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Journal articles on the topic 'RYRO'

Author: Grafiati

Published: 4 June 2021

Last updated: 9 February 2022

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1

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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2

Yang, Xiao-Ru, Mo-Jun Lin, Kay-Pong Yip, et al. "Multiple ryanodine receptor subtypes and heterogeneous ryanodine receptor-gated Ca2+ stores in pulmonary arterial smooth muscle cells." American Journal of Physiology-Lung Cellular and Molecular Physiology 289, no. 2 (2005): L338—L348. http://dx.doi.org/10.1152/ajplung.00328.2004.

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Ryanodine receptors (RyRs) of pulmonary arterial smooth muscle cells (PASMCs) play important roles in major physiological processes such as hypoxic pulmonary vasoconstriction and perinatal pulmonary vasodilatation. Recent studies show that three subtypes of RyRs are coexpressed and RyR-gated Ca2+ stores are distributed heterogeneously in systemic vascular myocytes. However, the molecular identity and subcellular distribution of RyRs have not been examined in PASMCs. In this study we detected mRNA and proteins of all three subtypes in rat intralobar PASMCs using RT-PCR and Western blot. Quantit

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3

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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4

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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5

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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6

Vaithianathan, Thirumalini, Damodaran Narayanan, Maria T. Asuncion-Chin, et al. "Subtype identification and functional characterization of ryanodine receptors in rat cerebral artery myocytes." American Journal of Physiology-Cell Physiology 299, no. 2 (2010): C264—C278. http://dx.doi.org/10.1152/ajpcell.00318.2009.

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Ryanodine receptors (RyRs) regulate contractility in resistance-size cerebral artery smooth muscle, yet their molecular identity, subcellular location, and phenotype in this tissue remain unknown. Following rat resistance-size cerebral artery myocyte sarcoplasmic reticulum (SR) purification and incorporation into POPE-POPS-POPC (5:3:2; wt/wt) bilayers, unitary conductances of 110 ± 8, 334 ± 15, and 441 ± 27 pS in symmetric 300 mM Cs+ were usually detected. The most frequent (34/40 bilayers) conductance (334 pS) decreased to ≤100 pS when Cs+ was replaced with Ca2+. The predominant conductance d

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7

Meissner, Gerhard. "The structural basis of ryanodine receptor ion channel function." Journal of General Physiology 149, no. 12 (2017): 1065–89. http://dx.doi.org/10.1085/jgp.201711878.

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Large-conductance Ca2+ release channels known as ryanodine receptors (RyRs) mediate the release of Ca2+ from an intracellular membrane compartment, the endo/sarcoplasmic reticulum. There are three mammalian RyR isoforms: RyR1 is present in skeletal muscle; RyR2 is in heart muscle; and RyR3 is expressed at low levels in many tissues including brain, smooth muscle, and slow-twitch skeletal muscle. RyRs form large protein complexes comprising four 560-kD RyR subunits, four ∼12-kD FK506-binding proteins, and various accessory proteins including calmodulin, protein kinases, and protein phosphatases

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8

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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9

Van Petegem, Filip. "The Ryanodine Receptor: Arrhythmias and Muscle Disorders at High Resolution." Acta Crystallographica Section A Foundations and Advances 70, a1 (2014): C798. http://dx.doi.org/10.1107/s2053273314092018.

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Calcium ions play crucial roles in our bodies, acting as second messengers in multiple signaling pathways. The resting calcium levels in the cytosol are very low, but can increase rapidly and transiently by influx from the extracellular space, or by release from intracellular stores. The Endoplasmic and Sarcoplasmic Reticulum (ER/SR) form major intracellular calcium stores. The `Ryanodine Receptor' (RyR) is a protein that dictates calcium release from the ER/SR. It forms a huge ion channel with a molecular weight exceeding 2 MegaDalton. RyRs are expressed in multiple cell types, but are partic

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10

Marks, A. R. "Intracellular calcium-release channels: regulators of cell life and death." American Journal of Physiology-Heart and Circulatory Physiology 272, no. 2 (1997): H597—H605. http://dx.doi.org/10.1152/ajpheart.1997.272.2.h597.

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Intracellular Ca2+-release channels on the sarcoplasmic reticulum of striated muscle [ryanodine receptors (RyRs)] and on the endoplasmic reticulum of almost all types of cells [inositol 1,4,5-trisphosphate receptors (IP3Rs)] comprise a unique family of molecules that are structurally and functionally distinct from all other known ion channels. These channels play crucial roles in Ca2+-mediated signaling that triggers excitation-contraction coupling, T-lymphocyte activation, fertilization, and many other cellular functions. Three forms of RyR have been identified: RyR1, expressed predominantly

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11

Morrissette, Jeffery, Le Xu, Alexandra Nelson, Gerhard Meissner, and Barbara A. Block. "Characterization of RyR1-slow, a ryanodine receptor specific to slow-twitch skeletal muscle." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 279, no. 5 (2000): R1889—R1898. http://dx.doi.org/10.1152/ajpregu.2000.279.5.r1889.

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Two distinct skeletal muscle ryanodine receptors (RyR1s) are expressed in a fiber type–specific manner in fish skeletal muscle (11). In this study, we compare [3H]ryanodine binding and single channel activity of RyR1-slow from fish slow-twitch skeletal muscle with RyR1-fast and RyR3 isolated from fast-twitch skeletal muscle. Scatchard plots indicate that RyR1-slow has a lower affinity for [3H]ryanodine when compared with RyR1-fast. In single channel recordings, RyR1-slow and RyR1-fast had similar slope conductances. However, the maximum open probability (Po) of RyR1-slow was threefold less tha

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12

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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13

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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14

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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15

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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16

Jo, Michiko, Andrea N. Trujillo, Ying Yang, and Jerome W. Breslin. "Evidence of functional ryanodine receptors in rat mesenteric collecting lymphatic vessels." American Journal of Physiology-Heart and Circulatory Physiology 317, no. 3 (2019): H561—H574. http://dx.doi.org/10.1152/ajpheart.00564.2018.

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In the current study, the potential contributions of ryanodine receptors (RyRs) to intrinsic pumping and responsiveness to substance P (SP) were investigated in isolated rat mesenteric collecting lymphatic vessels. Responses to SP were characterized in lymphatic vessels in the absence or presence of pretreatment with nifedipine to block L-type Ca2+ channels, caffeine to block normal release and uptake of Ca2+ from the sarcoplasmic reticulum, ryanodine to block all RyR isoforms, or dantrolene to more selectively block RyR1 and RyR3. RyR expression and localization in lymphatics was also assesse

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17

MOUTON, Jérôme, Isabelle MARTY, Michel VILLAZ, Anne FELTZ, and Yves MAULET. "Molecular interaction of dihydropyridine receptors with type-1 ryanodine receptors in rat brain." Biochemical Journal 354, no. 3 (2001): 597–603. http://dx.doi.org/10.1042/bj3540597.

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In striated muscles, Ca2+ release from internal stores through ryanodine receptor (RyR) channels is triggered by functional coupling to voltage-activated Ca2+ channels known as dihydropyridine receptors (DHPRs) located in the plasma membrane. In skeletal muscle, this occurs by a direct conformational link between the tissue-specific DHPR (Cav1.1) and RyR1, whereas in the heart the signal is carried from the cardiac-type DHPR (Cav1.2) to RyR2 by calcium ions acting as an activator. Subtypes of both channels are expressed in the central nervous system, but their functions and mechanisms of coupl

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18

Flucher, Bernhard E., Antonio Conti, Hiroshi Takeshima, and Vincenzo Sorrentino. "Type 3 and Type 1 Ryanodine Receptors Are Localized in Triads of the Same Mammalian Skeletal Muscle Fibers." Journal of Cell Biology 146, no. 3 (1999): 621–30. http://dx.doi.org/10.1083/jcb.146.3.621.

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The type 3 ryanodine receptor (RyR3) is a ubiquitous calcium release channel that has recently been found in mammalian skeletal muscles. However, in contrast to the skeletal muscle isoform (RyR1), neither the subcellular distribution nor the physiological role of RyR3 are known. Here, we used isoform-specific antibodies to localize RyR3 in muscles of normal and RyR knockout mice. In normal hind limb and diaphragm muscles of young mice, RyR3 was expressed in all fibers where it was codistributed with RyR1 and with the skeletal muscle dihydropyridine receptor. This distribution pattern indicates

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19

Haseeb, Mohsin, and Paul D. Thompson. "The effect of statins on RyR and RyR-associated disease." Journal of Applied Physiology 131, no. 2 (2021): 661–71. http://dx.doi.org/10.1152/japplphysiol.01003.2020.

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We sought to review the effects of statins on the ryanodine receptor (RyR) and on RyR-associated diseases, with an emphasis on catecholaminergic polymorphic ventricular tachycardia (CPVT). Statins can affect skeletal muscle and produce statin-associated muscle symptoms (SAMS) but have no adverse effects on cardiac muscle. These contrasting effects may be due to differences in how statins affect the skeletal (RyR1) and cardiac (RyR2) RyR. We searched PubMed to identify English language articles reporting the pathophysiology of the RyR, the effect of statins on RyR function, and on RyR-associate

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Lifshitz, Lawrence M., Jeffrey D. Carmichael, F. Anthony Lai, et al. "Spatial organization of RYRs and BK channels underlying the activation of STOCs by Ca2+ sparks in airway myocytes." Journal of General Physiology 138, no. 2 (2011): 195–209. http://dx.doi.org/10.1085/jgp.201110626.

