Skip to main content
Article thumbnail
Location of Repository

Hot on the Trail of TRP Channel Structure

By Vera Y. Moiseenkova-Bell and Theodore G. Wensel
Topics: Perspective
Publisher: The Rockefeller University Press
OAI identifier:
Provided by: PubMed Central

Suggested articles


  1. (2006). An introduction to TRP channels.
  2. (2001). Analysis of the native quaternary structure of vanilloid receptor 1.
  3. (2007). Assembly domains in TRP channels.
  4. (2007). Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment.
  5. (2001). Biochemical characterization of the vanilloid receptor 1 expressed in a dorsal root ganglia derived cell line.
  6. (2005). Conical tomography of freezefracture replicas: a method for the study of integral membrane proteins inserted in phospholipid bilayers.
  7. (2005). Crystal structure of a mammalian voltage-dependent Shaker family K+ channel.
  8. Crystal structure of the atypical protein kinase domain of a TRP channel with phosphotransferase activity.
  9. (2008). De novo backbone trace of GroEL from single particle electron cryomicroscopy.
  10. (2005). Electron cryomicroscopy of biological machines at subnanometer resolution.
  11. (2005). Electron cryomicroscopy of single particles at subnanometer resolution.
  12. (2007). Exceptional overproduction of a functional human membrane protein. Protein Expr.
  13. (2008). Functional analysis of Kv1.2 and paddle chimera Kv channels in planar lipid bilayers.
  14. (2004). Inositol 1,4,5-trisphosphate receptor contains multiple cavities and Lshaped ligand-binding domains.
  15. (2007). Insights into the roles of conserved and divergent residues in the ankyrin repeats of TRPV ion channels. Channels (Austin)
  16. (1984). Localization of binding sites for carboxyl terminal by the addition of phospholipids and detergent removal by dialysis to yield TRPV1 reconstituted in unilamellar phospholipids vesicles.
  17. (2003). Overexpression and purifi cation of the vanilloid receptor in yeast (Saccharomyces cerevisiae).
  18. (2005). Refi ned structure of the nicotinic acetylcholine receptor at 4A resolution.
  19. (2000). Single-particle electron cryo-microscopy: towards atomic resolution.
  20. (2002). Single-particle imaging of macromolecules by cryo-electron microscopy.
  21. (2008). Structural analyses of the ankyrin repeat domain of TRPV6 and related TRPV ion channels.
  22. (1998). Structural analysis of cloned plasma membrane proteins by freeze-fracture electron microscopy.
  23. (2003). Structure and gating mechanism of the acetylcholine receptor pore.
  24. (2007). Structure of acid-sensing ion channel 1 at 1.9 A resolution and low pH.
  25. (2006). Structure of the N-terminal ankyrin repeat domain of the TRPV2 ion channel.
  26. (2008). Structure of TRPV1 channel revealed by electron cryomicroscopy.
  27. (2007). The ankyrin repeats of TRPV1 bind multiple ligands and modulate channel sensitivity.
  28. (2008). The motor protein prestin is a bullet-shaped molecule with inner cavities.
  29. (2005). The non-selective cation-permeable channel TRPC3 is a tetrahedron with a cap on the large cytoplasmic end.
  30. (2007). The TRPC3 channel has a large internal chamber surrounded by signal sensing antennas.
  31. (2008). Three-dimensional reconstruction of human CFTR chloride channel revealed an ellipsoidal structure with orifi ces beneath the putative transmembrane domain.
  32. (2007). Three-dimensional reconstruction using transmission electron microscopy reveals a swollen, bell-shaped structure of transient receptor potential melastatin type 2 cation channel.
  33. (2007). Transient receptor potential cation channels in disease.
  34. (2005). Transient receptor potential ion channels as targets for the discovery of pain therapeutics.
  35. (2003). TRP channels as cellular sensors.
  36. (2007). TRP channels.
  37. (2008). X-ray crystal structure of a TRPM assembly domain reveals an antiparallel four-stranded coiled-coil.

To submit an update or takedown request for this paper, please submit an Update/Correction/Removal Request.