"Calmodulin" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
A heat-stable, low-molecular-weight activator protein found mainly in the brain and heart. The binding of calcium ions to this protein allows this protein to bind to cyclic nucleotide phosphodiesterases and to adenyl cyclase with subsequent activation. Thereby this protein modulates cyclic AMP and cyclic GMP levels.
- Calcium-Dependent Regulator
- Calcium Dependent Regulator
- Calcium-Dependent Activator Protein
- Activator Protein, Calcium-Dependent
- Calcium Dependent Activator Protein
- Protein, Calcium-Dependent Activator
- Phosphodiesterase Protein Activator
- Activator, Phosphodiesterase Protein
- Protein Activator, Phosphodiesterase
- Phosphodiesterase Activating Factor
- Activating Factor, Phosphodiesterase
- Factor, Phosphodiesterase Activating
- Phosphodiesterase Activator Protein
- Activator Protein, Phosphodiesterase
- Protein, Phosphodiesterase Activator
- Regulator, Calcium-Dependent
- Regulator, Calcium Dependent
Cyclic AMP-Phosphodiesterase Activator
- Cyclic AMP-Phosphodiesterase Activator
- AMP-Phosphodiesterase Activator, Cyclic
- Activator, Cyclic AMP-Phosphodiesterase
- Cyclic AMP Phosphodiesterase Activator
Below are MeSH descriptors whose meaning is more general than "Calmodulin".
Below are MeSH descriptors whose meaning is more specific than "Calmodulin".
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Below are the most recent publications written about "Calmodulin" by people in Profiles.
A novel Sporothrix brasiliensis genomic variant in Midwestern Brazil: evidence for an older and wider sporotrichosis epidemic. Emerg Microbes Infect. 2020 Dec; 9(1):2515-2525.
Different Roles of N-Terminal and C-Terminal Domains in Calmodulin for Activation of Bacillus anthracis Edema Factor. Toxins (Basel). 2015 Jul 13; 7(7):2598-614.
A New Versatile Immobilization Tag Based on the Ultra High Affinity and Reversibility of the Calmodulin-Calmodulin Binding Peptide Interaction. J Mol Biol. 2015 Aug 14; 427(16):2707-25.
Temperature-accelerated molecular dynamics gives insights into globular conformations sampled in the free state of the AC catalytic domain. Proteins. 2014 Oct; 82(10):2483-96.
Biochemistry. How proteins fold. Science. 2011 Oct 28; 334(6055):464-5.
Identification of sequence polymorphisms in CALM2 and analysis of association with hip osteoarthritis in a Japanese population. J Bone Miner Metab. 2010 Sep; 28(5):547-53.
The adenylyl cyclase activity of anthrax edema factor. Mol Aspects Med. 2009 Dec; 30(6):423-30.
Protein-protein docking and analysis reveal that two homologous bacterial adenylyl cyclase toxins interact with calmodulin differently. J Biol Chem. 2008 Aug 29; 283(35):23836-45.
Dynamic regulation of endothelial NOS mediated by competitive interaction with alpha-actinin-4 and calmodulin. FASEB J. 2008 May; 22(5):1450-7.
A 1.3-A structure of zinc-bound N-terminal domain of calmodulin elucidates potential early ion-binding step. J Mol Biol. 2007 Nov 23; 374(2):517-27.