December 1, 1981Journal of Biological ChemistryOpen Access

Identification of three phosphorylation sites on each heavy chain of Acanthamoeba myosin II.

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Population

Acanthamoeba myosin II

Comparison

Phosphorylation by a partially purified kinase… vs Dephosphorylated or unphosphorylated myosin II

Design

Preclinical

Authors

GCGraham P. CôtéRELX Group (Netherlands)JCJohn H. CollinsDuke University EKEdward D. KornNational Institutes of Health

Discussion

Member takes

Implication

Extends myosin regulation insights in Acanthamoeba; leaves open translation to human cardiac myosin function.

Structured PICO

Population

Acanthamoeba myosin II

Intervention

Phosphorylation by a partially purified kinase preparation from Acanthamoeba

Comparator

Dephosphorylated or unphosphorylated myosin II

Outcome

Actin-activated Mg2+-ATPase activity and phosphate incorporationsurrogate

Phosphorylation of three specific sites on the heavy chain of Acanthamoeba myosin II synergistically inhibits its actin-activated Mg2+-ATPase activity.

Cite This Study

Côté et al. (1981) studied this question.

synapsesocial.com/papers/6a8a9fbad88561daf2cc23cd https://doi.org/10.1016/s0021-9258(18)42967-5

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Identification of three phosphorylation sites on each heavy chain of Acanthamoeba myosin II.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Identification of three phosphorylation sites on each heavy chain of Acanthamoeba myosin II.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider