M
Monica J. S. Nadler
Researcher at Beth Israel Deaconess Medical Center
Publications - 22
Citations - 3119
Monica J. S. Nadler is an academic researcher from Beth Israel Deaconess Medical Center. The author has contributed to research in topics: Phosphorylation & Calcium. The author has an hindex of 16, co-authored 20 publications receiving 2927 citations. Previous affiliations of Monica J. S. Nadler include Purdue University & Harvard University.
Papers
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Journal ArticleDOI
LTRPC7 is a Mg·ATP-regulated divalent cation channel required for cell viability
Monica J. S. Nadler,Meredith C. Hermosura,Kazunori Inabe,Anne-Laure Perraud,Qiqin Zhu,Alexander J. Stokes,Tomohiro Kurosaki,Jean-Pierre Kinet,Reinhold Penner,Andrew M. Scharenberg,Andrew M. Scharenberg,Andrea Fleig +11 more
TL;DR: The data indicate that LTRPC7, by virtue of its sensitivity to physiological Mg·ATP levels, may be involved in a fundamental process that adjusts plasma membrane divalent cation fluxes according to the metabolic state of the cell.
Journal ArticleDOI
Amplification of CRAC current by STIM1 and CRACM1 (Orai1).
Christine Peinelt,Monika Vig,Dana Lynn T. Koomoa,Andreas Beck,Monica J. S. Nadler,Murielle Koblan-Huberson,Annette Lis,Andrea Fleig,Reinhold Penner,Jean-Pierre Kinet +9 more
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.
Journal ArticleDOI
TRPM7 provides an ion channel mechanism for cellular entry of trace metal ions.
Mahealani K. Monteilh-Zoller,Meredith C. Hermosura,Monica J. S. Nadler,Andrew M. Scharenberg,Reinhold Penner,Andrea Fleig +5 more
TL;DR: It is reported that heterologously overexpressed TRPM7 in HEK-293 cells conducts a range of essential and toxic divalent metal ions with strong preference for Zn2+ and Ni2+, which both permeate TR PM7 up to four times better than Ca2+.
Book ChapterDOI
Signal transduction by the high-affinity immunoglobulin E receptor Fc epsilon RI: coupling form to function.
Journal ArticleDOI
Identification of Major Binding Proteins and Substrates for the SH2-Containing Protein Tyrosine Phosphatase SHP-1 in Macrophages
John F. Timms,Kristen Carlberg,Haihua Gu,Haiyan Chen,Shubhangi Kamatkar,Monica J. S. Nadler,Larry R. Rohrschneider,Benjamin G. Neel +7 more
TL;DR: The data suggest that BIT and PIR-B recruit multiple signaling molecules to receptor complexes, where they are regulated bySHP-1 and/or SHP-2, andTyrosyl phosphorylation of these proteins and the level of the associated kinase activity are increased in the absence of SHp-1.