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anti-Human RYR1 Antibodies:
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Amphibian Monoclonal RYR1 Primary Antibody for BP, IF - ABIN152702
Olivares, Tanksley, Airey, Beck, Ouyang, Deerinck, Ellisman, Sutko: Nonmammalian vertebrate skeletal muscles express two triad junctional foot protein isoforms. in Biophysical journal 1991
Show all 12 Pubmed References
Amphibian Monoclonal RYR1 Primary Antibody for ICC, FACS - ABIN266948
Huang, Cheng, Wang, Shiao, Chen, Hung: High-fructose and high-fat feeding correspondingly lead to the development of lysoPC-associated apoptotic cardiomyopathy and adrenergic signaling-related cardiac hypertrophy. in International journal of cardiology 2016
Most of the ryanodine receptor 1b (ryr1b) mRNA in mutants carried a nonsense mutation that was generated by aberrant splicing due to a DNA insertion in an intron of the ryr1b gene, leading to a hypomorphic condition in relatively relaxed mutants.
sepn1 and ryr1 are required for the same cellular differentiation events and are needed for normal calcium fluxes
findings show alphaRYR & betaRYR use divergent mechanisms to generate molecular variations; alternative splicing generates variants of alphaRYR, whereas presence of SNPs may change the secondary mRNA structure of betaRYR.
All the hit compounds, except for oxolinic acid, inhibited [(3)H]ryanodine binding of WT and mutant RyR1.
Substitution of Gly-4941 with Asp or Lys of RyR1 results in functional channels as indicated by caffeine-induced Ca(2+) release.
RYR1 C6487T polymorphism might be associated with an increased risk of congenital hypospadias in Chinese Han children
Segregation analysis is of limited value in assessing pathogenicity of RYR1 variants in malignant hyperthermia
49 RYR1 variants were identified in 47 cases. In recessive cases, facial weakness, neonatal hypotonia, ophthalmoplegia/paresis, ptosis, and scapular winging were more frequently observed than in dominant/de novo cases. Variant mapping revealed patterns of clinical severity across RyR1 domains, including a structural plane of interest within the RyR1 cytosolic shell, in which 84% of variants affected the bridging solenoid.
Our FRET-based HTS detects RyR binding of accessory proteins calmodulin (CaM) or FKBP12.6...One compound increased FRET and inhibited RyR1, which was only significant at nM [Ca(2+)], and accentuated without CaM present.
Mutations in RYR1 should be considered as a significant cause of rhabdomyolysis and myalgia syndrome in patients with the characteristic combination of rhabdomyolysis, myalgia and cramps, creatine kinase elevation, no weakness and often muscle hypertrophy
The ryanodine receptor 1 (RyR1) is mainly expressed in the sarcoplasmic reticulum (SR) of skeletal muscle and is a calcium release channel which is coupled to the dihydropyridine receptor in the T-tubule of the sarcolemma.
in our series subarachnoid hemorrhage patients have an increased frequency of rare RYR1 variants
Findings signal a potential association between malignant hyperthermia (MH) susceptibility and exertional rhabdomyolysis (ER); the presence of MH-causative mutations and putative deleterious RYR1 variants in ER patients without a history of adverse anesthetic reactions suggests their possible increased risk for MH
Thus, RYR1 mutations may lead to prolonged bleeding by altering vascular smooth muscle cell function. The reversibility of the bleeding phenotype emphasizes the potential therapeutic value of dantrolene in the treatment of such bleeding disorders.
Results show that in disease-associated RYR1 mutations, there is increased gain and Ca(2+) sensitivity for activation in a site-specific manner which suggest that divergent CICR (Ca(2+) -induced Ca(2+) release) activity may cause various disease phenotypes by specific mutations.
the RYR1 SNP rs35364374 was not associated with Aneurysmal Subarachnoid Hemorrhage or its clinical squeal.
level of myotubes MTM1 mutations do not dramatically affect calcium homeostasis and calcium release mediated through the ryanodine receptor 1, though they do affect myotube size and nuclear content..mature muscles such as those obtained from patient muscle biopsies exhibit a significant decrease in expression of the ryanodine receptor 1, a decrease in muscle-specific microRNAs and a considerable up-regulation of HDAC4.
