Application of hydrogen/deuterium exchange mass spectrometry to study protein tyrosine phosphatase dynamics, ligand binding, and substrate specificity
- 31 July 2007
- Vol. 42 (3) , 227-233
- https://doi.org/10.1016/j.ymeth.2007.02.020
Abstract
No abstract availableKeywords
This publication has 19 references indexed in Scilit:
- Protein Analysis by Hydrogen Exchange Mass SpectrometryAnnual Review of Biophysics, 2003
- Probing the Molecular Basis for Potent and Selective Protein-tyrosine Phosphatase 1B InhibitionJournal of Biological Chemistry, 2002
- Protein Tyrosine Phosphatases: Structure and Function, Substrate Specificity, and Inhibitor DevelopmentAnnual Review of Pharmacology and Toxicology, 2002
- Design and Characterization of an Improved Protein Tyrosine Phosphatase Substrate-Trapping MutantBiochemistry, 2002
- Protein tyrosine phosphatases: prospects for therapeuticsCurrent Opinion in Chemical Biology, 2001
- Peer Reviewed: Investigating Protein Structure and Dynamics by Hydrogen Exchange MSAnalytical Chemistry, 2001
- Combinatorial control of the specificity of protein tyrosine phosphatasesCurrent Opinion in Cell Biology, 2001
- Bacterial expression of activated mitogen-activated protein kinasesPublished by Elsevier ,2001
- Thermodynamic Study of Ligand Binding to Protein-tyrosine Phosphatase 1B and Its Substrate-trapping MutantsJournal of Biological Chemistry, 2000
- Signaling—2000 and BeyondCell, 2000