May 1, 1998Biochemistry

Phosphorylation Changes the Spatial Relationship between Glu124−Arg143 and Cys18 and Cys165 of the Regulatory Light Chain in Smooth Muscle Myosin ,

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Population

Smooth muscle myosin regulatory light chain (RLC) mutants (RLC-C18 and RLC-C165)

Comparison

Phosphorylation vs Unphosphorylated state

Design

Preclinical

Authors

GWGuanming WuOregon Health & Science University AWAnna WongSUNY College of Optometry FQFang QianOil Crops Research Institute

Discussion

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Implication

Phosphorylation may enable smooth muscle myosin activation via RLC conformational shift; leaves open human relevance and therapeutic implications.

Structured PICO

Population

Smooth muscle myosin regulatory light chain (RLC) mutants (RLC-C18 and RLC-C165)

Intervention

Phosphorylation

Comparator

Unphosphorylated state

Outcome

Intrachain photo-cross-linking patterns and spatial relationshipssurrogate

Phosphorylation alters the spatial relationship between the Glu124-Arg143 region and the N and C termini of the regulatory light chain, which may underlie smooth muscle myosin activation.

Cite This Study

Wu et al. (1998) studied this question.

synapsesocial.com/papers/6a87228cc026610cc182d60b https://doi.org/10.1021/bi980054+

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Implication

Phosphorylation may enable smooth muscle myosin activation via RLC conformational shift; leaves open human relevance and therapeutic implications.

Phosphorylation Changes the Spatial Relationship between Glu124−Arg143 and Cys18 and Cys165 of the Regulatory Light Chain in Smooth Muscle Myosin ,

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Phosphorylation Changes the Spatial Relationship between Glu124−Arg143 and Cys18 and Cys165 of the Regulatory Light Chain in Smooth Muscle Myosin ,

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider