PMID-sentid Pub_year Sent_text comp_official_name comp_offset protein_name organism prot_offset 3938682-1 1985 An analysis of the cost-effectiveness of two transdermal nitroglycerin systems utilizing adhesive patches, TDN and ND, was performed by a health-care research and management consulting firm. Nitroglycerin 57-70 triadin Homo sapiens 107-110 10748065-6 2000 Alanine mutagenesis within this motif demonstrated that the critical amino acids of triadin binding to calsequestrin are the even-numbered residues Lys(210), Lys(212), Glu(214), Lys(216), Gly(218), Gln(220), Lys(222), and Lys(224). Glutamine 198-201 triadin Homo sapiens 84-91 10748065-6 2000 Alanine mutagenesis within this motif demonstrated that the critical amino acids of triadin binding to calsequestrin are the even-numbered residues Lys(210), Lys(212), Glu(214), Lys(216), Gly(218), Gln(220), Lys(222), and Lys(224). Lysine 158-161 triadin Homo sapiens 84-91 10748065-6 2000 Alanine mutagenesis within this motif demonstrated that the critical amino acids of triadin binding to calsequestrin are the even-numbered residues Lys(210), Lys(212), Glu(214), Lys(216), Gly(218), Gln(220), Lys(222), and Lys(224). Lysine 158-161 triadin Homo sapiens 84-91 7721813-2 1995 In order to identify the proteins in the skeletal muscle that interact with triadin, the cytoplasmic and luminal domains of triadin were expressed as glutathione S-transferase fusion proteins and immobilized to glutathione-Sepharose to form affinity columns. Glutathione 150-161 triadin Homo sapiens 124-131 7721813-3 1995 Using these affinity columns, we find that triadin binds specifically to the ryanodine receptor/Ca2+ release channel and the Ca(2+)-binding protein calsequestrin from CHAPS (3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonic acid)-solubilized skeletal muscle homogenates. 3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate 167-172 triadin Homo sapiens 43-50 7721813-3 1995 Using these affinity columns, we find that triadin binds specifically to the ryanodine receptor/Ca2+ release channel and the Ca(2+)-binding protein calsequestrin from CHAPS (3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonic acid)-solubilized skeletal muscle homogenates. 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonic acid 174-235 triadin Homo sapiens 43-50 15289928-1 2004 Triadin is a protein first identified as a member of the muscle calcium release complex, involved in calcium release for muscle contraction. Calcium 64-71 triadin Homo sapiens 0-7 15289928-1 2004 Triadin is a protein first identified as a member of the muscle calcium release complex, involved in calcium release for muscle contraction. Calcium 101-108 triadin Homo sapiens 0-7 10748065-3 2000 The lumenal domain of triadin contains multiple repeats of alternating lysine and glutamic acid residues, which have been defined as KEKE motifs and have been proposed to promote protein associations. Lysine 71-77 triadin Homo sapiens 22-29 10748065-3 2000 The lumenal domain of triadin contains multiple repeats of alternating lysine and glutamic acid residues, which have been defined as KEKE motifs and have been proposed to promote protein associations. Glutamic Acid 82-95 triadin Homo sapiens 22-29 10748065-6 2000 Alanine mutagenesis within this motif demonstrated that the critical amino acids of triadin binding to calsequestrin are the even-numbered residues Lys(210), Lys(212), Glu(214), Lys(216), Gly(218), Gln(220), Lys(222), and Lys(224). Alanine 0-7 triadin Homo sapiens 84-91 10748065-6 2000 Alanine mutagenesis within this motif demonstrated that the critical amino acids of triadin binding to calsequestrin are the even-numbered