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Collagen: Molecular Diversity in the Body's Protein Scaffold
Abstract
Intensive research in the last decade has revealed a wealth of detail on the mechanism of biosynthesis, molecular structure, and covalent cross-linking of collagen. Tissues of higher animals express a family of at least five genetically distinct types of collagen molecule, each apparently tailored for different construction work outside the cell. Within each genetic type of collagen, further chemical heterogeneity is also evident; the variations in hydroxylation, glycosylation, and cross-linking are dependent, for example, on tissue type, age, and hormonal status. The functional significance of collagen's molecular diversity and its control by different cells and tissues are not yet well understood but abnormalities of collagen in many human diseases keep this protein a focal molecule of medical research.
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Cited by
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Basement membrane complexes with biological activity
Kleinman, H. K., McGarvey, M. L., Hassell, J. R., Star, V. L., Cannon, F. B., Laurie, G. W., & Martin, G. R. (1986) · Biochemistry · doi:10.1021/bi00350a005 · Cited by 1,502
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Waite, J. H., & Tanzer, M. L. (1981) · Science · doi:10.1126/science.212.4498.1038 · Cited by 1,050
Extracellular Matrix and Dermal Fibroblast Function in the Healing Wound
Tracy, L. E., Minasian, R. A., & Caterson, E. J. (2016) · Advances in Wound Care · doi:10.1089/wound.2014.0561 · Cited by 1,008
Quantitation of hydroxypyridinium crosslinks in collagen by high-performance liquid chromatography
Eyre, D. R., Koob, T. J., & Van Ness, K. P. (1984) · Analytical Biochemistry · doi:10.1016/0003-2697(84)90101-5 · Cited by 658
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Metadata
- Authors
- Eyre, D. R.
- Venue
- Science
- Published
- 1980-03-21
- Volume
- 207
- Issue
- 4437
- Pages
- 1315-1322
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2088377273
- Cited by
- 451
- References
- 0
- FWCI
- 31.58
- Type
- journal article
- Language
- en
- Open access
- closed
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