PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 17614008-4 2007 The K(i) values for phenformin inhibition of [(3)H]-MPP and [(14)C]-TEA uptake by hOCT1-3/rOct1-3 were lower than that for metformin. Tetraethylammonium 68-71 solute carrier family 22 member 1 Rattus norvegicus 90-95 21896487-8 2011 For rOct1(6DeltaC-l) and rOct1(rOat1-l), similar K(m) values for 1-methyl-4-phenylpyridinium(+) (MPP(+)) and tetraethylammonium(+) (TEA(+)) were obtained that were higher compared with rOct1 wild type. Tetraethylammonium 109-127 solute carrier family 22 member 1 Rattus norvegicus 4-9 19435783-3 2009 The affinity of corticosterone was determined by measuring the inhibition of currents induced by tetraethylammonium(+) (TEA(+)) in Xenopus laevis oocytes expressing rOCT1. Tetraethylammonium 97-118 solute carrier family 22 member 1 Rattus norvegicus 165-170 15662045-5 2005 These amino acids (Ala443, Leu447, and Gln448 in rOCT1 and Ile443, Tyr447, and Glu448 in rOCT2) are probably located within the substrate binding region because in rOCT1 mutants, the K(m) values for uptake of tetraethylammonium (TEA) and 1-methyl-4-phenylpyridinium (MPP) were decreased in parallel with a decrease of the IC50 values for the inhibition of cation uptake by corticosterone. Tetraethylammonium 209-227 solute carrier family 22 member 1 Rattus norvegicus 49-54 15662045-5 2005 These amino acids (Ala443, Leu447, and Gln448 in rOCT1 and Ile443, Tyr447, and Glu448 in rOCT2) are probably located within the substrate binding region because in rOCT1 mutants, the K(m) values for uptake of tetraethylammonium (TEA) and 1-methyl-4-phenylpyridinium (MPP) were decreased in parallel with a decrease of the IC50 values for the inhibition of cation uptake by corticosterone. Tetraethylammonium 209-227 solute carrier family 22 member 1 Rattus norvegicus 164-169 15662045-5 2005 These amino acids (Ala443, Leu447, and Gln448 in rOCT1 and Ile443, Tyr447, and Glu448 in rOCT2) are probably located within the substrate binding region because in rOCT1 mutants, the K(m) values for uptake of tetraethylammonium (TEA) and 1-methyl-4-phenylpyridinium (MPP) were decreased in parallel with a decrease of the IC50 values for the inhibition of cation uptake by corticosterone. Tetraethylammonium 229-232 solute carrier family 22 member 1 Rattus norvegicus 49-54 15662045-5 2005 These amino acids (Ala443, Leu447, and Gln448 in rOCT1 and Ile443, Tyr447, and Glu448 in rOCT2) are probably located within the substrate binding region because in rOCT1 mutants, the K(m) values for uptake of tetraethylammonium (TEA) and 1-methyl-4-phenylpyridinium (MPP) were decreased in parallel with a decrease of the IC50 values for the inhibition of cation uptake by corticosterone. Tetraethylammonium 229-232 solute carrier family 22 member 1 Rattus norvegicus 164-169 15662045-6 2005 In mutant rOCT1(L447Y/Q448E), the IC50 value for the inhibition of [3H]MPP (0.1 microM) uptake by corticosterone (24 +/- 4 microM) was significantly higher compared with the IC50 value for inhibition of [14C]TEA (10 microM) uptake (5.3 +/- 1.7 microM). Tetraethylammonium 208-211 solute carrier family 22 member 1 Rattus norvegicus 10-15 12438515-4 2002 In Xenopus oocytes, the inhibitory potency of several rOCT1/2 inhibitors was similar for amantadine compared to TEA uptake and supports amantadine transport by rOCT1 and rOCT2. Tetraethylammonium 112-115 solute carrier family 22 member 1 Rattus norvegicus 54-59 12438515-5 2002 In proximal tubules, procainamide, quinine, cyanine(863), choline, and guanidine in concentrations that inhibit rOCT1/2-mediated TEA or amantadine uptake in Xenopus oocytes exhibited no effect on amantadine uptake. Tetraethylammonium 129-132 solute carrier family 22 member 1 Rattus norvegicus 112-117 12438515-11 2002 TEA uptake by the basolateral membrane may be mediated mainly by rOCT1 and rOCT2, but these transporters may be in a different functional or regulatory state when expressed in cells or oocytes compared with expression in vivo. Tetraethylammonium 0-3 solute carrier family 22 member 1 Rattus norvegicus 65-70 10966938-9 2000 The substrate specificity of hOCTN2 differs from rOCT-1 and hOCT-2 as hOCTN2 showed only small currents with classic OCT substrates such as choline or tetraethylammonium; by contrast hOCTN2 mediated transport of betaine. Tetraethylammonium 151-169 solute carrier family 22 member 1 Rattus norvegicus 49-55 10825466-9 2000 These findings suggest that protons, dTub, and TEA