Academic literature on the topic 'RyR3'

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Journal articles on the topic "RyR3"

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Dabertrand, Fabrice, Nicolas Fritz, Jean Mironneau, Nathalie Macrez, and Jean-Luc Morel. "Role of RYR3 splice variants in calcium signaling in mouse nonpregnant and pregnant myometrium." American Journal of Physiology-Cell Physiology 293, no. 3 (2007): C848—C854. http://dx.doi.org/10.1152/ajpcell.00069.2007.

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Alternative splicing of ryanodine receptor subtype 3 (RYR3) may generate a short isoform (RYR3S) without channel function and a functional full-length isoform (RYR3L). The RYR3S isoform has been shown to negatively regulate the native RYR2 subtype in smooth muscle cells as well as the RYR3L isoform when both isoforms were coexpressed in HEK-293 cells. Mouse myometrium expresses only the RYR3 subtype, but the role of RYR3 isoforms obtained by alternative splicing and their activation by cADP-ribose during pregnancy have never been investigated. Here, we show that both RYR3S and RYR3L isoforms a
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Zheng, Yun-Min, Qing-Song Wang, Rakesh Rathore, et al. "Type-3 Ryanodine Receptors Mediate Hypoxia-, but Not Neurotransmitter-induced Calcium Release and Contraction in Pulmonary Artery Smooth Muscle Cells." Journal of General Physiology 125, no. 4 (2005): 427–40. http://dx.doi.org/10.1085/jgp.200409232.

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In this study we examined the expression of RyR subtypes and the role of RyRs in neurotransmitter- and hypoxia-induced Ca2+ release and contraction in pulmonary artery smooth muscle cells (PASMCs). Under perforated patch clamp conditions, maximal activation of RyRs with caffeine or inositol triphosphate receptors (IP3Rs) with noradrenaline induced equivalent increases in [Ca2+]i and Ca2+-activated Cl− currents in freshly isolated rat PASMCs. Following maximal IP3-induced Ca2+ release, neither caffeine nor chloro-m-cresol induced a response, whereas prior application of caffeine or chloro-m-cre
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Protasi, Feliciano, Alexander Shtifman, Fred J. Julian, and Paul D. Allen. "All three ryanodine receptor isoforms generate rapid cooling responses in muscle cells." American Journal of Physiology-Cell Physiology 286, no. 3 (2004): C662—C670. http://dx.doi.org/10.1152/ajpcell.00081.2003.

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The rapid cooling (RC) response in muscle is an increase in cytoplasmic Ca2+concentration ([Ca2+]i) that is probably caused by Ca2+release from the sarcoplasmic reticulum (SR). However, the molecular bases of this response have not been completely elucidated. Three different isoforms of the SR Ca2+release channels, or ryanodine receptors (RyRs), have been isolated (RyR1, RyR2, and RyR3). In the current investigation, the RC response was studied in RyR-null muscle cells (1B5) before and after transduction with HSV-1 virions containing the cDNAs encoding for RyR1, RyR2, or RyR3. Cells were loade
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Giannini, G., A. Conti, S. Mammarella, M. Scrobogna, and V. Sorrentino. "The ryanodine receptor/calcium channel genes are widely and differentially expressed in murine brain and peripheral tissues." Journal of Cell Biology 128, no. 5 (1995): 893–904. http://dx.doi.org/10.1083/jcb.128.5.893.

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Ryanodine receptors (RyRs) are intracellular calcium release channels that participate in controlling cytosolic calcium levels. At variance with the probably ubiquitous inositol 1,4,5-trisphosphate-operated calcium channels (1,4,5-trisphosphate receptors), RyRs have been mainly regarded as the calcium release channels controlling skeletal and cardiac muscle contraction. Increasing evidence has recently suggested that RyRs may be more widely expressed, but this has never been extensively examined. Therefore, we cloned three cDNAs corresponding to murine RyR homologues to carry a comprehensive a
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Tian, Chengju, Caronda J. Moore, Puttappa Dodmane, et al. "Dust from hog confinement facilities impairs Ca2+ mobilization from sarco(endo)plasmic reticulum by inhibiting ryanodine receptors." Journal of Applied Physiology 114, no. 5 (2013): 665–74. http://dx.doi.org/10.1152/japplphysiol.00661.2012.

