Activation of lecithin:cholesterol acyltransferase by HDL ApoA-I central helices. - Wikidata - awgldk - TriplyDB

Activation of lecithin:cholesterol acyltransferase by HDL ApoA-I central helices.

Activation of lecithin:cholesterol acyltransferase by HDL ApoA-I central helices.

http://www.wikidata.org/entity/Q33937174

about

Structural Insights into High Density Lipoprotein: Old Models and New Facts Dysfunctional High-Density Lipoprotein: An Innovative Target for Proteomics and Lipidomics Apolipoprotein A-I and Cancer Ion-current-based proteomic profiling of the retina in a rat model of Smith-Lemli-Opitz syndrome.A robust all-atom model for LCAT generated by homology modeling.The effect of weight loss on HDL subfractions and LCAT activity in two genotypes of APOA-II -265T>C polymorphism Decreased serum apolipoprotein A1 levels are associated with poor survival and systemic inflammatory response in colorectal cancer.Conformation of dimeric apolipoprotein A-I milano on recombinant lipoprotein particles.Effect of the amyloidogenic L75P apolipoprotein A-I variant on HDL subpopulations.ApoA-I deficiency in mice is associated with redistribution of apoA-II and aggravated AApoAII amyloidosis.Apolipoprotein A-I helical structure and stability in discoidal high-density lipoprotein (HDL) particles by hydrogen exchange and mass spectrometry.High Density Lipoprotein and it's Dysfunction Binding of human apoA-I[K107del] variant to TG-rich particles: implications for mechanisms underlying hypertriglyceridemia.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/tetrafoil A Systematic Investigation of Structure/Function Requirements for the Apolipoprotein A-I/Lecithin Cholesterol Acyltransferase Interaction Loop of High-density Lipoprotein.Glycation of apoprotein A-I is associated with coronary artery plaque progression in type 2 diabetic patients.Molecules that mimic apolipoprotein A-I: potential agents for treating atherosclerosis.Solution structure of discoidal high-density lipoprotein particles with a shortened apolipoprotein A-I.Sequence-specific apolipoprotein A-I effects on lecithin:cholesterol acyltransferase activity.A retractable lid in lecithin:cholesterol acyltransferase provides a structural mechanism for activation by apolipoprotein A-I.Interaction of lecithin-cholesterol acyltransferase with lipid surfaces and apolipoprotein A-I derived peptides.

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P2860

Activation of lecithin:cholesterol acyltransferase by HDL ApoA-I central helices.

http://www.wikidata.org/entity/Q33937174

description

2009 nî lūn-bûn

@nan

2009 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年学术文章

@wuu

2009年学术文章

@zh-cn

2009年学术文章

@zh-hans

2009年学术文章

@zh-my

2009年学术文章

@zh-sg

2009年學術文章

@yue

name

Activation of lecithin:cholesterol acyltransferase by HDL ApoA-I central helices.

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Activation of lecithin:cholesterol acyltransferase by HDL ApoA-I central helices.

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type

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Activation of lecithin:cholesterol acyltransferase by HDL ApoA-I central helices.

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Activation of lecithin:cholesterol acyltransferase by HDL ApoA-I central helices.

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Activation of lecithin:cholesterol acyltransferase by HDL ApoA-I central helices.

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Activation of lecithin:cholesterol acyltransferase by HDL ApoA-I central helices.

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Clinical Lipidology

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Activation of lecithin:cholesterol acyltransferase by HDL ApoA-I central helices.

@en

P2093

Mary G Sorci-Thomas

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Michael J Thomas

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Shaila Bhat

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P2860

ApoA-I structure on discs and spheres. Variable helix registry and conformational states

Site-specific detection and structural characterization of the glycosylation of human plasma proteins lecithin:cholesterol acyltransferase and apolipoprotein D using HPLC/electrospray mass spectrometry and sequential glycosidase digestion

Crystal structure of pseudomonas aeruginosa lipase in the open conformation. The prototype for family I.1 of bacterial lipases

Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E

Crystal structure of truncated human apolipoprotein A-I suggests a lipid-bound conformation

Variations on a gene: rare and common variants in ABCA1 and their impact on HDL cholesterol levels and atherosclerosis

Apolipoprotein A-I alpha -helices 7 and 8 modulate high density lipoprotein subclass distribution

Structural and functional properties of two mutants of lecithin-cholesterol acyltransferase (T123I and N228K)

A three-dimensional molecular model of lipid-free apolipoprotein A-I determined by cross-linking/mass spectrometry and sequence threading.

Structure of spheroidal HDL particles revealed by combined atomistic and coarse-grained simulations.

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113-124

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10.2217/17584299.4.1.113

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