An elegant dissection of how EGFR activation depends on conformational coupling across the plasma membrane, revealing that ligand binding, transmembrane helix dimerization, and juxtamembrane interactions are essential to overcoming membrane-imposed inhibition and stabilizing the active kinase dimer.
A deep dive into the molecular dynamics and membrane interaction of EGFR, revealing distinct active and inactive conformations, the role of lipid environment, and subtle structural regulation.
A deep dive into the molecular dynamics and membrane interaction of EGFR, revealing distinct active and inactive conformations, the role of lipid environment, and subtle structural regulation.
An in-depth study of EGFR activation focusing on transmembrane and juxtamembrane coupling, density-dependent activation, and the role of the plasma membrane in maintaining autoinhibition.
An in-depth study of EGFR activation focusing on transmembrane and juxtamembrane coupling, density-dependent activation, and the role of the plasma membrane in maintaining autoinhibition.
A study demonstrating that EGFR activation is not tightly coupled to specific transmembrane dimerization interfaces, suggesting a loose linkage between extracellular ligand binding and intracellular kinase activation.
A study demonstrating that EGFR activation is not tightly coupled to specific transmembrane dimerization interfaces, suggesting a loose linkage between extracellular ligand binding and intracellular kinase activation.
Notes on the 2023 eLife review analyzing protein kinase activation loop autophosphorylation. Discusses cis vs. trans mechanisms, dimerization, regulation, and the biochemical, structural, and kinetic evidence for these processes, while addressing the enigmatic nature of autophosphorylation.
Notes on the 2023 eLife review analyzing protein kinase activation loop autophosphorylation. Discusses cis vs. trans mechanisms, dimerization, regulation, and the biochemical, structural, and kinetic evidence for these processes, while addressing the enigmatic nature of autophosphorylation.
