Studies on in vitro proteolytic sensitivity of peptides inhibiting herpes simplex virus ribonucleotide reductases lead to discovery of a stable and potent inhibitor
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1399-3011.1991.tb00735.x/fullpdf
Reference25 articles.
1. Specific inhibition of herpesvirus ribonucleotide reductase by a nonapeptide derived from the carboxy terminus of subunit 2
2. Specific inhibition of herpesvirus ribonucleotide reductase by synthetic peptides
3. Mechanism of inhibition of herpes simplex virus (HSV) ribonucleotide reductase by a nonapeptide corresponding to the carboxyl terminus of its subunit 2. Specific binding of a photoaffinity analog, [4′- azido-Phe6] HSV H2-6(6-15), to subunit 1.
4. Oligopeptides inhibit the ribonucleotide reductase of herpes simplex virus by causing subunit separation
5. Ribonucleotide Reductase Encoded by Herpes Simplex Virus Is a Determinant of the Pathogenicity of the Virus in Mice and a Valid Antiviral Target
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4. Inactivation of Herpes Simplex Virus Ribonucleotide Reductase by Subunit Association Inhibitors: A Potential Antiviral Strategy;The Search for Antiviral Drugs;1993
5. Substituted penta- and hexapeptides as potent inhibitors of herpes simplex virus type 2 ribonucleotide reductase;Bioorganic & Medicinal Chemistry Letters;1992-10
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