Metalloproteinases in biology and pathology of the nervous system
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Springer Science and Business Media LLC
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https://www.nature.com/articles/35081571.pdf
Reference100 articles.
1. Yong, V. W., Krekoski, C. A., Forsyth, P. A., Bell, R. & Edwards, D. R. Matrix metalloproteinases and diseases of the central nervous system. Trends Neurosci. 21, 75–80 (1998).
2. Stocker, W. et al. The metzincins — topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a superfamily of zinc-peptidases. Protein Sci. 4, 823–840 (1995).
3. Kojima, S., Itoh, Y., Matsumoto, S., Masuho, Y. & Seiki, M. Membrane-type 6 matrix metalloproteinase (MT6-MMP, MMP-25) is the second glycosyl-phosphatidyl inositol (GPI)-anchored MMP. FEBS Lett. 480, 142–146 (2000).
4. Schlondorff, J. & Blobel, C. P. Metalloprotease-disintegrins: modular proteins capable of promoting cell–cell interactions and triggering signals by protein-ectodomain shedding. J. Cell Sci. 112, 3603–3617 (1999).Excellent review that introduces the biology of ADAMs and then provides details on two members relevant to the CNS: ADAM10 and -17.
5. Izumi, Y. et al. A metalloprotease-disintegrin, MDC9/meltrin-γ/ADAM9 and PKC δ are involved in TPA-induced ectodomain shedding of membrane-anchored heparin-binding EGF-like growth factor. EMBO J. 17, 7260–7272 (1998).
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