PMID-sentid Pub_year Sent_text compound_name comp_offset prot_official_name organism prot_offset 1659152-1 1991 Unlike other classic NSAIDs, some fenamates given at therapeutic concentrations, have been shown to inhibit, both in vitro and in vivo, the 5-lipoxygenase pathway of arachidonic acid cascade as well as the synthesis of cyclooxygenase products. Fenamates 34-43 arachidonate 5-lipoxygenase Homo sapiens 140-154 6004860-0 1966 Fenamates as antagonists of bronchoconstriction and nociception induced by bradykinin and other substances. Fenamates 0-9 kininogen 1 Homo sapiens 75-85 35438288-3 2022 Mefenamic acid which belongs to fenamate group inhibits the NLRP3 inflammasome by inhibiting efflux of chloride ions and influx of calcium ions through blocking VRAC and TRPM2 respectively. Fenamates 32-40 NLR family pyrin domain containing 3 Homo sapiens 60-65 35438288-3 2022 Mefenamic acid which belongs to fenamate group inhibits the NLRP3 inflammasome by inhibiting efflux of chloride ions and influx of calcium ions through blocking VRAC and TRPM2 respectively. Fenamates 32-40 transient receptor potential cation channel subfamily M member 2 Homo sapiens 170-175 2551152-2 1989 In contrast to other classic NSAIDs, some fenamates in clinically achievable concentrations have been shown to inhibit synthesis of 5-lipoxygenase products in vitro. Fenamates 42-51 arachidonate 5-lipoxygenase Homo sapiens 132-146 7166179-2 1982 Structure of metabolites and C-13 NMR assignments of fenamates. Fenamates 53-62 homeobox C13 Homo sapiens 29-33 32162200-0 2020 Fenamates Inhibit Human Sodium Channel Nav1.2 and Protect Glutamate-Induced Injury in SH-SY5Y Cells. Fenamates 0-9 sodium voltage-gated channel alpha subunit 2 Homo sapiens 39-45 33259822-9 2021 Thus, SOD1 may selectively decrease the quinoneimine formation from fenamate-class NSAIDs. Fenamates 68-76 superoxide dismutase 1 Homo sapiens 6-10 32162200-9 2020 However, fenamates exhibited decreased inhibitory effects on hNav1.1 when compared to hNav1.2. Fenamates 9-18 sodium voltage-gated channel alpha subunit 1 Homo sapiens 61-68 32162200-11 2020 Fenamates inhibited glutamate-induced apoptosis through the modulation of the Bcl-2/Bax-dependent cell death pathways. Fenamates 0-9 BCL2 apoptosis regulator Homo sapiens 78-83 32162200-11 2020 Fenamates inhibited glutamate-induced apoptosis through the modulation of the Bcl-2/Bax-dependent cell death pathways. Fenamates 0-9 BCL2 associated X, apoptosis regulator Homo sapiens 84-87 32162200-13 2020 Nav1.2 and NMDAR might take part in the neuroprotection mechanism of the fenamates. Fenamates 73-82 sodium voltage-gated channel alpha subunit 2 Homo sapiens 0-6 32162200-14 2020 The fenamates inhibited glutamate-induced apoptosis through modulation of the Bcl-2/Bax-dependent cell death pathways. Fenamates 4-13 BCL2 apoptosis regulator Homo sapiens 78-83 32162200-14 2020 The fenamates inhibited glutamate-induced apoptosis through modulation of the Bcl-2/Bax-dependent cell death pathways. Fenamates 4-13 BCL2 associated X, apoptosis regulator Homo sapiens 84-87 30089357-3 2018 BL-1249, a compound from the fenamate class of nonsteroidal anti-inflammatory drugs is known to activate K2P2.1(TREK-1), the founding member of the thermo- and mechanosensitive TREK subfamily; however, its mechanism of action and effects on other K2P channels are not well-defined. Fenamates 29-37 potassium two pore domain channel subfamily K member 2 Homo sapiens 105-111 31072652-1 2019 This letter describes a focused, multi-dimensional optimization campaign around BL-1249, a fenamate class non-steroidal anti-inflammatory and a known activator of the K2P potassium channels TREK-1 (K2P2.1) and TREK-2 (K2P10.1). Fenamates 