Sequence conservation of apolipoprotein A-I affords novel insights into HDL structure-function

Bashtovyy, Denys; Jones, Martin K.; Anantharamaiah, G.M.; Segrest, Jere P.

doi:10.1194/jlr.r012658

Cited by 77 publications

(119 citation statements)

References 85 publications

Supporting

Mentioning

115

Contrasting

Order By: Relevance

“…S4) (67,74). Consistent with this observation, solvent accessibility and Trp fluorescence measurements of monomeric lipid-free apoA-I demonstrate that the tertiary structure folding provides a hydrophobic environment for all four tryptophans (62,74,75).…”

Section: Discussionsupporting

confidence: 63%

See 1 more Smart Citation

Impact of Self-association on Function of Apolipoprotein A-I

Jayaraman

Abe-Dohmae

Yokoyama

et al. 2011

Journal of Biological Chemistry

View full text Add to dashboard Cite

Background: Self-association is an intrinsic property of exchangeable apolipoproteins but an under-explored feature of the major protein of good cholesterol, apolipoprotein A-I. Result: Different degrees of apolipoprotein A-I self-association exhibit distinct in vitro lipid remodeling and cellular lipid release efficiencies. Conclusion: Self-association of apolipoprotein A-I modulates the biogenesis of high density lipoprotein. Significance: This is the first study to demonstrate that self-association of apolipoprotein A-I attunes key steps in reverse cholesterol transport.

show abstract

Section: Discussionsupporting

confidence: 63%

“…Interestingly, the other three tryptophans of human apoA-I are specific to mammals and are extremely well conserved in this class (67,68). Thus, we speculated that the acquisition of the four tryp- Table 1.…”

Section: Discussionmentioning

confidence: 99%

Impact of Self-association on Function of Apolipoprotein A-I

Jayaraman

Abe-Dohmae

Yokoyama

et al. 2011

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

“…Simulation by molecular dynamics shows interaction of Met112 and Met148 with Tyr115, creating a microenvironment unique to human apoA-I (Bashtovyy et al 2011) that may be optimal for such redox reactions. LOOH is also inactivated by apoA-II, although to a lesser extent.…”

Section: Mechanisms Of Protectionmentioning

confidence: 99%

Functionality of HDL: Antioxidation and Detoxifying Effects

Karlsson

Kontush

James

2014

High Density Lipoproteins

View full text Add to dashboard Cite

“…In ApoA1, the motifs of amphipathic α-helices are evolutionally preserved. 32 The total helix content is 53%, although β-sheets contribute for a total of 12% of the a.a. sequence of ApoA1. 26 Lipid-Binding and Lipid-Solubilizing Properties of ApoA1 ApoA1 binding to lipids (ie, entrance to a lipid particle) is induced by the interaction between a highly hydrophobic C-terminal domain with the surface lipids of a particle.…”

Section: Apoa1 Structure and Function Hdl Particles And Apoa1mentioning

confidence: 99%