The DOI matches its Crossref record; 225 of the 225 references it cites were found in a registry or an index.
Ectodomain shedding and ADAMs in development
Abstract
Proteolytic enzymes belonging to the A Disintegin And Metalloproteinase (ADAM) family are able to cleave transmembrane proteins close to the cell surface, in a process referred to as ectodomain shedding. Substrates for ADAMs include growth factors, cytokines, chemokines and adhesion molecules, and, as such, many ADAM proteins play crucial roles in cell-cell adhesion, extracellular and intracellular signaling, cell differentiation and cell proliferation. In this Review, we summarize the fascinating roles of ADAMs in embryonic and adult tissue development in both vertebrates and invertebrates.
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Items 201–225 of 225
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The shedding protease ADAM17: Physiology and pathophysiology
Zunke, F., & Rose-John, S. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.07.001 · Cited by 336
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Kuhn, P.-H., Colombo, A. V., Schusser, B., Dreymueller, D., Wetzel, S., Schepers, U., Herber, J., Ludwig, A., Kremmer, E., Montag, D., et al. (2016) · eLife · doi:10.7554/elife.12748 · Cited by 163
Self-citationBace1 and Neuregulin‐1 cooperate to control formation and maintenance of muscle spindles
Cheret, C., Willem, M., Fricker, F. R., Wende, H., Wulf‐Goldenberg, A., Tahirovic, S., Nave, K., Saftig, P., Haass, C., Garratt, A. N., et al. (2013) · The EMBO Journal · doi:10.1038/emboj.2013.146 · Cited by 124
Self-citationGoth, C. K., Halim, A., Khetarpal, S. A., Rader, D. J., Clausen, H., & Schjoldager, K. T.-B. G. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1511175112 · Cited by 123
Metadata
- Authors
- Weber, S., & Saftig, P.
- Venue
- Development
- Publisher
- The Company of Biologists
- Published
- 2012-10-15
- Volume
- 139
- Issue
- 20
- Pages
- 3693-3709
- ISSN
- 0950-1991 (ISSN-L)
- 1477-9129
- OpenAlex
- W1978607785
- Cited by
- 259
- References
- 225
- FWCI
- 5.28
- Type
- journal article
- Language
- en
- Open access
- closed
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