91-99 potassium two pore domain channel subfamily K member 2 Homo sapiens 190-196 30528877-0 2019 Fenamates inhibit human sodium channel Nav1.7 and Nav1.8. Fenamates 0-9 sodium voltage-gated channel alpha subunit 9 Homo sapiens 39-45 30528877-0 2019 Fenamates inhibit human sodium channel Nav1.7 and Nav1.8. Fenamates 0-9 sodium voltage-gated channel alpha subunit 10 Homo sapiens 50-56 30528877-4 2019 In this study, fenamates, including mefenamic acid, flufenamic acid and tolfenamic acid, were examined by whole-cell patch clamp techniques on the sodium channels hNav1.7 and hNav1.8, which are closely associated with pain. Fenamates 15-24 sodium voltage-gated channel alpha subunit 9 Homo sapiens 163-170 30528877-4 2019 In this study, fenamates, including mefenamic acid, flufenamic acid and tolfenamic acid, were examined by whole-cell patch clamp techniques on the sodium channels hNav1.7 and hNav1.8, which are closely associated with pain. Fenamates 15-24 sodium voltage-gated channel alpha subunit 10 Homo sapiens 175-182 30792624-3 2019 Fenamates are classical non-steroidal anti-inflammatory drugs but they are also highly subunit-selective modulators of GABAA receptors, activators of IKS potassium channels and antagonists of non-selective cation channels and the NLRP3 inflammosome. Fenamates 0-9 NLR family, pyrin domain containing 3 Rattus norvegicus 230-235 30089357-3 2018 BL-1249, a compound from the fenamate class of nonsteroidal anti-inflammatory drugs is known to activate K2P2.1(TREK-1), the founding member of the thermo- and mechanosensitive TREK subfamily; however, its mechanism of action and effects on other K2P channels are not well-defined. Fenamates 29-37 potassium two pore domain channel subfamily K member 2 Homo sapiens 112-118 24509840-5 2014 Furthermore, fenamates produce a marked enhancement of current through the shorter, truncated form of TREK1 and reveal a K(+)-selective channel, like the long form. Fenamates 13-22 potassium two pore domain channel subfamily K member 2 Homo sapiens 102-107 29942156-7 2018 Fenamates were more active against cyclooxygenase-2 expressing BxPC-3 than cyclooxygenase-2 non-expressing MIA PaCa-2 cell line. Fenamates 0-9 prostaglandin-endoperoxide synthase 2 Homo sapiens 35-51 29942156-7 2018 Fenamates were more active against cyclooxygenase-2 expressing BxPC-3 than cyclooxygenase-2 non-expressing MIA PaCa-2 cell line. Fenamates 0-9 prostaglandin-endoperoxide synthase 2 Homo sapiens 75-91 25903137-7 2015 D757R Slo2.1 channels were not activated by NaCl, but were activated by the fenamate niflumic acid, confirming their functional expression. Fenamates 76-84 potassium sodium-activated channel subfamily T member 2 Homo sapiens 6-12 27509875-0 2016 Fenamate NSAIDs inhibit the NLRP3 inflammasome and protect against Alzheimer"s disease in rodent models. Fenamates 0-8 NLR family, pyrin domain containing 3 Mus musculus 28-33 27509875-3 2016 Here we show that several clinically approved and widely used NSAIDs of the fenamate class are effective and selective inhibitors of the NLRP3 inflammasome via inhibition of the volume-regulated anion channel in macrophages, independently of COX enzymes. Fenamates 76-84 NLR family, pyrin domain containing 3 Mus musculus 137-142 27509875-6 2016 These data suggest that fenamate NSAIDs could be repurposed as NLRP3 inflammasome inhibitors and Alzheimer"s disease therapeutics. Fenamates 24-32 NLR family, pyrin domain containing 3 Mus musculus 63-68 22851714-0 2012 Structure-activity relationship of fenamates as Slo2.1 channel activators. Fenamates 35-44 potassium sodium-activated channel subfamily T member 2 Homo sapiens 48-54 22646516-0 2012 Pharmacological comparison of novel synthetic fenamate