S Shenolikar

Summary

Affiliation: Mount Sinai School of Medicine
Country: USA

Publications

  1. ncbi Gating of CaMKII by cAMP-regulated protein phosphatase activity during LTP
    R D Blitzer
    Bronx VA Medical Center and Department of Psychiatry, Mount Sinai School of Medicine, New York, NY 10029, USA
    Science 280:1940-2. 1998
  2. ncbi Amyloid beta peptides activate the phosphoinositide signaling pathway in oocytes expressing rat brain RNA
    R D Blitzer
    Department of Psychiatry, Mount Sinai School of Medicine, New York, NY 10029, USA
    Brain Res Mol Brain Res 76:115-20. 2000
  3. ncbi Protein phosphatase 1 regulation by inhibitors and targeting subunits
    T Watanabe
    Laboratory of Molecular and Cellular Neuroscience, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA
    Proc Natl Acad Sci U S A 98:3080-5. 2001

Collaborators

Detail Information

Publications3

  1. ncbi Gating of CaMKII by cAMP-regulated protein phosphatase activity during LTP
    R D Blitzer
    Bronx VA Medical Center and Department of Psychiatry, Mount Sinai School of Medicine, New York, NY 10029, USA
    Science 280:1940-2. 1998
    ..The blockade of LTP by a CaMKII inhibitor was not overcome by thiophosphorylated inhibitor-1. Thus, the cAMP pathway uses PP1 to gate CaMKII signaling in LTP...
  2. ncbi Amyloid beta peptides activate the phosphoinositide signaling pathway in oocytes expressing rat brain RNA
    R D Blitzer
    Department of Psychiatry, Mount Sinai School of Medicine, New York, NY 10029, USA
    Brain Res Mol Brain Res 76:115-20. 2000
    ..This pharmacology excludes the participation of known Abeta binding proteins. The results indicate that a PI coupled receptor for non-aggregated Abeta may be present in brain...
  3. ncbi Protein phosphatase 1 regulation by inhibitors and targeting subunits
    T Watanabe
    Laboratory of Molecular and Cellular Neuroscience, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA
    Proc Natl Acad Sci U S A 98:3080-5. 2001
    ..More limited alterations in residues in beta12, beta13, and beta14 strands highlighted a key role for M290 and C291 in the interaction of PP1 with thiophospho-DARPP-32, but not inhibitor-2...