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Short-lived, localized Ca2+ events mediate Ca2+ signaling with high efficiency and great fidelity largely as a result of the close proximity between Ca2+-permeable ion channels and their molecular targets. However, in most cases, direct evidence of the spatial relationship between these two types of molecules is lacking, and, thus, mechanistic understanding of local Ca2+ signaling is incomplete. In this study, we use an integrated approach to tackling this issue on a prototypical local Ca2+ signaling system composed of Ca2+ sparks resulting from the opening of ryanodine receptors (RYRs) and sp

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Chami, Mounia, and Frédéric Checler. "Targeting Post-Translational Remodeling of Ryanodine Receptor: A New Track for Alzheimer's Disease Therapy?" Current Alzheimer Research 17, no. 4 (2020): 313–23. http://dx.doi.org/10.2174/1567205017666200225102941.

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Pathologic calcium (Ca2+) signaling linked to Alzheimer’s Disease (AD) involves the intracellular Ca2+ release channels/ryanodine receptors (RyRs). RyRs are macromolecular complexes where the protein-protein interactions between RyRs and several regulatory proteins impact the channel function. Pharmacological and genetic approaches link the destabilization of RyRs macromolecular complexes to several human pathologies including brain disorders. In this review, we discuss our recent data, which demonstrated that enhanced neuronal RyR2-mediated Ca2+ leak in AD is associated with posttranslational

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Chen, Wenqian, Andrea Koop, Yingjie Liu, et al. "Reduced threshold for store overload-induced Ca2+ release is a common defect of RyR1 mutations associated with malignant hyperthermia and central core disease." Biochemical Journal 474, no. 16 (2017): 2749–61. http://dx.doi.org/10.1042/bcj20170282.

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Mutations in the skeletal muscle ryanodine receptor (RyR1) cause malignant hyperthermia (MH) and central core disease (CCD), whereas mutations in the cardiac ryanodine receptor (RyR2) lead to catecholaminergic polymorphic ventricular tachycardia (CPVT). Most disease-associated RyR1 and RyR2 mutations are located in the N-terminal, central, and C-terminal regions of the corresponding ryanodine receptor (RyR) isoform. An increasing body of evidence demonstrates that CPVT-associated RyR2 mutations enhance the propensity for spontaneous Ca2+ release during store Ca2+ overload, a process known as s

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23

Murayama, Takashi, and Yasuo Ogawa. "RyR1 exhibits lower gain of CICR activity than RyR3 in the SR: evidence for selective stabilization of RyR1 channel." American Journal of Physiology-Cell Physiology 287, no. 1 (2004): C36—C45. http://dx.doi.org/10.1152/ajpcell.00395.2003.

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We showed that frog α-ryanodine receptor (α-RyR) had a lower gain of Ca2+-induced Ca2+ release (CICR) activity than β-RyR in sarcoplasmic reticulum (SR) vesicles, indicating selective “stabilization” of the former isoform (Murayama T and Ogawa Y. J Biol Chem 276: 2953–2960, 2001). To know whether this is also the case with mammalian RyR1, we determined [3H]ryanodine binding of RyR1 and RyR3 in bovine diaphragm SR vesicles. The value of [3H]ryanodine binding (B) was normalized by the number of maximal binding sites (Bmax), whereby the specific activity of each isoform was expressed. This B/Bmax

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KISELYOV, Kirill, Dong Min SHIN, Nikolay SHCHEYNIKOV, Tomohiro KUROSAKI, and Shmuel MUALLEM. "Regulation of Ca2+-release-activated Ca2+ current (Icrac) by ryanodine receptors in inositol 1,4,5-trisphosphate-receptor-deficient DT40 cells." Biochemical Journal 360, no. 1 (2001): 17–22. http://dx.doi.org/10.1042/bj3600017.

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Persistence of capacitative Ca2+ influx in inositol 1,4,5-trisphosphate (IP3) receptor (IP3R)-deficient DT40 cells (DT40IP3R-/−) raises the question of whether gating of Ca2+-release activated Ca2+ current (Icrac) by conformational coupling to Ca2+-release channels is a general mechanism of gating of these channels. In the present work we examined the properties and mechanism of activation of Icrac Ca2+ current in wild-type and DT40IP3R-/− cells. In both cell types passive depletion of internal Ca2+ stores by infusion of EGTA activated a Ca2+ current with similar characteristics and time cours

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Hollingworth, Stephen, and Stephen M. Baylor. "Comparison of myoplasmic calcium movements during excitation–contraction coupling in frog twitch and mouse fast-twitch muscle fibers." Journal of General Physiology 141, no. 5 (2013): 567–83. http://dx.doi.org/10.1085/jgp.201310961.

