The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
Collagens—structure, function, and biosynthesis
Abstract
The extracellular matrix represents a complex alloy of variable members of diverse protein families defining structural integrity and various physiological functions. The most abundant family is the collagens with more than 20 different collagen types identified so far. Collagens are centrally involved in the formation of fibrillar and microfibrillar networks of the extracellular matrix, basement membranes as well as other structures of the extracellular matrix. This review focuses on the distribution and function of various collagen types in different tissues. It introduces their basic structural subunits and points out major steps in the biosynthesis and supramolecular processing of fibrillar collagens as prototypical members of this protein family. A final outlook indicates the importance of different collagen types not only for the understanding of collagen-related diseases, but also as a basis for the therapeutical use of members of this protein family discussed in other chapters of this issue.
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.
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
Strategies for MMP inhibition in cancer: innovations for the post-trial era
Overall, C. M., & López-Otín, C. (2002) · Nature Reviews Cancer · doi:10.1038/nrc884 · Cited by 1,349
Cited by
Molecular Mechanisms of Stress-Responsive Changes in Collagen and Elastin Networks in Skin
Aziz, J., Shezali, H., Radzi, Z., Yahya, N. A., Abu Kassim, N. H., Czernuszka, J., & Rahman, M. T. (2016) · Skin Pharmacology and Physiology · doi:10.1159/000447017 · Cited by 7,323
Biodegradable polymers as biomaterials
Nair, L. S., & Laurencin, C. T. (2007) · Progress in Polymer Science · doi:10.1016/j.progpolymsci.2007.05.017 · Cited by 4,416
Phenotype molding of stromal cells in the lung tumor microenvironment
Lambrechts, D., Wauters, E., Boeckx, B., Aibar, S., Nittner, D., Burton, O., Bassez, A., Decaluwé, H., Pircher, A., Van den Eynde, K., et al. (2018) · Nature Medicine · doi:10.1038/s41591-018-0096-5 · Cited by 1,648
The Basic Science of Wound Healing
Broughton, G., Janis, J. E., & Attinger, C. E. (2006) · Plastic and Reconstructive Surgery · doi:10.1097/01.prs.0000225430.42531.c2 · Cited by 1,519
Bioactive modification of poly (ethylene glycol) hydrogels for tissue engineering
Zhu, J. (2010) · Biomaterials · doi:10.1016/j.biomaterials.2010.02.044 · Cited by 1,457
Vroman, I., & Tighzert, L. (2009) · Materials · doi:10.3390/ma2020307 · Cited by 1,355
Jabłońska-Trypuć, A., Matejczyk, M., & Rosochacki, S. (2016) · Journal of Enzyme Inhibition and Medicinal Chemistry · doi:10.3109/14756366.2016.1161620 · Cited by 1,042
Diop-Frimpong, B., Chauhan, V. P., Krane, S., Boucher, Y., & Jain, R. K. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1018892108 · Cited by 733
Hierarchical Structures of Bone and Bioinspired Bone Tissue Engineering
Liu, Y., Luo, D., & Wang, T. (2016) · Small · doi:10.1002/smll.201600626 · Cited by 482
Advances in functionalized polymer coatings on biodegradable magnesium alloys–A review
Li, L.-Y., Cui, L.-Y., Zeng, R.-C., Li, S.-Q., Chen, X.-B., Zheng, Y., & Kannan, M. B. (2018) · Acta Biomaterialia · doi:10.1016/j.actbio.2018.08.030 · Cited by 466
Amirrah, I. N., Lokanathan, Y., Zulkiflee, I., Wee, M. F. M. R., Motta, A., & Fauzi, M. B. (2022) · Biomedicines · doi:10.3390/biomedicines10092307 · Cited by 426
Design and applications of man-made biomimetic fibrillar hydrogels
Prince, E., & Kumacheva, E. (2019) · Nature Reviews Materials · doi:10.1038/s41578-018-0077-9 · Cited by 379
Unraveling of Advances in 3D-Printed Polymer-Based Bone Scaffolds
Xu, Y., Zhang, F., Zhai, W., Cheng, S., Li, J., & Wang, Y. (2022) · Polymers · doi:10.3390/polym14030566 · Cited by 349
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
Skin collagen through the lifestages: importance for skin health and beauty
Reilly, D. M., & Lozano, J. (2021) · Plastic and Aesthetic Research · doi:10.20517/2347-9264.2020.153 · Cited by 241
