Disruption of the C-terminal helix by single amino acid deletion is directly responsible for impaired cholesterol efflux ability of apolipoprotein A-I Nichinan.

Disruption of the C-terminal helix by single amino acid deletion is directly responsible for impaired cholesterol efflux ability of apolipoprotein A-I Nichinan.

Item
http://www.wikidata.org/entity/Q33741251
Structural Insights into High Density Lipoprotein: Old Models and New FactsNew insights into the determination of HDL structure by apolipoproteins: Thematic review series: high density lipoprotein structure, function, and metabolismAmyloidogenic mutations in human apolipoprotein A-I are not necessarily destabilizing - a common mechanism of apolipoprotein A-I misfolding in familial amyloidosis and atherosclerosisStructure of apolipoprotein A-I N terminus on nascent high density lipoproteins.Impact of self-association on function of apolipoprotein A-INaturally occurring variant of mouse apolipoprotein A-I alters the lipid and HDL association properties of the protein.Dual role of an N-terminal amyloidogenic mutation in apolipoprotein A-I: destabilization of helix bundle and enhancement of fibril formation.Dietary fats and health: dietary recommendations in the context of scientific evidenceHelical domains that mediate lipid solubilization and ABCA1-specific cholesterol efflux in apolipoproteins C-I and A-IILipid-free Apolipoprotein A-I Structure: Insights into HDL Formation and Atherosclerosis Development.The roles of C-terminal helices of human apolipoprotein A-I in formation of high-density lipoprotein particles.Formation of stable nanodiscs by bihelical apolipoprotein A-I mimetic peptide.Effects of the Iowa and Milano mutations on apolipoprotein A-I structure and dynamics determined by hydrogen exchange and mass spectrometry.Probing the C-terminal domain of lipid-free apoA-I demonstrates the vital role of the H10B sequence repeat in HDL formation.Mimetic peptides of human apoA-I helix 10 get together to lower lipids and ameliorate atherosclerosis: is the action in the gut?
P2860

Disruption of the C-terminal helix by single amino acid deletion is directly responsible for impaired cholesterol efflux ability of apolipoprotein A-I Nichinan.

Item
http://www.wikidata.org/entity/Q33741251
description
2009 nî lūn-bûn
@nan
2009 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Disruption of the C-terminal h ...... f apolipoprotein A-I Nichinan.
@ast
Disruption of the C-terminal h ...... f apolipoprotein A-I Nichinan.
@en
type
label
Disruption of the C-terminal h ...... f apolipoprotein A-I Nichinan.
@ast
Disruption of the C-terminal h ...... f apolipoprotein A-I Nichinan.
@en
prefLabel
Disruption of the C-terminal h ...... f apolipoprotein A-I Nichinan.
@ast
Disruption of the C-terminal h ...... f apolipoprotein A-I Nichinan.
@en
P1433
P1476
P2093
P2860
P304
P31
P356
P433
P478
P577
P698
P932
P356
P1433
P1476
Disruption of the C-terminal h ...... f apolipoprotein A-I Nichinan.
@en
P2093
P2860
P304
P31
P356
P433
P478
P577
P698
P932