MeSH term | MeSH ID | Detail |
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Lung Neoplasms | D008175 | 171 associated lipids |
Body Weight | D001835 | 333 associated lipids |
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.
To understand associated biological information of 18194-24-6, we collected biological information of abnormalities, associated pathways, cellular/molecular locations, biological functions, related genes/proteins, lipids and common seen animal/experimental models with organized paragraphs from literatures.
18194-24-6 is suspected in Atherosclerosis, Cardiovascular Diseases, Dehydration, Abnormal shape, Renal tubular disorder, Hyperlipoproteinemia Type III and other diseases in descending order of the highest number of associated sentences.
Disease | Cross reference | Weighted score | Related literature |
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We collected disease MeSH terms mapped to the references associated with 18194-24-6
There are no associated biomedical information in the current reference collection.
Associated locations are in red color. Not associated locations are in black.
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Function | Cross reference | Weighted score | Related literatures |
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Lipid concept | Cross reference | Weighted score | Related literatures |
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Gene | Cross reference | Weighted score | Related literatures |
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Mouse Model are used in the study 'Association of a model class A (apolipoprotein) amphipathic alpha helical peptide with lipid: high resolution NMR studies of peptide.lipid discoidal complexes.' (Mishra VK et al., 2006).
Arthritis, Adjuvant-Induced are used in the study 'T cell antigen receptor peptide-lipid membrane interactions using surface plasmon resonance.' (Bender V et al., 2004).
Disease model are used in the study 'Kupffer cells do not play a role in governing the efficacy of liposomal mitoxantrone used to treat a tumor model designed to assess drug delivery to liver.' (Lim HJ et al., 2000).
Model | Cross reference | Weighted score | Related literatures |
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Authors | Title | Published | Journal | PubMed Link |
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de Jong K et al. | Phospholipid asymmetry in red blood cells and spectrin-free vesicles during prolonged storage. | 1996 | Biochim. Biophys. Acta | pmid:8652596 |
Nabet A et al. | Study by infrared spectroscopy of the interdigitation of C26:0 cerebroside sulfate into phosphatidylcholine bilayers. | 1996 | Biochemistry | pmid:8639617 |
Cajal Y et al. | Specificity for the exchange of phospholipids through polymyxin B mediated intermembrane molecular contacts. | 1996 | Biochemistry | pmid:8639528 |
pmid:8639231 | ||||
Woolf TB and Roux B | Structure, energetics, and dynamics of lipid-protein interactions: A molecular dynamics study of the gramicidin A channel in a DMPC bilayer. | 1996 | Proteins | pmid:8628736 |
Mason RP et al. | Molecular membrane interactions of a phospholipid metabolite. Implications for Alzheimer's disease pathophysiology. | 1996 | Ann. N. Y. Acad. Sci. | pmid:8624114 |
Schorn K and Marsh D | Lipid chain dynamics and molecular location of diacylglycerol in hydrated binary mixtures with phosphatidylcholine: spin label ESR studies. | 1996 | Biochemistry | pmid:8620006 |
Thomas JL et al. | Kinetics of membrane micellization by the hydrophobic polyelectrolyte poly(2-ethylacrylic acid). | 1996 | Biochim. Biophys. Acta | pmid:8611610 |
Wisniewska A et al. | Depth dependence of the perturbing effect of placing a bulky group (oxazolidine ring spin labels) in the membrane on the membrane phase transition. | 1996 | Biochim. Biophys. Acta | pmid:8611609 |
Semple SC et al. | Influence of cholesterol on the association of plasma proteins with liposomes. | 1996 | Biochemistry | pmid:8611555 |
Xiang TX and Anderson BD | Phospholipid surface density determines the partitioning and permeability of acetic acid in DMPC:cholesterol bilayers. | 1995 | J. Membr. Biol. | pmid:8606364 |
Warner DR et al. | Cell-free synthesis of functional type IV adenylyl cyclase. | 1995 | Anal. Biochem. | pmid:8600828 |
Axelsen PH et al. | The infrared dichroism of transmembrane helical polypeptides. | 1995 | Biophys. J. | pmid:8599683 |
North CL et al. | Membrane orientation of the N-terminal segment of alamethicin determined by solid-state 15N NMR. | 1995 | Biophys. J. | pmid:8599645 |
Matsumoto Y et al. | Specific hybrid liposomes composed of phosphatidylcholine and polyoxyethylenealkyl ether with markedly enhanced inhibitory effects on the growth of tumor cells in vitro. | 1995 | Biol. Pharm. Bull. | pmid:8593457 |
Milhaud J et al. | Association of polyene antibiotics with sterol-free lipid membranes: I. Hydrophobic binding of filipin to dimyristoylphosphatidylcholine bilayers. | 1996 | Biochim. Biophys. Acta | pmid:8593280 |
Xiang TX and Anderson BD | Development of a combined NMR paramagnetic ion-induced line-broadening/dynamic light scattering method for permeability measurements across lipid bilayer membranes. | 1995 | J Pharm Sci | pmid:8587048 |
Warriner HE et al. | Lamellar biogels: fluid-membrane-based hydrogels containing polymer lipids. | 1996 | Science | pmid:8584932 |
Bradrick TD et al. | Stopped-flow fluorometric study of the interaction of melittin with phospholipid bilayers: importance of the physical state of the bilayer and the acyl chain length. | 1995 | Biophys. J. | pmid:8580343 |
Bouchard M et al. | High-speed magic angle spinning solid-state 1H nuclear magnetic resonance study of the conformation of gramicidin A in lipid bilayers. | 1995 | Biophys. J. | pmid:8580336 |