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Individuals working in commercial hog confinement facilities have elevated incidences of headaches, depression, nausea, skeletal muscle weakness, fatigue, gastrointestinal disorders, and cardiovascular diseases, and the molecular mechanisms for these nonrespiratory ailments remain incompletely undefined. A common element underlying these diverse pathophysiologies is perturbation of intracellular Ca2+ homeostasis. This study assessed whether the dust generated inside hog confinement facilities contains compounds that alter Ca2+ mobilization via ryanodine receptors (RyRs), key intracellular chan
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OTTINI, Laura, Giovanna MARZIALI, Antonio CONTI, Alexandra CHARLESWORTH та Vincenzo SORRENTINO. "α and β isoforms of ryanodine receptor from chicken skeletal muscle are the homologues of mammalian RyR1 and RyR3". Biochemical Journal 315, № 1 (1996): 207–16. http://dx.doi.org/10.1042/bj3150207.

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To define the relationship between the two ryanodine receptor (RyR) isoforms present in chicken skeletal muscle, we cloned two groups of cDNAs encoding the chicken homologues of mammalian RyR1 and RyR3. Equivalent amounts of the two chicken isoform mRNAs were detected in thigh and pectoral skeletal muscles. RyR1 and RyR3 mRNAs were co-expressed in testis and cerebellum whereas RyR3 mRNA was expressed also in cerebrum and heart. The full-length sequence of the chicken RyR3 cDNA was established. The RyR3 receptor from chicken had the same general structure as mammalian and amphibian RyRs. The 15
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Perez, Claudio F., José R. López, and Paul D. Allen. "Expression levels of RyR1 and RyR3 control resting free Ca2+ in skeletal muscle." American Journal of Physiology-Cell Physiology 288, no. 3 (2005): C640—C649. http://dx.doi.org/10.1152/ajpcell.00407.2004.

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To better understand the role of the transient expression of ryanodine receptor (RyR) type 3 (RyR3) on Ca2+ homeostasis during the development of skeletal muscle, we have analyzed the effect of expression levels of RyR3 and RyR1 on the overall physiology of cultured myotubes and muscle fibers. Dyspedic myotubes were infected with RyR1 or RyR3 containing virions at 0.2, 0.4, 1.0, and 4.0 moieties of infection (MOI), and analysis of their pattern of expression, caffeine sensitivity, and resting free Ca2+ concentration ([Ca2+]r) was performed. Although increased MOI resulted in increased expressi
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Vanterpool, Conwin K., Elaine A. Vanterpool, William J. Pearce, and John N. Buchholz. "Advancing age alters the expression of the ryanodine receptor 3 isoform in adult rat superior cervical ganglia." Journal of Applied Physiology 101, no. 2 (2006): 392–400. http://dx.doi.org/10.1152/japplphysiol.00167.2006.

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Sympathetic nerves arising from the superior cervical ganglion (SCG) protect the cerebrovasculature during periods of acute hypertension and may play a role in homeostasis of target organs. The functions of these nerves depend on calcium release triggered by activation of ryanodine receptor (RyR) channels. The function of RyR channels is in part dependent on genetic expression and regulation by numerous protein modulators such as neuronal nitric oxide synthase (nNOS) neurons also found in the SCG. We have shown that release of calcium in SCG cells is altered during late maturation and advancin
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Rossi, Daniela, Ilenia Simeoni, Marcella Micheli, et al. "RyR1 and RyR3 isoforms provide distinct intracellular Ca2+signals in HEK 293 cells." Journal of Cell Science 115, no. 12 (2002): 2497–504. http://dx.doi.org/10.1242/jcs.115.12.2497.

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Ryanodine receptors (RyRs) are expressed on the endoplasmic reticulum of many cells, where they form intracellular Ca2+-release channels that participate in the generation of intracellular Ca2+ signals. Here we report studies on the intracellular localisation and functional properties of transfected RyR1 or RyR3 channels in HEK 293 cells. Immunofluorescence studies indicated that both RyR1 and RyR3 did not form clusters but were homogeneously distributed throughout the endoplasmic reticulum. Ca2+ release experiments showed that transfected RyR1 and RyR3 channels responded to caffeine, although
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CONTI, Antonio, L. GORZA, and Vincenzo SORRENTINO. "Differential distribution of ryanodine receptor type 3 (RyR3) gene product in mammalian skeletal muscles." Biochemical Journal 316, no. 1 (1996): 19–23. http://dx.doi.org/10.1042/bj3160019.

