pubmed-article:2124506 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:2124506 | lifeskim:mentions | umls-concept:C0024501 | lld:lifeskim |
pubmed-article:2124506 | lifeskim:mentions | umls-concept:C0035406 | lld:lifeskim |
pubmed-article:2124506 | lifeskim:mentions | umls-concept:C1305923 | lld:lifeskim |
pubmed-article:2124506 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
pubmed-article:2124506 | lifeskim:mentions | umls-concept:C0332514 | lld:lifeskim |
pubmed-article:2124506 | pubmed:issue | 45 | lld:pubmed |
pubmed-article:2124506 | pubmed:dateCreated | 1991-2-7 | lld:pubmed |
pubmed-article:2124506 | pubmed:abstractText | The human erythrocyte (RBC) Rh blood group system consists of a complex of distinct integral membrane polypeptides with physical properties common to the aminophospholipid transporter responsible for the transbilayer movement of phosphatidylserine (PS) in RBC. To assess the involvement of Rh polypeptides in PS translocation, the aminophospholipid translocase was labeled with a photoactivatable PS analogue, 125I-azido-PS, and with an inhibitor of PS transport, 125I-labeled 2-(2-pyridyldithio)ethylamine. The ability of monoclonal Rh antibodies to immunoprecipitate the labeled transporter was determined. Immunoprecipitated Rh polypeptides were found to be labeled with the aminophospholipid translocase markers, suggesting that Rh proteins are involved in the transbilayer movement of PS. | lld:pubmed |
pubmed-article:2124506 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2124506 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2124506 | pubmed:language | eng | lld:pubmed |
pubmed-article:2124506 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2124506 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:2124506 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2124506 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2124506 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2124506 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2124506 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2124506 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2124506 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2124506 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2124506 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2124506 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2124506 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:2124506 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:2124506 | pubmed:month | Nov | lld:pubmed |
pubmed-article:2124506 | pubmed:issn | 0006-2960 | lld:pubmed |
pubmed-article:2124506 | pubmed:author | pubmed-author:CartronJ PJP | lld:pubmed |
pubmed-article:2124506 | pubmed:author | pubmed-author:SchroitA JAJ | lld:pubmed |
pubmed-article:2124506 | pubmed:author | pubmed-author:ConnorJJ | lld:pubmed |
pubmed-article:2124506 | pubmed:author | pubmed-author:BloyCC | lld:pubmed |
pubmed-article:2124506 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:2124506 | pubmed:day | 13 | lld:pubmed |
pubmed-article:2124506 | pubmed:volume | 29 | lld:pubmed |
pubmed-article:2124506 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:2124506 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:2124506 | pubmed:pagination | 10303-6 | lld:pubmed |
pubmed-article:2124506 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
pubmed-article:2124506 | pubmed:meshHeading | pubmed-meshheading:2124506-... | lld:pubmed |
pubmed-article:2124506 | pubmed:meshHeading | pubmed-meshheading:2124506-... | lld:pubmed |
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pubmed-article:2124506 | pubmed:meshHeading | pubmed-meshheading:2124506-... | lld:pubmed |
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pubmed-article:2124506 | pubmed:meshHeading | pubmed-meshheading:2124506-... | lld:pubmed |
pubmed-article:2124506 | pubmed:meshHeading | pubmed-meshheading:2124506-... | lld:pubmed |
pubmed-article:2124506 | pubmed:meshHeading | pubmed-meshheading:2124506-... | lld:pubmed |
pubmed-article:2124506 | pubmed:meshHeading | pubmed-meshheading:2124506-... | lld:pubmed |
pubmed-article:2124506 | pubmed:meshHeading | pubmed-meshheading:2124506-... | lld:pubmed |
pubmed-article:2124506 | pubmed:meshHeading | pubmed-meshheading:2124506-... | lld:pubmed |
pubmed-article:2124506 | pubmed:year | 1990 | lld:pubmed |
pubmed-article:2124506 | pubmed:articleTitle | Involvement of Rh blood group polypeptides in the maintenance of aminophospholipid asymmetry. | lld:pubmed |
pubmed-article:2124506 | pubmed:affiliation | Department of Cell Biology, University of Texas M.D. Anderson Cancer Center, Houston 77030. | lld:pubmed |
pubmed-article:2124506 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:2124506 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:2124506 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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