The ECM path of senescence in aging: components and modifiers
Levi, N., Papismadov, N., Solomonov, I., Sagi, I., & Krizhanovsky, V. (2020) · The FEBS Journal · doi:10.1111/febs.15282 · Cited by 219
Type V Collagen in Health, Disease, and Fibrosis
Mak, K. M., Png, C. Y. M., & Lee, D. J. (2016) · The Anatomical Record · doi:10.1002/ar.23330 · Cited by 197
Collagen Derived from Fish Industry Waste: Progresses and Challenges
Rajabimashhadi, Z., Gallo, N., Salvatore, L., & Lionetto, F. (2023) · Polymers · doi:10.3390/polym15030544 · Cited by 192
Protective effect of porphyra-334 on UVA-induced photoaging in human skin fibroblasts
RYU, J., PARK, S.-J., KIM, I.-H., CHOI, Y. H., & NAM, T.-J. (2014) · International Journal of Molecular Medicine · doi:10.3892/ijmm.2014.1815 · Cited by 172
Review of the safety of application of cosmetic products containing parabens
Matwiejczuk, N., Galicka, A., & Brzóska, M. M. (2020) · Journal of Applied Toxicology · doi:10.1002/jat.3917 · Cited by 166
Collagen–Alginate Composite Hydrogel: Application in Tissue Engineering and Biomedical Sciences
Hu, T., & Lo, A. C. Y. (2021) · Polymers · doi:10.3390/polym13111852 · Cited by 155
Nikolov, A., & Popovski, N. (2021) · Diagnostics · doi:10.3390/diagnostics11030480 · Cited by 141
Munir, M. U., Salman, S., Ihsan, A., & Elsaman, T. (2022) · International Journal of Nanomedicine · doi:10.2147/ijn.s360670 · Cited by 132
“Collagen’s structural and biochemical properties have been extensively studied, and more than 25 collagen subtypes have been found.(87) Both human and mammalian bodies include hundreds of different bioorganic chemicals, proteins, and biological macromolecules, in addition to collagens.”
BackgroundCollagen peptides and the related synthetic peptides: A review on improving skin health
Zhao, X., Zhang, X., & Liu, D. (2021) · Journal of Functional Foods · doi:10.1016/j.jff.2021.104680 · Cited by 133
Holwerda, A. M., & van Loon, L. J. C. (2022) · Nutrition Reviews · doi:10.1093/nutrit/nuab083 · Cited by 117
“At least 28 different types of collagen proteins have been identified.(34,35) Table 1 Amino acid composition of different animalbased protein sources Amino acid Milk Casein Whey Egg Beef”
BackgroundBourgot, I., Primac, I., Louis, T., Noël, A., & Maquoi, E. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.01488 · Cited by 113
Stepanovska, J., Supova, M., Hanzalek, K., Broz, A., & Matejka, R. (2021) · Biomedicines · doi:10.3390/biomedicines9091137 · Cited by 112
Collagen and its modifications—crucial aspects with concern to its processing and analysis
Rýglová, Š., Braun, M., & Suchý, T. (2017) · Macromolecular Materials and Engineering · doi:10.1002/mame.201600460 · Cited by 106
Secreted gliomedin is a perinodal matrix component of peripheral nerves
Eshed, Y., Feinberg, K., Carey, D. J., & Peles, E. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200612139 · Cited by 103
Evans, M., Lewis, E. D., Zakaria, N., Pelipyagina, T., & Guthrie, N. (2021) · Journal of Cosmetic Dermatology · doi:10.1111/jocd.13676 · Cited by 102
Molecular pathways of cell-mediated degradation of fibrillar collagen
Sprangers, S., & Everts, V. (2019) · Matrix Biology · doi:10.1016/j.matbio.2017.11.008 · Cited by 102
Saini, K., Cho, S., Dooling, L. J., & Discher, D. E. (2020) · Matrix Biology · doi:10.1016/j.matbio.2019.06.001 · Cited by 90
Collagen Prolyl 4-Hydroxylase as a Therapeutic Target: Miniperspective
Vasta, J. D., & Raines, R. T. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b00822 · Cited by 82
D'hondt, S., Guillemyn, B., Syx, D., Symoens, S., De Rycke, R., Vanhoutte, L., Toussaint, W., Lambrecht, B. N., De Paepe, A., Keene, D. R., et al. (2018) · Matrix Biology · doi:10.1016/j.matbio.2018.03.008 · Cited by 79
Imle, A., Kumberger, P., Schnellbächer, N. D., Fehr, J., Carrillo-Bustamante, P., Ales, J., Schmidt, P., Ritter, C., Godinez, W. J., Müller, B., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-09879-3 · Cited by 76
Nano-hydroxyapatite/collagen composite as scaffold material for bone regeneration.
