The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.
Fibronectins, Their Fibrillogenesis, and In Vivo Functions
Open accessAbstract
Fibronectin (FN) is a multidomain protein with the ability to bind simultaneously to cell surface receptors, collagen, proteoglycans, and other FN molecules. Many of these domains and interactions are also involved in the assembly of FN dimers into a multimeric fibrillar matrix. When, where, and how FN binds to its various partners must be controlled and coordinated during fibrillogenesis. Steps in the process of FN fibrillogenesis including FN self-association, receptor activities, and intracellular pathways have been under intense investigation for years. In this review, the domain organization of FN including the extra domains and variable region that are controlled by alternative splicing are described. We discuss how FN-FN and cell-FN interactions play essential roles in the initiation and progression of matrix assembly using complementary results from cell culture and embryonic model systems that have enhanced our understanding of this process.
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Citations
Cites
Matrix elasticity directs stem cell lineage specification
Engler, A. J., Sen, S., Sweeney, H. L., & Discher, D. E. (2006) · Cell · doi:10.1016/j.cell.2006.06.044 · Cited by 13,915
Hynes (2002) · doi:10.1016/s0092-8674(02)00971-6 · Cited by 8,606
The Extracellular Matrix: Not Just Pretty Fibrils
Hynes, R. O. (2009) · Science · doi:10.1126/science.1176009 · Cited by 3,527
Comparative Genomics of the Eukaryotes
Rubin, G. M., Yandell, M. D., Wortman, J. R., Gabor, G. L., Miklos, Nelson, C. R., Hariharan, I. K., Fortini, M. E., Li, P. W., Apweiler, R., et al. (2000) · Science · doi:10.1126/science.287.5461.2204 · Cited by 1,698 · cited 1×
“FN-like genes have yet to be identified for any protostome (Hynes and Zhao 2000; Rubin et al. 2000) or nonchordate deuterostome (Whittaker et al. 2006; Tucker and Chiquet-Ehrismann 2009).”
BackgroundSilberblick/Wnt11 mediates convergent extension movements during zebrafish gastrulation
Heisenberg, C.-P., Tada, M., Rauch, G.-J., Saúde, L., Concha, M. L., Geisler, R., Stemple, D. L., Smith, J. C., & Wilson, S. W. (2000) · Nature · doi:10.1038/35011068 · Cited by 1,013
Muro, A. F., Chauhan, A. K., Gajovic, S., Iaconcig, A., Porro, F., Stanta, G., & Baralle, F. E. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200212079 · Cited by 319
Astrof, S., Crowley, D., & Hynes, R. O. (2007) · Developmental Biology · doi:10.1016/j.ydbio.2007.07.005 · Cited by 136
Cited by
Extracellular Matrix Assembly: A Multiscale Deconstruction
Mouw, J. K., Ou, G., & Weaver, V. M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3902 · Cited by 1,534
Overview of the Matrisome--An Inventory of Extracellular Matrix Constituents and Functions
Hynes, R. O., & Naba, A. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a004903 · Cited by 1,349
The extracellular matrix: tools and insights for the "omics" era
Naba, A., Clauser, K. R., Ding, H., Whittaker, C. A., Carr, S. A., & Hynes, R. O. (2016) · Matrix Biology · doi:10.1016/j.matbio.2015.06.003 · Cited by 1,037
Role of Extracellular Matrix in Development and Cancer Progression
Walker, C., Mojares, E., & Del Río Hernández, A. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19103028 · Cited by 1,084
Biology of the Extracellular Matrix: An Overview
Yue, B. (2014) · Journal of Glaucoma · doi:10.1097/ijg.0000000000000108 · Cited by 805
Metadata
- Authors
- Schwarzbauer, J. E., & DeSimone, D. W.
- Venue
- Cold Spring Harbor Perspectives in Biology
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2011-05-16
- Volume
- 3
- Issue
- 7
- Pages
- a005041-a005041
- ISSN
- 1943-0264 (ISSN-L)
- OpenAlex
- W2142761181
- Cited by
- 445
- References
- 7
- Type
- posted content
- Language
- en
- Open access
- green
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