메뉴 건너뛰기




Volumn 7, Issue 2, 2010, Pages 412-420

Effect of HEPES buffer on the uptake and transport of p-glycoprotein substrates and large neutral amino acids

Author keywords

ATP dependent; HEPES; MDCK MDR1; P gp substrates; Transport; Uptake

Indexed keywords

4 (2 HYDROXYETHYL) 1 PIPERAZINEETHANESULFONIC ACID; ADENOSINE TRIPHOSPHATE; CYCLOSPORIN A; DIAZEPAM; GLUTAMIC ACID; GLYCOPROTEIN P; LOPINAVIR; PHENYLALANINE; RITONAVIR; VERAPAMIL;

EID: 77950569257     PISSN: 15438384     EISSN: 15438392     Source Type: Journal    
DOI: 10.1021/mp900193e     Document Type: Article
Times cited : (29)

References (47)
  • 1
    • 0014264271 scopus 로고
    • Use of a new buffer in the culture of animal cells
    • Williamson, J. D.; Cox, P. Use of a new buffer in the culture of animal cells J. Gen. Virol. 1968, 2, 309-312
    • (1968) J. Gen. Virol. , vol.2 , pp. 309-312
    • Williamson, J.D.1    Cox, P.2
  • 2
    • 0024382107 scopus 로고
    • Effect of HEPES on the taurine uptake by cultured glial cells
    • Lleu, P. L.; Rebel, G. Effect of HEPES on the taurine uptake by cultured glial cells J. Neurosci. Res. 1989, 23, 78-86
    • (1989) J. Neurosci. Res. , vol.23 , pp. 78-86
    • Lleu, P.L.1    Rebel, G.2
  • 4
    • 0021881930 scopus 로고
    • Analysis of the cytotoxic effects of light-exposed HEPES-containing culture medium
    • Zigger, J. S., Jr.; Lepe-Zuniga, J. L.; Vistica, B.; Gery, I. Analysis of the cytotoxic effects of light-exposed HEPES-containing culture medium In Vitro Cell. Dev. Biol. 1985, 21, 282-287
    • (1985) Vitro Cell. Dev. Biol. , vol.21 , pp. 282-287
    • Zigger Jr., J.S.1    Lepe-Zuniga, J.L.2    Vistica, B.3    Gery, I.4
  • 5
    • 0023107893 scopus 로고
    • Blockage of chloride channels by HEPES buffer
    • Yamamoto, D.; Suzuki, N. Blockage of chloride channels by HEPES buffer Proc. R. Soc. London, Ser. B 1987, 230, 93-100
    • (1987) Proc. R. Soc. London, Ser. B , vol.230 , pp. 93-100
    • Yamamoto, D.1    Suzuki, N.2
  • 6
    • 0023137442 scopus 로고
    • Inhibition of carbamoyl-phosphate synthase (ammonia) by Tris and HEPES. Effect on Ka for N-acetylglutamate
    • Lund, P.; Wiggins, D. Inhibition of carbamoyl-phosphate synthase (ammonia) by Tris and HEPES. Effect on Ka for N-acetylglutamate Biochem. J. 1987, 243, 273-276
    • (1987) Biochem. J. , vol.243 , pp. 273-276
    • Lund, P.1    Wiggins, D.2
  • 7
    • 0024779132 scopus 로고
    • P-glycoprotein: Multidrug-resistance and a superfamily of membrane-associated transport proteins
    • Juranka, P. F.; Zastawny, R. L.; Ling, V. P-glycoprotein: multidrug-resistance and a superfamily of membrane-associated transport proteins FASEB J. 1989, 3, 2583-2592
    • (1989) FASEB J. , vol.3 , pp. 2583-2592
    • Juranka, P.F.1    Zastawny, R.L.2    Ling, V.3
  • 8
    • 0037131893 scopus 로고    scopus 로고
    • The influence of MDR1 polymorphisms on P-glycoprotein expression and function in humans
    • Fromm, M. F. The influence of MDR1 polymorphisms on P-glycoprotein expression and function in humans Adv. Drug Delivery Rev. 2002, 54, 1295-1310
    • (2002) Adv. Drug Delivery Rev. , vol.54 , pp. 1295-1310
    • Fromm, M.F.1
  • 9
    • 0035987203 scopus 로고    scopus 로고
    • Evaluation of drug interactions with P-glycoprotein in drug discovery: In vitro assessment of the potential for drug-drug interactions with P-glycoprotein
    • Hochman, J. H.; Yamazaki, M.; Ohe, T.; Lin, J. H. Evaluation of drug interactions with P-glycoprotein in drug discovery: in vitro assessment of the potential for drug-drug interactions with P-glycoprotein Curr. Drug Metab. 2002, 3, 257-273
    • (2002) Curr. Drug Metab. , vol.3 , pp. 257-273
    • Hochman, J.H.1    Yamazaki, M.2    Ohe, T.3    Lin, J.H.4
  • 10
    • 33645830172 scopus 로고
    • A surface glycoprotein modulating drug permeability in Chinese hamster ovary cell mutants
    • Juliano, R. L.; Ling, V. A surface glycoprotein modulating drug permeability in Chinese hamster ovary cell mutants Biochim. Biophys. Acta 1976, 455, 152-162
    • (1976) Biochim. Biophys. Acta , vol.455 , pp. 152-162
    • Juliano, R.L.1    Ling, V.2
  • 11
    • 0032843082 scopus 로고    scopus 로고
    • P-glycoprotein, secretory transport, and other barriers to the oral delivery of anti-HIV drugs