Kavitha Sri, A., Arthi, C., Neya, N. R., & Hikku, G. S. (2023) · Biomedical Materials · doi:10.1088/1748-605x/acc99e · Cited by 57
Bergeron, E., Leblanc, E., Drevelle, O., Giguère, R., Beauvais, S., Grenier, G., & Faucheux, N. (2012) · Tissue Engineering Part A · doi:10.1089/ten.tea.2011.0008 · Cited by 51
Engineering fiber anisotropy within natural collagen hydrogels
Ahmed, A., Joshi, I. M., Mansouri, M., Ahamed, N. N. N., Hsu, M.-C., Gaborski, T. R., & Abhyankar, V. V. (2021) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00036.2021 · Cited by 41
(2007) · PubMed · Cited by 39
Wang, L., Xu, Y., Yun, S., Yuan, Q., Satpute-Krishnan, P., & Ye, Y. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.112028 · Cited by 34
Wu, W., Zhou, Z., Sun, G., Liu, Y., Zhang, A., & Chen, X. (2021) · Materials Science and Engineering: C · doi:10.1016/j.msec.2021.111919 · Cited by 33
Vesicoureteral reflux and the extracellular matrix connection
Tokhmafshan, F., Brophy, P. D., Gbadegesin, R. A., & Gupta, I. R. (2017) · Pediatric Nephrology · doi:10.1007/s00467-016-3386-5 · Cited by 30
Ahmed, E., Saleh, T., Yu, L., Song, S., Park, K., Kwak, H., & Woo, H. (2020) · Journal of Biomedical Materials Research Part A · doi:10.1002/jbm.a.36988 · Cited by 23
Kim, M.-K., Kim, E. J., Cheng, Y., Shin, M. H., Oh, J.-H., Lee, D. H., & Chung, J. H. (2017) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2017.02.005 · Cited by 21
Tranfield, E. M., van Eeden, S. F., Yatera, K., Hogg, J. C., & Walker, D. C. (2010) · Canadian Journal of Cardiology · doi:10.1016/s0828-282x(10)70422-0 · Cited by 15
Sensitively humidity-driven actuator and sensor derived from natural skin system
Wang, Y., Duan, R., Tong, Z., Wang, B., Zhang, Z., & Li, Y. (2022) · Sensors and Actuators B: Chemical · doi:10.1016/j.snb.2022.132388 · Cited by 14
Local and Systemic Peptide Therapies for Soft Tissue Regeneration: A Narrative Review
Cushman, C. J., Ibrahim, A. F., Smith, A. D., Hernandez, E. J., MacKay, B., & Zumwalt, M. (2024) · The Yale Journal of Biology and Medicine · doi:10.59249/tknm3388 · Cited by 12
Constructing networks for comparison of collagen types
Wesp, V., Scholz, L., Ziermann-Canabarro, J. M., Schuster, S., & Stark, H. (2024) · Journal of Integrative Bioinformatics · doi:10.1515/jib-2024-0020 · Cited by 9
Genetics of the Ehlers–Danlos syndrome: More than collagen disorders
Van Damme, T., Syx, D., Coucke, P., Symoens, S., De Paepe, A., & Malfait, F. (2015) · Expert Opinion on Orphan Drugs · doi:10.1517/21678707.2015.1022528 · Cited by 4
Investigation of joint hypermobility in individuals with hyperbilirubinemia
Çınar, M., Çakar, M., Öztürk, K., Çetindağlı, İ., Yılmaz, S., & Dinç, A. (2019) · European Journal of Rheumatology · doi:10.5152/eurjrheum.2016.16051 · Cited by 1
Metadata
- Authors
- Gelse, K.
- Venue
- Advanced Drug Delivery Reviews
- Publisher
- Elsevier BV
- Published
- 2003-11-28
- Volume
- 55
- Issue
- 12
- Pages
- 1531-1546
- ISSN
- 0169-409X (ISSN-L)
- OpenAlex
- W2141871922
- Cited by
- 2,654
- References
- 1
- FWCI
- 13.31
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
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
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.