Associated Papers
Mechanisms of aggregation and fibril formation of the amyloidogenic N-terminal fragment of apolipoprotein A-I.
Mizuguchi C et al.
The Journal of Biological Chemistry, 2019
Human apolipoprotein A-I Gly26Arg stimulation of inflammatory responses via NF-kB activation: Potential roles in amyloidosis?
Ramella NA et al.
Pathophysiology : the Official Journal of the International Society for Pathophysiology, 2018
Iowa Mutant Apolipoprotein A-I (ApoA-IIowa) Fibrils Target Lysosomes.
Kameyama H et al.
Scientific Reports, 2016
Cellular interaction and cytotoxicity of the iowa mutation of apolipoprotein A-I (ApoA-IIowa) amyloid mediated by sulfate moieties of heparan sulfate.
Kuwabara K et al.
The Journal of Biological Chemistry, 2015
Amyloidogenic Mutation Promotes Fibril Formation of the N-terminal Apolipoprotein A-I on Lipid Membranes.
Mizuguchi C et al.
The Journal of Biological Chemistry, 2015
Chameleon 'aggregation-prone' segments of apoA-I: A model of amyloid fibrils formed in apoA-I amyloidosis.
Louros NN et al.
International Journal of Biological Macromolecules, 2015
The extreme N-terminal region of human apolipoprotein A-I has a strong propensity to form amyloid fibrils.
Adachi E et al.
Febs Letters, 2014
Interaction of thioflavin T with amyloid fibrils of apolipoprotein A-I N-terminal fragment: resonance energy transfer study.
Girych M et al.
Journal of Structural Biology, 2014
Dual role of an N-terminal amyloidogenic mutation in apolipoprotein A-I: destabilization of helix bundle and enhancement of fibril formation.
Adachi E et al.
The Journal of Biological Chemistry, 2013
The fibrillogenic L178H variant of apolipoprotein A-I forms helical fibrils.
Petrlova J et al.
Journal of Lipid Research, 2012
The crystal structure of the C-terminal truncated apolipoprotein A-I sheds new light on amyloid formation by the N-terminal fragment.
Gursky O et al.
Biochemistry, 2012
Effects of the known pathogenic mutations on the aggregation pathway of the amyloidogenic peptide of apolipoprotein A-I.
Raimondi S et al.
Journal of Molecular Biology, 2011
A novel apolipoprotein A-1 variant, Arg173Pro, associated with cardiac and cutaneous amyloidosis.
Hamidi Asl K et al.
Biochemical and Biophysical Research Communications, 1999
A new apolipoprotein Al variant, Trp50Arg, causes hereditary amyloidosis.
Booth DR et al.
Qjm : Monthly Journal of the Association of Physicians, 1995