Inhibitors of Metalloendopeptidase EC 3.4.24.15 and EC 3.4.24.16 Stabilized against Proteolysis by the Incorporation of β-Amino Acids-Reference-Cited by-同舟云学术

Inhibitors of Metalloendopeptidase EC 3.4.24.15 and EC 3.4.24.16 Stabilized against Proteolysis by the Incorporation of β-Amino Acids

Published:2002-08-03 Issue:35 Volume:41 Page:10819-10826
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Steer David¹,Lew Rebecca¹,Perlmutter Patrick¹,Smith A. Ian¹,Aguilar Marie-Isabel¹

Affiliation:

1. Department of Biochemistry and Molecular Biology, P.O. Box 13D, Monash University, Clayton, Vic 3800, Australia, Department of Chemistry, P.O. Box 23, Monash University, Clayton, Vic 3800, Australia, and Baker Medical Research Institute, PO Box 6492 Melbourne, Vic 8008 Australia

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi0203334

Reference41 articles.

1. A soluble metalloendopeptidase from rat brain. Purification of the enzyme and determination of specificity with synthetic and natural peptides

2. Synaptosomal Membrane-Bound Form of Endopeptidase-24.15 Generates Leu-Enkephalin from Dynorphin1-8, ?- and ?-Neoendorphin, and Met-Enkephalin from Met-Enkephalin-Arg6-Gly7-Leu

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