Journal
ANTI-CANCER AGENTS IN MEDICINAL CHEMISTRY
Volume 11, Issue 1, Pages 164-171Publisher
BENTHAM SCIENCE PUBL LTD
DOI: 10.2174/187152011794941271
Keywords
Protein tyrosine phosphatases; inhibitor; metal ions; vanadium complexes; copper complexes; zinc complexes; gold complexes; metal complexes; selectivity; phosphorylation
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Funding
- National Natural Science Foundation of China [20471033, 21001070]
- Scientific Research Foundation for the Returned Overseas Chinese Scholars, State Education Ministry [20093602]
- Natural Science Foundation of Shanxi Province [20051013, 2010011011-2]
- Shanxi Scholarship Council of China
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Protein tyrosine phosphatases (PTPs) are a large family of signaling enzymes playing critical role in signal transduction and regulation of cellular processes. Dysfunction of PTP activity is associated with diabetes, cancer, autoimmune disorders, and neural diseases. PTP inhibitors therefore emerged as promising therapeutic targets. Recent research indicates that besides small organic molecules, metal ions and metal complexes can also strongly inhibit PTPs both in vitro and in vivo, resulting in the increase of phosphorylation of corresponding substrates and the modulation of cellular process. Structure of metal complexes influences the potency and selectivity of PTP inhibition. Detailed studies on this subject are not only expected to yield metal-based drugs targeting individual PTPs, but also to support understanding the function of metals in organisms. This review focuses on recent advancements in this area of research.
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