A groundbreaking exploration of how sequence patterning, especially proline and charge distributions, governs the conformational behavior of intrinsically disordered regions (IDRs) even under multisite phosphorylation, with compensatory conformational changes maintaining overall dimensions.
A groundbreaking exploration of how sequence patterning, especially proline and charge distributions, governs the conformational behavior of intrinsically disordered regions (IDRs) even under multisite phosphorylation, with compensatory conformational changes maintaining overall dimensions.
A groundbreaking study connecting protein folding energy landscapes to functional conformational changes in signaling proteins, showing how transient, non-native hydrogen bonds lower transition barriers and facilitate activation without unfolding.
A groundbreaking study connecting protein folding energy landscapes to functional conformational changes in signaling proteins, showing how transient, non-native hydrogen bonds lower transition barriers and facilitate activation without unfolding.
Notes on 2002 Cell review discussing conformational plasticity of protein kinases, highlighting key structural elements, activation mechanisms, and pseudosubstrate regulation. Includes insights on αC helix, activation loop, and therapeutic implications (e.g., Gleevec binding).
Notes on 2002 Cell review discussing conformational plasticity of protein kinases, highlighting key structural elements, activation mechanisms, and pseudosubstrate regulation. Includes insights on αC helix, activation loop, and therapeutic implications (e.g., Gleevec binding).
Notes on a 2004 Plant Cell paper mapping Arabidopsis plasma membrane phosphoproteins and phosphorylation sites.
Notes on a 2004 Plant Cell paper mapping Arabidopsis plasma membrane phosphoproteins and phosphorylation sites.
Notes on the mechanism by which PDK1 is activated via PIP3-mediated dimerization and trans-autophosphorylation, highlighting the role of PH domain autoinhibition, linker-mediated dimerization, and switch-like activation mechanisms.
Notes on the mechanism by which PDK1 is activated via PIP3-mediated dimerization and trans-autophosphorylation, highlighting the role of PH domain autoinhibition, linker-mediated dimerization, and switch-like activation mechanisms.
