ArticleProceedings of the National Academy of Sciences of the United States of America2016
Conserved properties of individual Ca2+-binding sites in calmodulin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers, 1 of them a synthesis that pooled it.
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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
70 citing papers in PubMed, 1 synthesis or guideline pooled it, 116 citations in OpenAlex.
- An International, Multicentered, Evidence-Based Reappraisal of Genes Reported to Cause Congenital Long QT Syndrome.Circulation · 2020Pooled it
- Calmodulin: The Essential Biological Regulator Self-Regulates Its Activity, Structure and Function.Biology · 2026Review
- Hierarchical Organization of Evolutionary Constraint in Duplicated EF-Hand Motifs.Journal of molecular evolution · 2026Article
- An Ancestral Mechanism of Calmodulin Binding to Cds1 Kinase Inhibits Catalytic Activity.IUBMB life · 2026Article
- Redesign of Calmodulin for Genetically Encoded ZnChemical & biomedical imaging · 2026Article
- Functional consequences of calmodulin variants identified among schizophrenia patients and controls.Translational psychiatry · 2025Article
- Calmodulin D133H Disrupts CaCells · 2025Article
- Reversing Lanmodulin's Metal-Binding Sequence in Short Peptides Surprisingly Increases the Lanthanide Affinity.Angewandte Chemie (International ed. in English) · 2025Article
- Calcium dissociation with carbonate ions from Pf-SCP, sarcoplasmic calcium-binding protein in Pinctada fucata, contributes to calcium mineralization for shell formation.Protein science : a publication of the Protein Society · 2025Article
- Remolding laccase for whole-cell and in vivo modulation of dopamine signal.Science advances · 2025Article
- Structural insights into the dual CaNature communications · 2025Article
- Recent advances and future challenges in predictive modeling of metalloproteins by artificial intelligence.Molecules and cells · 2025Review
- Arrhythmogenic calmodulin variants D131E and Q135P disrupt interaction with the L-type voltage-gated CaActa physiologica (Oxford, England) · 2025Article
- Transcriptome, miRNA, and degradome sequencing reveal the leaf stripe (Pyrenophora graminea) resistance genes in Tibetan hulless barley.BMC plant biology · 2025Article
- Computationally derived structural insights into Rare Earth selectivity in lanmodulin and its variants.Computational and structural biotechnology journal · 2025Article
- Heart Failure: A Deficiency of Energy-A Path Yet to Discover and Walk.Biomedicines · 2024Review
- Can calmodulin bind to lipids of the cytosolic leaflet of plasma membranes?Open biology · 2024Article
- Real-time single-molecule imaging of CaMKII-calmodulin interactions.Biophysical journal · 2024Article
- Structure and Function of Calcium-Activated Chloride Channels and Phospholipid Scramblases in the TMEM16 Family.Handbook of experimental pharmacology · 2024Review
- Interaction of Calmodulin with TRPM: An Initiator of Channel Modulation.International journal of molecular sciences · 2023Review
10 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Calmodulin (CaM) is a Ca(2+)-sensing protein that is highly conserved and ubiquitous in eukaryotes. In humans it is a locus of life-threatening cardiomyopathies. The primary function of CaM is to transduce Ca(2+) concentration into cellular signals by binding to a wide range of target proteins in a Ca(2+)-dependent manner. We do not fully understand how CaM performs its role as a high-fidelity signal transducer for more than 300 target proteins, but diversity among its four Ca(2+)-binding sites, called EF-hands, may contribute to CaM's functional versatility. We therefore looked at the conservation of CaM sequences over deep evolutionary time, focusing primarily on the four EF-hand motifs. Expanding on previous work, we found that CaM evolves slowly but that its evolutionary rate is substantially faster in fungi. We also found that the four EF-hands have distinguishing biophysical and structural properties that span eukaryotes. These results suggest that all eukaryotes require CaM to decode Ca(2+) signals using four specialized EF-hands, each with specific, conserved traits. In addition, we provide an extensive map of sites associated with target proteins and with human disease and correlate these with evolutionary sequence diversity. Our comprehensive evolutionary analysis provides a basis for understanding the sequence space associated with CaM function and should help guide future work on the relationship between structure, function, and disease.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.