analogues with econazole and 2-APB on the inhibition of TRPM2 channels. Fenamates 46-54 transient receptor potential cation channel subfamily M member 2 Homo sapiens 111-116 22646516-1 2012 BACKGROUND AND PURPOSE: Fenamate analogues, econazole and 2-aminoethoxydiphenyl borate (2-APB) are inhibitors of transient receptor potential melastatin 2 (TRPM2) channels and are used as research tools. Fenamates 24-32 arginyl aminopeptidase Homo sapiens 90-93 22646516-1 2012 BACKGROUND AND PURPOSE: Fenamate analogues, econazole and 2-aminoethoxydiphenyl borate (2-APB) are inhibitors of transient receptor potential melastatin 2 (TRPM2) channels and are used as research tools. Fenamates 24-32 transient receptor potential cation channel subfamily M member 2 Homo sapiens 113-154 22646516-1 2012 BACKGROUND AND PURPOSE: Fenamate analogues, econazole and 2-aminoethoxydiphenyl borate (2-APB) are inhibitors of transient receptor potential melastatin 2 (TRPM2) channels and are used as research tools. Fenamates 24-32 transient receptor potential cation channel subfamily M member 2 Homo sapiens 156-161 22646516-3 2012 Here we have investigated the pharmacological profile of TRPM2 channels by application of newly synthesized fenamate analogues and the existing channel blockers. Fenamates 108-116 transient receptor potential cation channel subfamily M member 2 Homo sapiens 57-62 22646516-13 2012 CONCLUSION AND IMPLICATIONS: The fenamate analogue 3-MFA was more selective than other TRPM2 channel blockers. Fenamates 33-41 transient receptor potential cation channel subfamily M member 2 Homo sapiens 87-92 22851714-2 2012 In this study, we report that other fenamates, including flufenamic acid, mefenamic acid, tolfenamic acid, meclofenamic acid, and a phenyl acetic acid derivative, diclofenac, also are low-potency (EC(50) = 80 muM to 2.1 mM), partial agonists of human Slo2.1 channels heterologously expressed in Xenopus oocytes. Fenamates 36-45 potassium sodium-activated channel subfamily T member 2 Homo sapiens 251-257 22851714-3 2012 Substituent analysis determined that N-phenylanthranilic acid was the minimal pharmacophore for fenamate activation of Slo2.1 channels. Fenamates 96-104 potassium sodium-activated channel subfamily T member 2 Homo sapiens 119-125 22851714-8 2012 Together, our results suggest that fenamates bind to two sites on Slo2.1 channels: an extracellular accessible site to activate and a cytoplasmic accessible site in the pore to inhibit currents. Fenamates 35-44 potassium sodium-activated channel subfamily T member 2 Homo sapiens 66-72 22285229-0 2012 Effect of non-steroidal anti-inflammatory drugs and new fenamate analogues on TRPC4 and TRPC5 channels. Fenamates 56-64 transient receptor potential cation channel subfamily C member 4 Homo sapiens 78-83 22231719-3 2012 For example, fenamate NSAIDs potentiate GABA-A receptor function, indomethacin scavenges nitric oxide free radicals, and acetylsalicylic acid inhibits the translocation of NF-kappaB, all of which may contribute to their neuroprotective actions in selected experimental models of stroke. Fenamates 13-21 nuclear factor kappa B subunit 1 Homo sapiens 172-181 22285229-0 2012 Effect of non-steroidal anti-inflammatory drugs and new fenamate analogues on TRPC4 and TRPC5 channels. Fenamates 56-64 transient receptor potential cation channel subfamily C member 5 Homo sapiens 88-93 22285229-12 2012 Our results suggest that fenamate analogues are direct modulators of TRPC4 and TRPC5 channels. Fenamates 25-33 transient receptor potential cation channel subfamily C member 4 Homo sapiens 69-74 22285229-12 2012 Our results suggest that fenamate analogues are direct modulators of TRPC4 and TRPC5 channels. Fenamates 