18194-24-6

18194-24-6 is a lipid of Glycerophospholipids (GP) class. 18194-24-6 is associated with abnormalities such as Cerebrovascular accident, Renal tubular disorder, Atherosclerosis, Hyperlipoproteinemia Type III and Lipid Metabolism Disorders. The involved functions are known as Process, protein folding, Catalyst, Biochemical Pathway and Fold in Medical Device Material. 18194-24-6 often locates in Tissue membrane, Membrane, periplasm, vesicle membrane and outer membrane. The associated genes with 18194-24-6 are Integral Membrane Proteins, Protein Structure, RTN4 gene, RTN4R gene and Protein, Organized by Structure. The related lipids are Micelles, dimyristoylphosphatidylglycerol, 1,2-dihexadecyl-sn-glycero-3-phosphocholine, Unilamellar Vesicles and cholesteryl oleate. The related experimental models are Mouse Model, Arthritis, Adjuvant-Induced, Disease model and Xenograft Model.

References related to lipids published in J. Biol. Chem.

PMID	Journal	Published Date	Author	Title
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10419496	J. Biol. Chem.	1999	Weers PM et al.	Interaction of an exchangeable apolipoprotein with phospholipid vesicles and lipoprotein particles. Role of leucines 32, 34, and 95 in Locusta migratoria apolipophorin III.
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18845546	J. Biol. Chem.	2008	Mishra VK et al.	Effect of leucine to phenylalanine substitution on the nonpolar face of a class A amphipathic helical peptide on its interaction with lipid: high resolution solution NMR studies of 4F-dimyristoylphosphatidylcholine discoidal complex.
15485851	J. Biol. Chem.	2004	Bender V et al.	T cell antigen receptor peptide-lipid membrane interactions using surface plasmon resonance.
16877761	J. Biol. Chem.	2006	Tremouilhac P et al.	Synergistic transmembrane alignment of the antimicrobial heterodimer PGLa/magainin.
16159879	J. Biol. Chem.	2005	Pearson K et al.	Specific sequences in the N and C termini of apolipoprotein A-IV modulate its conformation and lipid association.
25398882	J. Biol. Chem.	2015	Smrt ST et al.	The influenza hemagglutinin fusion domain is an amphipathic helical hairpin that functions by inducing membrane curvature.