| pubmed-article:16708237 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16708237 | lifeskim:mentions | umls-concept:C0597357 | lld:lifeskim |
| pubmed-article:16708237 | lifeskim:mentions | umls-concept:C0005553 | lld:lifeskim |
| pubmed-article:16708237 | pubmed:issue | 5 | lld:pubmed |
| pubmed-article:16708237 | pubmed:dateCreated | 2006-7-6 | lld:pubmed |
| pubmed-article:16708237 | pubmed:abstractText | The P2X receptor is the baby brother of the ligand-gated ion channel super-family. An understanding of its role in human physiology is still developing, and no one truly knows how it works to transport ions across the membrane. In this study, we review some aspects of P2X channel biophysics, concentrating on ion permeation and gating. P2X channels transport both small and large cations and anions across cell membranes in a manner that depends on both the subunit composition of the receptor and the experimental conditions. We describe the pore properties of wild-type receptors and use the altered phenotypes of mutant receptors to point the way towards a structural model of the pore. | lld:pubmed |
| pubmed-article:16708237 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16708237 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16708237 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:16708237 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16708237 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16708237 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16708237 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16708237 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16708237 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:16708237 | pubmed:issn | 0031-6768 | lld:pubmed |
| pubmed-article:16708237 | pubmed:author | pubmed-author:EganTerrance... | lld:pubmed |
| pubmed-article:16708237 | pubmed:author | pubmed-author:LiZhiyuanZ | lld:pubmed |
| pubmed-article:16708237 | pubmed:author | pubmed-author:SamwaysDamien... | lld:pubmed |
| pubmed-article:16708237 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16708237 | pubmed:volume | 452 | lld:pubmed |
| pubmed-article:16708237 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16708237 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16708237 | pubmed:pagination | 501-12 | lld:pubmed |
| pubmed-article:16708237 | pubmed:dateRevised | 2010-11-18 | lld:pubmed |
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| pubmed-article:16708237 | pubmed:meshHeading | pubmed-meshheading:16708237... | lld:pubmed |
| pubmed-article:16708237 | pubmed:meshHeading | pubmed-meshheading:16708237... | lld:pubmed |
| pubmed-article:16708237 | pubmed:meshHeading | pubmed-meshheading:16708237... | lld:pubmed |
| pubmed-article:16708237 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16708237 | pubmed:articleTitle | Biophysics of P2X receptors. | lld:pubmed |
| pubmed-article:16708237 | pubmed:affiliation | Department of Pharmacological and Physiological Science, Saint Louis University School of Medicine, 1402 S. Grand Boulevard, St. Louis, MO 63104, USA. egantm@slu.edu | lld:pubmed |
| pubmed-article:16708237 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16708237 | pubmed:publicationType | Review | lld:pubmed |
| pubmed-article:16708237 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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