| pubmed-article:9098627 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:9098627 | lifeskim:mentions | umls-concept:C0025251 | lld:lifeskim |
| pubmed-article:9098627 | lifeskim:mentions | umls-concept:C0024518 | lld:lifeskim |
| pubmed-article:9098627 | lifeskim:mentions | umls-concept:C0392747 | lld:lifeskim |
| pubmed-article:9098627 | lifeskim:mentions | umls-concept:C0033625 | lld:lifeskim |
| pubmed-article:9098627 | lifeskim:mentions | umls-concept:C0456387 | lld:lifeskim |
| pubmed-article:9098627 | lifeskim:mentions | umls-concept:C0205349 | lld:lifeskim |
| pubmed-article:9098627 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:9098627 | pubmed:dateCreated | 1997-9-2 | lld:pubmed |
| pubmed-article:9098627 | pubmed:abstractText | The nature of charge distributions in membrane-bound macromolecular structures renders them susceptible to interaction with transmembrane potential fields. As a result, conformational changes in such species may be expected to occur when this potential is altered. We have detected reversible conformational change in the major histocompatibility complex (MHC) class I antigen in the plasma membrane of human JY cells, as monitored by flow-cytometric resonance energy-transfer, upon reduction of the transmembrane potential (depolarization). This change increased the intramolecular energy-transfer efficiency between fluorescent donor- and acceptor-labeled monoclonal antibodies directed, respectively, to epitopes on the light (beta 2-microglobulin) and the heavy chains of the MHC class I antigen. Repolarization of the depolarized samples restored the energy-transfer efficiency to the original values measured before depolarization. Depolarization caused similar relative changes in fluorescence resonance energy-transfer efficiency when Fab fragments were used for labeling MHC class I complex, suggesting that the observed phenomenon is not restricted to whole monoclonal antibodies. | lld:pubmed |
| pubmed-article:9098627 | pubmed:language | eng | lld:pubmed |
| pubmed-article:9098627 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9098627 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:9098627 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9098627 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9098627 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9098627 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9098627 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9098627 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9098627 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9098627 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:9098627 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:9098627 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:9098627 | pubmed:issn | 0196-4763 | lld:pubmed |
| pubmed-article:9098627 | pubmed:author | pubmed-author:DaleR ERE | lld:pubmed |
| pubmed-article:9098627 | pubmed:author | pubmed-author:BalázsMM | lld:pubmed |
| pubmed-article:9098627 | pubmed:author | pubmed-author:KesterRR | lld:pubmed |
| pubmed-article:9098627 | pubmed:author | pubmed-author:DamjanovichSS | lld:pubmed |
| pubmed-article:9098627 | pubmed:author | pubmed-author:BeneLL | lld:pubmed |
| pubmed-article:9098627 | pubmed:author | pubmed-author:SzöllósiJJ | lld:pubmed |
| pubmed-article:9098627 | pubmed:author | pubmed-author:MátyusLL | lld:pubmed |
| pubmed-article:9098627 | pubmed:author | pubmed-author:AmelootMM | lld:pubmed |
| pubmed-article:9098627 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:9098627 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:9098627 | pubmed:volume | 27 | lld:pubmed |
| pubmed-article:9098627 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:9098627 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:9098627 | pubmed:pagination | 353-7 | lld:pubmed |
| pubmed-article:9098627 | pubmed:dateRevised | 2007-11-15 | lld:pubmed |
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| pubmed-article:9098627 | pubmed:meshHeading | pubmed-meshheading:9098627-... | lld:pubmed |
| pubmed-article:9098627 | pubmed:meshHeading | pubmed-meshheading:9098627-... | lld:pubmed |
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| pubmed-article:9098627 | pubmed:meshHeading | pubmed-meshheading:9098627-... | lld:pubmed |
| pubmed-article:9098627 | pubmed:year | 1997 | lld:pubmed |
| pubmed-article:9098627 | pubmed:articleTitle | Major histocompatibility complex class I protein conformation altered by transmembrane potential changes. | lld:pubmed |
| pubmed-article:9098627 | pubmed:affiliation | Department of Biophysics, Medical University School, Debrecen, Hungary. | lld:pubmed |
| pubmed-article:9098627 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:9098627 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:9098627 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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