Aromatic residues in the C-terminal helix of human apoC-I mediate phospholipid interactions and particle morphology.
about
Chemical Synthesis and Characterization of an Equinatoxin II(1-85) Analogue.Detection of two distinct forms of apoC-I in great apes.Influence of C-terminal α-helix hydrophobicity and aromatic amino acid content on apolipoprotein A-I functionality.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.Sequence-specific apolipoprotein A-I effects on lecithin:cholesterol acyltransferase activity.Microwave Synthesis of Prion Protein Fragments up to 111 Amino Acids in Length Generates Biologically Active Peptides
P2860
Aromatic residues in the C-terminal helix of human apoC-I mediate phospholipid interactions and particle morphology.
description
2008 nî lūn-bûn
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2008年の論文
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2008年学术文章
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name
Aromatic residues in the C-ter ...... tions and particle morphology.
@en
Aromatic residues in the C-ter ...... tions and particle morphology.
@nl
type
label
Aromatic residues in the C-ter ...... tions and particle morphology.
@en
Aromatic residues in the C-ter ...... tions and particle morphology.
@nl
prefLabel
Aromatic residues in the C-ter ...... tions and particle morphology.
@en
Aromatic residues in the C-ter ...... tions and particle morphology.
@nl
P2093
P2860
P1476
Aromatic residues in the C-ter ...... ctions and particle morphology
@en
P2093
Con Dogovski
Denis B Scanlon
John A Karas
Kenneth N Goldie
Michael F Bailey
Patrick F James
Richard A J O'Hair
P2860
P304
P356
10.1194/JLR.M800529-JLR200
P577
2008-11-04T00:00:00Z