Folded functional lipid-poor apolipoprotein A-I obtained by heating of high-density lipoproteins: relevance to high-density lipoprotein biogenesis.

Folded functional lipid-poor apolipoprotein A-I obtained by heating of high-density lipoproteins: relevance to high-density lipoprotein biogenesis.

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http://www.wikidata.org/entity/Q37378312
Structural basis for distinct functions of the naturally occurring Cys mutants of human apolipoprotein A-IAmyloidogenic mutations in human apolipoprotein A-I are not necessarily destabilizing - a common mechanism of apolipoprotein A-I misfolding in familial amyloidosis and atherosclerosisThe crystal structure of the C-terminal truncated apolipoprotein A-I sheds new light on amyloid formation by the N-terminal fragment.High-density lipoprotein modulates thrombosis by preventing von Willebrand factor self-association and subsequent platelet adhesion.Impact of estimated HDL particle size via the ratio of HDL-C and apoprotein A-I on short-term prognosis of diabetic patients with stable coronary artery disease.An experimentally robust model of monomeric apolipoprotein A-I created from a chimera of two X-ray structures and molecular dynamics simulationsThermal transitions in serum amyloid A in solution and on the lipid: implications for structure and stability of acute-phase HDL.Structural stability and functional remodeling of high-density lipoproteins.Validation of previous computer models and MD simulations of discoidal HDL by a recent crystal structure of apoA-I.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/tetrafoilStructural Stability and Local Dynamics in Disease-Causing Mutants of Human Apolipoprotein A-I: What Makes the Protein Amyloidogenic?High-Density Lipoproteins for Therapeutic Delivery Systems.Proteolysis of apolipoprotein A-I by secretory phospholipase A₂: a new link between inflammation and atherosclerosisRole of apolipoprotein A-II in the structure and remodeling of human high-density lipoprotein (HDL): protein conformational ensemble on HDL.Amyloid-Forming Properties of Human Apolipoproteins: Sequence Analyses and Structural InsightsSerum amyloid A self-assembles with phospholipids to form stable protein-rich nanoparticles with a distinct structure: A hypothetical function of SAA as a "molecular mop" in immune response.Triglyceride increase in the core of high-density lipoproteins augments apolipoprotein dissociation from the surface: Potential implications for treatment of apolipoprotein deposition diseases.
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Folded functional lipid-poor apolipoprotein A-I obtained by heating of high-density lipoproteins: relevance to high-density lipoprotein biogenesis.

Item
http://www.wikidata.org/entity/Q37378312
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on March 2012
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Folded functional lipid-poor a ...... ensity lipoprotein biogenesis.
@en
Folded functional lipid-poor a ...... ensity lipoprotein biogenesis.
@nl
type
label
Folded functional lipid-poor a ...... ensity lipoprotein biogenesis.
@en
Folded functional lipid-poor a ...... ensity lipoprotein biogenesis.
@nl
prefLabel
Folded functional lipid-poor a ...... ensity lipoprotein biogenesis.
@en
Folded functional lipid-poor a ...... ensity lipoprotein biogenesis.
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698
P921
P932
P356
P1433
P1476
Folded functional lipid-poor a ...... density lipoprotein biogenesis
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698
P921
P932