Protein-Tyrosine Phosphatase Inhibitors
A special issue of Molecules (ISSN 1420-3049). This special issue belongs to the section "Bioorganic Chemistry".
Deadline for manuscript submissions: closed (30 January 2018) | Viewed by 39024
Special Issue Editors
2. Institute of Biology Leiden, Leiden University, Leiden, The Netherlands
Interests: protein-tyrosine phosphatase; signaling; PTEN; SHP2; RPTPalpha; zebrafish; gastrulation; cancer; Noonan Syndrome
Interests: peptidomimetics; protein mimics; synthetic vaccines; synthetic antibodies; protease inhibitors; protein phosphatase inhibitors; electrophilic traps; cancer; infections; inflammation
Special Issue Information
Dear Colleagues,
Protein-tyrosine phosphatases counteract protein-tyrosine kinases and, hence, have a central role in development and disease, as regulators of phosphotyrosine levels in cellular proteins. Protein-tyrosine phosphatases have been heralded as drug targets for decades, particularly for conditions such as cancer and diabetes. Over the years, many catalytic site-directed protein-tyrosine phosphatase inhibitors have been generated; however, the catalytic sites of protein-tyrosine phosphatases are highly conserved, which compromises the selectivity of small molecule compounds. In addition, the substrates of protein-tyrosine phosphatases contain negatively-charged phosphotyrosine, which hampers the transduction of substrate-mimetic inhibitors across the cell membrane. Recently, several allosteric inhibitors have been developed that are highly selective and do not contain negative charges. Looking forward, there is a bright future for small molecule inhibitors of protein-tyrosine phosphatases.
Prof. Jeroen den Hertog
Prof. Rob M. J. Liskamp
Guest Editors
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Keywords
- protein-tyrosine phosphatases
- (covalent) inhibitors
- small molecules
- peptidomimetics
- allosteric inhibitors
- cancer
- diabetes