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Andrew M. Scharenberg

Researcher at Beth Israel Deaconess Medical Center

Publications -  39
Citations -  4820

Andrew M. Scharenberg is an academic researcher from Beth Israel Deaconess Medical Center. The author has contributed to research in topics: Tyrosine phosphorylation & Tyrosine kinase. The author has an hindex of 22, co-authored 39 publications receiving 4729 citations. Previous affiliations of Andrew M. Scharenberg include National Institutes of Health & Harvard University.

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Recruitment of Tyrosine Phosphatase HCP by the Killer Cell Inhibitory Receptor

TL;DR: The data imply that the inhibitory function of p58 is dependent on its tyrosine phosphorylation and on recruitment and activation of HCP, and that introduction of an inactive mutant HCP into an NK cell line prevented the p58-mediated inhibition of target cell lysis.
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Phosphatidylinositol-3,4,5-trisphosphate (PtdIns-3,4,5-P3)/Tec kinase-dependent calcium signaling pathway: a target for SHIP-mediated inhibitory signals

TL;DR: It is demonstrated that phosphatidylinositol‐3,4,5‐trisphosphate interacting with the PH domain acts as an upstream activation signal for Tec kinases, resulting in Tec kinase‐dependent phospholipase Cγ tyrosine phosphorylation and inositol trisph phosphate production.
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Activation of BTK by a Phosphorylation Mechanism Initiated by SRC Family Kinases

TL;DR: The activated BTK was predominantly membrane-associated, which suggests that BTK integrates distinct receptor signals resulting in SRC kinase activation and BTK membrane targeting.
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Btk/tec kinases regulate sustained increases in intracellular ca2+ following b-cell receptor activation

TL;DR: Results suggest that Btk maintains increased intracellular calcium levels by controlling a Tg‐sensitive, IP3‐gated calcium store(s) that regulates store‐operated calcium entry.
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Sequential Involvement of Lck and SHP-1 with MHC-Recognizing Receptors on NK Cells Inhibits FcR-Initiated Tyrosine Kinase Activation

TL;DR: Overexpression of catalytically inactive SHP-1 restores the tyrosine phosphorylation of these signaling events and reverses KIR-mediated inhibition of NK cell cytotoxic function.