AbstractMultifunctional type II Ca2+/calmodulin-dependent protein kinase purified from rat brain cytosol was found to bind to actin filaments in vitro. The binding was saturable, and the dissociation constant for the binding was determined to be about 4 × 10−8 M. Electron microscopic observation indicated that the kinase binds to the side of actin filaments. Calmodulin inhibited the binding of the kinase to actin filaments in a Ca2+-dependent manner. The Ca2+/calmodulin-regulated binding of the kinase to actin filaments revealed here may be important for the substrate recognition of the kinase
Understanding the principles of calmodulin (CaM) activation of target enzymes will help delineate ho...
In preparations of synaptic terminals (synaptosomes) isolated from rat brain, the activity of phosph...
A calmodulin-dependent protein kinase has been purified from rat spleen. The enzyme showed a remarka...
AbstractMultifunctional type II Ca2+/calmodulin-dependent protein kinase purified from rat brain cyt...
AbstractAutophosphorylation of purified calmodulin kinase II dramatically inhibited protein kinase a...
Four monoclonal antibodies generated against the Type II CaM kinase have been characterized. Two of ...
A combination of biochemical, immunochemical, and molecular biological techniques have been employed...
A calcium and calmodulin-dependent protein kinase has been purified from rat brain. It was monitored...
AbstractCalmodulin-dependent glycogen synthase kinase from rabbit skeletal muscle and calmodulin-dep...
A calcium/calmodulin-dependent protein kinase, which phosphorylates a synaptic vesicle-associated pr...
A calcium/calmodulin-dependent protein kinase, which phosphorylates a synaptic vesicle-associated pr...
It is now well established that autophosphorylation of a threonine residue located next to each calm...
It is now well established that autophosphorylation of a threonine residue located next to each calm...
Biochemical and immunological approaches have been developed to study the regulation of the rat neur...
AbstractA new 84/82 kDa calmodulin-binding protein, which also interacts with actin filaments, tubul...
Understanding the principles of calmodulin (CaM) activation of target enzymes will help delineate ho...
In preparations of synaptic terminals (synaptosomes) isolated from rat brain, the activity of phosph...
A calmodulin-dependent protein kinase has been purified from rat spleen. The enzyme showed a remarka...
AbstractMultifunctional type II Ca2+/calmodulin-dependent protein kinase purified from rat brain cyt...
AbstractAutophosphorylation of purified calmodulin kinase II dramatically inhibited protein kinase a...
Four monoclonal antibodies generated against the Type II CaM kinase have been characterized. Two of ...
A combination of biochemical, immunochemical, and molecular biological techniques have been employed...
A calcium and calmodulin-dependent protein kinase has been purified from rat brain. It was monitored...
AbstractCalmodulin-dependent glycogen synthase kinase from rabbit skeletal muscle and calmodulin-dep...
A calcium/calmodulin-dependent protein kinase, which phosphorylates a synaptic vesicle-associated pr...
A calcium/calmodulin-dependent protein kinase, which phosphorylates a synaptic vesicle-associated pr...
It is now well established that autophosphorylation of a threonine residue located next to each calm...
It is now well established that autophosphorylation of a threonine residue located next to each calm...
Biochemical and immunological approaches have been developed to study the regulation of the rat neur...
AbstractA new 84/82 kDa calmodulin-binding protein, which also interacts with actin filaments, tubul...
Understanding the principles of calmodulin (CaM) activation of target enzymes will help delineate ho...
In preparations of synaptic terminals (synaptosomes) isolated from rat brain, the activity of phosph...
A calmodulin-dependent protein kinase has been purified from rat spleen. The enzyme showed a remarka...