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Single twitch fibers from frog leg muscles were isolated by dissection and micro-injected with furaptra, a rapidly responding fluorescent Ca2+ indicator. Indicator resting fluorescence (FR) and the change evoked by an action potential (ΔF) were measured at long sarcomere length (16°C); ΔF/FR was scaled to units of ΔfCaD, the change in fraction of the indicator in the Ca2+-bound form. ΔfCaD was simulated with a multicompartment model of the underlying myoplasmic Ca2+ movements, and the results were compared with previous measurements and analyses in mouse fast-twitch fibers. In frog fibers, sar

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Ji, Guangju, Morris E. Feldman, Kai Su Greene, Vincenzo Sorrentino, Hong-Bo Xin, and Michael I. Kotlikoff. "RYR2 Proteins Contribute to the Formation of Ca2+ Sparks in Smooth Muscle." Journal of General Physiology 123, no. 4 (2004): 377–86. http://dx.doi.org/10.1085/jgp.200308999.

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Calcium release through ryanodine receptors (RYR) activates calcium-dependent membrane conductances and plays an important role in excitation-contraction coupling in smooth muscle. The specific RYR isoforms associated with this release in smooth muscle, and the role of RYR-associated proteins such as FK506 binding proteins (FKBPs), has not been clearly established, however. FKBP12.6 proteins interact with RYR2 Ca2+ release channels and the absence of these proteins predictably alters the amplitude and kinetics of RYR2 unitary Ca2+ release events (Ca2+ sparks). To evaluate the role of specific

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Bultynck, Geert, Daniela Rossi, Geert Callewaert, et al. "The Conserved Sites for the FK506-binding Proteins in Ryanodine Receptors and Inositol 1,4,5-Trisphosphate Receptors Are Structurally and Functionally Different." Journal of Biological Chemistry 276, no. 50 (2001): 47715–24. http://dx.doi.org/10.1074/jbc.m106573200.

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We compared the interaction of the FK506-binding protein (FKBP) with the type 3 ryanodine receptor (RyR3) and with the type 1 and type 3 inositol 1,4,5-trisphosphate receptor (IP3R1 and IP3R3), using a quantitative GST-FKBP12 and GST-FKBP12.6 affinity assay. We first characterized and mapped the interaction of the FKBPs with the RyR3. GST-FKBP12 as well as GST-FKBP12.6 were able to bind ∼30% of the solubilized RyR3. The interaction was completely abolished by FK506, strengthened by the addition of Mg2+, and weakened in the absence of Ca2+but was not affected by the addition of cyclic ADP-ribos

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Rousseau, Eric, and Sonia Proteau. "Functional properties of the native type 3 ryanodine receptor Ca2+-release channel from canine diaphragm." Canadian Journal of Physiology and Pharmacology 79, no. 4 (2001): 310–19. http://dx.doi.org/10.1139/y00-127.

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mRNA and protein analyses have previously shown that the diaphragm expresses two ryanodine receptor isoforms: RyR1 and RyR3.RyR1 is the main Ca2+-releasing pathway in this muscle type. We now report the conducting, gating, and immunological properties of the native and purified forms of the less abundant RyR3 channel. The conductance of this native Ca2+-release channel was 330 pS in 50 mM/250 mM trans/cis CsCH3SO3. It was activated by Ca2+ concentrations of 1-1000 µM, and did not inactivate at mM concentrations of Ca2+. Both isoforms were purified by either a sucrose density gradient or immuno

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Oba, Toshiharu, Tatsuya Ishikawa, Takashi Murayama, Yasuo Ogawa, and Mamoru Yamaguchi. "H2O2 and ethanol act synergistically to gate ryanodine receptor/calcium-release channel." American Journal of Physiology-Cell Physiology 279, no. 5 (2000): C1366—C1374. http://dx.doi.org/10.1152/ajpcell.2000.279.5.c1366.

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We examined the effect of low concentrations of H2O2 on the Ca2+-release channel/ryanodine receptor (RyR) to determine if H2O2 plays a physiological role in skeletal muscle function. Sarcoplasmic reticulum vesicles from frog skeletal muscle and type 1 RyRs (RyR1) purified from rabbit skeletal muscle were incorporated into lipid bilayers. Channel activity of the frog RyR was not affected by application of 4.4 mM (0.02%) ethanol. Open probability ( P o) of such ethanol-treated RyR channels was markedly increased on subsequent addition of 10 μM H2O2. Increase of H2O2to 100 μM caused a further inc

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BOSE, Diptiman D., Roshanak RAHIMIAN, and David W. THOMAS. "Activation of ryanodine receptors induces calcium influx in a neuroblastoma cell line lacking calcium influx factor activity." Biochemical Journal 386, no. 2 (2005): 291–96. http://dx.doi.org/10.1042/bj20040900.

