Pages that link to "Q73141710"

The following pages link to Deletion of the C-terminal domain of apolipoprotein A-I impairs cell surface binding and lipid efflux in macrophage (Q73141710):

Displaying 26 items.

• Secondary structure of human apolipoprotein A-I(1-186) in lipid-mimetic solution (Q31861020) (← links)
• The helix bundle: a reversible lipid binding motif (Q33598704) (← links)
• Disruption of the C-terminal helix by single amino acid deletion is directly responsible for impaired cholesterol efflux ability of apolipoprotein A-I Nichinan (Q33741251) (← links)
• Analysis of covalent modifications of proteins by oxidized phospholipids using a novel method of peptide enrichment (Q33855231) (← links)
• Modifying apolipoprotein A-I by malondialdehyde, but not by an array of other reactive carbonyls, blocks cholesterol efflux by the ABCA1 pathway (Q33897803) (← links)
• Influence of Apolipoprotein (Apo) A-I Structure on Nascent High Density Lipoprotein (HDL) Particle Size Distribution (Q34186341) (← links)
• Structural models of human apolipoprotein A-I: a critical analysis and review (Q34201689) (← links)
• Novel N-terminal mutation of human apolipoprotein A-I reduces self-association and impairs LCAT activation (Q34395097) (← links)
• Impact of HDL oxidation by the myeloperoxidase system on sterol efflux by the ABCA1 pathway (Q35166941) (← links)
• Low high-density lipoprotein cholesterol: physiological background, clinical importance and drug treatment (Q35203793) (← links)
• Site-specific oxidation of apolipoprotein A-I impairs cholesterol export by ABCA1, a key cardioprotective function of HDL. (Q35783321) (← links)
• Molecules that mimic apolipoprotein A-I: potential agents for treating atherosclerosis (Q37671683) (← links)
• Reverse cholesterol transport: from classical view to new insights (Q37820949) (← links)
• Influence of C-terminal α-helix hydrophobicity and aromatic amino acid content on apolipoprotein A-I functionality. (Q39501024) (← links)
• Phosphatidylinositol promotes cholesterol transport and excretion (Q40654606) (← links)
• The C-terminal domain of apolipoprotein A-I is involved in ABCA1-driven phospholipid and cholesterol efflux. (Q40684965) (← links)
• The N-terminal globular domain and the first class A amphipathic helix of apolipoprotein A-I are important for lecithin:cholesterol acyltransferase activation and the maturation of high density lipoprotein in vivo. (Q40774548) (← links)
• Probing the C-terminal domain of lipid-free apoA-I demonstrates the vital role of the H10B sequence repeat in HDL formation. (Q42406157) (← links)
• Expression of the C-terminal domain of human apolipoprotein A-I using a chimeric apolipoprotein. (Q43791722) (← links)
• Heteronuclear NMR studies of human serum apolipoprotein A-I. Part I. Secondary structure in lipid-mimetic solution (Q44026004) (← links)
• Apolipoprotein composition and particle size affect HDL degradation by chymase: effect on cellular cholesterol efflux. (Q44300021) (← links)
• Alpha-helix formation is required for high affinity binding of human apolipoprotein A-I to lipids (Q44799709) (← links)
• Transfer of C-terminal residues of human apolipoprotein A-I to insect apolipophorin III creates a two-domain chimeric protein with enhanced lipid binding activity. (Q45968902) (← links)
• Charged Residues in the C-Terminal Domain of Apolipoprotein A-I Modulate Oligomerization (Q88172744) (← links)
• Lysine glycation of apolipoprotein A-I impairs its anti-inflammatory function in type 2 diabetes mellitus (Q90854036) (← links)
• First eight residues of apolipoprotein A-I mediate the C-terminus control of helical bundle unfolding and its lipidation (Q92689066) (← links)