-2 Biodistribution and Bone Regeneration in a Rat Femur Defect Model (2025) · cites this paper as [14]
Modification of the number of cysteine residues available for disulfide crosslinking can be achieved by mixing the KOS and KTN forms of keratin in different ratios.
“It has previously been demonstrated that modification of the number of cysteine residues available for disulfide crosslinking can be achieved by simply mixing the KOS and KTN forms of keratin in different ratios [14, 15].”
From Keratin Scaffold Formulation Impacts rhBMP-2 Biodistribution and Bone Regeneration in a Rat Femur Defect Model (2025) · cites this paper as [14]
Degradation profiles correlated closely with the level of disulfide crosslinking: KOS-only and formulations with higher KOS degraded more rapidly due to lower disulfide crosslinking, whereas KTN-only and formulations with higher KTN degraded more slowly due to the presence of disulfide crosslinks.
“The degradation profiles correlated closely with the level of disulfide crosslinking where KOS-only and formulations with higher levels of KOS degraded more rapidly due to lower levels of disulfide crosslinking whereas KTN-only and formulations with higher levels of KTN degraded more slowly due to the presence of disulfide crosslinks [14].”
From Keratin Scaffold Formulation Impacts rhBMP-2 Biodistribution and Bone Regeneration in a Rat Femur Defect Model (2025) · cites this paper as [14]
Prior work characterized the rates of degradation of the KOS:KTN formulations used in this manuscript.
“In prior work, we have characterized the rates of degradation of the KOS:KTN formulations that were used in this manuscript [14].”
From Keratin Scaffold Formulation Impacts rhBMP-2 Biodistribution and Bone Regeneration in a Rat Femur Defect Model (2025) · cites this paper as [14]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
2 retracted
RETRACTED: Clinical transplantation of a tissue-engineered airway
Macchiarini, P., Jungebluth, P., Go, T., Asnaghi, M. A., Rees, L., Cogan, T. A., Dodson, A., Martorell, J., Bellini, S., Parnigotto, P. P., et al. (2008) · The Lancet · doi:10.1016/s0140-6736(08)61598-6 · Cited by 1,431 · see citing works
RetractedRETRACTED: The first tissue-engineered airway transplantation: 5-year follow-up results
Gonfiotti, A., Jaus, M. O., Barale, D., Baiguera, S., Comin, C., Lavorini, F., Fontana, G. A., Sibila, O., Rombolà, G., Jungebluth, P., et al. (2013) · The Lancet · doi:10.1016/s0140-6736(13)62033-4 · Cited by 272 · see citing works
RetractedEllman, G. L. (1959) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(59)90090-6 · Cited by 26,824 · see citing works
Tissue-engineered autologous bladders for patients needing cystoplasty
Atala, A., Bauer, S. B., Söker, S., Yoo, J. J., & Retik, A. B. (2006) · The Lancet · doi:10.1016/s0140-6736(06)68438-9 · Cited by 1,835 · see citing works
Cell Encapsulation in Biodegradable Hydrogels for Tissue Engineering Applications
Nicodemus, G. D., & Bryant, S. J. (2008) · Tissue Engineering Part B Reviews · doi:10.1089/ten.teb.2007.0332 · Cited by 1,242 · see citing works
Why degradable polymers undergo surface erosion or bulk erosion
Burkersroda, F. V., Schedl, L., & Göpferich, A. (2002) · Biomaterials · doi:10.1016/s0142-9612(02)00170-9 · Cited by 1,146 · see citing works
Fracture healing: The diamond concept
Giannoudis, P. V., Einhorn, T. A., & Marsh, D. (2007) · Injury · doi:10.1016/s0020-1383(08)70003-2 · Cited by 1,092 · see citing works
