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 |
---|
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 |
---|
Function | Cross reference | Weighted score | Related literatures |
---|
Lipid concept | Cross reference | Weighted score | Related literatures |
---|
Gene | Cross reference | Weighted score | Related literatures |
---|
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 |
---|
Authors | Title | Published | Journal | PubMed Link |
---|---|---|---|---|
Helm CA et al. | Role of hydrophobic forces in bilayer adhesion and fusion. | 1992 | Biochemistry | pmid:1737032 |
Sankaram MB et al. | Interaction of carrier ionophores with phospholipid vesicles. | 1987 | Biochemistry | pmid:3117109 |
Sparrow JT et al. | Apolipoprotein E: phospholipid binding studies with synthetic peptides from the carboxyl terminus. | 1992 | Biochemistry | pmid:1734956 |
Weisz K et al. | Deuteron nuclear magnetic resonance study of the dynamic organization of phospholipid/cholesterol bilayer membranes: molecular properties and viscoelastic behavior. | 1992 | Biochemistry | pmid:1734959 |
Dluhy RA et al. | Interaction of dipalmitoylphosphatidylcholine and dimyristoylphosphatidylcholine-d54 mixtures with glycophorin. A fourier transform infrared investigation. | 1983 | Biochemistry | pmid:6687692 |
Elamrani K and Blume A | Incorporation kinetics of lysolecithin into lecithin vesicles. Kinetics of lysolecithin-induced vesicle fusion. | 1982 | Biochemistry | pmid:6896001 |
Pink DA et al. | Intrinsic proteins and their effect upon lipid hydrocarbon chain order. | 1981 | Biochemistry | pmid:6172147 |
Jacobs RE and White SH | Mixtures of a series of homologous hydrophobic peptides with lipid bilayers: a simple model system for examining the protein-lipid interface. | 1986 | Biochemistry | pmid:3718968 |
Lewis RN et al. | Fourier transform infrared spectroscopic study of the interactions of a strongly antimicrobial but weakly hemolytic analogue of gramicidin S with lipid micelles and lipid bilayer membranes. | 2003 | Biochemistry | pmid:12525171 |
Eklund KK et al. | Role of the polar head group stereoconfiguration in the cation-induced aggregation of dimyristoylphosphatidylglycerol vesicles. | 1987 | Biochemistry | pmid:3427093 |
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 |
Erb EM et al. | Integrin alphaIIb beta3 reconstituted into lipid bilayers is nonclustered in its activated state but clusters after fibrinogen binding. | 1997 | Biochemistry | pmid:9200686 |
Grosse W et al. | Structure-based engineering of a minimal porin reveals loop-independent channel closure. | 2014 | Biochemistry | pmid:24988371 |
Weers PM et al. | Factors affecting the stability and conformation of Locusta migratoria apolipophorin III. | 1994 | Biochemistry | pmid:8142360 |
Wimley WC and Thompson TE | Transbilayer and interbilayer phospholipid exchange in dimyristoylphosphatidylcholine/dimyristoylphosphatidylethanolamine large unilamellar vesicles. | 1991 | Biochemistry | pmid:1993185 |
Arêas JA et al. | Interaction of a type II myosin with biological membranes studied by 2H solid state NMR. | 1998 | Biochemistry | pmid:9548943 |
Struppe J et al. | 2H NMR studies of a myristoylated peptide in neutral and acidic phospholipid bicelles. | 1998 | Biochemistry | pmid:9799515 |
van der Wel PC et al. | Orientation and motion of tryptophan interfacial anchors in membrane-spanning peptides. | 2007 | Biochemistry | pmid:17530863 |
Beleznay Z et al. | ATP-dependent aminophospholipid translocation in erythrocyte vesicles: stoichiometry of transport. | 1993 | Biochemistry | pmid:8457575 |
Mitchell DC et al. | Rhodopsin in dimyristoylphosphatidylcholine-reconstituted bilayers forms metarhodopsin II and activates Gt. | 1991 | Biochemistry | pmid:1899020 |