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Development and Biological Evaluation of Acyl Protein Thioesterase 1 (APT1) Inhibitors
Author(s) -
Deck Patrick,
Pendzialek Dirk,
Biel Markus,
Wagner Melanie,
Popkirova Boriana,
Ludolph Björn,
Kragol Goran,
Kuhlmann Jürgen,
Giannis Athanassios,
Waldmann Herbert
Publication year - 2005
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200462625
Subject(s) - peptidomimetic , thioesterase , enzyme , chemistry , biochemistry , computational biology , computer science , combinatorial chemistry , biology , biosynthesis , peptide
It works both ways : The development of potent peptidomimetic acyl protein thioesterase 1 (APT1) inhibitors, such as Raspalin 3 (see structure), and their use in biological and biochemical investigations are reported. The results show that the enzyme can deacylate and acylate Ras proteins.