The DOI matches its Crossref record; 17 of the 17 references it cites were found in a registry or an index.
The Collagen Suprafamily: From Biosynthesis to Advanced Biomaterial Development
Open accessAbstract
Collagen is the oldest and most abundant extracellular matrix protein that has found many applications in food, cosmetic, pharmaceutical, and biomedical industries. First, an overview of the family of collagens and their respective structures, conformation, and biosynthesis is provided. The advances and shortfalls of various collagen preparations (e.g., mammalian/marine extracted collagen, cell‐produced collagens, recombinant collagens, and collagen‐like peptides) and crosslinking technologies (e.g., chemical, physical, and biological) are then critically discussed. Subsequently, an array of structural, thermal, mechanical, biochemical, and biological assays is examined, which are developed to analyze and characterize collagenous structures. Lastly, a comprehensive review is provided on how advances in engineering, chemistry, and biology have enabled the development of bioactive, 3D structures (e.g., tissue grafts, biomaterials, cell‐assembled tissue equivalents) that closely imitate native supramolecular assemblies and have the capacity to deliver in a localized and sustained manner viable cell populations and/or bioactive/therapeutic molecules. Clearly, collagens have a long history in both evolution and biotechnology and continue to offer both challenges and exciting opportunities in regenerative medicine as nature's biomaterial of choice.
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Cites
Decellularization of tissues and organs
Gilbert, T. W., Sellaro, T. L., & Badylak, S. F. (2006) · Biomaterials · doi:10.1016/j.biomaterials.2006.02.014 · Cited by 2,222
The role of collagen in bone strength
Viguet-Carrin, S., Garnero, P., & Delmas, P. D. (2006) · Osteoporosis International · doi:10.1007/s00198-005-2035-9 · Cited by 1,047
Ohuchi, E., Imai, K., Fujii, Y., Sato, H., Seiki, M., & Okada, Y. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.4.2446 · Cited by 938
Immune response to biologic scaffold materials
Badylak, S. F., & Gilbert, T. W. (2008) · Seminars in Immunology · doi:10.1016/j.smim.2007.11.003 · Cited by 857
Xenogeneic extracellular matrix as a scaffold for tissue reconstruction
Badylak, S. F. (2004) · Transplant Immunology · doi:10.1016/j.trim.2003.12.016 · Cited by 747
Growth of engineered human myocardium with mechanical loading and vascular coculture
Tulloch, N. L., Muskheli, V., Razumova, M. V., Korte, F. S., Regnier, M., Hauch, K. D., Pabon, L., Reinecke, H., & Murry, C. E. (2011) · Circulation Research · doi:10.1161/circresaha.110.237206 · Cited by 666
Organ engineering based on decellularized matrix scaffolds
Song, J. J., & Ott, H. C. (2011) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2011.03.005 · Cited by 501
Matrigel: From discovery and ECM mimicry to assays and models for cancer research
Benton, G., Arnaoutova, I., George, J., Kleinman, H. K., & Koblinski, J. (2014) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2014.06.005 · Cited by 477
Cross-linking of collagen and elastin. Properties of lysyl oxidase
Siegel, R. C., Pinnell, S. R., & Martin, G. R. (1970) · Biochemistry · doi:10.1021/bi00825a004 · Cited by 345
Collagen—emerging collagen based therapies hit the patient
Abou Neel, E. A., Bozec, L., Knowles, J. C., Syed, O., Mudera, V., Day, R., & Hyun, J. K. (2013) · Advanced Drug Delivery Reviews · doi:10.1016/j.addr.2012.08.010 · Cited by 296
Cited by
Soft Materials by Design: Unconventional Polymer Networks Give Extreme Properties
Zhao, X., Chen, X., Yuk, H., Lin, S., Liu, X., & Parada, G. (2021) · Chemical Reviews · doi:10.1021/acs.chemrev.0c01088 · Cited by 1,161
Collagen‐based biomaterials for biomedical applications
Rezvani Ghomi, E., Nourbakhsh, N., Akbari Kenari, M., Zare, M., & Ramakrishna, S. (2021) · Journal of Biomedical Materials Research Part B: Applied Biomaterials · doi:10.1002/jbm.b.34881 · Cited by 406
Liu, S., Yu, J.-M., Gan, Y.-C., Qiu, X.-Z., Gao, Z.-C., Wang, H., Chen, S.-X., Xiong, Y., Liu, G.-H., Lin, S.-E., et al. (2023) · Military Medical Research · doi:10.1186/s40779-023-00448-w · Cited by 357
Joyce, K., Fabra, G. T., Bozkurt, Y., & Pandit, A. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00512-8 · Cited by 316
Self-citationRecent advances in regenerative biomaterials
Cao, D., & Ding, J. (2022) · Regenerative Biomaterials · doi:10.1093/rb/rbac098 · Cited by 259
Metadata
- Authors
- Sorushanova, A., Delgado, L. M., Wu, Z., Shologu, N., Kshirsagar, A., Raghunath, R., Mullen, A. M., Bayon, Y., Pandit, A., Raghunath, M., & Zeugolis, D. I.
- Venue
- Advanced Materials
- Publisher
- Wiley
- Published
- 2018-08-20
- Volume
- 31
- Issue
- 1
- Pages
- e1801651-e1801651
- ISSN
- 0935-9648 (ISSN-L)
- 1521-4095
- OpenAlex
- W2889372700
- Cited by
- 1,151
- References
- 17
- FWCI
- 19.38
- Type
- journal article
- Language
- en
- Open access
- green
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- Sorushanova, A., Delgado, L. M., Wu, Z., Shologu, N., Kshirsagar, A., Raghunath, R., Mullen, A. M., Bayon, Y., Pandit, A., Raghunath, M., & Zeugolis, D. I. (2019). The Collagen Suprafamily: From Biosynthesis to Advanced Biomaterial Development. Advanced Materials. https://doi.org/10.1002/adma.201801651
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