Kricheldorf, H. R., Berl, M., & Scharnagl, N. (1988) · Macromolecules · doi:10.1021/ma00180a002 · Cited by 597 · see citing works
Zustiak, S. P., & Leach, J. B. (2010) · Biomacromolecules · doi:10.1021/bm100137q · Cited by 495 · see citing works
Polymeric Growth Factor Delivery Strategies for Tissue Engineering
Chen, R. R., & Mooney, D. J. (2003) · Pharmaceutical Research · doi:10.1023/a:1025034925152 · Cited by 435 · see citing works
Naturally and synthetic smart composite biomaterials for tissue regeneration
Pérez, R. A., Won, J., Knowles, J. C., & Kim, H. (2012) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2012.03.009 · Cited by 382 · 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 · see citing works
Hill, P. S., Garrett, J. P., Ma, J., Apel, P. J., Klorig, D. C., Smith, T. L., Koman, L. A., Atala, A., & Dyke, M. E. V. (2007) · Biomaterials · doi:10.1016/j.biomaterials.2007.08.023 · Cited by 346 · see citing works
Integrin Expression and Function on Human Osteoblast-like Cells
Gronthos, S., Stewart, K., Graves, S. E., Hay, S., & Simmons, P. J. (1997) · Journal of Bone and Mineral Research · doi:10.1359/jbmr.1997.12.8.1189 · Cited by 251 · see citing works
Haidar, Z. S., Hamdy, R. C., & Tabrizian, M. (2009) · Biotechnology Letters · doi:10.1007/s10529-009-0099-x · Cited by 244 · see citing works
Rheology of Biopolymer Solutions and Gels
Picout, D. R., & Ross‐Murphy, S. B. (2003) · The Scientific World JOURNAL · doi:10.1100/tsw.2003.15 · Cited by 234 · see citing works
Thermoresponsive self-assembled elastin-based nanoparticles for delivery of BMPs
Bessa, P. C., Machado, R., Nürnberger, S., et al. (2009) · Journal of Controlled Release · doi:10.1016/j.jconrel.2009.11.003 · Cited by 185 · 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
Rheological characterization of hydrogels formed by recombinantly produced spider silk
Rammensee, S., Huemmerich, D., Hermanson, K. D., et al. (2005) · Applied Physics A · doi:10.1007/s00339-005-3431-x · Cited by 162 · see citing works
Human hair keratin and its-based biomaterials for biomedical applications
Lee, H., Noh, K., Lee, S. C., Kwon, I.-K., Han, D., Lee, I.-S., & Hwang, Y. (2014) · Tissue Engineering and Regenerative Medicine · doi:10.1007/s13770-014-0029-4 · Cited by 150 · see citing works
Rheology and Photo-Cross-Linking of Thiol−Ene Polymers
Chiou, B., English, R. J., & Khan, S. A. (1996) · Macromolecules · doi:10.1021/ma960383e · 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-citationCallahan, L. A. S., Xie, S., Barker, I. A., Zheng, J., Reneker, D. H., Dove, A. P., & Becker, M. L. (2013) · Biomaterials · doi:10.1016/j.biomaterials.2013.08.028 · Cited by 134 · see citing works
Biological evaluation of human hair keratin scaffolds for skin wound repair and regeneration
Xu, S., Sang, L., Zhang, Y., Wang, X., & Li, X. (2012) · Materials Science and Engineering C · doi:10.1016/j.msec.2012.10.011 · Cited by 132 · see citing works
IGF-1 induces human myotube hypertrophy by increasing cell recruitment
Jacquemin, V., Furling, D., Bigot, A., Butler-Browne, G. S., & Mouly, V. (2004) · Experimental Cell Research · doi:10.1016/j.yexcr.2004.05.023 · Cited by 130 · see citing works
Separating viscoelasticity and poroelasticity of gels with different length and time scales
Wang, Q., Mohan, A. C., Oyen, M. L., et al. (2014) · Acta Mechanica Sinica · doi:10.1007/s10409-014-0015-z · Cited by 121 · see citing works