25-33 transient receptor potential cation channel subfamily C member 5 Homo sapiens 79-84 19888597-7 2010 The response to fenamate agonists was blocked by TRPA1 antagonists, AP-18, HC-030031, and ruthenium red. Fenamates 16-24 transient receptor potential cation channel subfamily A member 1 Homo sapiens 49-54 21828194-5 2011 Furthermore, we identified the fenamate flufenamic acid and related compounds as agonists of rBLINaC. Fenamates 31-39 acid sensing ion channel subunit family member 5 Rattus norvegicus 93-100 21828194-8 2011 Inhibition by diarylamidines and activation by fenamates define a unique pharmacological profile for BLINaC, which will be useful to unravel the physiological function of this ion channel. Fenamates 47-56 acid sensing ion channel subunit family member 5 Rattus norvegicus 101-107 19888597-0 2010 Activation of TRPA1 channels by fenamate nonsteroidal anti-inflammatory drugs. Fenamates 32-40 transient receptor potential cation channel subfamily A member 1 Homo sapiens 14-19 21198543-11 2011 Our results strongly suggest mefenamic acid is the most selective fenamate to interfere with TRPM3 function. Fenamates 66-74 transient receptor potential cation channel subfamily M member 3 Homo sapiens 93-98 19888597-8 2010 At subsaturating concentrations, the fenamate NSAIDs also potentiate the activation of TRPA1 by allyl isothiocyanate, cinnamaldehyde, and cold, demonstrating positive synergistic interactions with other well-characterized TRPA1 activators. Fenamates 37-45 transient receptor potential cation channel subfamily A member 1 Homo sapiens 87-92 19888597-8 2010 At subsaturating concentrations, the fenamate NSAIDs also potentiate the activation of TRPA1 by allyl isothiocyanate, cinnamaldehyde, and cold, demonstrating positive synergistic interactions with other well-characterized TRPA1 activators. Fenamates 37-45 transient receptor potential cation channel subfamily A member 1 Homo sapiens 222-227 19888597-10 2010 We conclude that fenamate NSAIDs are a novel class of potent and reversible direct agonists of TRPA1. Fenamates 17-25 transient receptor potential cation channel subfamily A member 1 Homo sapiens 95-100 18845642-10 2009 Ten micromolar of fenamate concentrations inhibited T(4) microvessel uptake with a similar hierarchical inhibition profile [fenamic acid (43%), diclofenac (78%), and meclofenamic acid (85%)], as observed for Oatp1c1 transfected cells. Fenamates 18-26 solute carrier organic anion transporter family member 1C1 Homo sapiens 208-215 19444608-2 2009 All fenamates inhibited EAAT1 currents; 100 microM flufenamic acid produced the most inhibition, decreasing the I (max) by 53 +/- 4% (P < 0.001). Fenamates 4-13 solute carrier family 1 member 3 L homeolog Xenopus laevis 24-29 19444608-4 2009 All fenamates inhibited GLYT1b currents; 100 microM flufenamic acid produced the most inhibition, decreasing the I (max) by 61 +/- 1% (P < 0.001). Fenamates 4-13 solute carrier family 6 member 9 S homeolog Xenopus laevis 24-30 19265444-4 2009 In this study we provide a detailed thermodynamic analysis of the binding and stability properties of I-FABP in complex with a series of fibrate and fenamate drugs to provide an insight into the forces driving drug binding to I-FABP. Fenamates 149-157 fatty acid binding protein 2 Homo sapiens 102-108 19265444-4 2009 In this study we provide a detailed thermodynamic analysis of the binding and stability properties of I-FABP in complex with a series of fibrate and fenamate drugs to provide an insight into the forces driving drug binding to I-FABP. Fenamates 149-157 fatty acid binding protein 2 Homo sapiens 226-232 18845642-12 2009 Together, these data suggest that Oatp1c1 transports fenamates into, and