AbstractThe binding of the MARCKS peptide to the lipid monolayer containing PIP2 increases the lateral pressure of the monolayer. The unbinding dynamics modulated by protein kinase C leads to oscillations in lateral pressure of lipid monolayers. These periodic dynamics can be attributed to changes in the crystalline lipid domain size. We have developed a mathematical model to explain these observations based on the changes in the physical structure of the monolayer by the translocation of MARCKS peptide. The model indicates that changes in lipid domain size drives these oscillations. The model is extended to an open system that sustains chemical oscillations
The relationship between lipid domains and protein kinase C activity was studied via the direct visu...
The relationship between lipid domains and protein kinase C activity was studied via the direct visu...
Despite extensive study the phase behavior of phospholipid monolayers at an air-water interface is s...
AbstractThe binding of the MARCKS peptide to the lipid monolayer containing PIP2 increases the later...
AbstractIn this present work we have studied the effect of MARCKS (151–175) peptide on a mixed DPPC/...
AbstractDirect fluorescence digital imaging microscopy observations demonstrate that a basic peptide...
AbstractThe binding of the myristoylated alanine-rich C kinase substrate (MARCKS) to mixed, fluid, p...
AbstractThe understanding of temporal pattern formation in biological systems is essential for insig...
Phosphorylation and dephosphorylation of proteins are mechanisms of activation and deactivation whic...
AbstractPositively charged polybasic domains are essential for recruiting multiple signaling protein...
Several groups have observed that phosphorylation causes the MARCKS (Myristoylated Alanine-Rich C Ki...
The spatial coincidence of lipid domains at both layers of the cell membrane is expected to play an ...
AbstractThe basic effector domain of myristoylated alanine-rich C kinase substrate (MARCKS), a major...
AbstractDirect fluorescence digital imaging microscopy observations demonstrate that a basic peptide...
AbstractAs charged macromolecules adsorb and diffuse on cell membranes in a large variety of cell si...
The relationship between lipid domains and protein kinase C activity was studied via the direct visu...
The relationship between lipid domains and protein kinase C activity was studied via the direct visu...
Despite extensive study the phase behavior of phospholipid monolayers at an air-water interface is s...
AbstractThe binding of the MARCKS peptide to the lipid monolayer containing PIP2 increases the later...
AbstractIn this present work we have studied the effect of MARCKS (151–175) peptide on a mixed DPPC/...
AbstractDirect fluorescence digital imaging microscopy observations demonstrate that a basic peptide...
AbstractThe binding of the myristoylated alanine-rich C kinase substrate (MARCKS) to mixed, fluid, p...
AbstractThe understanding of temporal pattern formation in biological systems is essential for insig...
Phosphorylation and dephosphorylation of proteins are mechanisms of activation and deactivation whic...
AbstractPositively charged polybasic domains are essential for recruiting multiple signaling protein...
Several groups have observed that phosphorylation causes the MARCKS (Myristoylated Alanine-Rich C Ki...
The spatial coincidence of lipid domains at both layers of the cell membrane is expected to play an ...
AbstractThe basic effector domain of myristoylated alanine-rich C kinase substrate (MARCKS), a major...
AbstractDirect fluorescence digital imaging microscopy observations demonstrate that a basic peptide...
AbstractAs charged macromolecules adsorb and diffuse on cell membranes in a large variety of cell si...
The relationship between lipid domains and protein kinase C activity was studied via the direct visu...
The relationship between lipid domains and protein kinase C activity was studied via the direct visu...
Despite extensive study the phase behavior of phospholipid monolayers at an air-water interface is s...