Associated Papers
The Structure of the Apolipoprotein A-I Monomer Provides Insights Into Its Oligomerisation and Lipid-binding Mechanisms.
Tou HI et al.
Journal of Molecular Biology, 2025
First eight residues of apolipoprotein A-I mediate the C-terminus control of helical bundle unfolding and its lipidation.
Brubaker G et al.
Plos One, 2020
The "beta-clasp" model of apolipoprotein A-I--a lipid-free solution structure determined by electron paramagnetic resonance spectroscopy.
Lagerstedt JO et al.
Biochimica Et Biophysica Acta, 2012
Influence of N-terminal helix bundle stability on the lipid-binding properties of human apolipoprotein A-I.
Tanaka M et al.
Biochimica Et Biophysica Acta, 2011
Evaluation of lipid-binding properties of the N-terminal helical segments in human apolipoprotein A-I using fragment peptides.
Tanaka M et al.
Journal of Peptide Science : an Official Publication of the European Peptide Society, 2009
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