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Activation of intracellular Ca2+-release channels/ryanodine receptors (RyRs) is a fundamental step in the regulation of muscle contraction. In mammalian skeletal muscle, Ca2+-release channels containing the type 1 isoform of RyR (RyR1) open to release Ca2+ from the sarcoplasmic reticulum (SR) upon stimulation by the voltage-activated dihydropyridine receptor on the T-tubule/plasma membrane. In addition to RyR1, low levels of the mRNA of the RyR3 isoform have been recently detected in mammalian skeletal muscles. Here we report data on the distribution of the RyR3 gene product in mammalian skele
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Dissertations / Theses on the topic "RyR3"

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BONCORAGLIO, GIORGIO BATTISTA. "Role of Ryanodine Receptor type 3 (RyR3) in ischemic stroke." Doctoral thesis, Università degli Studi di Milano-Bicocca, 2021. http://hdl.handle.net/10281/317052.

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L'ictus è una delle principali cause di mortalità e disabilità acquisita in tutto il mondo. Il primo studio di associazione genome-wide in pazienti con ictus ischemico italiano ha trovato un'associazione significativa con il polimorfismo missenso a singolo nucleotide (SNP) rs4780144 nel gene del recettore della rianodina di tipo 3 (RyR3), che porta a una potenziale perdita di funzione. Molteplici evidenze hanno suggerito che una ridotta funzione di RyR3 potrebbe migliorare l'esito dell'ictus. Con questo studio abbiamo mirato a indagare il ruolo di RyR3 nell'ictus ischemico a livello funzionale
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Dabertrand, Fabrice. "Identification et rôle fonctionnels de variants d'épissage du récepteur de la ryanodine de type 3 (RyR3)." Bordeaux 2, 2006. http://www.theses.fr/2006BOR21351.

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La fonction du sous-type RYR 3 du récepteur de la ryanodine ne peut se comprendre qu'à travers l'étude de ses différents variants d'épissage. Dans les muscles lisses de souris, nous avons mis en évidence l'existence d'un variant court dominant négatif. En effet, dans le duodenum, celui-ci inhibe le sous-type RYR 2 responsable de la libération du calcium stocké dans le reticulum. L'isoforme complète de RYR3 n'interagit pas avec l'isoforme courte et code des oscillations calciques spontanées lors d'une surharge du contenu en calcium du reticulum. Enfin, cet épissage alternatif est modulé dans le
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Chameau, Pascal. "Le recepteur de la ryanodine de type 3 (ryr3) : localisation et role dans l'excitabilite neuronale et la transmission synaptique." Paris 6, 1999. http://www.theses.fr/1999PA066101.

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Le recepteur de la ryanodine de type 3 (ryr3), exprime dans les neurones, est l'isoforme la moins caracterisee de cette famille de recepteurs-canaux ca 2 + du reticulum endoplasmique. J'ai developpe un anticorps polyclonal dirige contre ryr3 qui m'a permis de determiner la localisation de cette isoforme dans la region proximale des dendrites apicaux des neurones pyramidaux de la region ca1 de l'hippocampe de souris. Cet anticorps s'est avere bloquant du mecanisme de calcium-induced calcium release (cicr) dans lequel ryr3 est implique. Dans les neurones ca1, l'injection de l'anticorps anti-ryr3
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Whiteley, Gareth. "Molecular architecture of Caveolin-3 and the investigation of an interaction with the ryanodine receptor." Thesis, University of Manchester, 2012. https://www.research.manchester.ac.uk/portal/en/theses/molecular-architecture-of-caveolin3-and-the-investigation-of-an-interaction-with-the-ryanodine-receptor(d5d4e1f1-88c5-4619-b208-7742d0cd81f5).html.

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The muscle-specific membrane protein, Caveolin-3, is a building block of caveolae a type of specialised lipid raft. Caveolin-3 is proposed to play a central role in variety of cellular functions both structural and functional, from cell signalling to cholesterol homeostasis. Caveolin-3 has also been implicated in processes involved in targeting membrane proteins to the plasma membrane, as well as mediating a host of cell signalling processes. Initial attempts were made to express full-length Caveolin-3 in E.coli. However, more success was achieved in expressing and purifying domains of Caveoli
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King, James Harmsworth. "Arrhythmogenic mechanisms in RYR2-P2328S murine hearts." Thesis, University of Cambridge, 2014. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.648837.

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Klipp, Robert Carl. "Novel Compound, 84F2, Inhibits Calmodulin Deficient RyR2." PDXScholar, 2017. https://pdxscholar.library.pdx.edu/open_access_etds/3484.

