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.
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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Cascio M and Wallace BA | Conformation of alamethicin in phospholipid vesicles: implications for insertion models. | 1988 | Proteins | pmid:3227017 |
Venkatachalapathi YV et al. | Effect of end group blockage on the properties of a class A amphipathic helical peptide. | 1993 | Proteins | pmid:8460106 |
Veldkamp CT et al. | Monomeric structure of the cardioprotective chemokine SDF-1/CXCL12. | 2009 | Protein Sci. | pmid:19551879 |
Páli T et al. | Stoichiometry of lipid interactions with transmembrane proteins--Deduced from the 3D structures. | 2006 | Protein Sci. | pmid:16641489 |
Shin I et al. | Interaction of partially unfolded forms of Torpedo acetylcholinesterase with liposomes. | 1996 | Protein Sci. | pmid:8771195 |
Min D et al. | A simple DNA handle attachment method for single molecule mechanical manipulation experiments. | 2016 | Protein Sci. | pmid:27222403 |
Gan SW et al. | The transmembrane homotrimer of ADAM 1 in model lipid bilayers. | 2007 | Protein Sci. | pmid:17189481 |
Faham S et al. | Crystallization of bacteriorhodopsin from bicelle formulations at room temperature. | 2005 | Protein Sci. | pmid:15689517 |
Kun H and Mastai Y | Isothermal calorimetry study of the interactions of type I antifreeze proteins with a lipid model membrane. | 2010 | Protein Pept. Lett. | pmid:19995337 |
Watanabe L et al. | Initiating structural studies of Lys49-PLA2 homologues complexed with an anionic detergent, a fatty acid and a natural lipid. | 2003 | Protein Pept. Lett. | pmid:14561144 |
Prakash P and Sankararamakrishnan R | Molecular dynamics simulations of C-terminal decapeptide of gastrin-releasing peptide in DMPC bilayers: structure, stability and orientation of the peptide hormone within the bilayers. | 2007 | Protein Pept. Lett. | pmid:17627601 |
Pillot T et al. | Single-step purification of two functional human apolipoprotein E variants hyperexpressed in Escherichia coli. | 1996 | Protein Expr. Purif. | pmid:8776760 |
Yumen I et al. | Purification, characterization and reconstitution into membranes of the oligomeric c-subunit ring of thermophilic F(o)F(1)-ATP synthase expressed in Escherichia coli. | 2012 | Protein Expr. Purif. | pmid:22381465 |
Powers JD et al. | Purification of avidin from egg whites using affinity-modified unilamellar vesicles. | 1989 | Prog. Clin. Biol. Res. | pmid:2726906 |
Baldwin RL et al. | Structural changes of tumor necrosis factor alpha associated with membrane insertion and channel formation. | 1996 | Proc. Natl. Acad. Sci. U.S.A. | pmid:8577707 |
Szleifer I et al. | Spontaneous liposome formation induced by grafted poly(ethylene oxide) layers: theoretical prediction and experimental verification. | 1998 | Proc. Natl. Acad. Sci. U.S.A. | pmid:9448280 |
Chang YC and Bowie JU | Measuring membrane protein stability under native conditions. | 2014 | Proc. Natl. Acad. Sci. U.S.A. | pmid:24367094 |
MacDonald RC and Simon SA | Lipid monolayer states and their relationships to bilayers. | 1987 | Proc. Natl. Acad. Sci. U.S.A. | pmid:3473494 |
Prosser RS et al. | Using O2 to probe membrane immersion depth by 19F NMR. | 2000 | Proc. Natl. Acad. Sci. U.S.A. | pmid:10954744 |
Spector MS et al. | Chiral molecular self-assembly of phospholipid tubules: a circular dichroism study. | 1996 | Proc. Natl. Acad. Sci. U.S.A. | pmid:8917523 |