Neuropeptide processing by single-step cleavage: Conversion of leumorphin (dynorphin B-29) to dynorphin B
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference19 articles.
1. Cloning and sequence analysis of cDNA for porcine β-neo-endorphin/dynorphin precursor
2. The complete amino acid sequence of α-neo-endorphin
3. Leumorphin is a novel endogenous opioid peptide derived from preproenkephalin B
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1. Specificity of the Dynorphin-Processing Endoprotease: Comparison with Prohormone Convertases;Journal of Neurochemistry;2008-06-28
2. Aminopeptidase B, a glucagon-processing enzyme: site directed mutagenesis of the Zn2+-binding motif and molecular modelling;BMC Biochemistry;2007-10-31
3. Cysteinyl Proteinases and Their Selective Inactivation;Advances in Enzymology - and Related Areas of Molecular Biology;2006-11-22
4. Conversion of Leumorphin (Dynorphin B-29) to Dynorphin B and Dynorphin B-14 by Thiol Protease Activity;Journal of Neurochemistry;2006-10-05
5. Expression of aminopeptidase B in the developing and adult rat retina;Experimental Eye Research;2004-11
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