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The cardiac ryanodine receptor (RyR2) plays a key role in excitation-contraction coupling (ECC). Mutations in RyR2 are known to be linked to the arrhythmogenic disorder, catecholaminergic polymorphic ventricular tachycardia (CPVT), a deadly disease which is characterized by a leak of calcium from sarcoplasmic reticulum and a decrease in calmodulin (CaM) binding. A novel drug, 84F2, shown to inhibit arrhythmias in RyR2-R176Q heterozygous CPVT mouse hearts (2.5 µg/kg), decrease spark frequency in cells derived from CPVT mice (IC50 = 35 nM), and inhibit RyR2 single channel activity at low nanomol
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Wang, YueYi. "Ca2+ handling in a mice model of CPVT." Thesis, Université Paris-Saclay (ComUE), 2016. http://www.theses.fr/2016SACLS156/document.

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Le canal calcique de libération du Ca2+, appelé récepteur à la ryanodine (RyR) est localisé dans la membrane du réticulum sarcoplasmique des cardiomyocytes, en incluant ceux du pacemaker, et a un rôle important dans le couplage excitation contraction et la génération du rythme cardiaque. Des mutations dans leur gène sont responsables de la tachycardie catécholergique (CPVT), qui est une maladie létale, manifestée par des syncopes ou mort subite lors de stress émotionnel ou physique. Au repos, ces patients ont un électrocardiogramme normal, mais une tendance plus importante à la bradycardie.Nos
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Yin, Liheng. "Impact of the catecholaminergic polymorphic ventricular tachycardia (CPVT) mutation RyR2R420Q in cell function." Thesis, université Paris-Saclay, 2020. http://www.theses.fr/2020UPASS068.

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La tachycardie ventriculaire polymorphe catécholergique (CPVT) est une arythmie génétique létale qui se manifeste par une syncope ou une mort subite chez les enfants et les jeunes adultes dans des conditions de stress sans anomalie structurelle cardiaque évidente. Plusieurs mécanismes ont été proposés pour expliquer les altérations fonctionnelles sous-jacentes de la libération de Ca2+ dues aux mutations de RyR2 ou de ses protéines accessoires. Une nouvelle mutation CPVT située sur la partie N terminale de RyR2 a été identifiée dans une famille espagnole (RyR2R420Q). Ici, nous avons utilisé un
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Kathirvel, Paramasivam. "Mapping and manipulation of the murine ryanodine receptor gene (Ryr1)." Thesis, University of Edinburgh, 2000. http://hdl.handle.net/1842/12330.

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In this present study, experiments were carried out a) to characterise the mouse skeletal muscle ryanodine receptor (<i>Ryr1)</i> gene cDNA, b) to construct a contiguous map of the murine Ryr1 gene and c) to evaluate the phenotype of the <i>Ryr1</i> knockout transgenic mice and to develop a mouse model, which carries a homologue of the C1843T mutation, associated with MH in pigs and some humans. The murine <i>Ryrl</i> cDNA has been characterised by cDNA cloning and sequence analysis. Murine <i>Ryrl</i> exon-specific RT-PCR primers were designed and used to generate <i>Ryrl</i> cDNA fragments f
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Nicoll, Baines Katie Mhairi. "Muscle energetics and ageing in the context of RYR1 variants." Thesis, University of Leeds, 2017. http://etheses.whiterose.ac.uk/17288/.

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In aged muscle, from humans and mice, the ryanodine receptor (RyR1) is leaky, leading to increased levels of resting Ca2+ in the myoplasm. This is also a feature of skeletal muscle disorders caused by variants in RyR1 such as malignant hyperthermia (MH), central core disease (CCD), exertional heat illness (EHI) and late-onset axial myopathy (LOAM). Elevated Ca2+ is damaging to mitochondria, leading to production of reactive oxygen and nitrogen species associated with MH susceptibility to inhalational anaesthetics. Mice with Ryr1 variants show premature muscle ageing and highlight the cycle of
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Books on the topic "RyR3"

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Sörqvist, Kia. Lane-Ryr hembygdsbok. Lane-Ryrs hembygdsfören., 1985.

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RYRY Typography Octavo. Blurb, 2015.

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Robertson, Will C. Ryr: Rich Young Ruler. Covenant Books, 2020.

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Dialektord från Örs och Sundals-Ryrs socknar på Dal. 5th ed. Calluna, 2010.

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Schwartz, Peter J., and Lia Crotti. Monogenic and oligogenic cardiovascular diseases: genetics of arrhythmias—catecholaminergic polymorphic ventricular tachycardia. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780198784906.003.0152.

