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Jack E. Dixon

Researcher at University of California, San Diego

Publications -  412
Citations -  49376

Jack E. Dixon is an academic researcher from University of California, San Diego. The author has contributed to research in topics: Protein tyrosine phosphatase & Phosphorylation. The author has an hindex of 115, co-authored 408 publications receiving 47201 citations. Previous affiliations of Jack E. Dixon include Wake Forest University & University of California, Irvine.

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The Tumor Suppressor, PTEN/MMAC1, Dephosphorylates the Lipid Second Messenger, Phosphatidylinositol 3,4,5-Trisphosphate

TL;DR: It is demonstrated that overexpression of PTEN, a putative tumor suppressor, reduced insulin-induced PtdIns(3,4,5)P3 production in human 293 cells without effecting insulin- induced phosphoinositide 3-kinase activation.
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Protein Tyrosine Phosphatases in the Human Genome

TL;DR: The set of 107 genes in the human genome that encode members of the four protein tyrosine phosphatase (PTP) families are presented and the role of these enzymes in human disease will be discussed.
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Eukaryotic proteins expressed in Escherichia coli: an improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase.

TL;DR: The introduction of the glycine kinker into fusion proteins allows for the cleavage of the fusion proteins while they are attached to the affinity resin resulting in a single step purification of the recombinant protein.
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Drosophila Dscam Is an Axon Guidance Receptor Exhibiting Extraordinary Molecular Diversity

TL;DR: CDNA and genomic analyses reveal the existence of multiple forms of Dscam with a conserved architecture containing variable Ig and transmembrane domains, which may contribute to the specificity of neuronal connectivity.
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Crystal Structure of the PTEN Tumor Suppressor: Implications for Its Phosphoinositide Phosphatase Activity and Membrane Association

TL;DR: The PTEN structure reveals a phosphatase domain that is similar to protein phosphatases but has an enlarged active site important for the accommodation of the phosphoinositide substrate and a C2 domain that may serve to productively position the catalytic domain on the membrane.