A proposal for a three-dimensional representation of the S1 subsite of α-chymotrypsin
Author:
Publisher
Elsevier BV
Subject
Organic Chemistry,Clinical Biochemistry,Drug Discovery,Pharmaceutical Science,Molecular Biology,Molecular Medicine,Biochemistry
Reference18 articles.
1. On the size of the active site in proteases. I. Papain
2. Structure and mechanism of chymotrypsin
3. AN INVERSION OF THE USUAL ANTIPODAL SPECIFICITY OBSERVED IN α-CHYMOTRYPSIN CATALYZED REACTIONS1
4. Steric Course and Specificity of α-Chymotrypsin-catalyzed Reactions. I
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1. Metal vapour derived supported rhodium nanoparticles in the synthesis of β-lactams and β-lactones derivatives;Journal of Organometallic Chemistry;2012-03
2. Design of protease inhibitors on the basis of substrate stereospecificity;Biopolymers;1999
3. A novel type of structurally simple nonpeptide inhibitors for α-chymotrypsin. Induced-fit binding of methyl 2-allyl-3-benzene-propanoate to the S2 subsite pocket;Bioorganic & Medicinal Chemistry;1998-02
4. Inhibition of papain with 2-benzyl-3,4-epoxybutanoic acid esters. Mechanistic and stereochemical probe for cysteine protease catalysis;Bioorganic & Medicinal Chemistry;1997-11
5. Peptidyl epoxides as inhibitors of α-chymotrypsin: Remarkable change from irreversible to reversible competitive inhibitor as a consequence of the improvement of binding affinity;Bioorganic & Medicinal Chemistry Letters;1996-12
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