An investigation of the molecular properties and stability of intermediates of proenkephalin in isolated bovine adrenal medullary chromaffin granules.-Reference-Cited by-同舟云学术

An investigation of the molecular properties and stability of intermediates of proenkephalin in isolated bovine adrenal medullary chromaffin granules.

Published:1987-03 Issue:7 Volume:262 Page:3382-3387
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Birch N.P.,Davies A.D.,Christie D.L.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference26 articles.

1. Strategies for the biosynthesis of bioactive peptides

2. The Enzymology and Intracellular Organization of Peptide Precursor Processing: The Secretory Vesicle Hypothesis

3. Proteolysis in Neuropeptide Processing and Other Neural Functions

4. Biochemistry of the enkephalins and enkephalin-containing peptides

5. Cloning and sequence analysis of cDNA for bovine adrenal preproenkephalin

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1. Cathepsin L in secretory vesicles functions as a prohormone-processing enzyme for production of the enkephalin peptide neurotransmitter;Proceedings of the National Academy of Sciences;2003-07-17

2. Role of endogenous pro-enkephalin A-derived peptides in human T cell proliferation and monocyte IL-6 production;Journal of Neuroimmunology;1998-04

3. Proenkephalin-processing Enzymes in Chromaffin Granules;Annals of the New York Academy of Sciences;1996-06

4. Posttranslational processing of proenkephalins and chromogranins/secretogranins;Neurochemistry International;1993-04

5. Proteases for Neuropeptide Precursor Processing in Bovine Adrenal Medullary Chromaffin Granules;Growth Factors, Peptides and Receptors;1993