The synthesis, purification, and evaluation of a chromophoric substrate for pepsin and other aspartyl proteases: Design of a substrate based on subsite preferences-Reference-Cited by-同舟云学术

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The synthesis, purification, and evaluation of a chromophoric substrate for pepsin and other aspartyl proteases: Design of a substrate based on subsite preferences

Published:1984-04 Issue:1 Volume:138 Page:68-73
ISSN:0003-2697
Container-title:Analytical Biochemistry
language:en
Short-container-title:Analytical Biochemistry

Author:

Dunn Ben M.,Kammermann Bruce,McCurry Kenneth R.

Funder

National Institutes of Health

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference34 articles.

1. Penicillopepsin from Penicillium janthinellum crystal structure at 2.8 Å and sequence homology with porcine pepsin

2. Acid Proteases, Structure, Function and Biology;Jenkins,1977

3. Structure of acid protease from Endothia parasitica in crosslinked form at 2.45-.ANG. resolution

4. Acid Proteases, Structure, Function and Biology;Hsu,1977

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1. Chymosin, Pepsins and Other Aspartyl Proteinases: Structures, Functions, Catalytic Mechanism and Milk-Clotting Properties;Cheese;2017

2. Cathepsin E;Handbook of Proteolytic Enzymes;2013

3. Ionic derivatives of betulinic acid as novel HIV-1 protease inhibitors;Journal of Enzyme Inhibition and Medicinal Chemistry;2011-10-10

4. Introduction to the Aspartic Proteinase Family;Aspartic Acid Proteases as Therapeutic Targets;2011-04-04

5. Quantitative determination and localization of cathepsin D and its inhibitors.;Folia Histochemica et Cytobiologica;2009-12-10

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