Endopeptidase-24.11 (Neprilysin) and Relatives
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Publisher
Springer US
Link
http://link.springer.com/content/pdf/10.1007/978-1-4613-0335-0_17.pdf
Reference35 articles.
1. Abassi, Z. A., Golomb, E., Bridenbaugh, R. and Keiser, H. R., 1993, Metabolism of endothelin-1 and big endothelin-1 by recombinant neutral endopeptidase EC 3.4.24.11., Brit J Pharmacol. 109:1024–1028.
2. Barnes, K., Matsas, R., Hooper, N. M., Turner, A. J., and Kenny, A. J., 1988a, Endopeptidase-24.11 is striosomally ordered in pig brain and, in contrast to aminopeptidase N and peptidyl dipeptidase A, is a marker for a set of striatal efferent fibres, Neuroscience 27:799–817.
3. Barnes, K., Turner, A. J., and Kenny, A. J., 1988b, Electron microscopic immunocytochemistryof pig brain shows that endopeptidase-24.11 is localised in neuronal membranes, Neurosci. Lett., 94:64–69.
4. Barnes, K., Turner, A. J., and Kenny, A. J., 1992, Membrane localisation of endopeptidase-24.11 and peptidyl dipeptidase A in the pig brain: a study using subcellular fractionation and electron microscopic immunocytochemistry, J. Neurochem. 58:2088–2096.
5. Barnes, K., Turner, A. J., and Kenny, A. J., 1993, An immunoelectron microscopic study of pig substantia nigra shows co-localisation of endopeptidase-24.11 with substance P, Neuroscience, 53:1073–1082.
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