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Collagen family of proteins
Abstract
Collagen molecules are structural macromolecules of the extracellular matrix that include in their structure one or several domains that have a characteristic triple helical conformation. They have been classified by types that define distinct sets of polypeptide chains that can form homo‐ and heterotrimeric assemblies. All the collagen molecules participate in supramolecular aggregates that are stabilized in part by interactions between triple helical domains. Fourteen collagen types have been defined so far. They form a wide range of structures. Most notable are 1 ) fibrils that are found in most connective tissues and are made by alloys of fibrillar collagens (types I, II, III, V, and XI) and 2 ) sheets constituting basement membranes (type IV collagen), Descemet's membrane (type VIII collagen), worm cuticle, and organic exoskeleton of sponges. Other collagens, present in smaller quantities in tissues, play the role of connecting elements between these major structures and other tissue components. The fibril‐associated collagens with interrupted triple helices (FACITs) (types IX, XII, and XIV) appear to connect fibrils to other matrix elements. Type VII collagen assemble into anchoring fibrils that bind epithelial basement membranes and entrap collagen fibrils from the underlying stroma to glue the two structures together. Type VI collagen forms thin‐beaded filaments that may interact with fibrils and cells.—van der Rest, M.; Garrone, R. Collagen family of proteins. FASEB J. 5: 2814‐2823; 1991.
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Ricard-Blum, S. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004978 · Cited by 2,305
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Hubbell, J. A. (1995) · Nature Biotechnology · doi:10.1038/nbt0695-565 · Cited by 1,060
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
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Brown, B. N., Valentin, J. E., Stewart-Akers, A. M., McCabe, G. P., & Badylak, S. F. (2009) · Biomaterials · doi:10.1016/j.biomaterials.2008.11.040 · Cited by 896
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Hussey, G. S., Dziki, J. L., & Badylak, S. F. (2018) · Nature Reviews Materials · doi:10.1038/s41578-018-0023-x · Cited by 844
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Berneburg, M., Plettenberg, H., & Krutmann, J. (2000) · Photodermatology, Photoimmunology & Photomedicine · doi:10.1034/j.1600-0781.2000.160601.x · Cited by 403
Singh, B., Fleury, C., Jalalvand, F., & Riesbeck, K. (2012) · FEMS Microbiology Reviews · doi:10.1111/j.1574-6976.2012.00340.x · Cited by 302
Venstrom, K. A., & Reichardt, L. F. (1993) · The FASEB Journal · doi:10.1096/fasebj.7.11.8370483 · Cited by 269
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Metadata
- Authors
- Van Der Rest, M., & Garrone, R.
- Venue
- The FASEB Journal
- Publisher
- Wiley
- Published
- 1991-10
- Volume
- 5
- Issue
- 13
- Pages
- 2814-2823
- ISSN
- 0892-6638 (ISSN-L)
- 1530-6860
- OpenAlex
- W2144985870
- Cited by
- 1,271
- References
- 0
- FWCI
- 41.62
- Type
- journal article
- Language
- en
- Open access
- closed
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