Stability of protease inhibitors based on the Bowman-Birk reactive site loop to hydrolysis by proteases
Author:
Publisher
Wiley
Subject
Endocrinology,Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1399-3011.1997.tb01153.x/fullpdf
Reference30 articles.
1. Amino Acid Sequences of Trypsin-Chymotrypsin Inhibitors (A-I, A-II, B-I, and B-II) from Peanut (Arachis hypogaea)1: A Discussion on the Molecular Evolution of Legume Bowman-Birk Type Inhibitors
2. Wound-Induced Proteinase Inhibitor in Plant Leaves: A Possible Defense Mechanism against Insects
3. Proteolytic Enzymes and Endogenous Trypsin Inhibitor in Germinating Lettuce Seeds
4. Reactive sites of an anticarcinogenic Bowman-Birk proteinase inhibitor are similar to other trypsin inhibitors.
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1. Blood pressure-lowering effects of a Bowman-Birk inhibitor and its derived peptides in normotensive and hypertensive rats;Scientific Reports;2020-07-15
2. Crystallographic structure of a complex between trypsin and a nonapeptide derived from a Bowman-Birk inhibitor found in Vigna unguiculata seeds;Archives of Biochemistry and Biophysics;2019-04
3. Bowman-Birk inhibitors from legumes as colorectal chemopreventive agents;World Journal of Gastroenterology;2014
4. Inhibitory properties and solution structure of a potent Bowman-Birk protease inhibitor from lentil (Lens culinaris, L) seeds;FEBS Journal;2006-07-31
5. Template-assisted rational design of peptide inhibitors of furin using the lysine fragment of the mung bean trypsin inhibitor;FEBS Journal;2006-07-28
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