residues Lys(210), Lys(212), Glu(214), Lys(216), Gly(218), Gln(220), Lys(222), and Lys(224). Lysine 148-151 triadin Homo sapiens 84-91 10748065-6 2000 Alanine mutagenesis within this motif demonstrated that the critical amino acids of triadin binding to calsequestrin are the even-numbered residues Lys(210), Lys(212), Glu(214), Lys(216), Gly(218), Gln(220), Lys(222), and Lys(224). Lysine 158-161 triadin Homo sapiens 84-91 10748065-6 2000 Alanine mutagenesis within this motif demonstrated that the critical amino acids of triadin binding to calsequestrin are the even-numbered residues Lys(210), Lys(212), Glu(214), Lys(216), Gly(218), Gln(220), Lys(222), and Lys(224). Glutamic Acid 168-171 triadin Homo sapiens 84-91 10748065-6 2000 Alanine mutagenesis within this motif demonstrated that the critical amino acids of triadin binding to calsequestrin are the even-numbered residues Lys(210), Lys(212), Glu(214), Lys(216), Gly(218), Gln(220), Lys(222), and Lys(224). Lysine 158-161 triadin Homo sapiens 84-91 10748065-6 2000 Alanine mutagenesis within this motif demonstrated that the critical amino acids of triadin binding to calsequestrin are the even-numbered residues Lys(210), Lys(212), Glu(214), Lys(216), Gly(218), Gln(220), Lys(222), and Lys(224). Glycine 188-191 triadin Homo sapiens 84-91 34866386-3 2022 TPA-TRDN could selectively detect HSA with fast response (10 min), superior sensitivity (LOD 0.34 mug/mL, about 60-fold fluorescence enhancement), and wide detection range (0.00-0.30 mg/mL). Tetradecanoylphorbol Acetate 0-3 triadin Homo sapiens 4-8 35481495-6 2022 Genetic analysis revealed a homozygous mutation of c.531_533delinsGG, p.(Lys179Asnfs * 44) frameshift variant in TRDN(NM_006073) gene. lys179asnfs 73-84 triadin Homo sapiens 113-117 32569964-8 2020 Overall results suggest that 3-mercaptohexanol is responsible for tropical/citrus fruit, TDN for kerosene, volatile phenols for woody/toasty, beta-damascenone and massoia lactone, likely with Z-1,5-octadien-3-one for fruit-in-syrup and alcoholic notes. 3-mercaptohexanol 29-46 triadin Homo sapiens 89-92 27595738-4 2016 Selective alanine substitutions show that K218, K220, and K224 together facilitate normal Trisk 95 binding to RyR1 and channel activation. Alanine 10-17 triadin Homo sapiens 90-95 32115705-4 2020 At present, mutations in six genes involved in SR calcium release have been identified as the genetic cause of CPVT: RYR2 (encoding ryanodine receptor calcium release channel), CASQ2 (encoding cardiac calsequestrin), TRDN (encoding triadin), CALM1, CALM2 and CALM3 (encoding identical calmodulin protein). Calcium 50-57 triadin Homo sapiens 217-221 31754805-1 2019 The authors describe a tetrahedral DNA nanostructure loaded with SYBR Green (SG-TDN) for fluorometric determination of nucleic acids. sybr green 65-75 triadin Homo sapiens 80-83 31437535-1 2020 BACKGROUND: Triadin is a protein expressed in cardiac and skeletal muscle that has an essential role in the structure and functional regulation of calcium release units and excitation-contraction coupling. Calcium 147-154 triadin Homo sapiens 12-19 31437535-7 2020 Expression of a green fluorescent protein (GFP)-tagged mutant human cardiac triadin isoform (TRISK32-L56P-GFP) in heterologous systems revealed that the mutation alters protein dynamics. trisk32 93-100 triadin Homo sapiens 76-83 29536183-9 2018 Patients with TDn had a higher PIP, larger initial OD/TD and higher incidence of pneumonia. pip 31-34 triadin Homo sapiens 14-17 27595738-4 2016 Selective alanine substitutions show that K218, K220, and K224 together facilitate normal Trisk 95 binding to RyR1 and channel activation. Fmoc-Glu(OtBu)-OH 42-46 triadin