ReviewBiophysics and physicobiology2017
Domain-to-domain coupling in voltage-sensing phosphatase.
Review in Biophysics and physicobiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed, 5 citations in OpenAlex.
- Nonsubstrate PI(4,5)PProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Dynamics and structural stability effects of germline PTEN mutations associated with cancer versus autism phenotypes.Journal of biomolecular structure & dynamics · 2019Article
- Molecular mechanisms of coupling to voltage sensors in voltage-evoked cellular signals.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2019Review
- Membrane properties that shape the evolution of membrane enzymes.Current opinion in structural biology · 2018Review
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Voltage-sensing phosphatase (VSP) consists of a transmembrane voltage sensor and a cytoplasmic enzyme region. The enzyme region contains the phosphatase and C2 domains, is structurally similar to the tumor suppressor phosphatase PTEN, and catalyzes the dephosphorylation of phosphoinositides. The transmembrane voltage sensor is connected to the phosphatase through a short linker region, and phosphatase activity is induced upon membrane depolarization. Although the detailed molecular characteristics of the voltage sensor domain and the enzyme region have been revealed, little is known how these two regions are coupled. In addition, it is important to know whether mechanism for coupling between the voltage sensor domain and downstream effector function is shared among other voltage sensor domain-containing proteins. Recent studies in which specific amino acid sites were genetically labeled using a fluorescent unnatural amino acid have enabled detection of the local structural changes in the cytoplasmic region of
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