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We have further characterized the Ca2+ signalling properties of the NG115-401L (or 401L) neuroblastoma cell line, which has served as an important cell line for investigating SOC (store-operated channel) influx pathways. These cells possess an unusual Ca2+ signalling phenotype characterized by the absence of Ca2+ influx when Ca2+ stores are depleted by inhibitors of SERCA (sarcoplasmic/endoplasmic reticulum Ca2+-ATPase). Previous studies found that Ca2+-store depletion does not produce a CIF (Ca2+ influx factor) activity in 401L cells. These observations have prompted the question whether 401L

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HAYEK, Salim M., Xinsheng ZHU, Manjunatha B. BHAT, et al. "Characterization of a calcium-regulation domain of the skeletal-muscle ryanodine receptor." Biochemical Journal 351, no. 1 (2000): 57–65. http://dx.doi.org/10.1042/bj3510057.

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A negatively charged region of the N-terminal portion of the skeletal ryanodine receptor (RyR), located between residues 1872–1923, is involved in Ca 2+-dependent regulation of the Ca2+-release channel. This region is divergent between the skeletal (RyR1) and cardiac (RyR2) isoforms of the channel, and is known as D3. Ca2+ exerts important regulatory functions on the RyR, being involved in both activation and inactivation functions of the channel, i.e. the effects occurring at micromolar and millimolar Ca2+ concentrations respectively. To characterize the role of D3 in the Ca2+-dependent regul

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Iyer, Kavita A., Yifan Hu, Ashok R. Nayak, Nagomi Kurebayashi, Takashi Murayama, and Montserrat Samsó. "Structural mechanism of two gain-of-function cardiac and skeletal RyR mutations at an equivalent site by cryo-EM." Science Advances 6, no. 31 (2020): eabb2964. http://dx.doi.org/10.1126/sciadv.abb2964.

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Mutations in ryanodine receptors (RyRs), intracellular Ca2+ channels, are associated with deadly disorders. Despite abundant functional studies, the molecular mechanism of RyR malfunction remains elusive. We studied two single-point mutations at an equivalent site in the skeletal (RyR1 R164C) and cardiac (RyR2 R176Q) isoforms using ryanodine binding, Ca2+ imaging, and cryo–electron microscopy (cryo-EM) of the full-length protein. Loss of the positive charge had greater effect on the skeletal isoform, mediated via distortion of a salt bridge network, a molecular latch inducing rotation of a cyt

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Martin, Cécile, Jean-Marc Hyvelin, Karen E. Chapman, Roger Marthan, Richard H. Ashley, and Jean-Pierre Savineau. "Pregnant rat myometrial cells show heterogeneous ryanodine- and caffeine-sensitive calcium stores." American Journal of Physiology-Cell Physiology 277, no. 2 (1999): C243—C252. http://dx.doi.org/10.1152/ajpcell.1999.277.2.c243.

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Intracellular Ca2+ release channels such as ryanodine receptors play crucial roles in the Ca2+-mediated signaling that triggers excitation-contraction coupling in muscles. Although the existence and the role of these channels are well characterized in skeletal and cardiac muscles, their existence in smooth muscles, and more particularly in the myometrium, is very controversial. We have now clearly demonstrated the expression of ryanodine receptor Ca2+ release channels in rat myometrial smooth muscle, and for the first time, intracellular Ca2+ concentration experiments with indo 1 on single myo

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PAUL-PLETZER, Kalanethee, Takeshi YAMAMOTO, Noriaki IKEMOTO, et al. "Probing a putative dantrolene-binding site on the cardiac ryanodine receptor." Biochemical Journal 387, no. 3 (2005): 905–9. http://dx.doi.org/10.1042/bj20041336.

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Dantrolene is an inhibitor of intracellular Ca2+ release from skeletal muscle SR (sarcoplasmic reticulum). Direct photoaffinity labelling experiments using [3H]azidodantrolene and synthetic domain peptides have demonstrated that this drug targets amino acids 590–609 [termed DP1 (domain peptide 1)] of RyR1 (ryanodine receptor 1), the skeletal muscle RyR isoform. Although the identical sequence exists in the cardiac isoform, RyR2 (residues 601–620), specific labelling of RyR2 by dantrolene has not been demonstrated, even though some functional studies show protective effects of dantrolene on hea

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BULTYNCK, Geert, Patrick DE SMET, Daniela ROSSI, et al. "Characterization and mapping of the 12kDa FK506-binding protein (FKBP12)-binding site on different isoforms of the ryanodine receptor and of the inositol 1,4,5-trisphosphate receptor." Biochemical Journal 354, no. 2 (2001): 413–22. http://dx.doi.org/10.1042/bj3540413.