Homo sapiens 90-95 27595738-4 2016 Selective alanine substitutions show that K218, K220, and K224 together facilitate normal Trisk 95 binding to RyR1 and channel activation. Fmoc-Ser(tBu)-OH 48-52 triadin Homo sapiens 90-95 27595738-4 2016 Selective alanine substitutions show that K218, K220, and K224 together facilitate normal Trisk 95 binding to RyR1 and channel activation. DL-Arginine 58-62 triadin Homo sapiens 90-95 22422768-0 2012 Absence of triadin, a protein of the calcium release complex, is responsible for cardiac arrhythmia with sudden death in human. Calcium 37-44 triadin Homo sapiens 11-18 25922419-5 2015 After whole-exome sequencing and variant filtration, a homozygous p.D18fs*13 TRDN-encoded triadin frameshift mutation was discovered in a 10-year-old female patient with LQTS with a QTc of 500 milliseconds who experienced recurrent exertion-induced syncope/cardiac arrest beginning at 1 year of age. qtc 182-185 triadin Homo sapiens 77-81 25922419-5 2015 After whole-exome sequencing and variant filtration, a homozygous p.D18fs*13 TRDN-encoded triadin frameshift mutation was discovered in a 10-year-old female patient with LQTS with a QTc of 500 milliseconds who experienced recurrent exertion-induced syncope/cardiac arrest beginning at 1 year of age. qtc 182-185 triadin Homo sapiens 90-97 22422768-10 2012 The mutations identified in the two families lead to the absence of the protein, thereby demonstrating the importance of triadin for the normal function of the cardiac calcium release complex in humans. Calcium 168-175 triadin Homo sapiens 121-128 18620751-0 2009 Altered stored calcium release in skeletal myotubes deficient of triadin and junctin. Calcium 15-22 triadin Homo sapiens 65-72 21416510-3 2011 For the trisubstituted triazatrinaphthylenes (TrisK), the length of the substituents and the presence of terminal hydrogen-bond-donor groups (NH(2)) were shown to be crucial for ensuring a high quadruplex affinity (DeltaT(1/2) values of up to 20 C at 1 muM for the best candidate, TrisK3-NH) and selectivity versus duplex DNA. triazatrinaphthylenes 23-44 triadin Homo sapiens 46-51 21416510-3 2011 For the trisubstituted triazatrinaphthylenes (TrisK), the length of the substituents and the presence of terminal hydrogen-bond-donor groups (NH(2)) were shown to be crucial for ensuring a high quadruplex affinity (DeltaT(1/2) values of up to 20 C at 1 muM for the best candidate, TrisK3-NH) and selectivity versus duplex DNA. Hydrogen 114-122 triadin Homo sapiens 46-51 19403623-2 2009 First thought of as the missing link between the ryanodine receptor and the dihydropyridine receptor and responsible of skeletal type excitation-contraction coupling, the current hypothesis on triadin function has slowly evolved, and triadin is envisaged now as a regulator of calcium release, both in cardiac and skeletal muscle. Calcium 277-284 triadin Homo sapiens 234-241 18620751-1 2009 Triadin and junctin are integral sarcoplasmic reticulum membrane proteins that form a macromolecular complex with the skeletal muscle ryanodine receptor (RyR1) but their roles in skeletal muscle calcium homeostasis remain incompletely understood. Calcium 195-202 triadin Homo sapiens 0-7 18620751-3 2009 Knocking down either triadin or junctin in these cells reduced Ca2+ release induced by depolarization (10mM KCl) by 20-25%. Potassium Chloride 108-111 triadin Homo sapiens 21-28 18620751-7 2009 The results suggest that triadin has a role in facilitating KCl depolarization-induced Ca2+ release in contrast to junctin which has a role in maintaining sarcoplasmic reticulum Ca2+ store size in C2C12 myotubes. Potassium Chloride 60-63 triadin Homo sapiens 25-32