DMPG is a lipid of Glycerophospholipids (GP) class. Dmpg is associated with abnormalities such as Infection, Malaria, Dehydration, Gigantism and Abnormal shape. The involved functions are known as Signal Transduction, Binding (Molecular Function), inhibitors, Agent and Light Scattering. Dmpg often locates in Membrane, integral to membrane, Blood, Protoplasm and Face. The associated genes with DMPG are synthetic peptide, Amino Acids, Basic, Homologous Gene, Integral Membrane Proteins and penetratin. The related lipids are Lipopolysaccharides, dimyristoylphosphatidylglycerol, Micelles, Fatty Acids and Liposomes.
To understand associated biological information of DMPG, 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.
DMPG is suspected in Dehydration, Abnormal shape, Influenza, Infection, Malaria, Gigantism 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 DMPG
| MeSH term | MeSH ID | Detail |
|---|---|---|
| Hemolysis | D006461 | 131 associated lipids |
| Neurotoxicity Syndromes | D020258 | 34 associated lipids |
| Mycoses | D009181 | 18 associated lipids |
| Lymphoma, Large B-Cell, Diffuse | D016403 | 13 associated lipids |
| Hypocalcemia | D006996 | 12 associated lipids |
| Malignant Hyperthermia | D008305 | 6 associated lipids |
| Blastomycosis | D001759 | 5 associated lipids |
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 |
|---|
There are no associated biomedical information in the current reference collection.
| Authors | Title | Published | Journal | PubMed Link |
|---|---|---|---|---|
| Swenson CE et al. | In vitro and in vivo antifungal activity of amphotericin B lipid complex: are phospholipases important? | 1998 | Antimicrob. Agents Chemother. | pmid:9559780 |
| Arêas JA et al. | Interaction of a type II myosin with biological membranes studied by 2H solid state NMR. | 1998 | Biochemistry | pmid:9548943 |
| Magez S et al. | The glycosyl-inositol-phosphate and dimyristoylglycerol moieties of the glycosylphosphatidylinositol anchor of the trypanosome variant-specific surface glycoprotein are distinct macrophage-activating factors. | 1998 | J. Immunol. | pmid:9469458 |
| Pedrós J et al. | A fluorescence spectroscopy study of the interaction of monocationic quinine with phospholipid vesicles. Effect of the ionic strength and lipid composition. | 1997 | Spectrochim Acta A Mol Biomol Spectrosc | pmid:9437875 |
| Biaggi MH et al. | Melanotropic peptides-lipid bilayer interaction. Comparison of the hormone alpha-MSH to a biologically more potent analog. | 1997 | Biophys. Chem. | pmid:9397523 |
| Kleinschmidt JH and Marsh D | Spin-label electron spin resonance studies on the interactions of lysine peptides with phospholipid membranes. | 1997 | Biophys. J. | pmid:9370448 |
| Sodano P et al. | 1H NMR and fluorescence studies of the complexation of DMPG by wheat non-specific lipid transfer protein. Global fold of the complex. | 1997 | FEBS Lett. | pmid:9369197 |
| Stevanato R et al. | Interaction of spermine with dimyristoyl-L-alpha-phosphatidyl-DL-glycerol multilamellar liposomes. | 1997 | Arch. Biochem. Biophys. | pmid:9343367 |
| Borbat PP et al. | Multifrequency two-dimensional Fourier transform ESR: an X/Ku-band spectrometer. | 1997 | J. Magn. Reson. | pmid:9281479 |
| Wiese A et al. | Mechanisms of action of the bactericidal/permeability-increasing protein BPI on endotoxin and phospholipid monolayers and aggregates. | 1997 | Biochemistry | pmid:9254629 |