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Annette Salmeen
Researcher at Stanford University
Publications - 8
Citations - 2303
Annette Salmeen is an academic researcher from Stanford University. The author has contributed to research in topics: Protein tyrosine phosphatase & Phosphorylation. The author has an hindex of 7, co-authored 8 publications receiving 2186 citations. Previous affiliations of Annette Salmeen include Icahn School of Medicine at Mount Sinai & Institute of Cancer Research.
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Journal ArticleDOI
Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate
Annette Salmeen,Jannik N. Andersen,Michael P. Myers,Tzu-Ching Meng,John A. Hinks,Nicholas K. Tonks,David Barford +6 more
TL;DR: It is proposed that this unusual protein modification both protects the active-site cysteine residue of PTP1B from irreversible oxidation to sulphonic acid and permits redox regulation of the enzyme by promoting its reversible reduction by thiols.
Journal ArticleDOI
TYK2 and JAK2 Are Substrates of Protein-tyrosine Phosphatase 1B
Michael P. Myers,Jannik N. Andersen,Alan Cheng,Michel L. Tremblay,Curt M. Horvath,Jean Patrick Parisien,Annette Salmeen,David Barford,Nicholas K. Tonks +8 more
TL;DR: It is demonstrated that (E/D)-pY-pY-(R/K) is a consensus substrate recognition motif for PTP1B and that the substrate recognition site within theses kinases is similar to the site of dephosphorylation previously identified within the insulin receptor.
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Molecular basis for the dephosphorylation of the activation segment of the insulin receptor by protein tyrosine phosphatase 1B.
TL;DR: The protein tyrosine phosphatase PTP1B is responsible for negatively regulating insulin signaling by dephosphorylating the phosphotyrosine residues of the insulin receptor kinase (IRK) activation segment by integrating crystallographic, kinetic, and PTP2B peptide binding studies to define the molecular specificity of this reaction.
Journal ArticleDOI
Functions and Mechanisms of Redox Regulation of Cysteine-Based Phosphatases
Annette Salmeen,David Barford +1 more
TL;DR: The evidence implicating ROS as mediators of CBP activity within signaling pathways and how specificity of ROS-dependent signaling involving CBPs may be achieved are discussed and the molecular mechanisms that facilitate the stabilization of a reversibly oxidized form of the catalytic cysteine are discussed.
Journal ArticleDOI
Conformation-Sensing Antibodies Stabilize the Oxidized Form of PTP1B and Inhibit Its Phosphatase Activity
TL;DR: Conformation-sensor antibodies are generated, in the form of single-chain variable fragments (scFvs), that stabilize PTP1B-OX and thereby inhibit its phosphatase function and suggest that stabilization of the oxidized, inactive form of P TP1B with appropriate therapeutic molecules may offer a paradigm for phosphat enzyme drug development.