References
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.
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.
Dolenga, M.; Hechtman, P. Cytotoxicity of carbobenzoxy-protected amino acids. In Vitro Cell. Dev. Biol. 28A:300–302; 1992.
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.
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.
Moses, M. A.; Langer, R. A metalloproteinase inhibitor as an inhibitor of neovascularization. J. Cell. Biochem. 47:230–235; 1991.
Mundy, D.; Hermann, T.; Strittmatter, W. J. Specific inhibitors implicate a soluble metalloendoprotease in exocytosis. Cell Mol. Neurobiol. 7:425–437; 1987.
Mundy, D. I.; Strittmatter, W. J. Requirement for metalloendoprotease in exocytosis: evidence in mast cells and adrenal chromaffin cells. Cell 40:645–656; 1985.
Yuli, I.; Lelkes, P. I. Neutral endopeptidase activity in the interaction ofN-formyl-l-methionyl-l-leucyl-L-phenylalanine with human polymorphonuclear leukocytes. Eur. J. Biochem. 201:421–430; 1991.
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Lelkes, P.I. Cytotoxicity of carbobenzoxy-protected amino acids. In Vitro Cell Dev Biol - Animal 30, 75–76 (1994). https://doi.org/10.1007/BF02631394
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DOI: https://doi.org/10.1007/BF02631394