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Monika Vig

Researcher at Washington University in St. Louis

Publications -  19
Citations -  3985

Monika Vig is an academic researcher from Washington University in St. Louis. The author has contributed to research in topics: T cell & ORAI1. The author has an hindex of 14, co-authored 19 publications receiving 3805 citations. Previous affiliations of Monika Vig include Tata Institute of Fundamental Research & Massachusetts Institute of Technology.

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CRACM1 is a plasma membrane protein essential for store-operated Ca2+ entry.

TL;DR: The human ortholog of CRACM1, a plasma membrane–resident protein encoded by gene FLJ14466, was characterized and overexpression of CRacM1 did not affect CRAC currents, but RNAi-mediated knockdown disrupted its activation.
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Amplification of CRAC current by STIM1 and CRACM1 (Orai1).

TL;DR: Overexpression of both proteins greatly potentiates ICRAC, suggesting that STIM1 and CRACM1 mutually limit store-operated currents and that CRacM1 may be the long-sought CRAC channel.
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CRACM1 Multimers Form the Ion-Selective Pore of the CRAC Channel

TL;DR: It is shown here that CRACM1 forms multimeric assemblies that bind STIM1 and that acidic residues in the transmembrane and extracellular domains of CRacM1 contribute to the ionic selectivity of the CRAC-channel pore.
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Calcium signaling in immune cells

TL;DR: This review highlights advances in the understanding of Ca2+ signaling in lymphocytes with special emphasis on SOC entry and discusses outstanding questions and probable future directions of the field.
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Defective mast cell effector functions in mice lacking the CRACM1 pore subunit of store-operated calcium release-activated calcium channels.

TL;DR: CRACM1 is crucial in mouse mast cell effector function, but mouse T cell calcium release–activated calcium channels are functional in the absence of CRACM2, and CRACm2 expression to be much higher in mouse T cells.