Mapping sequence differences between thimet oligopeptidase and neurolysin implicates key residues in substrate recognition-Reference-Cited by-同舟云学术

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Mapping sequence differences between thimet oligopeptidase and neurolysin implicates key residues in substrate recognition

Published:2009-01-01 Issue:9 Volume:11 Page:2237-2246
ISSN:0961-8368
Container-title:Protein Science
language:en
Short-container-title:Protein Science

Author:

Ray Kallol,Hines Christina S.,Rodgers David W.

Publisher

Wiley

Subject

Molecular Biology,Biochemistry

Reference40 articles.

1. Proteolysis in eukaryotic cells: Proteinase yscE, a new yeast peptidase;Achstetter;J. Biol. Chem.,1984

2. Proteinase yscD: Purification and characterization of a new yeast peptidase;Achstetter;J. Biol. Chem.,1985

3. Role of endopeptidase 3.4.24.16 in the catabolism of neurotensin, in vivo, in the vascularly perfused dog ileum;Barelli;Br. J. Pharmacol.,1994

4. Thimet oligopeptidase and oligopeptidase M or neurolysin;Barrett;Meth. Enzymol.,1995

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1. Structural basis of divergent substrate recognition and inhibition of human neurolysin;Scientific Reports;2024-08-08

2. Thimet oligopeptidase (THOP 1) distribution in cane toad (Bufo Marinus, Linnaeus, 1758) brain;Journal of Chemical Neuroanatomy;2023-11

3. Neurolysin Knockout Mice in a Diet-Induced Obesity Model;International Journal of Molecular Sciences;2023-10-14

4. Development of fluorogenic substrates for colorectal tumor-related neuropeptidases for activity-based diagnosis;Chemical Science;2023

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