Effect of locally delivered IGF‐1 on nerve regeneration during aging: An experimental study in rats
Apel, P. J., Ma, J., Callahan, M. F., et al. (2009) · Muscle & Nerve · doi:10.1002/mus.21485 · Cited by 116 · see citing works
Culturing Fibroblasts in 3D Human Hair Keratin Hydrogels
Wang, S., Wang, Z., Foo, S. E. M., Tan, N. S., Yuan, Y., Lin, W., Zhang, Z., & Ng, K. W. (2015) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.5b00854 · Cited by 115 · 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 · see citing works
Self-citationFitzgerald, M. M., Bootsma, K., Berberich, J. A., & Sparks, J. L. (2015) · Biomacromolecules · doi:10.1021/bm501845j · Cited by 110 · see citing works
Pace, L. A., Plate, J. F., Smith, T. L., & Dyke, M. E. V. (2013) · Biomaterials · doi:10.1016/j.biomaterials.2013.04.024 · Cited by 107 · see citing works
Spiller, K. L., Liu, Y., Holloway, J. L., et al. (2011) · Journal of Controlled Release · doi:10.1016/j.jconrel.2011.09.057 · Cited by 105 · see citing works
Photocontrolled Nanoparticles for On-Demand Release of Proteins
Azagarsamy, M. A., Alge, D. L., Radhakrishnan, S. J., Tibbitt, M. W., & Anseth, K. S. (2012) · Biomacromolecules · doi:10.1021/bm300646q · Cited by 102 · see citing works
Repair of Peripheral Nerve Defects in Rabbits Using Keratin Hydrogel Scaffolds
Hill, P. S., Apel, P. J., Barnwell, J. C., Smith, T., Koman, L. A., Atala, A., & Dyke, M. E. V. (2011) · Tissue Engineering Part A · doi:10.1089/ten.tea.2010.0184 · Cited by 102 · see citing works
A mechanistic investigation of the effect of keratin-based hemostatic agents on coagulation
Rahmany, M. B., Hantgan, R. R., & Dyke, M. E. V. (2013) · Biomaterials · doi:10.1016/j.biomaterials.2012.12.008 · Cited by 97 · see citing works
Minimally Invasive Approach to the Repair of Injured Skeletal Muscle With a Shape-memory Scaffold
Wang, L., Cao, L., Shansky, J., Wang, Z., Mooney, D. J., & Vandenburgh, H. H. (2014) · Molecular Therapy · doi:10.1038/mt.2014.78 · Cited by 95 · see citing works
Modified keratin sponge: Binding of bone morphogenetic protein-2 and osteoblast differentiation
Tachibana, A., Nishikawa, Y., Nishino, M., Kaneko, S., Tanabe, T., & Yamauchi, K. (2006) · Journal of Bioscience and Bioengineering · doi:10.1263/jbb.102.425 · 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-citationFabiilli, M. L., Wilson, C. G. M., Padilla, F. R., et al. (2013) · Acta Biomaterialia · doi:10.1016/j.actbio.2013.03.027 · Cited by 82 · see citing works
Tomblyn, 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-citationShen, D., Wang, X., Zhang, L., Zhao, X., Li, J., Cheng, K., & Zhang, J. (2011) · Biomaterials · doi:10.1016/j.biomaterials.2011.08.057 · Cited by 78 · see citing works
Smart biomaterials - regulating cell behavior through signaling molecules
Mieszawska, A. J., & Kaplan, D. L. (2010) · BMC Biology · doi:10.1186/1741-7007-8-59 · Cited by 72 · see citing works
Pace, L. A., Plate, J. F., Mannava, S., Barnwell, J. C., Koman, L. A., Li, Z., Smith, T. L., & Dyke, M. E. V. (2013) · Tissue Engineering Part A · doi:10.1089/ten.tea.2013.0084 · Cited by 71 · see citing works
Poranki, D. R., Whitener, W., Howse, S., Mesen, T., Howse, E., Burnell, J. M., Greengauz-Roberts, O. K., Molnar, J. A., & Dyke, M. E. V. (2013) · Journal of Biomaterials Applications · doi:10.1177/0885328213513310 · Cited by 71 · see citing works
Keratin Gel Filler for Peripheral Nerve Repair in a Rodent Sciatic Nerve Injury Model
