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.
Notes on a 1992 Science paper introducing the concept of ‘calmodulin trapping’ by CaMKII via Thr286 autophosphorylation, establishing a mechanism for potentiating and decoding transient calcium signals through enhanced CaM binding.
Notes on a 1992 Science paper introducing the concept of ‘calmodulin trapping’ by CaMKII via Thr286 autophosphorylation, establishing a mechanism for potentiating and decoding transient calcium signals through enhanced CaM binding.
A 2006 JMB study presenting the crystal structure of Arabidopsis CDPK’s regulatory domain, revealing a domain-swapped dimer and an unexpected mechanism of calmodulin-like domain (CaM-LD) recognition, challenging classical calmodulin-target models.
A 2006 JMB study presenting the crystal structure of Arabidopsis CDPK’s regulatory domain, revealing a domain-swapped dimer and an unexpected mechanism of calmodulin-like domain (CaM-LD) recognition, challenging classical calmodulin-target models.
Note on the seminal 1994 paper unveiling calmodulin’s dual role in CaMKII autophosphorylation and proposing a model for calcium frequency decoding in neurons. Includes reflections on CDPK parallels and a comparative framework for calcium signaling kinases.
Note on the seminal 1994 paper unveiling calmodulin’s dual role in CaMKII autophosphorylation and proposing a model for calcium frequency decoding in neurons. Includes reflections on CDPK parallels and a comparative framework for calcium signaling kinases.
Notes on a 1996 Biochemistry paper revealing that activation of CDPK involves intramolecular binding between its calmodulin-like domain (CaM-LD) and junction/autoinhibitor, offering deep insights into Ca2+-regulated protein kinase activation.
Notes on a 1996 Biochemistry paper revealing that activation of CDPK involves intramolecular binding between its calmodulin-like domain (CaM-LD) and junction/autoinhibitor, offering deep insights into Ca2+-regulated protein kinase activation.
