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DNA and Cell Biology|March 12, 1999
Cloning and expression of Aplysia carboxypeptidase D, a candidate prohormone-processing enzymeX Fan, Y Qian, L D Fricker, et al.
Proceedings of the National Academy of Sciences of the United States of America|August 2, 2001
Identification of peptides from brain and pituitary of Cpe(fat)/Cpe(fat) miceF Y Che, L Yan, H Li, et al.
Molecular Endocrinology (Baltimore, Md.)|December 1, 1992
Expression of the rat carboxypeptidase-E gene in neuroendocrine and nonneuroendocrine cell linesY K Jung, C J Kunczt, R K Pearson, et al.
The Journal of Biological Chemistry|May 19, 2000
The C-terminal region of proSAAS is a potent inhibitor of prohormone convertase 1Y Qian, L A Devi, N Mzhavia, et al.
Molecular Endocrinology (Baltimore, Md.)|September 1, 1991
Structural characterization of the rat carboxypeptidase-E geneY K Jung, C J Kunczt, R K Pearson, et al.
Endocrinology|November 5, 1997
Beta-cell lines derived from transgenic Cpe(fat)/Cpe(fat) mice are defective in carboxypeptidase E and proinsulin processingO Varlamov, L D Fricker, H Furukawa, et al.
Molecular Endocrinology (Baltimore, Md.)|April 1, 1989
Isolation and sequence analysis of cDNA for rat carboxypeptidase E [EC 3.4.17.10], a neuropeptide processing enzymeL D Fricker, J P Adelman, J Douglass, et al.
DNA and Cell Biology|July 1, 1997
Cloning and sequence analysis of cDNA encoding rat carboxypeptidase DX Xin, O Varlamov, R Day, et al.
The Journal of Biological Chemistry|July 4, 2001
Inhibitory specificity and potency of proSAAS-derived peptides toward proprotein convertase 1A Basak, P Koch, M Dupelle, et al.
Proceedings of the National Academy of Sciences of the United States of America|July 1, 1985
Immunochemical characterization of carboxypeptidase B-like peptide-hormone-processing enzymeV Y Hook, E Mezey, L D Fricker, et al.
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