Allosteric mechanism of RyR1, including a key interaction between a peripheral domain and the Ca-binding EF hand domain
fetuses with lethal myopathy were compound heterozygous for a paternally inherited missense variant (c.2113G > A; p.Gly705Arg) and a novel maternally inherited truncating frameshift deletion (c.8843delC; p.Ser2948Cysfs*58)
Data suggest that reduced SOICR (store overload-induced Ca2+ release) threshold is a common defect of malignant hyperthermia- or central core disease-associated RyR1 mutations; carvedilol (a beta-blocker), like dantrolene (a central muscle relaxant), can suppress RyR1-mediated SOICR. Here, human disease-associated point mutations were induced in recombinant rabbit RyR1 via site-directed mutagenesis.
results suggest that nine RyR1 mutants associated with skeletal muscle diseases were differently regulated by Ca(2+) and Mg(2+) Four malignant hyperthermia-associated RyR1 mutations in the S2-S3 loop conferred RyR2-type Ca(2+)- and Mg(2+)-dependent channel regulation
This review summarizes the progress in the structural determination of RyR by cryoEM and, bearing in mind the leap in resolution provided by the recent implementation of direct electron detection, analyzes the first near-atomic structures of RyR.
Data indicate that unlike ryanodine receptor RyRs, inositol 145-trisphosphate receptor IP3Rs are present and continually functional at early stages of cardiomyocyte differentiation.
Gain of Ca(2+)-induced Ca(2+) release activity of RyR1 is markedly lower than that of RyR3 in mammalian skeletal muscle, indicating selective stabilization of RyR1
In-depth structural analyses elucidated a novel channel-gating mechanism and a novel ion selectivity mechanism of RyR1.
the cryo-electron microscopy structures of rabbit RyR1 in three closed conformations at about 4 A resolution and an open state at 5.7 A, are reported.
Data suggest that RyR1 exhibits conformation consistent with an open-channel model sufficient for movement of Ca2+ except for a pore constriction site; molecular dynamics simulations suggest Ca2+ passage could be allowed by rotation of upper portion of pore-lining S6 helix away from 4-fold channel axis and twisting of Ile-4937 at channel constriction site out of the channel pore.
RyR1-G4934A had reduced K(+) conductance and ion selectivity compared with WT. Mutations further increasing the side chain volume at these positions (G4934V and G4941I) resulted in reduced caffeine-induced Ca(2+) release.
Structural insights into the roles of divergent regions in RyR1 allosteric regulation during excitation contraction coupling.
architecture of rabbit RyR1 at a resolution of 6.1 A, using electron cryomicroscopy
closed-state structure of the 2.3-megadalton complex of the rabbit skeletal muscle type 1 RyR (RyR1), solved by single-particle electron cryomicroscopy at an overall resolution of 4.8 A
Diminishing S-palmitoylation directly suppresses RyR1 activity as well as stimulus-coupled Ca(2+) release through RyR1.
Two regions of the ryanodine receptor calcium channel are involved in Ca(2+)-dependent inactivation
Data indicate that S107 increased FKBP12 binding to RyR1 in sarcoplasmic reticulum vesicles in the presence of reduced glutathione and the NO-donor NOC12.
These results suggest that the intersubunit contact region between N-terminal domains of RyR1 is a prime target for disease mutations.
Sequence data of the ATP binding regions of the RyR1 protein was presented.
a 2.2 A resolution crystal structure of the RyR domain revealing a two-fold, symmetric, extended four-helix bundle stabilized by a beta sheet.
Coupled events reveal complex interactions among RyR1, differentially modulated by cytosolic ATP/Mg2+ and Ca2+ under ionic conditions.
3D localization of a SPRY2 domain in RYR1
Both basic and acidic amino acid residues of IpTx(a) are involved in triggering substate of RyR1.
Chloroform extract of hog barn dust modulates skeletal muscle ryanodine receptor calcium-release channel (RyR1).
RyRsl subunit is expressed in corpus cavernosum smooth muscle cells.
phosphorylation and K201 acted similarly to change the conformation of RyR1/2 and regulate FKBP12/12.6 binding.
These results suggest that the heterogeneity of immunological and neuroendocrine response to exercise stress in pigs could be influenced by RYR1 gene mutation.
Interleukin 1, IL-2, IL-10, and TNF-alpha measures were positively intercorrelated in each of the three RYR1 genotype group
T-tubules proximity modulates RyR cluster properties resulting in intracellular heterogeneity of diastolic spark activity.
Results support the hypothesis that Ca(2)(+) binding to CaM's C-terminal acts as the switch converting CaM from a RyR1 activator into a channel inhibitor.
The RYR1 genotype had a significant effect on IGF-2 expression in pig longissimus dorsi muscle.
Binding to RyR1 targets evokes significant changes in calmodulin structure and sensitivity.