act at a common site on rOCT1, and that rOCT1 participates in the renal secretion of dTub and other nucleosides. Tetraethylammonium 47-50 solute carrier family 22 member 1 Rattus norvegicus 75-80 10825466-7 2000 Protons acted as competitive inhibitors for the rOCT1-mediated uptake of dTub or tetraethylammonium (TEA), with K(i) values corresponding to a pH of about 6.1. Tetraethylammonium 81-99 solute carrier family 22 member 1 Rattus norvegicus 48-53 10825466-7 2000 Protons acted as competitive inhibitors for the rOCT1-mediated uptake of dTub or tetraethylammonium (TEA), with K(i) values corresponding to a pH of about 6.1. Tetraethylammonium 101-104 solute carrier family 22 member 1 Rattus norvegicus 48-53 10825466-8 2000 TEA and dTub mutually inhibited the uptake of one another by rOCT1, competitively, with K(i) values approximately the same as their respective K(m) values. Tetraethylammonium 0-3 solute carrier family 22 member 1 Rattus norvegicus 61-66 10825452-5 2000 When expressed heterologously in mammalian cells, rat OCTN1 mediates Na(+)-independent and pH-dependent transport of the prototypical organic cation tetraethylammonium. Tetraethylammonium 149-167 solute carrier family 22 member 1 Rattus norvegicus 54-59 9405386-2 1997 rOCT1 is the first member of a new protein family comprising electrogenic and polyspecific cation transporters that transport hydrophilic cations like tetraethylammonium, choline, and monoamine neurotransmitters. Tetraethylammonium 151-169 solute carrier family 22 member 1 Rattus norvegicus 0-5 9808712-3 1998 Tetraethylammonium (TEA) uptake by both MDCK-OCT1 and MDCK-OCT2 cells was markedly elevated when TEA was added to the basolateral medium, but not to the apical medium. Tetraethylammonium 0-18 solute carrier family 22 member 1 Rattus norvegicus 40-49 9808712-3 1998 Tetraethylammonium (TEA) uptake by both MDCK-OCT1 and MDCK-OCT2 cells was markedly elevated when TEA was added to the basolateral medium, but not to the apical medium. Tetraethylammonium 20-23 solute carrier family 22 member 1 Rattus norvegicus 40-49 9808712-3 1998 Tetraethylammonium (TEA) uptake by both MDCK-OCT1 and MDCK-OCT2 cells was markedly elevated when TEA was added to the basolateral medium, but not to the apical medium. Tetraethylammonium 97-100 solute carrier family 22 member 1 Rattus norvegicus 40-49 9808712-4 1998 Efflux of TEA from MDCK-OCT1 and MDCK-OCT2 cells was not changed by extracellular pH from 5.4 to 8.4, whereas TEA uptake by both transfectants was decreased by acidification of extracellular medium. Tetraethylammonium 10-13 solute carrier family 22 member 1 Rattus norvegicus 19-28 9808712-5 1998 Apparent Km values for TEA uptake by MDCK-OCT1 and MDCK-OCT2 cells were 38 and 45 microM, respectively. Tetraethylammonium 23-26 solute carrier family 22 member 1 Rattus norvegicus 42-46 9808712-6 1998 Although various hydrophilic organic cations such as 1-methyl-4-phenylpyridinium, cimetidine, quinidine, nicotine, N1-methylnicotinamide and guanidine markedly inhibited TEA uptake by both MDCK-OCT1 and MDCK-OCT2 cells, there were no significant differences in the apparent inhibition constants (Ki) against these organic cations between both transfectants. Tetraethylammonium 170-173 solute carrier family 22 member 1 Rattus norvegicus 189-198 8955087-2 1996 rOCT1 induced highly active transport of a variety of cations, including the classical substrates for cation transport, such as N-1-methylnicotinamide, 1-methyl-4-phenylpyridinium (MPP), and tetraethylammonium (TEA), but also the physiologically important choline. Tetraethylammonium 191-209 solute carrier family 22 member 1 Rattus norvegicus 0-5 8955087-2 1996 rOCT1 induced highly active transport of a variety of cations, including the classical substrates for cation transport, such as N-1-methylnicotinamide, 1-methyl-4-phenylpyridinium (MPP), and tetraethylammonium (TEA), but also the physiologically important choline. Tetraethylammonium 211-214 solute carrier family 22 member 1 Rattus norvegicus 0-5 8955087-3 1996 In oocytes rOCT1 also mediated efflux of MPP, which could be trans-stimulated by MPP and TEA. Tetraethylammonium 89-92 solute carrier family 22 member 1 Rattus norvegicus 11-16 8955087-5 1996 In voltage-clamped oocytes, transport of TEA and choline via rOCT1 produced inwardly directed currents, which were independent of extracellular ion composition or pH. Tetraethylammonium 41-44 solute carrier family 22 member 1 Rattus norvegicus 61-66