Cytotoxicity of carbobenzoxy-protected amino acids
Author:
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Developmental Biology,General Medicine
Link
http://link.springer.com/content/pdf/10.1007/BF02631394.pdf
Reference9 articles.
1. Aiello, L. P.; Wessling-Resnick, M.; Pilch, P. F. Dipeptide metalloendoprotease substrates are glucose transport inhibitors and membrane structure perturbants. Biochemistry 25:3944–3950; 1986.
2. Baxter, D. A.; Johnston, D.; Strittmatter, W. J. Protease inhibitors implicate metalloendoprotease in synaptic transmission at the mammalian neuromuscular junction. Proc. Natl. Acad. Sci. USA 80:4174–4178; 1983.
3. Dolenga, M.; Hechtman, P. Cytotoxicity of carbobenzoxy-protected amino acids. In Vitro Cell. Dev. Biol. 28A:300–302; 1992.
4. Harris, B.; Cheek, T. R.; Burgoyne, R. D. Effects of metalloendoprotease inhibitors on secretion and intracellular free calcium in bovine adrenal chromaffin cells. Biochim. Biophys. Acta 889:1–5; 1986.
5. Lelkes, P. I.; Pollard, H. B. Oligopeptide inhibitors of metalloendoprotease activity inhibit catecholamine secretion form bovine adrenal chromaffin cells by modulating intracellular calcium homeostasis. J. Biol. Chem. 262:15496–15505; 1987.
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