Lin, Y.-C., Ramadan, M., Dyke, M. E. V., Kokai, L. E., Philips, B. J., Rubin, J. P., & Marra, K. G. (2011) · Plastic & Reconstructive Surgery · doi:10.1097/prs.0b013e3182268ae0 · Cited by 68 · see citing works
Hatzfeld, M., & Burba, M. (1994) · Journal of Cell Science · doi:10.1242/jcs.107.7.1959 · Cited by 67 · see citing works
Mechanisms of hepatocyte attachment to keratin biomaterials
Richter, J. R., de Guzman, R. C., & Dyke, M. E. V. (2011) · Biomaterials · doi:10.1016/j.biomaterials.2011.06.061 · Cited by 63 · see citing works
Karam, J., Muscari, C., Sindji, L., et al. (2014) · Journal of Controlled Release · doi:10.1016/j.jconrel.2014.06.052 · Cited by 59 · see citing works
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. (2014) · Biomaterials · doi:10.1016/j.biomaterials.2013.12.087 · Cited by 58 · see citing works
Self-citationMariner, P. D., Wudel, J. M., Miller, D. E., Genova, E. E., Streubel, S., & Anseth, K. S. (2012) · Journal of Orthopaedic Research® · doi:10.1002/jor.22243 · Cited by 57 · see citing works
Controlled Release of IGF-1 and HGF from a Biodegradable Polyurethane Scaffold
Nelson, D. M., Baraniak, P. R., Ma, Z., Guan, J., Mason, N. S., & Wagner, W. R. (2011) · Pharmaceutical Research · doi:10.1007/s11095-011-0391-z · Cited by 56 · see citing works
Burnett, L., Richter, J. G., Rahmany, M. B., et al. (2013) · Journal of Biomaterials Applications · doi:10.1177/0885328213484975 · Cited by 55 · see citing works
Self-citationStructure–property relationships of meta-kerateine biomaterials derived from human hair
Richter, J. R., de Guzman, R. C., Greengauz-Roberts, O. K., & Dyke, M. E. V. (2011) · Acta Biomaterialia · doi:10.1016/j.actbio.2011.08.020 · Cited by 54 · see citing works
Combined effects of direct current stimulation and immobilized BMP‐2 for enhancement of osteogenesis
Zhang, J., Neoh, K. G., Hu, X., et al. (2012) · Biotechnology and Bioengineering · doi:10.1002/bit.24796 · Cited by 52 · see citing works
Thilagar, S., Jothi, N. A., Omar, A. R. S., Kamaruddin, M. Y., & Ganabadi, S. (2007) · Journal of Biomedical Materials Research Part B Applied Biomaterials · doi:10.1002/jbm.b.31024 · Cited by 50 · see citing works
Biocompatibility and osseointegration of reconstituted keratin in an ovine model
Dias, G. J., Peplow, P. V., McLaughlin, A. W., Teixeira, F. S., & Kelly, R. J. (2009) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.32394 · Cited by 49 · see citing works
Bernot, K. M., Lee, C., & Coulombe, P. A. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200408116 · Cited by 43 · see citing works
Nakata, R., Osumi, Y., Miyagawa, S., Tachibana, A., & Tanabe, T. (2015) · Journal of Bioscience and Bioengineering · doi:10.1016/j.jbiosc.2014.12.005 · Cited by 40 · see citing works
Ozaki, Y., Takagi, Y., Mori, H., et al. (2014) · Materials Science and Engineering C · doi:10.1016/j.msec.2014.05.018 · Cited by 38 · see citing works
Thermogelling Chitosan-g-(PAF-PEG) Aqueous Solution As an Injectable Scaffold
Kang, E. Y., Moon, H. J., Joo, M. K., et al. (2012) · Biomacromolecules · doi:10.1021/bm300085c · Cited by 38 · see citing works
Rosellini, E., Cristallini, C., Guerra, G. D., et al. (2015) · Journal of Biomaterials Science Polymer Edition · doi:10.1080/09205063.2015.1030991 · Cited by 30 · see citing works
Synthesis of PAMAM dendrimer-based fast cross-linking hydrogel for biofabrication
