The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Structure and biological activity of basement membrane proteins
Open accessAbstract
Collagen type IV, laminin, heparan sulfate proteoglycans, nidogen (entactin) and BM‐40 (osteonectin, SPARC) represent major structural proteins of basement membranes. They are well‐characterized in their domain structures, amino acid sequences and potentials for molecular interactions. Such interactions include self‐assembly processes and heterotypic binding between individual constituents, as well as binding of calcium (laminin. BM‐40) and are likely to be used for basement membrane assembly. Laminin, collagen IV and nidogen also possess several cell‐binding sites which interact with distinct cellular receptors. Some evidence exists that those interactions are involved in the control of cell behaviour. These observations have provided a more defined understanding of basement membrane function and the definition of new research goals in the future.
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Cites
Laminin–a glycoprotein from basement membranes
Timpl, R., Rohde, H., Robey, P. G., Rennard, S. I., Foidart, J. M., & Martin, G. R. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)83607-4 · Cited by 2,378
Self-citationBasement 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
Domains of laminin with growth-factor activity
Panayotou, G., End, P., Aumailley, M., Timpl, R., & Engel, J. (1989) · Cell · doi:10.1016/0092-8674(89)90987-2 · Cited by 341
Self-citationParthasarathy, N., & Spiro, R. G. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)90809-4 · Cited by 99
Cited by
Vukicevic, S., Kleinman, H. K., Luyten, F. P., Roberts, A. B., Roche, N. S., & Reddi, A. H. (1992) · Experimental Cell Research · doi:10.1016/0014-4827(92)90397-q · Cited by 696
Hudson, B. G., Reeders, S. T., & Tryggvason, K. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74270-7 · Cited by 623
Leung-Hagesteijn, C., Spence, A. M., Stern, B. D., Zhou, Y., Su, M.-W., Hedgecock, E. M., & Culotti, J. G. (1992) · Cell · doi:10.1016/0092-8674(92)90357-i · Cited by 414
Two contrary functions of tenascin: Dissection of the active sites by recombinant tenascin fragments
Spring, J., Beck, K., & Chiquet-Ehrismann, R. (1989) · Cell · doi:10.1016/0092-8674(89)90294-8 · Cited by 413
Peles, E., Nativ, M., Lustig, M., Grumet, M., Schilling, J., Martinez, R., Plowman, G. D., & Schlessinger, J. (1997) · The EMBO Journal · doi:10.1093/emboj/16.5.978 · Cited by 400
Metadata
- Authors
- TIMPL, R.
- Venue
- European Journal of Biochemistry
- Publisher
- Wiley
- Published
- 1989-04
- Volume
- 180
- Issue
- 3
- Pages
- 487-502
- ISSN
- 0014-2956 (ISSN-L)
- 1432-1033
- OpenAlex
- W1973064020
- Cited by
- 973
- References
- 4
- FWCI
- 19.30
- Type
- journal article
- Language
- en
- Open access
- bronze
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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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