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These data for the first time demonstrate that Trisk 95's 200-231 region is responsible for ryanodine receptor activation.
The lncRNA TRDN-AS regulates the balance between cardiac and skeletal isoforms of triadin.
CLIMP-63 (also known as CKAP4), is the partner of triadin, is responsible for this association of triads and microtubules.
The minimal KEKE motif of TRN involved in the interactions with CSQ2, HRC and RyR2 within the Ca2+ release units of cardiac sarcoplasmic reticulum has been defined.
Three regions in triadin are identified that mediate targeting to the junctional domain of sarcoplasmic reticulum.
in skeletal muscle the disruption of Tdn/CASQ link has a more profound effect on jSR architecture and myoplasmic Ca(2+) regulation than Jct/CASQ association.
The triadin-to-calsequestrin ratio is a critical modulator of the sarcoplasmic reticulum Ca(2+) signaling in ventricular myocytes.
Ablation of skeletal muscle triadin impairs FKBP12/RyR1 channel interactions essential for maintaining resting cytoplasmic Ca2+.
caveolin 3-containing membrane domains and the calcium release complex are functionally linked and Trdn is instrumental to the regulation of this interaction, the integrity of which may be crucial for muscle physiology.
Results demonstrate a reduction in muscle strength in triadin knockout mice, indicating that triadin plays an essential role in skeletal muscle function and in skeletal muscle structure.
triadin 1 overexpression triggered time-dependent alterations in SR protein expression, Ca(2+) homeostasis, and contractility, indicating for the first time an inhibitory function of triadin 1 on SR-Ca(2+) release in vivo.
Triadin(TRD)xjunctin(JCN) mice were studied to compensate the down-regulation of junctin expression in triadin-expressing mice; exercise or stress provoked repetitive ventricular tachycardia in freely roaming TRDxJCN mice.
Histidine-rich Ca-binding protein may play a key role in the regulation of SR Ca cycling through its direct interactions with SERCA2 and triadin, mediating a fine cross talk between SR Ca uptake and release in the heart.
triadin has a role in regulating myoplasmic Ca(2+) homeostasis and organizing the molecular complex of the triad but not in regulating skeletal-type excitation-contraction coupling
triadin knockdown skeletal myotubes display reduced Ca2+ release following KCl-induced depolarization
Trisk 95 negatively regulates ryanodine receptor function by suppressing localized calcium release events and global calcium signals in cultured muscle cells.
triadin is critically important for maintaining the structural and functional integrity of the cardiac Ca2+ release units.
A compound heterozygous mutation in the triadin gene resulted in a particularly arrhythmogenic phenotype with with cardiac arrest in two siblings.
We describe a new family with cathecholaminergic polymorphic ventricular tachycardia (CPVT) linked to the Triadin gene.
Common variants in TRDN and CALM1 are associated with increased risk of sudden cardiac death in patients with chronic heart failure.
TRDN is a novel underlying genetic basis for recessively inherited Long-QT syndrome.
Data show that triadin (TRDN) is a new gene responsible for an autosomal recessive form of ctecholaminergic polymorphic ventricular tachycardia (CPVT).
The researchers found evidence that TRDN may be a susceptibility or marker gene for IgA nephropathy
gene organization and cloning of the major isoform
proteasome inhibition led to an accumulation of two new modified forms of triadin-1 that were seen with triadin-1 only when it is not glycosylated on Asn(75).
This gene encodes an integral membrane protein that contains a single transmembrane domain. As similar protein in rabbits plays a role in skeletal muscle excitation-contraction coupling as part of the calcium release complex in association with the ryanodine receptor. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene, and single nucleotide polymorphisms in this gene may be markers for IgA nephritis.
, junctional sarcoplasmic reticulum glycoprotein
, cardiac triadin
, triadin 1
, triadin 32 kDa (TRISK 32)
, triadin 49 kDa (TRISK 49)
, triadin 95