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.
Notes on a 2002 JBC review dissecting CaMKII’s structure-function relationship, covering autoinhibition, isoform diversity, holoenzyme assembly, autophosphorylation, subunit exchange, and Ca2+/CaM frequency decoding — a foundational reference for understanding this multifunctional kinase as a calcium signal integrator.
Notes on a 2002 JBC review dissecting CaMKII’s structure-function relationship, covering autoinhibition, isoform diversity, holoenzyme assembly, autophosphorylation, subunit exchange, and Ca2+/CaM frequency decoding — a foundational reference for understanding this multifunctional kinase as a calcium signal integrator.
Notes on a 2000 JBC paper dissecting the autoinhibitory mechanism of CaMKK, identifying Ile441 as critical for maintaining the inactive state, and showing that CaM-binding peptide orientation does not dictate relief from autoinhibition — a pivotal insight into CaMKK regulation.
Notes on a 2000 JBC paper dissecting the autoinhibitory mechanism of CaMKK, identifying Ile441 as critical for maintaining the inactive state, and showing that CaM-binding peptide orientation does not dictate relief from autoinhibition — a pivotal insight into CaMKK regulation.
Notes on a 2005 Cell paper revealing the crystal structure of autoinhibited CaMKII kinase domain and small-angle X-ray scattering (SAXS) analysis of the full holoenzyme, uncovering mechanisms for tight autoinhibition and explaining frequency-dependent activation.
Notes on a 2005 Cell paper revealing the crystal structure of autoinhibited CaMKII kinase domain and small-angle X-ray scattering (SAXS) analysis of the full holoenzyme, uncovering mechanisms for tight autoinhibition and explaining frequency-dependent activation.
Notes on a 2011 Cell paper that reveals the full-length crystal structure of human CaMKII in its autoinhibited state and introduces a tunable mechanism for calcium signal decoding based on linker length-dependent conformational dynamics.
Notes on a 2011 Cell paper that reveals the full-length crystal structure of human CaMKII in its autoinhibited state and introduces a tunable mechanism for calcium signal decoding based on linker length-dependent conformational dynamics.