perhaps across, brain barrier cells. Fenamates 53-62 solute carrier organic anion transporter family member 1C1 Homo sapiens 34-41 17343829-6 2007 Diverse kinetics were observed for fenamate glucuronidation by UGT2B7 and UGT1A9. Fenamates 35-43 UDP glucuronosyltransferase family 2 member B7 Homo sapiens 63-69 17343829-6 2007 Diverse kinetics were observed for fenamate glucuronidation by UGT2B7 and UGT1A9. Fenamates 35-43 UDP glucuronosyltransferase family 1 member A9 Homo sapiens 74-80 17343829-11 2007 These data suggest that inhibitory metabolic interactions may occur between fenamates and other substrates metabolised by UGT2B7 and UGT1A9 in human kidney. Fenamates 76-85 UDP glucuronosyltransferase family 2 member B7 Homo sapiens 122-128 17343829-11 2007 These data suggest that inhibitory metabolic interactions may occur between fenamates and other substrates metabolised by UGT2B7 and UGT1A9 in human kidney. Fenamates 76-85 UDP glucuronosyltransferase family 1 member A9 Homo sapiens 133-139 11858641-3 2002 Molecular models of the complexes between indomethacin, fenamates, 2-phenylpropionic acids and the selective cyclooxygenase-2 (COX-2) inhibitors, with the cyclooxygenase active site of human PGHS-2 have been built by combining homology modelling, conformational searching and automated docking techniques. Fenamates 56-65 prostaglandin-endoperoxide synthase 2 Homo sapiens 109-125 16244177-0 2006 Activation and inhibition of kidney CLC-K chloride channels by fenamates. Fenamates 63-72 chloride channel, voltage-sensitive Kb L homeolog Xenopus laevis 36-41 12359267-0 2002 Fenamate-induced enhancement of heterologously expressed HERG currents in Xenopus oocytes. Fenamates 0-8 potassium voltage-gated channel subfamily H member 2 Homo sapiens 57-61 12359267-7 2002 Fenamates accelerated the activation rate of HERG channels and decelerated their deactivation. Fenamates 0-9 potassium voltage-gated channel subfamily H member 2 Homo sapiens 45-49 12359267-11 2002 The effects of the fenamates were blocked by the HERG channel blocker, E-4031 and were also not observed in water-injected oocytes. Fenamates 19-28 potassium voltage-gated channel subfamily H member 2 Homo sapiens 49-53 12359267-12 2002 Our data suggest that fenamates enhance HERG currents and affect the action potential duration in the heart. Fenamates 22-31 potassium voltage-gated channel subfamily H member 2 Homo sapiens 40-44 11858641-3 2002 Molecular models of the complexes between indomethacin, fenamates, 2-phenylpropionic acids and the selective cyclooxygenase-2 (COX-2) inhibitors, with the cyclooxygenase active site of human PGHS-2 have been built by combining homology modelling, conformational searching and automated docking techniques. Fenamates 56-65 prostaglandin-endoperoxide synthase 2 Homo sapiens 127-132 10428953-0 1999 Stilbenes and fenamates rescue the loss of I(KS) channel function induced by an LQT5 mutation and other IsK mutants. Fenamates 14-23 potassium voltage-gated channel subfamily E regulatory subunit 1 Homo sapiens 80-84 11504800-14 2001 Voltage-clamp step response measurements in confluent monolayers of SKHep1 cells that had been stably transfected with Cx43 revealed that fenamates are potent blockers of Cx43-mediated intercellular communication. Fenamates 138-147 gap junction protein alpha 1 Homo sapiens 119-123 11504800-14 2001 Voltage-clamp step response measurements in confluent monolayers of SKHep1 cells that had been stably transfected with Cx43 revealed that fenamates are potent blockers of Cx43-mediated intercellular communication. Fenamates 138-147 gap junction protein alpha 1 Homo sapiens 171-175 11504800-15 2001 In conclusion, fenamates represent a novel class of