July 1, 1985Biochemistry

Limited proteolysis of smooth muscle myosin light chain kinase

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Population

Smooth muscle myosin light chain kinase (phosphorylated and nonphosphorylated)

Comparison

Limited digestion by four proteases in the… vs Nonphosphorylated kinase vs phosphorylated…

Design

Preclinical

Authors

MWMichael P. WalshUniversity College Dublin

Discussion

Member takes

Implication

Maps MLCK domains without major conformational shifts; leaves open relevance to human vascular regulation or targeted therapies.

Structured PICO

Population

Smooth muscle myosin light chain kinase (phosphorylated and nonphosphorylated)

Intervention

Limited digestion by four proteases (trypsin, chymotrypsin, Staphylococcus aureus V8 protease, and thrombin) in the presence and absence of bound calmodulin

Comparator

Nonphosphorylated kinase vs phosphorylated kinase; presence vs absence of bound calmodulin

Outcome

Conformational changes, distribution of phosphorylation sites, and Ca2+ dependence of kinase activitysurrogate

This biochemical study maps the functional domains of smooth muscle myosin light chain kinase, demonstrating that neither phosphorylation nor calmodulin binding induces dramatic conformational changes.

Cite This Study

Michael P. Walsh (1985) studied this question.

synapsesocial.com/papers/6a87d369f8efd6d7e4fb17ff https://doi.org/10.1021/bi00335a047

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Limited proteolysis of smooth muscle myosin light chain kinase

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Limited proteolysis of smooth muscle myosin light chain kinase

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider