FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2071122867> ?p ?o ?g. }

• W2071122867 endingPage "13164" @default.
• W2071122867 startingPage "13156" @default.
• W2071122867 abstract "Because of its role in reverse cholesterol transport, human apolipoprotein A-I is the most widely studied exchangeable apolipoprotein. Residues 1−43 of human apoA-I, encoded by exon 3 of the gene, are highly conserved and less well understood than residues 44−243, encoded by exon 4. In contrast to residues 44−243, residues 1−43 do not contain the 22 amino acid tandem repeats thought to form lipid binding amphipathic helices. To understand the structural and functional roles of the N-terminal region, we studied a synthetic peptide representing the first 44 residues of human apoA-I ([1−44]apoA-I). Far-ultraviolet circular dichroism spectra showed that [1−44]apoA-I is unfolded in aqueous solution. However, in the presence of n-octyl β-d-glucopyranoside, a nonionic lipid mimicking detergent, above its critical micelle concentration (∼0.7% at 25 °C), sodium dodecyl sulfate, an ionic detergent, above its CMC (∼0.2%), trimethylamine N-oxide, a folding inducing organic osmolyte, or trifluoroethanol, an α-helix inducer, α-helical structure was formed in [1−44]apoA-I up to ∼45%. Characterization by density gradient ultracentrifugation and visualization by negative staining electron microscopy demonstrated that [1−44]apoA-I interacts with dimyristoylphosphatidylcholine (DMPC) over a wide range of lipid:peptide ratios from 1:1 to 12:1 (w/w). At 1:1 DMPC:[1−44]apoA-I (w/w) ratio, discoidal complexes with composition ∼4:1 (w/w) and ∼100 Å diameter were formed in equilibrium with free peptide. At higher ratios, discoidal complexes were shown to exist together with a heterogeneous population of lipid vesicles with peptide bound also in equilibrium with free peptide. When bound to DMPC, [1−44]apoA-I has ∼60% helical structure, independent of whether it forms discoidal or vesicular complexes. This helical content is consistent with that of the predicted G* helix (residues 8−33). Our data provide the first strong and direct evidence that the N-terminal region of apoA-I binds lipid and can form discoidal structures and a heterogeneous population of vesicles. In doing so, ∼60% of this region folds into α-helix from random coil. The composition of the 100 Å discoidal complex is ∼5 [1−44]apoA-I and ∼150 DMPC molecules per disk. The helix length of 5 [1−44]apoA-I molecules in lipid-bound form is just long enough to wrap around the DMPC bilayer disk once." @default.
• W2071122867 created "2016-06-24" @default.
• W2071122867 creator A5024374500 @default.
• W2071122867 creator A5080929565 @default.
• W2071122867 date "2004-09-25" @default.
• W2071122867 modified "2023-09-27" @default.
• W2071122867 title "Conformation and Lipid Binding of the N-Terminal (1−44) Domain of Human Apolipoprotein A-I" @default.
• W2071122867 cites W156678813 @default.
• W2071122867 cites W1605185004 @default.
• W2071122867 cites W1775749144 @default.
• W2071122867 cites W1947043095 @default.
• W2071122867 cites W1967312649 @default.
• W2071122867 cites W1969668277 @default.
• W2071122867 cites W1980937891 @default.
• W2071122867 cites W2069141366 @default.
• W2071122867 cites W2107940734 @default.
• W2071122867 cites W2155032726 @default.
• W2071122867 cites W2181164354 @default.
• W2071122867 cites W2285831485 @default.
• W2071122867 cites W2401829918 @default.
• W2071122867 cites W4625298 @default.
• W2071122867 doi "https://doi.org/10.1021/bi0487894" @default.
• W2071122867 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15476409" @default.
• W2071122867 hasPublicationYear "2004" @default.
• W2071122867 type Work @default.
• W2071122867 sameAs 2071122867 @default.
• W2071122867 citedByCount "29" @default.
• W2071122867 countsByYear W20711228672013 @default.
• W2071122867 countsByYear W20711228672014 @default.
• W2071122867 countsByYear W20711228672015 @default.
• W2071122867 countsByYear W20711228672016 @default.
• W2071122867 countsByYear W20711228672019 @default.
• W2071122867 countsByYear W20711228672022 @default.
• W2071122867 countsByYear W20711228672023 @default.
• W2071122867 crossrefType "journal-article" @default.
• W2071122867 hasAuthorship W2071122867A5024374500 @default.
• W2071122867 hasAuthorship W2071122867A5080929565 @default.
• W2071122867 hasConcept C133571119 @default.
• W2071122867 hasConcept C185592680 @default.
• W2071122867 hasConcept C2778163477 @default.
• W2071122867 hasConcept C2779281246 @default.
• W2071122867 hasConcept C55493867 @default.
• W2071122867 hasConcept C62746215 @default.
• W2071122867 hasConcept C71240020 @default.
• W2071122867 hasConcept C8010536 @default.
• W2071122867 hasConceptScore W2071122867C133571119 @default.
• W2071122867 hasConceptScore W2071122867C185592680 @default.
• W2071122867 hasConceptScore W2071122867C2778163477 @default.
• W2071122867 hasConceptScore W2071122867C2779281246 @default.
• W2071122867 hasConceptScore W2071122867C55493867 @default.
• W2071122867 hasConceptScore W2071122867C62746215 @default.
• W2071122867 hasConceptScore W2071122867C71240020 @default.
• W2071122867 hasConceptScore W2071122867C8010536 @default.
• W2071122867 hasIssue "41" @default.
• W2071122867 hasLocation W20711228671 @default.
• W2071122867 hasLocation W20711228672 @default.
• W2071122867 hasOpenAccess W2071122867 @default.
• W2071122867 hasPrimaryLocation W20711228671 @default.
• W2071122867 hasRelatedWork W1999350466 @default.
• W2071122867 hasRelatedWork W2038551902 @default.
• W2071122867 hasRelatedWork W2042501173 @default.
• W2071122867 hasRelatedWork W2045401917 @default.
• W2071122867 hasRelatedWork W2047661239 @default.
• W2071122867 hasRelatedWork W2060469118 @default.
• W2071122867 hasRelatedWork W2061876750 @default.
• W2071122867 hasRelatedWork W2063509704 @default.
• W2071122867 hasRelatedWork W2065388695 @default.
• W2071122867 hasRelatedWork W2110944637 @default.
• W2071122867 hasVolume "43" @default.
• W2071122867 isParatext "false" @default.
• W2071122867 isRetracted "false" @default.
• W2071122867 magId "2071122867" @default.
• W2071122867 workType "article" @default.