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Catecholaminergic polymorphic ventricular tachycardia (CPVT) is a rare inherited disorder associated with syncope and sudden death manifesting in the young during sympathetic activation. The electrocardiogram is normal and the heart is structurally normal. The diagnosis is usually made with an exercise stress test that shows a typical pattern of onset and offset of adrenergically induced ventricular arrhythmias. Molecular screening of RyR2, the major CPVT gene, is recommended whenever the suspicion of CPVT is high. If a disease-causing mutation is identified, cascade screening allows pre-sympt
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Book chapters on the topic "RyR3"

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Nederend, Ineke, Christian van der Werf, and Arthur A. M. Wilde. "RyR2 in Cardiac Disorders." In Pathologies of Calcium Channels. Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-40282-1_29.

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Aracena, Paula, Cecilia Hidalgo, and Susan L. Hamilton. "RYR1 Modulation by Calmodulin." In Ryanodine Receptors. Springer US, 2005. http://dx.doi.org/10.1007/0-387-23188-9_16.

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Van Petegem, Filip, and Kelvin Lau. "Ryanodine Receptor (RyR)." In Encyclopedia of Signaling Molecules. Springer International Publishing, 2018. http://dx.doi.org/10.1007/978-3-319-67199-4_99.

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Martemyanov, Kirill A., Pooja Parameswaran, Irene Aligianis, et al. "Ryanodine Receptor (RyR)." In Encyclopedia of Signaling Molecules. Springer New York, 2012. http://dx.doi.org/10.1007/978-1-4419-0461-4_99.

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Parness, Jerome. "The Dantrolene Binding Site on RYR1." In Ryanodine Receptors. Springer US, 2005. http://dx.doi.org/10.1007/0-387-23188-9_24.

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Besch, Henry R., Chun Hong Shao, and Keshore R. Bidasee. "Ryanoids, Receptor Affinity and RYR Channel Subconductance." In Ryanodine Receptors. Springer US, 2005. http://dx.doi.org/10.1007/0-387-23188-9_18.

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Patel, Seema, and Nadeem Akhtar. "Fungus Monascus-Fermented Red Yeast Rice (RYR): Natural Therapeutic Statin Source or Mycotoxin?" In Fungi and their Role in Sustainable Development: Current Perspectives. Springer Singapore, 2018. http://dx.doi.org/10.1007/978-981-13-0393-7_38.

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Koivumaki, J. T., J. Takalo, T. Korhonen, M. Weckstrom, and P. Tavi. "Calcium Dependent Release and Its Regulation in Cardiac Myocytes: Mathematical Model of the RyR Channel." In IFMBE Proceedings. Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-642-03882-2_179.

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MacLennan, David H. "Mutations in the Skeletal Muscle Ryanodine Receptor (RYR1) Gene are Linked to Malignant Hyperthermia and Central-Core Disease." In Malignant Hyperthermia. Springer Japan, 1996. http://dx.doi.org/10.1007/978-4-431-68346-9_12.

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Sako, Shinji, Ryuichi Yamamoto, and Tadashi Kitamura. "Ryry: A Real-Time Score-Following Automatic Accompaniment Playback System Capable of Real Performances with Errors, Repeats and Jumps." In Active Media Technology. Springer International Publishing, 2014. http://dx.doi.org/10.1007/978-3-319-09912-5_12.

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Conference papers on the topic "RyR3"

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Fonseca, Alulin Tácio Quadros Santos Monteiro. "Genetic profiling of RYR1- related myopathy in a tertiary neuromuscular center." In XIV Congresso Paulista de Neurologia. Zeppelini Editorial e Comunicação, 2023. http://dx.doi.org/10.5327/1516-3180.141s1.518.

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Introduction: The RYR1 gene encodes the skeletal muscle ryanodine channel, an ion channel responsible for regulating calcium release from the sarcoplasmic reticulum. Variants in RYR1 are cause of a wide phenotype of myopathies, with autosomal dominant and recessive inheritance. Objectives: In this work we present the clinical and genetic data of 43 patients with myopathies presumably related to the RYR1 gene, carrying 47 different variants Material and methods: Clinical and genetic data are presented. RYR1 gene were analyzed by next-generation sequencing. Results: Twenty patients have an autos
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Wilson, Kirsty, Maslinda Musa, Lynne Bingle, C. Jeremy Craven, and Colin D. Bingle. "Vomeromodulin/RYF3: PLUNC’s Most Distant Cousin." In American Thoracic Society 2011 International Conference, May 13-18, 2011 • Denver Colorado. American Thoracic Society, 2011. http://dx.doi.org/10.1164/ajrccm-conference.2011.183.1_meetingabstracts.a2090.

