MeSH term | MeSH ID | Detail |
---|---|---|
Alzheimer Disease | D000544 | 76 associated lipids |
Adenocarcinoma | D000230 | 166 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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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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Seetharam B et al. | Membrane interactions of rat intestinal alkaline phosphatase: role of polar head groups. | 1985 | Biochemistry | pmid:4084543 |
Kouaouci R et al. | Calcium-induced lateral phase separations in phosphatidylcholine-phosphatidic acid mixtures. A Raman spectroscopic study. | 1985 | Biochemistry | pmid:4084568 |
Surewicz WK and Epand RM | Role of peptide structure in lipid-peptide interactions: a fluorescence study of the binding of pentagastrin-related pentapeptides to phospholipid vesicles. | 1984 | Biochemistry | pmid:6525344 |
Post JF et al. | Fluorine-19 nuclear magnetic resonance investigation of fluorine-19-labeled phospholipids. 1. A multiple-pulse study. | 1984 | Biochemistry | pmid:6525352 |
Losonczi JA and Prestegard JH | Nuclear magnetic resonance characterization of the myristoylated, N-terminal fragment of ADP-ribosylation factor 1 in a magnetically oriented membrane array. | 1998 | Biochemistry | pmid:9425095 |
Mims MP and Morrisett JD | Lipolysis of phospholipids in model cholesteryl ester rich lipoproteins and related systems: effect of core and surface lipid phase state. | 1988 | Biochemistry | pmid:3167047 |
Hinderliter AK et al. | Activation of protein kinase C by coexisting diacylglycerol-enriched and diacylglycerol-poor lipid domains. | 1997 | Biochemistry | pmid:9166785 |
Yowler BC and Schengrund CL | Botulinum neurotoxin A changes conformation upon binding to ganglioside GT1b. | 2004 | Biochemistry | pmid:15274627 |
Burke TG and Tritton TR | Location and dynamics of anthracyclines bound to unilamellar phosphatidylcholine vesicles. | 1985 | Biochemistry | pmid:3866609 |
Berclaz T and McConnell HM | Phase Equilibria in binary mixtures of dimyristoylphosphatidylcholine and cardiolipin. | 1981 | Biochemistry | pmid:6272842 |
Papadopoulos E et al. | NMR solution structure of the peptide fragment 1-30, derived from unprocessed mouse Doppel protein, in DHPC micelles. | 2006 | Biochemistry | pmid:16388591 |
Short KW et al. | Comparison of lipid/gramicidin dispersions and cocrystals by Raman scattering. | 1987 | Biochemistry | pmid:2435320 |
Mao D et al. | Folding of the mitochondrial proton adenosinetriphosphatase proteolipid channel in phospholipid vesicles. | 1982 | Biochemistry | pmid:6291595 |
Dempsey CE and Watts A | A deuterium and phosphorus-31 nuclear magnetic resonance study of the interaction of melittin with dimyristoylphosphatidylcholine bilayers and the effects of contaminating phospholipase A2. | 1987 | Biochemistry | pmid:3676290 |
Ollmann M et al. | Pyrene-labeled gangliosides: micelle formation in aqueous solution, lateral diffusion, and thermotropic behavior in phosphatidylcholine bilayers. | 1987 | Biochemistry | pmid:3676298 |
Riley ML et al. | Slow alpha helix formation during folding of a membrane protein. | 1997 | Biochemistry | pmid:8993333 |
Booth PJ et al. | Evidence that bilayer bending rigidity affects membrane protein folding. | 1997 | Biochemistry | pmid:8993334 |
Sugihara T et al. | Hydrophobic oligopeptides in solution and in phospholipid vesicles: synthetic fragments of bacteriorhodopsin. | 1982 | Biochemistry | pmid:7115678 |
Macdonald PM et al. | Response of phosphatidylcholine in the gel and liquid-crystalline states to membrane surface charges. | 1991 | Biochemistry | pmid:2012813 |
Pownall H et al. | Kinetics and mechanism of association of human plasma apolipoproteins with dimyristoylphosphatidylcholine: effect of protein structure and lipid clusters on reaction rates. | 1981 | Biochemistry | pmid:7306528 |