jlb104

Jeffrey L. Benovic, PhD

Contact Dr. Benovic

233 S. 10th Street
Philadelphia, PA 19107

(215) 503-4607
(215) 503-5393 fax

Most Recent Peer-reviewed Publications

  1. Dysregulated GPCR signaling and therapeutic options in uveal melanoma
  2. Structural and Functional Analysis of a β2-Adrenergic Receptor Complex with GRK5
  3. G protein-coupled receptor kinase-2 (GRK-2) regulates serotonin metabolism through the monoamine oxidase AMX-2 in Caenorhabditis elegans
  4. β-arrestin-biased signaling through the β2-adrenergic receptor promotes cardiomyocyte contraction
  5. The αarrestin ARRDC3 regulates the endosomal residence time and intracellular signaling of the β2-adrenergic receptor
  6. From biased signalling to polypharmacology: Unlocking unique intracellular signalling using pepducins
  7. Interdicting Gq activation in airway disease by receptor-dependent and receptor-independent mechanisms
  8. Atomic structure of GRK5 reveals distinct structural features novel for G protein-coupled receptor kinases
  9. Structural biology: Arresting developments in receptor signalling
  10. New frontiers in kinases
  11. Herpes simplex virus enhances chemokine function through modulation of receptor trafficking and oligomerization
  12. Consequence of the tumor-associated conversion to cyclin D1b
  13. Development and characterization of pepducins as Gs-biased allosteric agonists
  14. Role of β-arrestins and arrestin domain-containing proteins in G protein-coupled receptor trafficking
  15. Call for papers! a special thematic compilation/special issue crossover with ACS chemical biology, ACS medicinal chemistry letters, and the journal of medicinal chemistry focused on new frontiers in kinases
  16. Editorial overview: Cell regulation: The ins and outs of G protein-coupled receptors
  17. β-Arrestins and G protein-coupled receptor trafficking
  18. β-Arrestins and G protein-coupled receptor trafficking
  19. Caspase-cleaved arrestin-2 and BID cooperatively facilitate cytochrome C release and cell death
  20. Pepducin targeting the C-X-C chemokine receptor type 4 acts as a biased agonist favoring activation of the inhibitory G protein