reversible gap junction blockers that can be used to study the role of Cx43-mediated gap junctional intercellular communication in biological processes. Fenamates 15-24 gap junction protein alpha 1 Homo sapiens 123-127 10718119-6 2000 HL-CST was less susceptible than HL-PST to the inhibition by fenamates and the IC50 for HL-CST were 36 microM (tolfenamic acid); 70 microM (flufenamic acid); 76 microM (mefenamic acid); 180 microM (niflumic acid) and 185 microM (meclofenamic acid). Fenamates 61-70 sulfotransferase family 1A member 1 Homo sapiens 36-39 10428953-0 1999 Stilbenes and fenamates rescue the loss of I(KS) channel function induced by an LQT5 mutation and other IsK mutants. Fenamates 14-23 potassium voltage-gated channel subfamily E regulatory subunit 1 Homo sapiens 104-107 10428953-5 1999 Here we show that binding of I(KS) channel activators, such as stilbenes and fenamates, to an extracellular domain flanking the human IsK transmembrane segment, restores normal I(KS) channel gating in otherwise inactive IsK C-terminal mutants, including the naturally occurring LQT5 mutant, D76N. Fenamates 77-86 potassium voltage-gated channel subfamily E regulatory subunit 1 Homo sapiens 134-137 10428953-5 1999 Here we show that binding of I(KS) channel activators, such as stilbenes and fenamates, to an extracellular domain flanking the human IsK transmembrane segment, restores normal I(KS) channel gating in otherwise inactive IsK C-terminal mutants, including the naturally occurring LQT5 mutant, D76N. Fenamates 77-86 potassium voltage-gated channel subfamily E regulatory subunit 1 Homo sapiens 220-223 10428953-5 1999 Here we show that binding of I(KS) channel activators, such as stilbenes and fenamates, to an extracellular domain flanking the human IsK transmembrane segment, restores normal I(KS) channel gating in otherwise inactive IsK C-terminal mutants, including the naturally occurring LQT5 mutant, D76N. Fenamates 77-86 potassium voltage-gated channel subfamily E regulatory subunit 1 Homo sapiens 278-282 10428953-8 1999 Owing to allosteric interactions, stilbene and fenamate compounds can rescue the dominant-negative suppression of I(KS) produced by IsK mutations and thus, may have important therapeutic relevance for LQT syndrome. Fenamates 47-55 potassium voltage-gated channel subfamily E regulatory subunit 1 Homo sapiens 132-135 9351445-6 1997 The fenamates (niflumic and flufenamic acid) were found to have large effects on the position of the steady state inactivation curve of the Kv4.3 channel. Fenamates 4-13 potassium voltage-gated channel subfamily D member 3 Homo sapiens 140-145 10216835-0 1999 The structural and electronical factors that contribute affinity for the time-dependent inhibition of PGHS-1 by indomethacin, diclofenac and fenamates. Fenamates 141-150 prostaglandin-endoperoxide synthase 1 Homo sapiens 102-108 9016346-8 1997 These results demonstrate that the sensitivity to inhibition by NSAIDs of the 15-HETE production by ASA-treated PGHS-2 is different than that of prostaglandin production by PGHS-2 and that Ser516 plays an important role in the interaction with fenamate inhibitors. Fenamates 244-252 prostaglandin-endoperoxide synthase 2 Homo sapiens 112-118 7632163-8 1995 The action of fenamates resembled that of the inhibitor of receptor-mediated calcium entry, SK&F 96365, especially when A23187, fMLP or PMA were used to stimulate the cells. Fenamates 14-23 formyl peptide receptor 1 Homo sapiens 132-136 7632163-10 1995 The two fenamates inhibited the fMLP-induced increase in intracellular free calcium in fura-2 loaded PMNs in the presence but not in the absence of extracellular calcium. Fenamates 8-17 formyl peptide receptor 1 Homo sapiens 32-36