J
Jannik N. Andersen
Researcher at University of Texas MD Anderson Cancer Center
Publications - 45
Citations - 5081
Jannik N. Andersen is an academic researcher from University of Texas MD Anderson Cancer Center. The author has contributed to research in topics: Phosphorylation & Protein tyrosine phosphatase. The author has an hindex of 25, co-authored 41 publications receiving 4682 citations. Previous affiliations of Jannik N. Andersen include Cold Spring Harbor Laboratory & Merck & Co..
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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.
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Structural and Evolutionary Relationships among Protein Tyrosine Phosphatase Domains
Jannik N. Andersen,Ole Hartvig Mortensen,Günther H.J. Peters,Paul G. Drake,Lars Fogh Iversen,Ole Hvilsted Olsen,Peter Gildsig Jansen,Henrik Sune Andersen,Nicholas K. Tonks,Niels Møller +9 more
TL;DR: A comparative analysis of the structural relationships among vertebrate PTP domains is presented and a comprehensive resource for sequence analysis of phosphotyrosine-specific PTPs is provided.
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Cancer genomics: from discovery science to personalized medicine
TL;DR: The importance of establishing the biological relevance of a cancer genomic discovery in realizing its clinical potential is emphasized and some of the major obstacles to moving from the bench to the bedside are discussed.
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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.
Journal ArticleDOI
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.