Prediction and verification of novel peptide targets of protein tyrosine phosphatase 1B
Abstract: Phosphotyrosine peptides are useful starting points for inhibitor design and for the search for protein tyrosine phosphatase (PTP) phosphoprotein substrates. To identify novel phosphopeptide substrates of PTP1B, we developed a computational prediction protocol based on a virtual library of protein sequences with known phosphotyrosine sites. To these we applied sequence-based methods, biologically meaningful filters and molecular docking. Five peptides were selected for biochemical testing of their potential as PTP1B substrates. All five peptides were equally good substrates for PTP1B compared to a known peptide substrate whereas appropriate control peptides were not recognized, showing that our protocol can be used to identify novel peptide substrates of PTP1B
- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Notes
-
Bioorganic & medicinal chemistry. - 24, 15 (2016) , 3255-3258, ISSN: 1464-3391
- DOI
-
10.1016/j.bmc.2016.03.030
- URN
-
urn:nbn:de:bsz:25-freidok-2212757
- Rights
-
Kein Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
25.03.2025, 1:44 PM CET
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Li, Xun
- Köhn, Maja
- Universität
Time of origin
- 2021
Other Objects (12)
Investigations of Protein Tyrosine Phosphatase Functions
Interaction of the disordered Gab1 with tyrosine phosphatase Shp2
Characterisation and modulation of the phosphatase activity of phosphatase of regenerating liver-3 (PRL-3) and SH2 containing protein tyrosine phosphatase 2 (SHP2)
Role of the novel protein tyrosine phosphatase AUM for cell adhesion
Role of the novel protein tyrosine phosphatase AUM for cell adhesion
Development of a photoactivatable protein phosphatase-1-disrupting peptide
Requirement of the tyrosine phosphatase Shp2 in mammary gland tumorgenesis in mice
Inactivation of the tyrosine phosphatase SHP-2 drives vascular dysfunction in sepsis
Oxidation of the Mycobacterium tuberculosis key virulence factor protein tyrosine phosphatase A (MptpA) reduces its phosphatase activity
PEST-domain enriched tyrosine phosphatase as a positive regulator of mast cell signaling
Synthesis, Characterization and Application of Stabilized Natural Substrates as Protein Tyrosine Phosphatase Inhibitors
Synthesis, characterization and application of stabilized natural substrates as protein tyrosine phosphatase inhibitors
Investigations of Protein Tyrosine Phosphatase Functions
Interaction of the disordered Gab1 with tyrosine phosphatase Shp2
Characterisation and modulation of the phosphatase activity of phosphatase of regenerating liver-3 (PRL-3) and SH2 containing protein tyrosine phosphatase 2 (SHP2)
Role of the novel protein tyrosine phosphatase AUM for cell adhesion
Role of the novel protein tyrosine phosphatase AUM for cell adhesion
Development of a photoactivatable protein phosphatase-1-disrupting peptide
Requirement of the tyrosine phosphatase Shp2 in mammary gland tumorgenesis in mice
Inactivation of the tyrosine phosphatase SHP-2 drives vascular dysfunction in sepsis
Oxidation of the Mycobacterium tuberculosis key virulence factor protein tyrosine phosphatase A (MptpA) reduces its phosphatase activity
PEST-domain enriched tyrosine phosphatase as a positive regulator of mast cell signaling
Synthesis, Characterization and Application of Stabilized Natural Substrates as Protein Tyrosine Phosphatase Inhibitors
Synthesis, characterization and application of stabilized natural substrates as protein tyrosine phosphatase inhibitors
Investigations of Protein Tyrosine Phosphatase Functions
Interaction of the disordered Gab1 with tyrosine phosphatase Shp2
Characterisation and modulation of the phosphatase activity of phosphatase of regenerating liver-3 (PRL-3) and SH2 containing protein tyrosine phosphatase 2 (SHP2)
Role of the novel protein tyrosine phosphatase AUM for cell adhesion
Role of the novel protein tyrosine phosphatase AUM for cell adhesion
Development of a photoactivatable protein phosphatase-1-disrupting peptide
Requirement of the tyrosine phosphatase Shp2 in mammary gland tumorgenesis in mice
Inactivation of the tyrosine phosphatase SHP-2 drives vascular dysfunction in sepsis
Oxidation of the Mycobacterium tuberculosis key virulence factor protein tyrosine phosphatase A (MptpA) reduces its phosphatase activity
PEST-domain enriched tyrosine phosphatase as a positive regulator of mast cell signaling
Synthesis, Characterization and Application of Stabilized Natural Substrates as Protein Tyrosine Phosphatase Inhibitors