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Protein Structure, Secondary
In vivo studies of HDL assembly and metabolism using adenovirus-mediated transfer of ApoA-I mutants in ApoA-I-deficient mice.
Apolipoprotein A-I alpha -helices 7 and 8 modulate high density lipoprotein subclass distribution.
Engineering mouse apolipoprotein A-I into a monomeric, active protein useful for structural determination.
An apoA-I mimetic peptide containing a proline residue has greater in vivo HDL binding and anti-inflammatory ability than the 4F peptide.
Apoprotein A-I mimetic peptides and their potential anti-atherogenic mechanisms of action.
Helix-turn-helix peptides that form alpha-helical fibrils: turn sequences drive fibril structure.
The specific amino acid sequence between helices 7 and 8 influences the binding specificity of human apolipoprotein A-I for high density lipoprotein (HDL) subclasses: a potential for HDL preferential generation.
HDL apolipoprotein-related peptides in the treatment of atherosclerosis and other inflammatory disorders.
Protein Structure Secondary