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We investigated the interaction of the 12kDa FK506-binding protein (FKBP12) with two ryanodine-receptor isoforms (RyR1 and RyR3) and with two myo-inositol 1,4,5-trisphosphate (IP3) receptor isoforms (IP3R1 and IP3R3). Using glutathione S-transferase (GST)-FKBP12 affinity chromatography, we could efficiently extract RyR1 (42±7% of the solubilized RyR1) from terminal cisternae of skeletal muscle as well as RyR3 (32±4% of the solubilized RyR3) from RyR3-overexpressing HEK-293 cells. These interactions were completely abolished by FK506 (20µM) but were largely unaffected by RyR-channel modulators.

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Murayama, Takashi, Toshiharu Oba, Shigeki Kobayashi, Noriaki Ikemoto, and Yasuo Ogawa. "Postulated role of interdomain interactions within the type 1 ryanodine receptor in the low gain of Ca2+-induced Ca2+ release activity of mammalian skeletal muscle sarcoplasmic reticulum." American Journal of Physiology-Cell Physiology 288, no. 6 (2005): C1222—C1230. http://dx.doi.org/10.1152/ajpcell.00415.2004.

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Ryanodine receptor (RyR) type 1 (RyR1) exhibits a markedly lower gain of Ca2+-induced Ca2+ release (CICR) activity than RyR type 3 (RyR3) in the sarcoplasmic reticulum (SR) of mammalian skeletal muscle (selective stabilization of the RyR1 channel), and this reduction in the gain is largely eliminated using 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonic acid (CHAPS). We have investigated whether the hypothesized interdomain interactions within RyR1 are involved in the selective stabilization of the channel using [3H]ryanodine binding, single-channel recordings, and Ca2+ release from t

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Craps, J., C. Wilvers, V. Joris, et al. "Involvement of Nitric Oxide in Iodine Deficiency-Induced Microvascular Remodeling in the Thyroid Gland: Role of Nitric Oxide Synthase 3 and Ryanodine Receptors." Endocrinology 156, no. 2 (2014): 707–20. http://dx.doi.org/10.1210/en.2014-1729.

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Iodine deficiency (ID) induces microvascular changes in the thyroid gland via a TSH-independent reactive oxygen species-hypoxia inducible factor (HIF)-1α-vascular endothelial growth factor (VEGF) pathway. The involvement of nitric oxide (NO) in this pathway and the role of calcium (Ca2+) and of ryanodine receptors (RYRs) in NO synthase 3 (NOS3) activation were investigated in a murine model of goitrogenesis and in 3 in vitro models of ID, including primary cultures of human thyrocytes. ID activated NOS3 and the production of NO in thyrocytes in vitro and increased the thyroid blood flow in viv

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O-Uchi, Jin, Bong Sook Jhun, Stephen Hurst, et al. "Overexpression of ryanodine receptor type 1 enhances mitochondrial fragmentation and Ca2+-induced ATP production in cardiac H9c2 myoblasts." American Journal of Physiology-Heart and Circulatory Physiology 305, no. 12 (2013): H1736—H1751. http://dx.doi.org/10.1152/ajpheart.00094.2013.

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Ca+ influx to mitochondria is an important trigger for both mitochondrial dynamics and ATP generation in various cell types, including cardiac cells. Mitochondrial Ca2+ influx is mainly mediated by the mitochondrial Ca2+ uniporter (MCU). Growing evidence also indicates that mitochondrial Ca2+ influx mechanisms are regulated not solely by MCU but also by multiple channels/transporters. We have previously reported that skeletal muscle-type ryanodine receptor (RyR) type 1 (RyR1), which expressed at the mitochondrial inner membrane, serves as an additional Ca2+ uptake pathway in cardiomyocytes. Ho

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Wang, Yong-Xiao, Yun-Min Zheng, Qi-Bing Mei, et al. "FKBP12.6 and cADPR regulation of Ca2+ release in smooth muscle cells." American Journal of Physiology-Cell Physiology 286, no. 3 (2004): C538—C546. http://dx.doi.org/10.1152/ajpcell.00106.2003.

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Intracellular Ca2+ release through ryanodine receptors (RyRs) plays important roles in smooth muscle excitation-contraction coupling, but the underlying regulatory mechanisms are poorly understood. Here we show that FK506 binding protein of 12.6 kDa (FKBP12.6) associates with and regulates type 2 RyRs (RyR2) in tracheal smooth muscle. FKBP12.6 binds to RyR2 but not other RyR or inositol 1,4,5-trisphosphate receptors, and FKBP12, known to bind to and modulate skeletal RyRs, does not associate with RyR2. When dialyzed into tracheal myocytes, cyclic ADP-ribose (cADPR) alters spontaneous Ca2+ rele

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AWAD, Suad S., Heather K. LAMB, Joanna M. MORGAN, William DUNLOP, and James I. GILLESPIE. "Differential expression of ryanodine receptor RyR2 mRNA in the non-pregnant and pregnant human myometrium." Biochemical Journal 322, no. 3 (1997): 777–83. http://dx.doi.org/10.1042/bj3220777.

