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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Calcium/calmodulin-dependent protein kinase II alpha

CaM, CaMKII, CaM kinase II
This gene encodes a protein with an N-terminal filamin-binding domain, a central proline-rich domain, and, multiple C-terminal LIM domains. This protein localizes at cell junctions and may link cell adhesion structures to the actin cytoskeleton. This protein may be involved in the assembly and stabilization of actin-filaments and likely plays a role in modulating cell adhesion, cell morphology and cell motility. This protein also localizes to the nucleus and may affect cardiomyocyte differentiation after binding with the CSX/NKX2-5 transcription factor. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: CAN, V1a, ACID, HAD, CREB
Papers using CaM antibodies
A GluR1-cGKII interaction regulates AMPA receptor trafficking
Traynelis Stephen F. et al., In Nature neuroscience, 2006
... Purified CaMKII and calmodulin were obtained from New England Biolabs (Ipswich, MA) and activated ...
NCAM promotes assembly and activity-dependent remodeling of the postsynaptic signaling complex
Schachner Melitta et al., In The Journal of Cell Biology, 1996
... Biotechnology; mouse monoclonal antibodies against CaMKII were obtained from Stressgen Biotechnologies; rabbit polyclonal antibodies against phospho-CaMKII (Thr286) were purchased from Cell Signaling Technology; mouse monoclonal antibodies ...
Three-dimensional structures of the periplasmic lysine/arginine/ornithine-binding protein with and without a ligand.
Abraham Edathara, In PLoS ONE, 1992
... type AQP0) and the pCMV6-XL5 expression vector containing the full-length sequence of the human calmodulin (CaM) gene were obtained from OriGene (Rockville, US) ...
Papers on CaM
A bHLH gene from Tamarix hispida improves abiotic stress tolerance by enhancing osmotic potential and decreasing reactive oxygen species accumulation.
Wang et al., Ürümqi, China. In Tree Physiol, Feb 2016
Additionally, ThbHLH1 regulates the expression of the genes including P5CS, BADH, CaM, POD and SOD, to activate the above physiological changes, and also induces the expression of stress tolerance-related genes LEAs and HSPs.
Se Enhances MLCK Activation by Regulating Selenoprotein T (SelT) in the Gastric Smooth Muscle of Rats.
Guo et al., Wuhan, China. In Biol Trace Elem Res, Feb 2016
Western blot and qPCR were performed to determine SelT, CaM, MLCK, and MLC expressions.
NMDAR-dependent Proteasome Activity in the Gustatory Cortex is Necessary for Conditioned Taste Aversion.
Rosenblum et al., Haifa, Israel. In Neurobiol Learn Mem, Feb 2016
This increase in proteasome activity was abolished by local administration to the GC of the NMDA antagonist, APV, as well as a CaMKII inhibitor, at the time of acquisition.
The chick embryo as a model for the effects of Prenatal exposure to alcohol on craniofacial development.
Kiecker, London, United Kingdom. In Dev Biol, Feb 2016
At the cellular level, ethanol appears to inhibit Sonic hedgehog signalling, alter levels of retionoic acid activity, trigger a Ca(2+)-CamKII-dependent pathway that antagonises WNT signalling, affect cytoskeletal dynamics and increase oxidative stress.
Atrial remodeling in atrial fibrillation: CaMKII as a nodal proarrhythmic signal.
Anderson et al., Baltimore, United States. In Cardiovasc Res, Feb 2016
UNASSIGNED: CaMKII is a serine-threonine protein kinase that is abundant in myocardium.
CaMKII regulates proteasome phosphorylation and activity and promotes memory destabilization following retrieval.
Helmstetter et al., Milwaukee, United States. In Neurobiol Learn Mem, Feb 2016
Here, we found that proteasome activity is increased in the amygdala in a CaMKII-dependent manner following the retrieval of a contextual fear memory.
CaMKII is a RIP3 substrate mediating ischemia- and oxidative stress-induced myocardial necroptosis.
Xiao et al., Beijing, China. In Nat Med, Feb 2016
Here we show that receptor-interacting protein 3 (RIP3) triggers myocardial necroptosis, in addition to apoptosis and inflammation, through activation of Ca(2+)-calmodulin-dependent protein kinase (CaMKII) rather than through the well-established RIP3 partners RIP1 and MLKL.
CaM Kinases: From Memories to Addiction.
