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.
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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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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).
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Authors | Title | Published | Journal | PubMed Link |
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La Rosa C et al. | Lipid-assisted protein transport: A diffusion-reaction model supported by kinetic experiments and molecular dynamics simulations. | 2016 | J Chem Phys | pmid:27179503 |
Aoun B et al. | Direct comparison of elastic incoherent neutron scattering experiments with molecular dynamics simulations of DMPC phase transitions. | 2016 | Eur Phys J E Soft Matter | pmid:27112937 |
Neumann A et al. | Membrane Sterols Modulate the Binding Mode of Amphotericin B without Affecting Its Affinity for a Lipid Bilayer. | 2016 | Langmuir | pmid:27007267 |
Palacios-Ortega J et al. | Regulation of Sticholysin II-Induced Pore Formation by Lipid Bilayer Composition, Phase State, and Interfacial Properties. | 2016 | Langmuir | pmid:27003246 |
Yang J et al. | Free energy landscapes of sodium ions bound to DMPC-cholesterol membrane surfaces at infinite dilution. | 2016 | Phys Chem Chem Phys | pmid:26967312 |
Mei X et al. | Probing the C-terminal domain of lipid-free apoA-I demonstrates the vital role of the H10B sequence repeat in HDL formation. | 2016 | J. Lipid Res. | pmid:27317763 |
Min D et al. | A simple DNA handle attachment method for single molecule mechanical manipulation experiments. | 2016 | Protein Sci. | pmid:27222403 |
Ma J et al. | Stable Small Composite Microbubbles Decorated with Magnetite Nanoparticles - A Synergistic Effect between Surfactant Molecules and Nanoparticles. | 2016 | J Oleo Sci | pmid:27087000 |
Pluhackova K et al. | A Critical Comparison of Biomembrane Force Fields: Structure and Dynamics of Model DMPC, POPC, and POPE Bilayers. | 2016 | J Phys Chem B | pmid:27035634 |
Hirst DJ et al. | The impact of cell-penetrating peptides on membrane bilayer structure during binding and insertion. | 2016 | Biochim. Biophys. Acta | pmid:27163492 |