The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.
COMP (cartilage oligomeric matrix protein) is structurally related to the thrombospondins.
Open accessAbstract
Cloning and sequence analysis of cartilage oligomeric matrix protein (COMP) cDNA, representing a cartilage pentameric protein, revealed a protein of 755 amino acid residues with a calculated molecular mass of 82,700 Da. Expression of the cDNA in COS cells showed that COMP is a homopolymer composed of five identical disulfide-linked subunits. COMP is homologous to the carboxyl-terminal half of thrombospondin, and the homologies include 89% and 54% of the residues in COMP and thrombospondin, respectively. The similarities are most pronounced in the carboxyl-terminal domains and in the calcium binding type 3 repeat domains in which about 60% of the amino acid residues are identical. In the type 2/epidermal growth factor repeat domains the two proteins contain 41% identical residues. The sequence of the amino-terminal 84-amino acid residues is unique for COMP. Comparison of the amino acid sequences in the type 2 and type 3 repeat domains of COMP and the thrombospondins shows that COMP is the product of a unique gene and not the result of an alternatively spliced thrombospondin gene.
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Lawler, J., & Hynes, R. O. (1986) · The Journal of cell biology · doi:10.1083/jcb.103.5.1635 · Cited by 575
Extracellular proteins that modulate cell-matrix interactions. SPARC, tenascin, and thrombospondin
Sage, E. H., & Bornstein, P. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)98545-5 · Cited by 556
Cartilage matrix proteins. An acidic oligomeric protein (COMP) detected only in cartilage.
Hedbom, E., Antonsson, P., Hjerpe, A., Aeschlimann, D., Paulsson, M., Rosa-Pimentel, E., Sommarin, Y., Wendel, M., Oldberg, A., & Heinegård, D. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42671-3 · Cited by 525
Self-citationCell attachment to thrombospondin: the role of ARG-GLY-ASP, calcium, and integrin receptors.
Lawler, J., Weinstein, R., & Hynes, R. O. (1988) · The Journal of cell biology · doi:10.1083/jcb.107.6.2351 · Cited by 474
Transcending the impenetrable: How proteins come to terms with membranes
von Heijne, G. (1988) · Biochimica et Biophysica Acta (BBA) - Reviews on Biomembranes · doi:10.1016/0304-4157(88)90013-5 · Cited by 466
Regulation of the activity of a new inhibitor of angiogenesis by a cancer suppressor gene
Rastinejad, F., Polverini, P. J., & Bouck, N. P. (1989) · Cell · doi:10.1016/0092-8674(89)90238-9 · Cited by 463
The structural and functional properties of thrombospondin
Lawler, J. (1986) · Blood · doi:10.1182/blood.v67.5.1197.1197 · Cited by 350
Structure and function of epidermal growth factor‐like regions in proteins
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Cited by
Barry, F., Boynton, R. E., Liu, B., & Murphy, J. M. (2001) · Experimental Cell Research · doi:10.1006/excr.2001.5278 · Cited by 1,020
Tolsma, S., Volpert, O., Good, D., Frazier, W., Polverini, P., & Bouck, N. (1993) · The Journal of cell biology · doi:10.1083/jcb.122.2.497 · Cited by 573
Cartilage in normal and osteoarthritis conditions
Martel-Pelletier, J., Boileau, C., Pelletier, J.-P., & Roughley, P. J. (2008) · Best Practice & Research Clinical Rheumatology · doi:10.1016/j.berh.2008.02.001 · Cited by 559
Halper, J., & Kjaer, M. (2014) · Advances in Experimental Medicine and Biology · doi:10.1007/978-94-007-7893-1_3 · Cited by 532
Mechanism of longitudinal bone growth and its regulation by growth plate chondrocytes
Hunziker, E. B. (1994) · Microscopy Research and Technique · doi:10.1002/jemt.1070280606 · Cited by 461
Metadata
- Authors
- Oldberg, A., Antonsson, P., Lindblom, K., & Heinegård, D.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1992-11
- Volume
- 267
- Issue
- 31
- Pages
- 22346-22350
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1605960013
- Cited by
- 324
- References
- 26
- FWCI
- 9.88
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Oldberg, A., Antonsson, P., Lindblom, K., & Heinegård, D. (1992). COMP (cartilage oligomeric matrix protein) is structurally related to the thrombospondins. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)41677-8
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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