Significant interactions between CAST and RYR1 genotypes indicate that the quality of meat influenced by RYR1 genotype may be modified by the simultaneous influence of genotype as regards the CAST locus
Our data suggest that non-coplanar PCBs are more potent and efficacious toward (MH)RyR1 than (Wt)RyR1, and have more profound effects on its cation regulation.
stimulation of the RyR1 malignant hyperthermia susceptible channel caused by affected inter-domain interaction between regions 1 and 2 is an underlying mechanism for dysfunction of Ca2+ homoeostasis seen in the malignant hyperthermia phenotype
altered luminal Ca(2+) regulation of RyR1 represents a primary causal mechanism of malignant hyperthermia
Donor-acceptor distances derived from our FRET measurements provide insights into calmodulin (CaM)'s location and orientation within the RyR1 3D architecture and the conformational switching that underlies CaM regulation of the channel
RYR1 pG2435R mice demonstrated gene dose-dependent in vitro and in vivo responses to pharmacological and environmental stressors that parallel those seen in patients with the human RYR1 variant p.G2434R
Results suggest distinct functional roles for type 1 ryanodine receptor (RYR1) and Ca2+ channels-the 1,4-dihydropyridine receptor (Cav1.1) in skeletal primary and secondary myogenesis.
Results show that MG53-Orai1 interaction enhances extracellular Ca2+ entry via Orai1, and decreases intracellular Ca2+ release via RyR1 for skeletal muscle contraction.
These results suggest that common molecular mechanisms underlie malignant hyperthermia (MH) crises and exertional HS in mice.-
This molecular rearrangement is compatible with direct inhibition of RyR opening by junctophilin-2 to intrinsically stabilise the Ca(2+) signalling properties of the junction and thus the contractile function of the cell.
These data demonstrate that modulating Ryrs has neuroprotective effects in nGD through mechanisms that protect the mitochondria, autophagy, Ryr expression and enhance GCase activity
these findings suggest an important non-contractile role of RyR1 or RYR1-mediated Ca(2+) signaling during muscle organ development.
mutating residue E4242 affects RyR1 structures critical for retrograde communication with CaV1.1
High-intensity interval training exercise induces a ROS-dependent RyR1 fragmentation in muscles of recreationally active subjects, and the resulting changes in muscle fiber Ca(2+)-handling trigger muscular adaptations
The present study reveals that the C-terminal of the beta1a subunit changes conformation in the presence of RyR1 consistent with an interaction between the C-terminal of beta1a and RyR1 in resting myotubes.
Ryanodine receptor sensitization results in abnormal calcium signaling in airway smooth muscle cells.
major finding from this study is the novel region- and cell-specific relationship between the localization of the plasma membrane Kv2.1 channel and intracellular RyR Ca2+ release channels
RyR1 is required for proper release of transmitter at the neuromuscular junction, and postsynaptic RyR1 is required for the size and distribution of acetylcholine receptor clusters.
Spindle abnormalities precede those in extrafusal fibers, indicating that they are a primary pathological feature in this murine Ryr1-related core myopathy. [review]
The motif Leu(496)-Leu(500)-Trp(503) within the bet1a C-terminal tail plays a nonessential role in the bidirectional DHPR/RyR1 signaling that supports skeletal-type excitation-contraction coupling.
these results provide novel evidence that CaN regulates ASMC Ca(2+) sparks specifically through RyR1, which plays an important role in the control of Ca(2+) signaling and contraction in ASMCs.
Results suggest that RyR1 and RyR2 expressed by Purkinje and granule cells play important roles in promoting the dendritic differentiation of Purkinje cells and that RyR2 expressed by granule cells is involved in the secretion of BDNF from granule cells
CaM-binding domain of RyR2 is an important determinant of Ca2+-release termination and activation.
This gene encodes a ryanodine receptor found in skeletal muscle. The encoded protein functions as a calcium release channel in the sarcoplasmic reticulum but also serves to connect the sarcoplasmic reticulum and transverse tubule. Mutations in this gene are associated with malignant hyperthermia susceptibility, central core disease, and minicore myopathy with external ophthalmoplegia. Alternatively spliced transcripts encoding different isoforms have been described.
ryanodine receptor 1 (skeletal)
, ryanodine receptor type 1
, ryanodine receptor 1a (slow muscle)
, ryanodine receptor alpha isoform
, central core disease of muscle
, ryanodine receptor 1
, sarcoplasmic reticulum calcium release channel
, skeletal muscle calcium release channel
, skeletal muscle ryanodine receptor
, type 1-like ryanodine receptor
, skeletal muscle-type ryanodine receptor
, type 1 ryanodine receptor
, ryanodine receptor 1, skeletal muscle
, ryanodine receptor 1-like, skeletal muscle
, calcium release channel
, porcine stress syndrome