ArticleNature communications2016
Conformational heterogeneity of the calmodulin binding interface.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 28 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
28 citing papers in PubMed, 59 citations in OpenAlex.
- Article
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- Probing calmodulin-NO synthase interactions via site-specific infrared spectroscopy: an introductory investigation.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024Article
- Calcium-Associated Proteins in Neuroregeneration.Biomolecules · 2024Review
- Human disease-associated calmodulin mutations alter calcineurin function through multiple mechanisms.Cell calcium · 2023Article
- Markov state modelling reveals heterogeneous drug-inhibition mechanism of Calmodulin.PLoS computational biology · 2022Article
- Role of water-bridged interactions in metal ion coupled protein allostery.PLoS computational biology · 2022Article
- Pre-exascale HPC approaches for molecular dynamics simulations. Covid-19 research: A use case.Wiley interdisciplinary reviews. Computational molecular science · 2022Article
- Further Evidence of the Melatonin Calmodulin Interaction: Effect on CaMKII Activity.International journal of molecular sciences · 2022Article
- Non-Canonical Interaction between Calmodulin and Calcineurin Contributes to the Differential Regulation of Plant-Derived Calmodulins on Calcineurin.Journal of chemical information and modeling · 2021Article
- Assessing the Role of Calmodulin's Linker Flexibility in Target Binding.International journal of molecular sciences · 2021Article
- Unraveling the energetic significance of chemical events in enzyme catalysis via machine-learning based regression approach.Communications chemistry · 2020Article
- Molecular Dynamics Simulation-assisted Ionic Liquid Screening for Deep Coverage Proteome Analysis.Molecular & cellular proteomics : MCP · 2020Article
- Comparative Analyses of the Conformational Dynamics Between the Soluble and Membrane-Bound Cytokine Receptors.Scientific reports · 2020Article
- Resolved Structural States of Calmodulin in Regulation of Skeletal Muscle Calcium Release.Biophysical journal · 2020Article
- Calmodulin and Calmodulin Binding Proteins inInternational journal of molecular sciences · 2020Review
- Molecular Insights from Conformational Ensembles via Machine Learning.Biophysical journal · 2020Article
- Molecular dynamics simulations of an engineered T4 lysozyme exclude helix to sheet transition, and provide insights into long distance, intra-protein switchable motion.Protein science : a publication of the Protein Society · 2020Article
- Molecular Dynamics Study of the Changes in Conformation of Calmodulin with Calcium Binding and/or Target Recognition.Scientific reports · 2019Article
Corrections and comments
- Erratum issued
Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Calmodulin (CaM) is a ubiquitous Ca(2+) sensor and a crucial signalling hub in many pathways aberrantly activated in disease. However, the mechanistic basis of its ability to bind diverse signalling molecules including G-protein-coupled receptors, ion channels and kinases remains poorly understood. Here we harness the high resolution of molecular dynamics simulations and the analytical power of Markov state models to dissect the molecular underpinnings of CaM binding diversity. Our computational model indicates that in the absence of Ca(2+), sub-states in the folded ensemble of CaM's C-terminal domain present chemically and sterically distinct topologies that may facilitate conformational selection. Furthermore, we find that local unfolding is off-pathway for the exchange process relevant for peptide binding, in contrast to prior hypotheses that unfolding might account for binding diversity. Finally, our model predicts a novel binding interface that is well-populated in the Ca(2+)-bound regime and, thus, a candidate for pharmacological intervention.
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Registered trials
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.