Giese et al., Erlangen, Germany. In Trends Pharmacol Sci, Jan 2016
Ca(2+)/calmodulin-dependent protein kinases (CaMKs) are important Ca(2+) sensors translating glutamatergic activation into synaptic plasticity during learning and memory formation.
Hippocampal Dopamine/DRD1 Signaling Dependent on the Ghrelin Receptor.
Smith et al., Jupiter, United States. In Cell, Dec 2015
Activation by a DRD1 agonist produced non-canonical signal transduction via Gαq-PLC-IP3-Ca(2+) at the expense of canonical DRD1 Gαs cAMP signaling to result in CaMKII activation, glutamate receptor exocytosis, synaptic reorganization, and expression of early markers of hippocampal synaptic plasticity.
Analysis of Two Complementary Single-Gene Deletion Mutant Libraries of Salmonella Typhimurium in Intraperitoneal Infection of BALB/c Mice.
McClelland et al., Irvine, United States. In Front Microbiol, 2014
The two mutant libraries differed in the orientation of the antibiotic resistance cassettes (either sense-oriented Kan(R), SGD-K, or antisense-oriented Cam(R), SGD-C).
Calcium/calmodulin-dependent kinase II and Alzheimer's disease.
Giese et al., London, United Kingdom. In Mol Brain, 2014
CaMKII is a remarkably complex protein kinase, known to have a fundamental role in synaptic plasticity and memory formation.
Abiotic stress responses in plants: roles of calmodulin-regulated proteins.
Singh et al., Amritsar, India. In Front Plant Sci, 2014
Calmodulin (CaM) is one of the most extensively studied Ca(2+)-sensing proteins and has been shown to be involved in transduction of Ca(2+) signals.
Apocalmodulin itself promotes ion channel opening and Ca(2+) regulation.
Yue et al., Baltimore, United States. In Cell, 2014
The Ca(2+)-free form of calmodulin (apoCaM) often appears inert, modulating target molecules only upon conversion to its Ca(2+)-bound form.
Mission CaMKIIγ: shuttle calmodulin from membrane to nucleus.
Hell et al., Davis, United States. In Cell, 2014
Calmodulin (CaM) activated by Ca(2+) initiates the nuclear events, but how CaM makes its way to the nucleus has remained elusive.
γCaMKII shuttles Ca²⁺/CaM to the nucleus to trigger CREB phosphorylation and gene expression.
Tsien et al., New York City, United States. In Cell, 2014
This mechanism resolves long-standing puzzles about CaM/CaMK-dependent signaling to the nucleus.
The motif of human cardiac myosin-binding protein C is required for its Ca2+-dependent interaction with calmodulin.
Trewhella et al., Sydney, Australia. In J Biol Chem, 2012
CaM may act as a structural conduit that links cMyBP-C with Ca(2+) signaling pathways to help coordinate phosphorylation events and synchronize the multiple interactions between cMyBP-C, myosin, and actin during the heart muscle contraction.
Alternative pathways for association and dissociation of the calmodulin-binding domain of plasma membrane Ca(2+)-ATPase isoform 4b (PMCA4b).
Strehler et al., Boston, United States. In J Biol Chem, 2012
Alternative pathways for association and dissociation of the calmodulin-binding domain of plasma membrane Ca(2+)-ATPase isoform 4b (PMCA4b).
Ca(2+)/calmodulin-dependent protein kinase IIα (αCaMKII) controls the activity of the dopamine transporter: implications for Angelman syndrome.
Kudlacek et al., Vienna, Austria. In J Biol Chem, 2012
Ca(2+)/calmodulin-dependent protein kinase IIalpha (alphaCaMKII) controls the activity of the dopamine transporter: implications for Angelman syndrome.
Characterization of the structure and intermolecular interactions between the connexin 32 carboxyl-terminal domain and the protein partners synapse-associated protein 97 and calmodulin.
Sorgen et al., Omaha, United States. In J Biol Chem, 2012
Cx32 is differentially phosphorylated and exists in a complex with SAP97 and CaM.
CaMKIIδC slows [Ca]i decline in cardiac myocytes by promoting Ca sparks.
Bers et al., Davis, United States. In Biophys J, 2012
These results demonstrate that there are dramatic CaMKII-mediated effects on RyR Calcium release that occur via regulation of both RyR activation and termination processes.
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