ArticlePloS one2015
Calcineurin Undergoes a Conformational Switch Evoked via Peptidyl-Prolyl Isomerization.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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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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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
7 citing papers in PubMed, 13 citations in OpenAlex.
- Using deep-learning predictions reveals a large number of register errors in PDB depositions.IUCrJ · 2024Article
- The Neurotoxic Effect of Environmental Temperature Variation in Adult Zebrafish (International journal of molecular sciences · 2023Article
- Harnessing IGF-1 and IL-2 as biomarkers for calcineurin activity to tailor optimal FK506 dosage in α-synucleinopathies.Frontiers in molecular biosciences · 2023Article
- Functional and Regulatory Roles of Fold-Switching Proteins.Structure (London, England : 1993) · 2021Review
- Inaccurate secondary structure predictions often indicate protein fold switching.Protein science : a publication of the Protein Society · 2019Article
- FKBP12 contributes to α-synuclein toxicity by regulating the calcineurin-dependent phosphoproteome.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Structure of the WipA protein reveals a novel tyrosine protein phosphatase effector fromThe Journal of biological chemistry · 2017Article
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A limited repertoire of PPP family of serine/threonine phosphatases with a highly conserved catalytic domain acts on thousands of protein targets to orchestrate myriad central biological roles. A major structural reorganization of human calcineurin, a ubiquitous Ser/Thr PPP regulated by calcium and calmodulin and targeted by immunosuppressant drugs cyclosporin A and FK506, is unveiled here. The new conformation involves trans- to cis-isomerization of proline in the SAPNY sequence, highly conserved across PPPs, and remodels the main regulatory site where NFATc transcription factors bind. Transitions between cis- and trans-conformations may involve peptidyl prolyl isomerases such as cyclophilin A and FKBP12, which are known to physically interact with and modulate calcineurin even in the absence of immunosuppressant drugs. Alternative conformations in PPPs provide a new perspective on interactions with substrates and other protein partners and may foster development of more specific inhibitors as drug candidates.
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Registered trials
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