MeSH term | MeSH ID | Detail |
---|---|---|
Anemia, Hemolytic, Congenital | D000745 | 5 associated lipids |
Lymphoma, Primary Effusion | D054685 | 2 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.
Location | Cross reference | Weighted score | Related literatures |
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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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Watts A | Magnetic resonance studies of lipid-protein interfaces and lipophilic molecule partitioning. | 1991 | Ann. N. Y. Acad. Sci. | pmid:1647741 |
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Van Gorkom LC et al. | Identification of trapped and boundary lipid binding sites in M13 coat protein/lipid complexes by deuterium NMR spectroscopy. | 1990 | Biochemistry | pmid:2354153 |
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Zakim D and Wong PT | A high-pressure, infrared spectroscopic study of the solvation of bilirubin in lipid bilayers. | 1990 | Biochemistry | pmid:2328234 |
Dong LM et al. | Enhanced binding activity of an apolipoprotein E mutant, APO E5, to LDL receptors on human fibroblasts. | 1990 | Biochem. Biophys. Res. Commun. | pmid:2334412 |
Grainger DW et al. | Hydrolytic action of phospholipase A2 in monolayers in the phase transition region: direct observation of enzyme domain formation using fluorescence microscopy. | 1990 | Biochim. Biophys. Acta | pmid:2334729 |
Gruszecki WI and Sielewiesiuk J | Orientation of xanthophylls in phosphatidylcholine multibilayers. | 1990 | Biochim. Biophys. Acta | pmid:2334732 |
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Light WR and Olson JS | Transmembrane movement of heme. | 1990 | J. Biol. Chem. | pmid:2394740 |
Light WR and Olson JS | The effects of lipid composition on the rate and extent of heme binding to membranes. | 1990 | J. Biol. Chem. | pmid:2394741 |
Tendian SW and Lentz BR | Evaluation of membrane phase behavior as a tool to detect extrinsic protein-induced domain formation: binding of prothrombin to phosphatidylserine/phosphatidylcholine vesicles. | 1990 | Biochemistry | pmid:2397210 |
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