Apolipoprotein AI tertiary structures determine stability and phospholipid-binding activity of discoidal high-density lipoprotein particles of different sizes.
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IPET and FETR: experimental approach for studying molecular structure dynamics by cryo-electron tomography of a single-molecule structureIsolation, characterization, and stability of discretely-sized nanolipoprotein particles assembled with apolipophorin-IIIStructural basis of transfer between lipoproteins by cholesteryl ester transfer protein.Optimized negative staining: a high-throughput protocol for examining small and asymmetric protein structure by electron microscopy.Dynamics of activation of lecithin:cholesterol acyltransferase by apolipoprotein A-IEffects of cholesterol on thermal stability of discoidal high density lipoproteins.An optimized negative-staining protocol of electron microscopy for apoE4 POPC lipoproteinMorphology and structure of lipoproteins revealed by an optimized negative-staining protocol of electron microscopy.Assessment of the validity of the double superhelix model for reconstituted high density lipoproteins: a combined computational-experimental approach.Optimized negative-staining electron microscopy for lipoprotein studies.Crystal structure of Δ(185-243)ApoA-I suggests a mechanistic framework for the protein adaptation to the changing lipid load in good cholesterol: from flatland to sphereland via double belt, belt buckle, double hairpin and trefoil/tetrafoilPET Imaging of Tumor-Associated Macrophages with 89Zr-Labeled High-Density Lipoprotein NanoparticlesRole of apolipoprotein A-II in the structure and remodeling of human high-density lipoprotein (HDL): protein conformational ensemble on HDL.Revising the high-density lipoprotein targeting strategies - insights from human and preclinical studies.Nanodiscs in Membrane Biochemistry and Biophysics.Characterization of ApoJ-reconstituted high-density lipoprotein (rHDL) nanodisc for the potential treatment of cerebral β-amyloidosis.Sequence-specific apolipoprotein A-I effects on lecithin:cholesterol acyltransferase activity.Nuclear Magnetic Resonance Spectroscopy in the Detection and Characterisation of Cardiovascular Disease: Key Studies
P2860
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P2860
Apolipoprotein AI tertiary structures determine stability and phospholipid-binding activity of discoidal high-density lipoprotein particles of different sizes.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on May 2009
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Apolipoprotein AI tertiary str ...... particles of different sizes.
@en
Apolipoprotein AI tertiary str ...... particles of different sizes.
@nl
type
label
Apolipoprotein AI tertiary str ...... particles of different sizes.
@en
Apolipoprotein AI tertiary str ...... particles of different sizes.
@nl
prefLabel
Apolipoprotein AI tertiary str ...... particles of different sizes.
@en
Apolipoprotein AI tertiary str ...... particles of different sizes.
@nl
P2093
P2860
P356
P1433
P1476
Apolipoprotein AI tertiary str ...... particles of different sizes.
@en
P2093
Daniel Sparks
David W Hoyt
Jianjun Wang
Tracey Neville
W Gray Jerome
Xuefeng Ren
P2860
P304
P356
10.1002/PRO.101
P577
2009-05-01T00:00:00Z