Apolipoprotein C-I binds more strongly to phospholipid/triolein/water than triolein/water interfaces: a possible model for inhibiting cholesterol ester transfer protein activity and triacylglycerol-rich lipoprotein uptake.
about
The biophysics and cell biology of lipid dropletsTestosterone replacement in hypogonadal men alters the HDL proteome but not HDL cholesterol efflux capacityChanges in helical content or net charge of apolipoprotein C-I alter its affinity for lipid/water interfaces.Apolipoproteins C-I and C-III inhibit lipoprotein lipase activity by displacement of the enzyme from lipid droplets.Surface behavior of apolipoprotein A-I and its deletion mutants at model lipoprotein interfaces.The potential of cholesteryl ester transfer protein as a therapeutic target.A Pressure-dependent Model for the Regulation of Lipoprotein Lipase by Apolipoprotein C-II.Interfacial properties of high-density lipoprotein-like lipid droplets with different lipid and apolipoprotein A-I compositions.Mechanism and Determinants of Amphipathic Helix-Containing Protein Targeting to Lipid Droplets.
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P2860
Apolipoprotein C-I binds more strongly to phospholipid/triolein/water than triolein/water interfaces: a possible model for inhibiting cholesterol ester transfer protein activity and triacylglycerol-rich lipoprotein uptake.
description
2012 nî lūn-bûn
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2012年の論文
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2012年論文
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2012年論文
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2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
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2012年论文
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name
Apolipoprotein C-I binds more ...... cerol-rich lipoprotein uptake.
@en
Apolipoprotein C-I binds more ...... cerol-rich lipoprotein uptake.
@nl
type
label
Apolipoprotein C-I binds more ...... cerol-rich lipoprotein uptake.
@en
Apolipoprotein C-I binds more ...... cerol-rich lipoprotein uptake.
@nl
prefLabel
Apolipoprotein C-I binds more ...... cerol-rich lipoprotein uptake.
@en
Apolipoprotein C-I binds more ...... cerol-rich lipoprotein uptake.
@nl
P2093
P2860
P356
P1433
P1476
Apolipoprotein C-I binds more ...... cerol-rich lipoprotein uptake.
@en
P2093
Donald M Small
Nathan L Meyers
P2860
P304
P356
10.1021/BI2015212
P407
P577
2012-02-02T00:00:00Z