Search Results - "Ormond, Susan J"

Atomic Force Microscopy Imaging Demonstrates that P2X2 Receptors Are Trimers but That P2X6 Receptor Subunits Do Not Oligomerize by Barrera, Nelson P., Ormond, Susan J., Henderson, Robert M., Murrell-Lagnado, Ruth D., Edwardson, J. Michael

“…P2X receptors are cation-selective channels activated by extracellular ATP. The architecture of these receptors is still not completely clear. Here we have…”
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An uncharged region within the N terminus of the P2X6 receptor inhibits its assembly and exit from the endoplasmic reticulum by Ormond, Susan J, Barrera, Nelson P, Qureshi, Omar S, Henderson, Robert M, Edwardson, J Michael, Murrell-Lagnado, Ruth D

“…ATP-gated P2X receptors are trimeric complexes formed by the homomeric or heteromeric assembly of seven different subunits. We have shown previously that,…”
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Atomic Force Microscopy Imaging Demonstrates that P2X sub(2) Receptors Are Trimers but That P2X sub(6) Receptor Subunits Do Not Oligomerize by Barrera, Nelson P, Ormond, Susan J, Henderson, Robert M, Murrell-Lagnado, Ruth D, Edwardson, JMichael

“…P2X receptors are cation-selective channels activated by extracellular ATP. The architecture of these receptors is still not completely clear. Here we have…”
Get full text