27EC Covarrubias, Manuel - Thomas Jefferson University - Thomas Jefferson University

Manuel Covarrubias, MD, PhD

Contact Dr. Covarrubias

900 Walnut Street
JHN 4th floor
Philadelphia, PA 19107

(215) 503-4340
(215) 503-4358 fax

Most Recent Peer-reviewed Publications

  1. Mechanistic Insights into the Modulation of Voltage-Gated Ion Channels by Inhalational Anesthetics
  2. Positive allosteric modulation of Kv channels by sevoflurane: Insights into the structural basis of inhaled anesthetic action
  3. Role for the Propofol Hydroxyl in Anesthetic Protein Target Molecular Recognition
  4. Kv3.4 channel function and dysfunction in nociceptors
  5. Dysregulation of Kv3.4 channels in dorsal root ganglia following spinal cord injury
  6. Modulation of a voltage-gated Na+ channel by sevoflurane involves multiple sites and distinct mechanisms
  7. Dipeptidyl-peptidase-like proteins cast in a new role: Enabling scorpion toxin block of A-type K+ channels
  8. Insight into the modulation of Shaw2 Kv channels by general anesthetics: Structural and functional studies of S4-S5 linker and S6 C-terminal peptides in micelles by NMR
  9. Modeling-independent elucidation of inactivation pathways in recombinant and native A-type Kv channels
  10. Novel activation of voltage-gated K+ channels by sevoflurane
  11. Modulation of Kv3.4 channel N-type inactivation by protein kinase C shapes the action potential in dorsal root ganglion neurons
  12. Molecular mapping of general anesthetic sites in a voltage-gated ion channel
  13. Cortactin is required for N-cadherin regulation of Kv1.5 channel function
  14. Mechanisms of closed-state inactivation in voltage-gated ion channels
  15. Simulating complex ion channel kinetics with IonChannelLab
  16. Simulating complex ion channel kinetics with IonChannelLab.
  17. Azi-isoflurane, a photolabel analog of the commonly used inhaled general anesthetic isoflurane
  18. Inhalational anaesthetics and n-alcohols share a site of action in the neuronal Shaw2 K v channel: Research paper
  19. A novel N-terminal motif of dipeptidyl peptidase-like proteins produces rapid inactivation of KV4.2 channels by a pore-blocking mechanism
  20. A novel N-terminal motif of dipeptidy 017E l peptidase-like proteins produces rapid inactivation of KV4.2 channels by a pore-blocking mechanism.