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Myosin VI has a short lever-arm with a single IQ motif that binds calmodulin but very little is known about how calcium binding to this calmodulin affects the structure and intracellular functions of the myosin.
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This type of dynamic modulation was also observed for Ca2+ binding to calmodulin, where this effect was dubbed entropy compensation (Lee et al., 2000).
Increase in cytosolic Ca2+ directly activates the GP-phosphorylating enzyme phosphorylase kinase (PK) by binding to its calmodulin subunit.
Zinc inhibits calmodulin by competing with Ca2+ binding to calmodulin, which has also resulted in a conformational change of the protein [ 40- 43].
At higher values of this rate constant of autophosphorylation, however, the calmodulin affinity to CaMKII becomes a more important parameter as binding to calmodulin needs to occur before CaMKII autophosphorylation can take place [ 15].
Activation of MLCK depends on cytosolic calcium (Ca2+) binding to calmodulin.
The shorter sequence possesses better binding to calmodulin, which is encouraging in terms of the development of non-peptide analogues as therapeutic agents.
After binding to calmodulin, ACT AC raises the intracellular cAMP concentration in host cells cAMP to a pathological level [8], [9].
GAPA contains a putative IQ motif that can mediate binding to calmodulin as in IQGAP1, allowing that Ca2+ affects GAPA functions in actin remodeling.
Ca Zn binding to calmodulin 12.5.
The precise mechanisms underlying calcium binding to calmodulin are still, however, quite poorly understood.
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