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We describe here the expression of the ryanodine receptor isoforms RyR2 and RyR3 in human non-pregnant and pregnant (non-labouring) myometrium, and in isolated cultured myometrial cells. The mRNA encoding the RyR3 isoform was found in both non-pregnant and pregnant myometrial tissue samples; however, the mRNA for RyR2 was found only in pregnant samples. It can be speculated that the appearance of this additional isoform in the pregnant myometrium may increase the ability of this tissue to contract at term. Control of expression of the RyR2 gene may therefore be another example of an up-regulat

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Ríos, Eduardo, Dirk Gillespie, and Clara Franzini-Armstrong. "The binding interactions that maintain excitation–contraction coupling junctions in skeletal muscle." Journal of General Physiology 151, no. 4 (2019): 593–605. http://dx.doi.org/10.1085/jgp.201812268.

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Calcium for contraction of skeletal muscles is released via tetrameric ryanodine receptor (RYR1) channels of the sarcoplasmic reticulum (SR), which are assembled in ordered arrays called couplons at junctions where the SR abuts T tubules or plasmalemma. Voltage-gated Ca2+ (CaV1.1) channels, found in tubules or plasmalemma, form symmetric complexes called CaV tetrads that associate with and activate underlying RYR tetramers during membrane depolarization by conveying a conformational change. Intriguingly, CaV tetrads regularly skip every other RYR tetramer within the array; therefore, the RYRs

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Essin, Kirill, and Maik Gollasch. "Role of Ryanodine Receptor Subtypes in Initiation and Formation of Calcium Sparks in Arterial Smooth Muscle: Comparison with Striated Muscle." Journal of Biomedicine and Biotechnology 2009 (2009): 1–15. http://dx.doi.org/10.1155/2009/135249.

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Calcium sparks represent local, rapid, and transient calcium release events from a cluster of ryanodine receptors (RyRs) in the sarcoplasmic reticulum. In arterial smooth muscle cells (SMCs), calcium sparks activate calcium-dependent potassium channels causing decrease in the global intracellular[Ca2+]and oppose vasoconstriction. This is in contrast to cardiac and skeletal muscle, where spatial and temporal summation of calcium sparks leads to global increases in intracellular[Ca2+]and myocyte contraction. We summarize the present data on local RyR calcium signaling in arterial SMCs in compari

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Gomez, Angela C., Timothy W. Holford, and Naohiro Yamaguchi. "Malignant hyperthermia-associated mutations in the S2-S3 cytoplasmic loop of type 1 ryanodine receptor calcium channel impair calcium-dependent inactivation." American Journal of Physiology-Cell Physiology 311, no. 5 (2016): C749—C757. http://dx.doi.org/10.1152/ajpcell.00134.2016.

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Channel activities of skeletal muscle ryanodine receptor (RyR1) are activated by micromolar Ca2+ and inactivated by higher (∼1 mM) Ca2+. To gain insight into a mechanism underlying Ca2+-dependent inactivation of RyR1 and its relationship with skeletal muscle diseases, we constructed nine recombinant RyR1 mutants carrying malignant hyperthermia or centronuclear myopathy-associated mutations and determined RyR1 channel activities by [3H]ryanodine binding assay. These mutations are localized in or near the RyR1 domains which are responsible for Ca2+-dependent inactivation of RyR1. Four RyR1 mutat

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Dahan, Diana, Thomas Ducret, Jean-François Quignard, Roger Marthan, Jean-Pierre Savineau, and Eric Estève. "Implication of the ryanodine receptor in TRPV4-induced calcium response in pulmonary arterial smooth muscle cells from normoxic and chronically hypoxic rats." American Journal of Physiology-Lung Cellular and Molecular Physiology 303, no. 9 (2012): L824—L833. http://dx.doi.org/10.1152/ajplung.00244.2011.

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There is a growing body of evidence indicating that transient receptor potential (TRP) channels are implicated in calcium signaling and various cellular functions in the pulmonary vasculature. The aim of this study was to investigate the expression, functional role, and coupling to reticulum calcium channels of the type 4 vanilloid TRP subfamily (TRPV4) in the pulmonary artery from both normoxic (Nx) and chronically hypoxic (CH) rats. Activation of TRPV4 with the specific agonist 4α-phorbol-12,13-didecanoate (4α-PDD, 5 μM) increased the intracellular calcium concentration ([Ca2+]i). This effec

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FITZSIMMONS, Timothy J., Ilya GUKOVSKY, James A. McROBERTS, Edward RODRIGUEZ, F. Anthony LAI, and Stephen J. PANDOL. "Multiple isoforms of the ryanodine receptor are expressed in rat pancreatic acinar cells." Biochemical Journal 351, no. 1 (2000): 265–71. http://dx.doi.org/10.1042/bj3510265.

