H-Ras, a small G protein, can activate several downstream effectors and cause diverse effects in the cell. These effects include cell cycle and gene transcription regulation. In order to produce these effects, H-Ras must localize at the plasma membrane via three lipid modifications, although its precise location, inside or outside of detergent resistant membranes (DRMs), is still being debated. Several transmembrane Ras proteins (EHR61L, EHRwt, and CHR61L) were designed to localize to the plasma membrane in a lipid-independent manner. Both EHR proteins were found, by detergent extraction, to be located outside of DRMs. Based on this localization, the question was asked if Ras would still be able to find its proper downstream effectors. EHR6...
Plasma membrane (PM) localization of Ras proteins is crucial for transmitting signals upon mitogen s...
In PC12 cells, Ha-Ras modulates multiple effector proteins that induce neuronal differentiation. To ...
Ha-Ras undergoes post-translational modifications (including attachment of farnesyl and palmitate) t...
Ras proteins are small G proteins that play key roles in many aspect of cell signal transduction. H-...
An intriguing aspect of the cell membrane that provokes study is lipid-anchor enrichment of lipidate...
The Ras GTPases operate as molecular switches that link extracellular stimuli with a diverse range o...
H-Ras must adhere to the plasma membrane to be functional. This is accomplished by posttranslational...
Ha-Ras and Ki-Ras have different distributions across plasma membrane microdomains. The Ras C-termin...
H-Ras, N-Ras, and K-Ras proteins have distinct biological properties, despite ubiquitous expression ...
The Ras proteins (H-Ras, N-Ras and K-Ras4B) are monomeric GTP-binding proteins that play key roles i...
Membrane proteins constitute a third of all proteins in the cell and more than 50% of drug targets. ...
Ras proteins must be localized to the inner surface of the plasma membrane to be biologically active...
In the GTP bound state, Ras proteins activate multiple downstream effector proteins, the combination...
Ras GTPases were long thought to function exclusively from the plasma membrane (PM). However, a curr...
Plasma membrane (PM) localization of Ras proteins is crucial for transmitting signals upon mitogen s...
Plasma membrane (PM) localization of Ras proteins is crucial for transmitting signals upon mitogen s...
In PC12 cells, Ha-Ras modulates multiple effector proteins that induce neuronal differentiation. To ...
Ha-Ras undergoes post-translational modifications (including attachment of farnesyl and palmitate) t...
Ras proteins are small G proteins that play key roles in many aspect of cell signal transduction. H-...
An intriguing aspect of the cell membrane that provokes study is lipid-anchor enrichment of lipidate...
The Ras GTPases operate as molecular switches that link extracellular stimuli with a diverse range o...
H-Ras must adhere to the plasma membrane to be functional. This is accomplished by posttranslational...
Ha-Ras and Ki-Ras have different distributions across plasma membrane microdomains. The Ras C-termin...
H-Ras, N-Ras, and K-Ras proteins have distinct biological properties, despite ubiquitous expression ...
The Ras proteins (H-Ras, N-Ras and K-Ras4B) are monomeric GTP-binding proteins that play key roles i...
Membrane proteins constitute a third of all proteins in the cell and more than 50% of drug targets. ...
Ras proteins must be localized to the inner surface of the plasma membrane to be biologically active...
In the GTP bound state, Ras proteins activate multiple downstream effector proteins, the combination...
Ras GTPases were long thought to function exclusively from the plasma membrane (PM). However, a curr...
Plasma membrane (PM) localization of Ras proteins is crucial for transmitting signals upon mitogen s...
Plasma membrane (PM) localization of Ras proteins is crucial for transmitting signals upon mitogen s...
In PC12 cells, Ha-Ras modulates multiple effector proteins that induce neuronal differentiation. To ...
Ha-Ras undergoes post-translational modifications (including attachment of farnesyl and palmitate) t...