Biochemical and Biophysical Research Communications
Regular ArticleMolecular Assembly of the Extracellular Domain of P2X2, an ATP-Gated Ion Channel
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Purinergic systems, neuropathic pain and the role of microglia
2012, Experimental NeurologyA consensus segment in the M2 domain of the hP2X <inf>7</inf> receptor shows ion channel activity in planar lipid bilayers and in biological membranes
2012, Biochimica et Biophysica Acta - BiomembranesCitation Excerpt :Recent X-ray crystallographic studies of P2X4R indicated trimeric functional organization [21]. When expressed heterologously, most P2X receptors (P2XR) isoforms form channels with distinct pharmacological and kinetic properties [15,22,23]. Their primary sequences contain between 379 (P2X1R) and 595 (P2X7R) amino acids, and a sequence alignment of the first 400 residues reveals more than 30% homology [9].
Pain and purinergic signaling
2010, Brain Research ReviewsA truncated P2X<inf>7</inf> receptor variant (P2X<inf>7-j</inf>) endogenously expressed in cervical cancer cells antagonizes the full-length P2X<inf>7</inf> receptor through hetero-oligomerization
2006, Journal of Biological ChemistryCitation Excerpt :The molecular mechanism by which single P2X7 molecules oligomerize is unclear. The present results support the speculation that ectodomains of the P2X receptor are essential to carry out the oligomerization (47). However, our data do not support the speculation that residues in or near the second membrane-spanning segment are critical for multimerization of P2X receptors (50) because the P2X7-j could interact with the full-length P2X7 despite lacking the second transmembrane stretch.
Chapter 9 P2X Receptors in Sensory Neurons
2006, Current Topics in MembranesCitation Excerpt :One functional P2X receptor channel is presumably formed by a number of P2X subunits, as is considered to be the case in other ligand‐gated ion channels. The number of subunits of a P2X receptor has been proposed to be three (Nicke et al., 1998; Stoop et al., 1999; Jiang et al., 2003; Nicke et al., 2003) or four (Kim et al., 1997; Ding and Sachs, 2000). It appears that all three or four subunits are either identical, namely homomeric receptors, or not identical, namely heteromeric receptors.
Purification and aqueous phase atomic force microscopic observation of recombinant P2X<inf>2</inf> receptor
2005, European Journal of Pharmacology
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