Inhibitory properties of nonapeptide loop structures related to reactive sites of soybean Bowman-Birk inhibitor
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(78)80304-4/fullpdf
Reference17 articles.
1. Further evidence for a dual, independent, activity against trypsin and α-chymotrypsin of inhibitor AA from soybeans
2. Studies on Soybean Trypsin Inhibitors
3. Synthesis and activity of nonapeptide fragments of soybean Bowman-Birk inhibitor
4. Studies on the Synthesis of Proteinase Inhibitors
5. On the size of the active site in proteases. I. Papain
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2. Inactivation of Soybean Bowman–Birk Inhibitor by Stevioside: Interaction Studies and Application to Soymilk;Journal of Agricultural and Food Chemistry;2019-02-07
3. Evidence for Ancient Origins of Bowman-Birk Inhibitors from Selaginella moellendorffii;The Plant Cell;2017-03
4. Tailoring elastase inhibition with synthetic peptides;European Journal of Pharmacology;2011-09
5. Molecular engineering of a small trypsin inhibitor based on the binding loop of horsegram seed Bowman-Birk inhibitor;Journal of Enzyme Inhibition and Medicinal Chemistry;2010-12-20
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