DMPG

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.

References related to lipids published in Biochim. Biophys. Acta


PMIDJournalPublished DateAuthorTitle
27163492Biochim. Biophys. Acta2016Hirst DJ et al.The impact of cell-penetrating peptides on membrane bilayer structure during binding and insertion.
25511587Biochim. Biophys. Acta2015Beck Z et al.Detection of liposomal cholesterol and monophosphoryl lipid A by QS-21 saponin and Limulus polyphemus amebocyte lysate.
27475297Biochim. Biophys. Acta2016Almeida C et al.Membrane re-arrangements and rippled phase stabilisation by the cell penetrating peptide penetratin.
27425030Biochim. Biophys. Acta2016Agopian A et al.Structure and interaction with lipid membrane models of Semliki Forest virus fusion peptide.
25843678Biochim. Biophys. Acta2015Wrobel D et al.Interaction study between maltose-modified PPI dendrimers and lipidic model membranes.
25511586Biochim. Biophys. Acta2015Misiewicz J et al.Control and role of pH in peptide-lipid interactions in oriented membrane samples.
25497765Biochim. Biophys. Acta2015Bodor A et al.Membrane interactions in small fast-tumbling bicelles as studied by 31P NMR.
25450807Biochim. Biophys. Acta2015Joshi T et al.Real-time examination of aminoglycoside activity towards bacterial mimetic membranes using Quartz Crystal Microbalance with Dissipation monitoring (QCM-D).
25433311Biochim. Biophys. Acta2015Ding Y et al.Influence of the lipid membrane environment on structure and activity of the outer membrane protein Ail from Yersinia pestis.