Title : Alteration of negatively charged residues in the 89 to 99 domain of apoA-I affects lipid homeostasis and maturation of HDL.

Pub. Date : 2011 Jul

PMID : 21504968






2 Functional Relationships(s)
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1 Physicochemical studies showed that the apoA-I[D89A/E91A/E92A] mutant had reduced alpha-helical content and effective enthalpy of thermal denaturation, increased exposure of hydrophobic surfaces, and increased affinity for triglyceride-rich emulsions. Triglycerides apolipoprotein A1 Homo sapiens
2 We conclude that residues D89, E91, and E92 of apoA-I are important for plasma cholesterol and triglyceride homeostasis as well as for the maturation of HDL. Triglycerides apolipoprotein A1 Homo sapiens