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Regulation of cytosolic Ca2+ is important for a variety of cell functions. The ryanodine receptor (RyR) is a Ca2+ channel that conducts Ca2+ from internal pools to the cytoplasm. To demonstrate the presence of the RyR in the pancreatic acinar cell, we performed reverse transcriptase (RT)-PCR, Western blot, immunocytochemistry and microscopic Ca2+-release measurements on these cells. RT-PCR showed the presence of mRNA for RyR isoforms 1, 2 and 3 in both rat pancreas and dispersed pancreatic acini. Furthermore, mRNA expression for RyR isoforms 1 and 2 was demonstrated by RT-PCR in individual pan

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Kong, Huihui, Peter P. Jones, Andrea Koop, Lin Zhang, Henry J. Duff, and S. R. Wayne Chen. "Caffeine induces Ca2+ release by reducing the threshold for luminal Ca2+ activation of the ryanodine receptor." Biochemical Journal 414, no. 3 (2008): 441–52. http://dx.doi.org/10.1042/bj20080489.

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Caffeine has long been used as a pharmacological probe for studying RyR (ryanodine receptor)-mediated Ca2+ release and cardiac arrhythmias. However, the precise mechanism by which caffeine activates RyRs is elusive. In the present study, we investigated the effects of caffeine on spontaneous Ca2+ release and on the response of single RyR2 (cardiac RyR) channels to luminal or cytosolic Ca2+. We found that HEK-293 cells (human embryonic kidney cells) expressing RyR2 displayed partial or ‘quantal’ Ca2+ release in response to repetitive additions of submaximal concentrations of caffeine. This quan

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Altafaj, Xavier, Julien France, Janos Almassy, et al. "Maurocalcine interacts with the cardiac ryanodine receptor without inducing channel modification." Biochemical Journal 406, no. 2 (2007): 309–15. http://dx.doi.org/10.1042/bj20070453.

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We have previously shown that MCa (maurocalcine), a toxin from the venom of the scorpion Maurus palmatus, binds to RyR1 (type 1 ryanodine receptor) and induces strong modifications of its gating behaviour. In the present study, we investigated the ability of MCa to bind to and modify the gating process of cardiac RyR2. By performing pull-down experiments we show that MCa interacts directly with RyR2 with an apparent affinity of 150 nM. By expressing different domains of RyR2 in vitro, we show that MCa binds to two domains of RyR2, which are homologous with those previously identified on RyR1.

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O'Brien, Fiona, Elisa Venturi, and Rebecca Sitsapesan. "The ryanodine receptor provides high throughput Ca2+-release but is precisely regulated by networks of associated proteins: a focus on proteins relevant to phosphorylation." Biochemical Society Transactions 43, no. 3 (2015): 426–33. http://dx.doi.org/10.1042/bst20140297.

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Once opened, ryanodine receptors (RyR) are efficient pathways for the release of Ca2+ from the endoplasmic/sarcoplasmic reticulum (ER/SR). The precise nature of the Ca2+-release event, however, requires fine-tuning for the specific process and type of cell involved. For example, the spatial organization of RyRs, the luminal [Ca2+] and the influence of soluble regulators that fluctuate under physiological and pathophysiological control mechanisms, all affect the amplitude and duration of RyR Ca2+ fluxes. Various proteins are docked tightly to the huge bulky structure of RyR and there is growing

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Mattei, M. G., G. Giannini, F. Moscatelli, and V. Sorrentino. "Chromosomal Localization of Murine Ryanodine Receptor Genes RYR1, RYR2, and RYR3 by in Situ Hybridization." Genomics 22, no. 1 (1994): 202–4. http://dx.doi.org/10.1006/geno.1994.1362.

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Wasserstrom, J. Andrew, Leslie A. Wasserstrom, Andrew J. Lokuta, James E. Kelly, Sireen T. Reddy, and Andrew J. Frank. "Activation of cardiac ryanodine receptors by the calcium channel agonist FPL-64176." American Journal of Physiology-Heart and Circulatory Physiology 283, no. 1 (2002): H331—H338. http://dx.doi.org/10.1152/ajpheart.00788.2001.

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We investigated the possibility that the Ca2+ channel agonist FPL-64176 (FPL) might also activate the cardiac sarcoplasmic reticulum (SR) Ca2+ release channel ryanodine receptor (RyR). The effects of FPL were tested on single channel activity of purified and crude vesicular RyR (RyR2) isolated from human and dog hearts using the planar lipid bilayer technique. FPL (100–200 μM) increased single channel open probability ( P o) when added to the cytoplasmic side of the channel ( P o = 0.070 ± 0.021 in control RyR2; 0.378 ± 0.086 in 150 μM FPL, n = 9, P < 0.01) by prolonging open times and decr

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