Bi, X., Luckanagul, J. A., Allen, A. N., Ramaboli, M. C., Campbell, E., West, D., Maturavongsadit, P., Brummett, K., & Wang, Q. (2015) · Journal of Biomaterials Science Polymer Edition · doi:10.1080/09205063.2015.1056716 · Cited by 30 · see citing works
Identification of Ligand Binding Sites on Integrin α4β1 through Chemical Cross-Linking
Chen, L. L., Lobb, R. R., Cuervo, J. H., et al. (1998) · Biochemistry · doi:10.1021/bi980311a · Cited by 29 · see citing works
de Luca, A. C., Faroni, A., Downes, S., et al. (2013) · Journal of Tissue Engineering and Regenerative Medicine · doi:10.1002/term.1804 · Cited by 29 · see citing works
Poranki, D. R., & Dyke, M. E. V. (2014) · Biomaterials · doi:10.1016/j.biomaterials.2014.02.044 · Cited by 12 · see citing works
Photoinitiator-free synthesis of endothelial cell-adhesive and enzymatically degradable hydrogels
Jones, D. R., Marchant, R., von Recum, H. A., et al. (2014) · Acta Biomaterialia · doi:10.1016/j.actbio.2014.11.012 · Cited by 11 · see citing works
Flagged first, then by citations
Research works printed but not linked: 1
- [61]Pace LA Plate JF Mannava S Barnwell JC Koman LA Li Z Smith TL Van Dyke M A human hair keratin hydrogel scaffold enhances median nerve regeneration in nonhuman primates: an electrophysiological and histological study Tissue. Eng., Part A 2014 20 3–4 507 17 24083825 PMC3926186
Cited by
Sorted by citations
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-citationSaul, 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
“It has previously been demonstrated that modification of the number of cysteine residues available for disulfide crosslinking can be achieved by simply mixing the KOS and KTN forms of keratin in different ratios [14, 15].”
InfluentialSelf-citation
- Authors
- Ham, T. R., Lee, R. T., Han, S., Haque, S., Vodovotz, Y., Gu, J., Burnett, L. R., Tomblyn, S., & Saul, J. M.
- Affiliations
- University of Akron (US)
- Miami University (US)
- The Ohio State University (US)
- KeraNetics (United States) (US)
- Corresponding author
- Saul, Justin M.
- ORCID
- Venue
- Biomacromolecules
- Publisher
- American Chemical Society (ACS)
- Published
- 2015-12-14
- Volume
- 17
- Issue
- 1
- Pages
- 225-236
- ISSN
- 1525-7797 (ISSN-L)
- 1526-4602
- PMC
- PMC5565161
- OpenAlex
- W2298706874
- Cited by
- 111
- References
- 66
- Citations by year
- 2026: 4 · 2025: 8 · 2024: 10 · 2023: 9 · 2022: 10 · 2021: 16 · 2020: 14 · 2019: 12 · 2018: 11 · 2017: 9 · 2016: 8
- FWCI
- 3.87
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Biomacromolecules (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Medical Research and Materiel Command, U.S. Army Medical Department (W81XWH-11-C-0060)
- National Institute of Arthritis and Musculoskeletal and Skin Diseases (R01AR061391)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Medicine › Hydrogels: synthesis, properties, applications
- Physical Sciences › Materials Science › Biomaterials › Silk-based biomaterials and applications
- Physical Sciences › Materials Science › Biomaterials › Collagen: Extraction and Characterization
- Keywords
- keratin hydrogels, keratosis, cysteine cross-linking, disulfide cross-links, keratin extraction, controlled release, insulin-like growth factor I, elastic modulus, tissue engineering scaffolds
- MeSH terms
- Biocompatible Materials, Hair, Humans, Insulin-Like Growth Factor I, Keratins, Materials Testing, Hydrogels, Tissue Engineering, Elastic Modulus
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
