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Q28116206-4BBA28E4-264F-4A22-A743-8D6F0F6FFE58
Q28116206-4BBA28E4-264F-4A22-A743-8D6F0F6FFE58
BestRank
Statement
http://www.wikidata.org/entity/statement/Q28116206-4BBA28E4-264F-4A22-A743-8D6F0F6FFE58
Amyloidogenic mutations in human apolipoprotein A-I are not necessarily destabilizing - a common mechanism of apolipoprotein A-I misfolding in familial amyloidosis and atherosclerosis
P2860
Q28116206-4BBA28E4-264F-4A22-A743-8D6F0F6FFE58
BestRank
Statement
http://www.wikidata.org/entity/statement/Q28116206-4BBA28E4-264F-4A22-A743-8D6F0F6FFE58
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Statement
wasDerivedFrom
497c54595d1553ab4a910f95e19869435664d216
P2860
Crystal structure of Δ(185-243)ApoA-I suggests a mechanistic framework for the protein adaptation to the changing lipid load in good cholesterol: from flatland to sphereland via double belt, belt buckle, double hairpin and trefoil/tetrafoil