FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1575458839> ?p ?o ?g. }

• W1575458839 endingPage "14268" @default.
• W1575458839 startingPage "14264" @default.
• W1575458839 abstract "In order to define the influence of skeletal protein organization on transmembrane phospholipid movement in erythrocyte membranes, we measured the translocation rate of lysophosphatidylcholine in pathologic red cells. A simple method based on the differential extraction of lysophosphatidylcholine from the red cell membrane by saline and albumin solutions was used to quantitate the translocation rate. Two groups of pathologic red cells were chosen for these studies: red cells with quantitative deficiencies of the skeletal proteins, spectrin and protein 4.1, and sickle erythrocytes in which controlled reorganization of the membrane was induced by hemoglobin polymerization. Marked increase in lipid translocation rate was seen in red cells having quantitative deficiencies of spectrin and protein 4.1. The magnitude of the increase in translocation rate in spectrin-deficient red cells was related to the magnitude of protein deficiency. Translocation rate in sickle erythrocyte membranes increased by 50% upon deoxygenation as a result of sickle hemoglobin polymerization. No increase in translocation rate was seen in normal cells upon deoxygenation. By manipulating the extent of membrane reorganization that occurred following deoxygenation of sickle cells, we have been able to show that skeletal reorganization induced by hemoglobin polymerization and not hemoglobin polymerization per se is responsible for the increase in translocation rate. Together, these findings imply that the structural organization of membrane skeletal proteins plays an important role in regulating the rate of transbilayer movement of lipids across the erythrocyte membrane." @default.
• W1575458839 created "2016-06-24" @default.
• W1575458839 creator A5034746599 @default.
• W1575458839 creator A5042767527 @default.
• W1575458839 creator A5062366315 @default.
• W1575458839 creator A5079907001 @default.
• W1575458839 creator A5080177028 @default.
• W1575458839 creator A5082267944 @default.
• W1575458839 creator A5090681994 @default.
• W1575458839 date "1985-11-01" @default.
• W1575458839 modified "2023-10-16" @default.
• W1575458839 title "The structural organization of skeletal proteins influences lipid translocation across erythrocyte membrane." @default.
• W1575458839 cites W1608391891 @default.
• W1575458839 cites W1977986845 @default.
• W1575458839 cites W1978809713 @default.
• W1575458839 cites W1981776612 @default.
• W1575458839 cites W1990198778 @default.
• W1575458839 cites W1994690314 @default.
• W1575458839 cites W2004656105 @default.
• W1575458839 cites W2006831581 @default.
• W1575458839 cites W2013257106 @default.
• W1575458839 cites W2035591072 @default.
• W1575458839 cites W2060759428 @default.
• W1575458839 cites W2062828619 @default.
• W1575458839 cites W2083665434 @default.
• W1575458839 cites W2091647374 @default.
• W1575458839 cites W2092768865 @default.
• W1575458839 cites W2136604692 @default.
• W1575458839 cites W2157719407 @default.
• W1575458839 cites W4235956780 @default.
• W1575458839 doi "https://doi.org/10.1016/s0021-9258(17)38712-4" @default.
• W1575458839 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/4055777" @default.
• W1575458839 hasPublicationYear "1985" @default.
• W1575458839 type Work @default.
• W1575458839 sameAs 1575458839 @default.
• W1575458839 citedByCount "29" @default.
• W1575458839 countsByYear W15754588392021 @default.
• W1575458839 crossrefType "journal-article" @default.
• W1575458839 hasAuthorship W1575458839A5034746599 @default.
• W1575458839 hasAuthorship W1575458839A5042767527 @default.
• W1575458839 hasAuthorship W1575458839A5062366315 @default.
• W1575458839 hasAuthorship W1575458839A5079907001 @default.
• W1575458839 hasAuthorship W1575458839A5080177028 @default.
• W1575458839 hasAuthorship W1575458839A5082267944 @default.
• W1575458839 hasAuthorship W1575458839A5090681994 @default.
• W1575458839 hasBestOaLocation W15754588391 @default.
• W1575458839 hasConcept C104317684 @default.
• W1575458839 hasConcept C12554922 @default.
• W1575458839 hasConcept C138626823 @default.
• W1575458839 hasConcept C144647389 @default.
• W1575458839 hasConcept C185592680 @default.
• W1575458839 hasConcept C2993443003 @default.
• W1575458839 hasConcept C41625074 @default.
• W1575458839 hasConcept C55493867 @default.
• W1575458839 hasConcept C86803240 @default.
• W1575458839 hasConcept C95444343 @default.
• W1575458839 hasConceptScore W1575458839C104317684 @default.
• W1575458839 hasConceptScore W1575458839C12554922 @default.
• W1575458839 hasConceptScore W1575458839C138626823 @default.
• W1575458839 hasConceptScore W1575458839C144647389 @default.
• W1575458839 hasConceptScore W1575458839C185592680 @default.
• W1575458839 hasConceptScore W1575458839C2993443003 @default.
• W1575458839 hasConceptScore W1575458839C41625074 @default.
• W1575458839 hasConceptScore W1575458839C55493867 @default.
• W1575458839 hasConceptScore W1575458839C86803240 @default.
• W1575458839 hasConceptScore W1575458839C95444343 @default.
• W1575458839 hasIssue "26" @default.
• W1575458839 hasLocation W15754588391 @default.
• W1575458839 hasOpenAccess W1575458839 @default.
• W1575458839 hasPrimaryLocation W15754588391 @default.
• W1575458839 hasRelatedWork W2002197521 @default.
• W1575458839 hasRelatedWork W2004545843 @default.
• W1575458839 hasRelatedWork W2072917526 @default.
• W1575458839 hasRelatedWork W2155593527 @default.
• W1575458839 hasRelatedWork W2417662865 @default.
• W1575458839 hasRelatedWork W2466040811 @default.
• W1575458839 hasRelatedWork W2949796571 @default.
• W1575458839 hasRelatedWork W3011024476 @default.
• W1575458839 hasRelatedWork W3120553706 @default.
• W1575458839 hasRelatedWork W4364361946 @default.
• W1575458839 hasVolume "260" @default.
• W1575458839 isParatext "false" @default.
• W1575458839 isRetracted "false" @default.
• W1575458839 magId "1575458839" @default.
• W1575458839 workType "article" @default.