ReviewMolecular biotechnology2004
Calmodulin's flexibility allows for promiscuity in its interactions with target proteins and peptides.
Review in Molecular biotechnology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 160 papers.
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Who cites it
160 citing papers in PubMed, 322 citations in OpenAlex.
- iPLAScience advances · 2026Article
- Structural differences in Apo-, D132E- and Holo-Calmodulin bound to the IQ domain of the cardiac L-type calcium channel.Molecular simulation · 2026Article
- Calmodulin Interaction Interface with Plasma Membrane CaInternational journal of molecular sciences · 2025Article
- Unconventional binding of calmodulin to CHK2 kinase inhibits catalytic activity.The Biochemical journal · 2025Article
- Structural Insights and Calcium-Switching Mechanism ofInternational journal of molecular sciences · 2025Article
- Evaluating protein complexes between human aquaporin and calmodulin using biomolecular fluorescence complementation.Scientific reports · 2025Article
- Distinct intracellular spatiotemporal expression of Calmodulin genes underlies functional diversity of Calmodulin-dependent signalling in cardiac myocytes.Cardiovascular research · 2025Article
- Article
- Structural and functional insights into α-actinin isoforms and their implications in cardiovascular disease.The Journal of general physiology · 2025Review
- Predicting the role of β-GAL genes in bean under abiotic stress and genome-wide characterization of β-GAL gene family members.Protoplasma · 2025Article
- Genome-Wide Identification and Expression Analysis of thePlants (Basel, Switzerland) · 2024Article
- Neurogranin modulates the rate of association between calmodulin and target peptides.Biophysical journal · 2024Article
- Architecture and activation of human muscle phosphorylase kinase.Nature communications · 2024Article
- Hypothesis paper: the development of a regulatory layer in P2B autoinhibited CaPlant signaling & behavior · 2023Article
- Simulations of Amyloid-Forming Peptides in the Crystal State.The protein journal · 2023Article
- Structural Analysis and Diversity of Calmodulin-Binding Domains in Membrane and Intracellular CaThe Journal of membrane biology · 2023Article
- Article
- Genome-wide identification ofFrontiers in plant science · 2023Article
- Regulation of KInternational journal of molecular sciences · 2022Review
- Binding and Functional Folding (BFF): A Physiological Framework for Studying Biomolecular Interactions and Allostery.Journal of molecular biology · 2022Review
100 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The small bilobal calcium regulatory protein calmodulin (CaM) activates numerous target enzymes in response to transient changes in intracellular calcium concentrations. Binding of calcium to the two helix-loop-helix calcium-binding motifs in each of the globular domains induces conformational changes that expose a methionine-rich hydrophobic patch on the surface of each domain of the protein, which it uses to bind to peptide sequences in its target enzymes. Although these CaM-binding domains typically have little sequence identity, the positions of several bulky hydrophobic residues are often conserved, allowing for classification of CaM-binding domains into recognition motifs, such as the 1-14 and 1-10 motifs. For calcium-independent binding of CaM, a third motif known as the IQ motif is also common. Many CaM-peptide complexes have globular conformations, where CaM's central linker connecting the two domains unwinds, allowing the protein to wrap around a single predominantly alpha-helical target peptide sequence. However, novel structures have recently been reported where the conformation of CaM is highly dissimilar to these globular complexes, in some instances with less than a full compliment of bound calcium ions, as well as novel stoichiometries. Furthermore, many divergent CaM isoforms from yeast and plant species have been discovered with unique calcium-binding and enzymatic activation characteristics compared to the single CaM isoform found in mammals.
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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.