Notes on 2005 Biophysical Journal article analyzing atomistic pathways of Ca²⁺ binding to calmodulin, highlighting stepwise binding, dehydration coupling, and residue dynamics.
Notes on 2005 Biophysical Journal article analyzing atomistic pathways of Ca²⁺ binding to calmodulin, highlighting stepwise binding, dehydration coupling, and residue dynamics.
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.
Notes on a landmark Nature (1999) paper detailing how calmodulin (CaM) adopts a unique binding mode when interacting with CaMKK, revealing an extended 26-residue peptide interface and an opposite binding orientation, distinguishing it from classical CaM-target interactions — a new paradigm in calcium signaling complexes.
Notes on a landmark Nature (1999) paper detailing how calmodulin (CaM) adopts a unique binding mode when interacting with CaMKK, revealing an extended 26-residue peptide interface and an opposite binding orientation, distinguishing it from classical CaM-target interactions — a new paradigm in calcium signaling complexes.
Notes on a 2001 Journal of Molecular Biology paper revealing the crystal structure of Ca2+/CaM bound to a CaMKK-derived peptide, highlighting how calmodulin achieves conformational flexibility to accommodate diverse targets — offering a mechanistic basis for how CaM relieves autoinhibition of kinases like CaMKK and mediates calcium signal transduction.
Notes on a 2001 Journal of Molecular Biology paper revealing the crystal structure of Ca2+/CaM bound to a CaMKK-derived peptide, highlighting how calmodulin achieves conformational flexibility to accommodate diverse targets — offering a mechanistic basis for how CaM relieves autoinhibition of kinases like CaMKK and mediates calcium signal transduction.
Notes on a 2017 Scientific Reports study proposing the Calmodulin-Fused Kinase (CFK) family as the principal system for converting calcium signals to protein phosphorylation responses in plants, based on deep phylogenetic analysis tracing their evolutionary origins and functional diversification.
Notes on a 2017 Scientific Reports study proposing the Calmodulin-Fused Kinase (CFK) family as the principal system for converting calcium signals to protein phosphorylation responses in plants, based on deep phylogenetic analysis tracing their evolutionary origins and functional diversification.
A 1991 Science paper reporting the discovery of a soybean CDPK as a novel class of calcium-dependent kinases, providing structural and evolutionary insights that shaped the understanding of CDPKs as CaM-like autonomous calcium sensors.
