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Structure–Activity Relationships of Glycogen Phosphorylase Inhibitor FR258900 and Its Analogues: A Combined Synthetic, Enzyme Kinetics, and Computational Study
Author(s) -
Juhász László,
Varga Gergely,
Sztankovics Andrea,
Béke Ferenc,
Docsa Tibor,
KissSzikszai Attila,
Gergely Pál,
Kóňa Juraj,
Tvaroška Igor,
Somsák László
Publication year - 2014
Publication title -
chempluschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.801
H-Index - 61
ISSN - 2192-6506
DOI - 10.1002/cplu.201402302
Subject(s) - allosteric regulation , glycogen phosphorylase , natural product , enzyme , chemistry , cover (algebra) , stereochemistry , enzyme kinetics , kinetics , biochemistry , active site , physics , engineering , mechanical engineering , quantum mechanics
Invited for this month’s cover are a group of collaborators from the University of Debrecen (L. Somsák and P. Gergely) and the Institute of Chemistry of the Slovak Academy of Sciences (I. Tvaroška). The cover picture shows the natural product FR258900, some synthetic analogues, and the binding of the most active inhibitor to the allosteric site of the enzyme. Read the full text of the article at 10.1002/cplu.201402181