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Ryvkin, Alexander, and Nikita Markov. "RyRs Coupling Causes a Calcium Leak in Cardiac Cell." In 2018 Computing in Cardiology Conference. Computing in Cardiology, 2018. http://dx.doi.org/10.22489/cinc.2018.323.

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Hermann, Katharina, Katja Kloth, Jessika Johannsen, and Jonas Denecke. "P 1147. Pyridostigmine Leads to Relevant Improvement of Motor Function in an Infant with RYR1-Related Congenital Myopathy." In Abstracts of the 44th Annual Meeting of the Society for Neuropediatrics. Georg Thieme Verlag KG, 2018. http://dx.doi.org/10.1055/s-0038-1676024.

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Lu, Haiquan, and Gregg Semenza. "Abstract 3066: Chemotherapy-induced GSTO1 interacts with ryanodine receptor RYR1 to trigger Ca2+-dependent breast cancer stem cell enrichment." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-3066.

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Souvannakitti, Dangjai, Guoxiang Yuan, Jayasri Nanduri, Ganesh K. Kumar, Aaron Fox, and Nanduri R. Prabhakar. "Intermittent Hypoxia Activates Ryanodine Receptors (RyRs) Via S-glutathionylation In Neonatal Rat Adrenal Chromaffin Cells And Contributes To Augmented Catecholamines secretion." In American Thoracic Society 2010 International Conference, May 14-19, 2010 • New Orleans. American Thoracic Society, 2010. http://dx.doi.org/10.1164/ajrccm-conference.2010.181.1_meetingabstracts.a2479.

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Resende, Ana Flávia Morais, Guilherme Rabelo Nasuk, Bruna Calixto de Jesus, Allan Luis Barboza Atum, and José Antônio Silva Júnior. "EXPRESSÃO MIOCÁRDICA RELACIONADA À CINÉTICA DO CÁLCIO EM ANIMAIS COM EXPOSIÇÃO PRÉ-NATAL AO ÁLCOOL." In Congresso Médico Acadêmico da Universidade Nove de Julho. Universidade Nove de Julho, 2022. http://dx.doi.org/10.5585/comamedvg.2022.16.

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Introdução: A exposição alcoólica pré-natal (E.P.A.) é considerada uma das principais responsáveis pelas alterações congênitas humanas. No sistema cardiovascular, a E.P.A. pode levar a alterações na expressão de genes relacionados à homeostase cardiovascular. Estudos têm mostrado que miócitos cardíacos expostos ao etanol durante a embriogênese não amadurecem morfológica ou funcionalmente, bem como apresentam alterações no transporte e captação/ligação de Ca2+ pelo retículo sarcoplasmático (SR). Uma diminuição da concentração citosólica de Ca2+ resultante do um efeito inibitório do álcool nas p
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Reports on the topic "RyR3"

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Klipp, Robert. Novel Compound, 84F2, Inhibits Calmodulin Deficient RyR2. Portland State University Library, 2000. http://dx.doi.org/10.15760/etd.5368.

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Zhao, Fangfang, Chunli Lu, Luying Chen, et al. Red yeast rice preparations for dyslipidemia: A protocol for an overview of systematic review and meta-analysis. INPLASY - International Platform of Registered Systematic Review and Meta-analysis Protocols, 2022. http://dx.doi.org/10.37766/inplasy2022.3.0032.

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Review question / Objective: What is the quality of systematic reviews/meta-analysis of red yeast rice (RYR) preparations for dyslipidemia? What is the comparative benefit of red yeast rice preparations on dyslipidemia compared to other lipid-lowering drugs? Based on the current controversies in dyslipidemia guidelines and clinical practice, to explore the relative benefits of red yeast rice compared with other lipid-lowering drugs, we plan to perform an overview of existing SRs/MAs. Condition being studied: Red yeast rice (RYR) has been used as an alternative to statin therapy in treating pat
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Dornan, Thomas. Antioxidant Anthocyanidins and Calcium Transport Modulation of the Ryanodine Receptor of Skeletal Muscle (RyR1). Portland State University Library, 2000. http://dx.doi.org/10.15760/etd.319.

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Dornan, Thomas. Calcium Transport Inhibition, Stimulation, and Light Dependent Modulation of the Skeletal Calcium Release Channel (RyR1) by the Prototropic Forms of Pelargonidin. Portland State University Library, 2000. http://dx.doi.org/10.15760/etd.1930.

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