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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 08 Dec 2016.

Calsequestrin 1

Calsequestrin
The protein encoded by this gene is a mitochondrial calcium-binding protein located in the luminal space of the terminal cisternae of the sarcoplasmic reticulum. The protein binds and putatively stores calcium ions. The protein is absent in patients with Duchenne and Becker types of muscular dystrophy. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ATPase, ACID, FasT, CASQ2, Triadin
Papers on Calsequestrin
Characterization of Two Human Skeletal Calsequestrin Mutants Implicated in Malignant Hyperthermia and Vacuolar Aggregate Myopathy.
New
Kang et al., Pullman, United States. In J Biol Chem, Dec 2015
Calsequestrin 1 is the principal Ca(2+) storage protein of the sarcoplasmic reticulum of skeletal muscle.
Calsequestrins in skeletal and cardiac muscle from adult Danio rerio.
New
Nori et al., Padova, Italy. In J Muscle Res Cell Motil, Dec 2015
UNASSIGNED: Calsequestrin (Casq) is a high capacity, low affinity Ca(2+)-binding protein, critical for Ca(2+)-buffering in cardiac and skeletal muscle sarcoplasmic reticulum.
Calsequestrin 2 deletion causes sinoatrial node dysfunction and atrial arrhythmias associated with altered sarcoplasmic reticulum calcium cycling and degenerative fibrosis within the mouse atrial pacemaker complex1.
New
Fedorov et al., Columbus, United States. In Eur Heart J, Apr 2015
AIMS: Loss-of-function mutations in Calsequestrin 2 (CASQ2) are associated with catecholaminergic polymorphic ventricular tachycardia (CPVT).
The disorders of the calcium release unit of skeletal muscles: what have we learned from mouse models?
Review
New
Cancellara et al., Padova, Italy. In J Muscle Res Cell Motil, Feb 2015
The release from the Sarcoplasmic Reticulum stores (SR) is handled by a multiprotein complex called Calcium Release Unit and composed of DiHydroPyridine Receptor or DHPR, Ryanodine Receptor or RYR, Calsequestrin or CASQ, junctin, Triadin, Junctophilin and Mitsugumin 29.
The C-terminal calcium-sensitive disordered motifs regulate isoform-specific polymerization characteristics of calsequestrin.
Periasamy et al., Columbus, United States. In Biopolymers, 2015
Calsequestrin (CASQ) exists as two distinct isoforms CASQ1 and CASQ2 in all vertebrates.
Association of CASQ2 polymorphisms with sudden cardiac arrest and heart failure in patients with coronary artery disease.
Tseng et al., Beirut, Lebanon. In Heart Rhythm, 2014
Calsequestrin 2 (CASQ2) mutations affect calcium release and initiate malignant ventricular arrhythmias (VAs) and SCA syndromes.
Potential role of cardiac calsequestrin in the lethal arrhythmic effects of cocaine.
Kang et al., Pullman, United States. In Drug Alcohol Depend, 2014
Calsequestrin (CASQ) is a major Ca(2+)-storage protein within the sarcoplasmic reticulum (SR) of both cardiac and skeletal muscles.
Flecainide therapy suppresses exercise-induced ventricular arrhythmias in patients with CASQ2-associated catecholaminergic polymorphic ventricular tachycardia.
Boulos et al., In Heart Rhythm, 2013
BACKGROUND: Calsequestrin-associated catecholaminergic polymorphic ventricular tachycardia (CPVT2) can cause sudden death in young individuals in response to stress.
Novel details of calsequestrin gel conformation in situ.
Franzini-Armstrong et al., Philadelphia, United States. In J Biol Chem, 2013
Calsequestrin (CASQ) is the major component of the sarcoplasmic reticulum (SR) lumen in skeletal and cardiac muscles.
Altered calsequestrin glycan processing is common to diverse models of canine heart failure.
Cala et al., Detroit, United States. In Mol Cell Biochem, 2013
Calsequestrin-2 (CSQ2) is a resident glycoprotein of junctional sarcoplasmic reticulum that functions in the regulation of SR Ca(2+) release.
Regulation of sarco(endo)plasmic reticulum Ca2+-ATPase and calsequestrin gene expression in the heart.
Review
Fragoso-Medina et al., Mexico. In Can J Physiol Pharmacol, 2012
Calsequestrin (Casq2) is the main protein in the SR lumen, functioning as a Ca(2+) buffer and participating in Ca(2+) release by interacting with the ryanodine receptor 2 (RyR2) Ca(2+)-release channel.
Calsequestrin mutations and catecholaminergic polymorphic ventricular tachycardia.
Review
Knollmann et al., Nashville, United States. In Pediatr Cardiol, 2012
Cardiac calsequestrin (Casq2) is the major Ca2+ binding protein in the sarcoplasmic reticulum, which is the principle Ca2+ storage organelle of cardiac muscle.
Specific effects of endurance and sprint training on protein expression of calsequestrin and SERCA in mouse skeletal muscle.
GeneRIF
Mänttäri et al., Oulu, Finland. In J Muscle Res Cell Motil, 2012
Protein levels of CSQ1, SERCA1, and SERCA2 are re-adjusted in skeletal muscles depending on the demands of diverse exercise training programs.
High-capacity Ca2+ binding of human skeletal calsequestrin.
GeneRIF
Kang et al., Pullman, United States. In J Biol Chem, 2012
a mechanism for the observed in vitro and in vivo dynamic high-capacity and low-affinity Ca(2+)-binding activity of calsequestrin
Calsequestrin 2 and arrhythmias.
Review
Knollmann et al., Nashville, United States. In Am J Physiol Heart Circ Physiol, 2012
Calsequestrin is the most abundant Ca-binding protein of the specialized endoplasmic reticulum found in muscle, the sarcoplasmic reticulum (SR).
Calsequestrin (CASQ1) rescues function and structure of calcium release units in skeletal muscles of CASQ1-null mice.
GeneRIF
Nori et al., Padova, Italy. In Am J Physiol Cell Physiol, 2012
results support the view that in skeletal muscles, CASQ1 plays a key role in both Ca(2+) homeostasis and terminal cisternae structure
Molecular mechanisms of pharmaceutical drug binding into calsequestrin.
Kang et al., Pullman, United States. In Int J Mol Sci, 2011
Calsequestrin (CASQ) is a major Ca2+-storage/buffer protein present in the sarcoplasmic reticulum of both skeletal (CASQ1) and cardiac (CASQ2) muscles.
Differential effect of calsequestrin ablation on structure and function of fast and slow skeletal muscle fibers.
GeneRIF
Protasi et al., Chieti, Italy. In J Biomed Biotechnol, 2010
The results presented in this paper unmask a differential effect of CASQ1&2 ablation in fast versus slow fibers
Calsequestrin distribution, structure and function, its role in normal and pathological situations and the effect of thyroid hormones.
Review
Soukup et al., Praha, Czech Republic. In Physiol Res, 2010
Calsequestrin is the main calcium binding protein of the sarcoplasmic reticulum, serving as an important regulator of Ca(2+).
Increased store-operated Ca2+ entry in skeletal muscle with reduced calsequestrin-1 expression.
GeneRIF
Ma et al., United States. In Biophys J, 2010
effect of nockdown of CSQ1 in adult mouse skeletal muscle on Store-operated Ca(2+) entry
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