MeSH term | MeSH ID | Detail |
---|---|---|
Blastomycosis | D001759 | 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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Daum U et al. | Apolipoprotein A-I (R151C)Paris is defective in activation of lecithin: cholesterol acyltransferase but not in initial lipid binding, formation of reconstituted lipoproteins, or promotion of cholesterol efflux. | 1999 | J. Mol. Med. | pmid:10543393 |
Castelli F et al. | Differences between coumaric and cinnamic acids in membrane permeation as evidenced by time-dependent calorimetry. | 1999 | J. Agric. Food Chem. | pmid:10552403 |
Huebner S et al. | EDTA-induced self-assembly of cationic lipid-DNA multilayers near a monolayer-covered air-water interface. | 1999 | Biochim. Biophys. Acta | pmid:10561466 |
Yamazaki A et al. | Modification of liposomes with N-substituted polyacrylamides: identification of proteins adsorbed from plasma. | 1999 | Biochim. Biophys. Acta | pmid:10561475 |
Käsbauer M and Bayerl TM | Formation of domains of cationic or anionic lipids in binary lipid mixtures increases the electrostatic coupling strength of water-soluble proteins to supported bilayers. | 1999 | Biochemistry | pmid:10563810 |
Chen GQ and Gouaux E | Probing the folding and unfolding of wild-type and mutant forms of bacteriorhodopsin in micellar solutions: evaluation of reversible unfolding conditions. | 1999 | Biochemistry | pmid:10563824 |
Shen YM et al. | Lipid-dependent activation of protein kinase C-alpha by normal alcohols. | 1999 | J. Biol. Chem. | pmid:10567370 |
Klein-Seetharaman J et al. | NMR spectroscopy in studies of light-induced structural changes in mammalian rhodopsin: applicability of solution (19)F NMR. | 1999 | Proc. Natl. Acad. Sci. U.S.A. | pmid:10570143 |
Prosser RS et al. | Lanthanide chelates as bilayer alignment tools in NMR studies of membrane-associated peptides. | 1999 | J. Magn. Reson. | pmid:10579948 |
Gröbner G et al. | Probing membrane surfaces and the location of membrane-embedded peptides by (13)C MAS NMR using lanthanide ions. | 1999 | J. Magn. Reson. | pmid:10579957 |