FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1566992573> ?p ?o ?g. }

• W1566992573 endingPage "5" @default.
• W1566992573 startingPage "5" @default.
• W1566992573 abstract "The classic model of estrogen action requires that the estrogen receptor (ER) activates gene expression by binding directly or indirectly to DNA. Recent studies, however, strongly suggest that ER can act through nongenomic signal transduction pathways and may be mediated by a membrane bound form of the ER. Estradiol covalently linked to membrane impermeable BSA (E2-BSA) has been widely used as an agent to study these novel membrane-associated ER events. However, a recent report suggests that E2-BSA does not compete for E2 binding to purified ER in vitro. To resolve this apparent discrepancy, we performed competition studies examining the binding of E2 and E2-BSA to both purified ER preparations and ER within intact cells. To eliminate potential artifacts due to contamination of commercially available E2-BSA preparations with unconjugated E2 (usually between 3–5%), the latter was carefully removed by ultrafiltration. As previously reported, a 10-to 1000-fold molar excess of E2-BSA was unable to compete with 3H-E2 binding to ER when added simultaneously. However, when ER was pre-incubated with the same concentrations of E2-BSA, the binding of 3H-E2 was significantly reduced. E2-BSA binding to a putative membrane-associated ER was directly visualized using fluorescein labeled E2-BSA (E2-BSA-FITC). Staining was restricted to the cell membrane when E2-BSA-FITC was incubated with stable transfectants of the murine ERα within ER-negative HeLa cells and with MC7 cells that endogenously produce ERα. This staining appeared highly specific since it was competed by pre-incubation with E2 in a dose dependent manner and with the competitor ICI-182,780. These results demonstrate that E2-BSA does bind to purified ER in vitro and to ER in intact cells. It seems likely that the size and structure of E2-BSA requires more energy for it to bind to the ER and consequently binds more slowly than E2. More importantly, these findings demonstrate that in intact cells that express ER, E2-BSA binding is localized to the cell membrane, strongly suggesting a membrane bound form of the ER." @default.
• W1566992573 created "2016-06-24" @default.
• W1566992573 creator A5023706392 @default.
• W1566992573 creator A5047928767 @default.
• W1566992573 creator A5058545312 @default.
• W1566992573 date "2004-01-01" @default.
• W1566992573 modified "2023-09-30" @default.
• W1566992573 cites W1509103176 @default.
• W1566992573 cites W1662062786 @default.
• W1566992573 cites W1967908614 @default.
• W1566992573 cites W1980050810 @default.
• W1566992573 cites W1981746913 @default.
• W1566992573 cites W1985941840 @default.
• W1566992573 cites W2005766913 @default.
• W1566992573 cites W2017618663 @default.
• W1566992573 cites W2019154970 @default.
• W1566992573 cites W2024638388 @default.
• W1566992573 cites W2027501985 @default.
• W1566992573 cites W2037603641 @default.
• W1566992573 cites W2039952305 @default.
• W1566992573 cites W2055752761 @default.
• W1566992573 cites W2062835756 @default.
• W1566992573 cites W2063212877 @default.
• W1566992573 cites W2073088048 @default.
• W1566992573 cites W2075055531 @default.
• W1566992573 cites W2078280901 @default.
• W1566992573 cites W2080987913 @default.
• W1566992573 cites W2082354713 @default.
• W1566992573 cites W2084216857 @default.
• W1566992573 cites W2087022731 @default.
• W1566992573 cites W2128721915 @default.
• W1566992573 cites W2160084272 @default.
• W1566992573 cites W2217539151 @default.
• W1566992573 doi "https://doi.org/10.1186/1478-1336-2-5" @default.
• W1566992573 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/516042" @default.
• W1566992573 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15318942" @default.
• W1566992573 hasPublicationYear "2004" @default.
• W1566992573 type Work @default.
• W1566992573 sameAs 1566992573 @default.
• W1566992573 citedByCount "79" @default.
• W1566992573 countsByYear W15669925732012 @default.
• W1566992573 countsByYear W15669925732013 @default.
• W1566992573 countsByYear W15669925732014 @default.
• W1566992573 countsByYear W15669925732015 @default.
• W1566992573 countsByYear W15669925732016 @default.
• W1566992573 countsByYear W15669925732017 @default.
• W1566992573 countsByYear W15669925732018 @default.
• W1566992573 countsByYear W15669925732019 @default.
• W1566992573 countsByYear W15669925732020 @default.
• W1566992573 countsByYear W15669925732021 @default.
• W1566992573 countsByYear W15669925732022 @default.
• W1566992573 crossrefType "journal-article" @default.
• W1566992573 hasAuthorship W1566992573A5023706392 @default.
• W1566992573 hasAuthorship W1566992573A5047928767 @default.
• W1566992573 hasAuthorship W1566992573A5058545312 @default.
• W1566992573 hasBestOaLocation W15669925731 @default.
• W1566992573 hasConcept C107824862 @default.
• W1566992573 hasConcept C121608353 @default.
• W1566992573 hasConcept C12554922 @default.
• W1566992573 hasConcept C153911025 @default.
• W1566992573 hasConcept C185592680 @default.
• W1566992573 hasConcept C202751555 @default.
• W1566992573 hasConcept C2777366897 @default.
• W1566992573 hasConcept C41625074 @default.
• W1566992573 hasConcept C530470458 @default.
• W1566992573 hasConcept C54355233 @default.
• W1566992573 hasConcept C55493867 @default.
• W1566992573 hasConcept C84606932 @default.
• W1566992573 hasConcept C86803240 @default.
• W1566992573 hasConcept C86807702 @default.
• W1566992573 hasConcept C95444343 @default.
• W1566992573 hasConceptScore W1566992573C107824862 @default.
• W1566992573 hasConceptScore W1566992573C121608353 @default.
• W1566992573 hasConceptScore W1566992573C12554922 @default.
• W1566992573 hasConceptScore W1566992573C153911025 @default.
• W1566992573 hasConceptScore W1566992573C185592680 @default.
• W1566992573 hasConceptScore W1566992573C202751555 @default.
• W1566992573 hasConceptScore W1566992573C2777366897 @default.
• W1566992573 hasConceptScore W1566992573C41625074 @default.
• W1566992573 hasConceptScore W1566992573C530470458 @default.
• W1566992573 hasConceptScore W1566992573C54355233 @default.
• W1566992573 hasConceptScore W1566992573C55493867 @default.
• W1566992573 hasConceptScore W1566992573C84606932 @default.
• W1566992573 hasConceptScore W1566992573C86803240 @default.
• W1566992573 hasConceptScore W1566992573C86807702 @default.
• W1566992573 hasConceptScore W1566992573C95444343 @default.
• W1566992573 hasIssue "1" @default.
• W1566992573 hasLocation W15669925731 @default.
• W1566992573 hasLocation W15669925732 @default.
• W1566992573 hasLocation W15669925733 @default.
• W1566992573 hasLocation W15669925734 @default.
• W1566992573 hasOpenAccess W1566992573 @default.
• W1566992573 hasPrimaryLocation W15669925731 @default.
• W1566992573 hasRelatedWork W1982218634 @default.
• W1566992573 hasRelatedWork W1986415591 @default.
• W1566992573 hasRelatedWork W2006465774 @default.
• W1566992573 hasRelatedWork W2191374078 @default.
• W1566992573 hasRelatedWork W2223109887 @default.

• next