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David N. Shapiro

Researcher at St. Jude Children's Research Hospital

Publications -  53
Citations -  7506

David N. Shapiro is an academic researcher from St. Jude Children's Research Hospital. The author has contributed to research in topics: Rhabdomyosarcoma & Gene. The author has an hindex of 33, co-authored 53 publications receiving 7286 citations. Previous affiliations of David N. Shapiro include University of Tennessee & University of Tennessee Health Science Center.

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Fusion of a Kinase Gene, ALK, to a Nucleolar Protein Gene, NPM, in Non-Hodgkin's Lymphoma

TL;DR: In the predicted hybrid protein, the amino terminus of nucleophosmin (NPM) is linked to the catalytic domain of anaplastic lymphoma kinase (ALK), and unscheduled expression of the truncated ALK may contribute to malignant transformation in these lymphomas.
Journal Article

A variant ewing's sarcoma translocation (7;22) fuses the ews gene to the ets gene etv1

TL;DR: A third Ewing's sarcoma translocation is identified, the t(7;22)(p22;q12), that fuses EWS to the human homologue of the murine ETS gene ER81, and this gene, designated ETV1 (for ETS Translocation Variant), is located on chromosome band 7p22.
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Pax3 modulates expression of the c-Met receptor during limb muscle development.

TL;DR: It is shown that c-met expression is markedly reduced in the lateral dermomyotome of Splotch embryos lacking Pax3, and a potential Pax3 binding site in the human c-MET promoter that may contribute to direct transcriptional regulation is identified.
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Fusion of PAX3 to a Member of the Forkhead Family of Transcription Factors in Human Alveolar Rhabdomyosarcoma

TL;DR: Formation of chimeric transcription factors has now been implicated in diverse human tumors of myogenic, hematopoietic, neuroectodermal, and adipocytic origin, suggesting that transcriptional deregulation is a common mechanism of tumorigenesis.
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Functional characterization of the human interleukin-15 receptor alpha chain and close linkage of IL15RA and IL2RA genes.

TL;DR: The isolation of three differentially spliced human IL-15Rα variants that are all capable of high affinity binding ofIL-15 are extended into the human system, suggesting a broader range of cellular targets for IL- 15.