PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 23558838-10 2013 Maximal contractures in the caffeine-halothane contracture test were greater in those who had a known MH mutation or variant of uncertain significance in RYR1 than in those who did not. Halothane 37-46 ryanodine receptor 1 Homo sapiens 154-158 20023768-7 2009 The MH-triggering volatile anesthetic, halothane, activates RyR1(R615C) and RyR1(WT) to a similar extent, using [(3)H]ryanodine binding as a measure of activation. Halothane 39-48 ryanodine receptor 1 Homo sapiens 60-64 20978128-2 2011 Heterozygous mice expressing the human MH/central core disease RyR1 R163C mutation exhibit MH when exposed to halothane or heat stress. Halothane 110-119 ryanodine receptor 1 Homo sapiens 63-67 20023768-7 2009 The MH-triggering volatile anesthetic, halothane, activates RyR1(R615C) and RyR1(WT) to a similar extent, using [(3)H]ryanodine binding as a measure of activation. Halothane 39-48 ryanodine receptor 1 Homo sapiens 76-80 20023768-8 2009 Modeling RyR1 array function with parameters modified to simulate the loss of functional inter-RyR coupling recapitulates the MH molecular phenotype-RyR1 channels leaky to Ca(2+) at rest and long open-times following exposure to halothane. Halothane 229-238 ryanodine receptor 1 Homo sapiens 9-13 20023768-8 2009 Modeling RyR1 array function with parameters modified to simulate the loss of functional inter-RyR coupling recapitulates the MH molecular phenotype-RyR1 channels leaky to Ca(2+) at rest and long open-times following exposure to halothane. Halothane 229-238 ryanodine receptor 1 Homo sapiens 9-12 20023768-8 2009 Modeling RyR1 array function with parameters modified to simulate the loss of functional inter-RyR coupling recapitulates the MH molecular phenotype-RyR1 channels leaky to Ca(2+) at rest and long open-times following exposure to halothane. Halothane 229-238 ryanodine receptor 1 Homo sapiens 149-153 12959958-1 2004 Mutations in the skeletal muscle RyR1 isoform of the ryanodine receptor (RyR) Ca2+-release channel confer susceptibility to malignant hyperthermia, which may be triggered by inhalational anesthetics such as halothane. Halothane 207-216 ryanodine receptor 1 Homo sapiens 33-37 18505726-6 2008 Furthermore, the MH-triggering agent, halothane, potentiated the response of RyR1 to luminal Ca(2+) and SOICR. Halothane 38-47 ryanodine receptor 1 Homo sapiens 77-81 15269663-17 2004 Functional studies of the RYR1 mutations have shown that MHS mutations were mainly associated with an alteration of the calcium fluxes in response to caffeine or halothane while CCD mutations would result in a leaky RYR1 channel or would alter the Excitation-Contraction coupling at the level of the CMC. Halothane 162-171 ryanodine receptor 1 Homo sapiens 26-30 12959958-5 2004 In the concentration range of 0.014-0.35 mM halothane, anesthetic-induced oligomerization of the RyR1 complex was observed at a lower threshold concentration in the sarcoplasmic reticulum from patients with malignant hyperthermia. Halothane 44-53 ryanodine receptor 1 Homo sapiens 97-101 12151923-2 2002 This study was designed to investigate the effects of different mutations in the RYR1 gene on contracture development in in vitro contracture tests (IVCT) with halothane, caffeine, and ryanodine. Halothane 160-169 ryanodine receptor 1 Homo sapiens 81-85 14641996-6 2003 In myotubes of individuals carrying the RyR1 Ile2182Phe or the RyR1 Gly2375Ala mutation, the EC(50) for caffeine and halothane was reduced; in the Ile2182Phe myotubes, the EC(50) for 4CmC was also reduced, all consistent with facilitated calcium release from the sarcoplasmic reticulum. Halothane 117-126 ryanodine receptor 1 Homo sapiens 40-44 14641996-6 2003 In myotubes of individuals carrying the RyR1 Ile2182Phe or the RyR1 Gly2375Ala mutation, the EC(50) for caffeine and halothane was reduced; in the Ile2182Phe myotubes, the EC(50) for 4CmC was also reduced, all consistent with facilitated calcium release from the sarcoplasmic reticulum. Halothane 117-126 ryanodine receptor 1 Homo sapiens 63-67 12393358-3 2002 Our aim was to establish if measurements of halothane-induced increases in intracellular calcium ion concentration [Ca(2+)](i) in cultured human skeletal muscle cells can be used to phenotype MH susceptibility and if different mutations in the ryanodine receptor (RYR1) gene affect halothane-induced increases in [Ca(2+)](i). Halothane 44-53 ryanodine receptor 1 Homo sapiens 264-268 12151923-10 2002 CONCLUSIONS: The differences between the groups in the halothane and caffeine IVCT threshold concentrations and in the time course of contracture development in the ryanodine IVCT underline the hypothesis that certain mutations in the RYR1 gene could make the ryanodine receptor more sensitive to specific ligands. Halothane 55-64 ryanodine receptor 1 Homo sapiens 235-239 12124989-8 2002 RYR1 mutations associated with both CCD and MH (R163C, R2163H, R2435H) had more severe caffeine and halothane response phenotypes than those associated with MH alone. Halothane 100-109 ryanodine receptor 1 Homo sapiens 0-4 9873004-6 1999 When heterotetrameric (1:1) combinations of MH/CCD mutant and wild type RyR1 were expressed together with SERCA1 to enhance Ca2+ reuptake, the amplitude of Ca2+ release in response to low concentrations of caffeine and halothane was higher than that observed in cells expressing wild type RyR1 and SERCA1. Halothane 219-228 ryanodine receptor 1 Homo sapiens 72-76 10097181-5 1999 The response of the mutant RyR1 Ca2+ channel to the agonists halothane and caffeine in a Ca2+ photometry assay was completely abolished. Halothane 61-70 ryanodine receptor 1 Homo sapiens 27-30 10097181-6 1999 Coexpression of normal and mutant RYR1 cDNAs in a 1:1 ratio, however, produced RyR1 channels with normal halothane and caffeine sensitivities, but maximal levels of Ca2+ release were reduced by 67%. Halothane 105-114 ryanodine receptor 1 Homo sapiens 34-38 9743407-8 1998 This finding suggests that a mutation in FKBP12 or changes in its capacity to bind to the ryanodine receptor could alter the halothane sensitivity of the skeletal muscle ryanodine receptor and thereby predispose the person to malignant hyperthermia. Halothane 125-134 ryanodine receptor 1 Homo sapiens 154-188