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Irwin Levitan, PhD

Contact Dr. Levitan

900 Walnut Street
JHN 4th floor
Philadelphia, PA 19107

(215) 503-5996
(215) 955-5861 fax

Most Recent Peer-reviewed Publications

  1. Sugar and spice and potassium channel modulation
  2. Regulation of synaptic development and function by the Drosophila PDZ protein Dyschronic
  3. Defects in synapse structure and function precede motor neuron degeneration in Drosophila models of FUS-related ALS
  4. Cell-specific fine-tuning of neuronal excitability by differential expression of modulator protein isoforms
  5. SLOB, a SLOWPOKE channel binding protein, regulates insulin pathway signaling and metabolism in Drosophila
  6. Slob, a slowpoke channel-binding protein, modulates synaptic transmission
  7. Editorial for first issue in January 2011
  8. Identification of a Neural Circuit that Underlies the Effects of Octopamine on Sleep:Wake Behavior
  9. In vivo role of a potassium channel-binding protein in regulating neuronal excitability and behavior
  10. miXED Messages in Ion Channel Modulation
  11. In Vivo Roles of Ion Channel Regulatory Protein Complexes in Neuronal Physiology and Behavior
  12. Drosophila ortholog of succinyl-CoA synthetase β subunit: A novel modulator of Drosophila KCNQ channels
  13. Mechanisms of two modulatory actions of the channel-binding protein slob on the Drosophila slowpoke calcium-dependent potassium channel
  14. Signaling protein complexes associated with neuronal ion channels
  15. Expression and function of variants of Slob, Slowpoke channel binding protein, in Drosophila
  16. Expression of a calmodulin-binding KCNQ2 potassium channel fragment modulates neuronal M-current and membrane excitability
  17. A Drosophila KCNQ channel essential for early embryonic development
  18. MONaKA, a novel modulator of the plasma membrane Na,K-ATPase
  19. The amino terminus of slob, slowpoke channel binding protein, critically influences its modulation of the channel
  20. Syntaxin-1A binds to and modulates the Slo calcium-activated potassium channel via an interaction that excludes syntaxin binding to calcium channels