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http://purl.uniprot.org/citations/11940599http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11940599http://www.w3.org/2000/01/rdf-schema#comment"We used a panel of recombinant human apolipoprotein (apo) A-IV truncation mutants, in which pairs of 22-mer alpha-helices were sequentially deleted along the primary sequence, to examine the impact of protein structure and interfacial activity on the ability of apoA-IV to activate cholesterol ester transfer protein. Circular dichroism and fluorescence spectroscopy revealed that the secondary structure, conformation, and molecular stability of recombinant human apoA-IV were identical to the native protein. However, deletion of any of the alpha-helical domains in apoA-IV disrupted its tertiary structure and impaired its molecular stability. Surprisingly, determination of the water/phospholipid interfacial exclusion pressure of the apoA-IV truncation mutants revealed that, for most, deletion of amphipathic alpha-helical domains increased their affinity for phospholipid monolayers. All of the truncation mutants activated the transfer of fluorescent-labeled cholesterol esters between high and low density lipoproteins at a rate higher than native apoA-IV. There was a strong positive correlation (r = 0.790, p = 0.002) between the rate constant for cholesterol ester transfer and interfacial exclusion pressure. We conclude that molecular interfacial exclusion pressure, rather than specific helical domains, determines the degree to which apoA-IV, and likely other apolipoproteins, facilitate cholesterol ester transfer protein-mediated lipid exchange."xsd:string
http://purl.uniprot.org/citations/11940599http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m202197200"xsd:string
http://purl.uniprot.org/citations/11940599http://purl.uniprot.org/core/author"Steinmetz A."xsd:string
http://purl.uniprot.org/citations/11940599http://purl.uniprot.org/core/author"Denefle P."xsd:string
http://purl.uniprot.org/citations/11940599http://purl.uniprot.org/core/author"Tall A.R."xsd:string
http://purl.uniprot.org/citations/11940599http://purl.uniprot.org/core/author"Anderson R.A."xsd:string
http://purl.uniprot.org/citations/11940599http://purl.uniprot.org/core/author"Cook V.R."xsd:string
http://purl.uniprot.org/citations/11940599http://purl.uniprot.org/core/author"Weinberg R.B."xsd:string
http://purl.uniprot.org/citations/11940599http://purl.uniprot.org/core/author"Emmanuel F."xsd:string
http://purl.uniprot.org/citations/11940599http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/11940599http://purl.uniprot.org/core/name"J Biol Chem"xsd:string
http://purl.uniprot.org/citations/11940599http://purl.uniprot.org/core/pages"21549-21553"xsd:string
http://purl.uniprot.org/citations/11940599http://purl.uniprot.org/core/title"Interfacial exclusion pressure determines the ability of apolipoprotein A-IV truncation mutants to activate cholesterol ester transfer protein."xsd:string
http://purl.uniprot.org/citations/11940599http://purl.uniprot.org/core/volume"277"xsd:string
http://purl.uniprot.org/citations/11940599http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11940599
http://purl.uniprot.org/citations/11940599http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11940599
http://purl.uniprot.org/uniprot/P06727#attribution-7F4F5E73D25F3377EDC6E7EA21DFDDF9http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/11940599
http://purl.uniprot.org/uniprot/#_P06727-mappedCitation-11940599http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11940599
http://purl.uniprot.org/uniprot/#_Q13784-mappedCitation-11940599http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/11940599
http://purl.uniprot.org/uniprot/P06727http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/11940599
http://purl.uniprot.org/uniprot/Q13784http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/11940599