The Core Structures of Roseophilin and the Prodigiosin Alkaloids Define a New Class of Protein Tyrosine Phosphatase Inhibitors

• Published in: Chembiochem : a European journal of chemical biology Vol. 5; no. 11; pp. 1575 - 1579
• Main Authors: Fürstner, Alois, Reinecke, Kerstin, Prinz, Heino, Waldmann, Herbert
• Format: Journal Article
• Language: English
• Published: Weinheim WILEY-VCH Verlag 05-11-2004; WILEY‐VCH Verlag
• Subjects: alkaloids; Alkaloids - chemistry; Alkaloids - classification; Alkaloids - pharmacology; biological activity; Enzyme Inhibitors - chemistry; Enzyme Inhibitors - classification; Enzyme Inhibitors - pharmacology; enzymes; Heterocyclic Compounds, 3-Ring - chemistry; Heterocyclic Compounds, 3-Ring - classification; Heterocyclic Compounds, 3-Ring - pharmacology; Humans; inhibitors; Molecular Structure; phosphatases; prodigiosin; Prodigiosin - chemistry; Prodigiosin - classification; Prodigiosin - pharmacology; Protein Tyrosine Phosphatase, Non-Receptor Type 1; Protein Tyrosine Phosphatases - antagonists & inhibitors; Pyrroles - chemistry; Pyrroles - classification; Pyrroles - pharmacology
• ISSN: 1439-4227; 1439-7633
• DOI: 10.1002/cbic.200400135

A common core. Protein phosphatases, such as the dual‐specificity phosphatase VHR and the tyrosine phosphatase PTP1B, are key regulators of innumerable cellular processes, and new classes of phosphatase inhibitors are in demand. The azafulvene‐containing core structures of the roseophilin and prodigiosin alkaloids define such a new class.