    • Aungst, B. J. P-glycoprotein, secretory transport, and other barriers to the oral delivery of anti-HIV drugs Adv. Drug Delivery Rev. 1999, 39, 105-116
    • (1999) Adv. Drug Delivery Rev. , vol.39 , pp. 105-116
    • Aungst, B.J.1
  • 12
    • 0034121122 scopus 로고    scopus 로고
    • Pharmacological inhibition of P-glycoprotein transport enhances the distribution of HIV-1 protease inhibitors into brain and testes
    • Choo, E. F.; Leake, B.; Wandel, C.; Imamura, H.; Wood, A. J.; Wilkinson, G. R.; Kim, R. B. Pharmacological inhibition of P-glycoprotein transport enhances the distribution of HIV-1 protease inhibitors into brain and testes Drug Metab. Dispos. 2000, 28, 655-660
    • (2000) Drug Metab. Dispos. , vol.28 , pp. 655-660
    • Choo, E.F.1    Leake, B.2    Wandel, C.3    Imamura, H.4    Wood, A.J.5    Wilkinson, G.R.6    Kim, R.B.7
  • 13
    • 0030588644 scopus 로고    scopus 로고
    • The use of the intestinal epithelial cell culture model, Caco-2, in pharmaceutical development
    • Bailey, C. A.; Bryla, P.; Malick, A. W. The use of the intestinal epithelial cell culture model, Caco-2, in pharmaceutical development Adv. Drug Delivery Rev. 1996, 22, 85-103
    • (1996) Adv. Drug Delivery Rev. , vol.22 , pp. 85-103
    • Bailey, C.A.1    Bryla, P.2    Malick, A.W.3
  • 14
    • 0036293772 scopus 로고    scopus 로고
    • Are MDCK cells transfected with the human MDR1 gene a good model of the human intestinal mucosa?
    • DOI 10.1023/A:1016140429238
    • Tang, F.; Horie, K.; Borchardt, R. T. Are MDCK cells transfected with the human MDR1 gene a good model of the human intestinal mucosa Pharm. Res. 2002, 19, 765-772 (Pubitemid 34686734)
    • (2002) Pharmaceutical Research , vol.19 , Issue.6 , pp. 765-772
    • Tang, F.1    Horie, K.2    Borchardt, R.T.3
  • 15
    • 0030910379 scopus 로고    scopus 로고
    • Use of the intestinal bile acid transporter for the uptake of cholic acid conjugates with HIV-1 protease inhibitory activity
    • Kagedahl, M.; Swaan, P. W.; Redemann, C. T.; Tang, M.; Craik, C. S.; Szoka, F. C., Jr.; Oie, S. Use of the intestinal bile acid transporter for the uptake of cholic acid conjugates with HIV-1 protease inhibitory activity Pharm. Res. 1997, 14, 176-180
    • (1997) Pharm. Res. , vol.14 , pp. 176-180
    • Kagedahl, M.1    Swaan, P.W.2    Redemann, C.T.3    Tang, M.4    Craik, C.S.5    Szoka Jr., F.C.6    Oie, S.7
  • 16
    • 0031946993 scopus 로고    scopus 로고
    • In vitro blood-brain barrier permeability of nevirapine compared to other HIV antiretroviral agents
    • Glynn, S. L.; Yazdanian, M. In vitro blood-brain barrier permeability of nevirapine compared to other HIV antiretroviral agents J. Pharm. Sci. 1998, 87, 306-310
    • (1998) J. Pharm. Sci. , vol.87 , pp. 306-310
    • Glynn, S.L.1    Yazdanian, M.2
  • 17
    • 0036827595 scopus 로고    scopus 로고
    • Secretory transport of ranitidine and famotidine across Caco-2 cell monolayers
    • Lee, K.; Ng, C.; Brouwer, K. L.; Thakker, D. R. Secretory transport of ranitidine and famotidine across Caco-2 cell monolayers J. Pharmacol. Exp. Ther. 2002, 303, 574-580
    • (2002) J. Pharmacol. Exp. Ther. , vol.303 , pp. 574-580
    • Lee, K.1    Ng, C.2    Brouwer, K.L.3    Thakker, D.R.4
  • 18
    • 0041402719 scopus 로고    scopus 로고
    • Rhodamine 123 requires Carrier-mediated influx for its activity as a P-glycoprotein substrate in Caco-2 cells
    • Troutman, M. D.; Thakker, D. R. Rhodamine 123 requires Carrier-mediated influx for its activity as a P-glycoprotein substrate in Caco-2 cells Pharm. Res. 2003, 20, 1192-1199
    • (2003) Pharm. Res. , vol.20 , pp. 1192-1199
    • Troutman, M.D.1    Thakker, D.R.2
  • 19
    • 0043127383 scopus 로고    scopus 로고
    • Effect of the flavonoids A and silymarin on the P-glycoprotein-mediated transport of digoxin and vinblastine in human intestinal Caco-2 cells
    • Zhang, S.; Morris, M. E. Effect of the flavonoids A and silymarin on the P-glycoprotein-mediated transport of digoxin and vinblastine in human intestinal Caco-2 cells Pharm. Res. 2003, 20, 1184-1191
    • (2003) Pharm. Res. , vol.20 , pp. 1184-1191
    • Zhang, S.1    Morris, M.E.2
  • 20
    • 0032865554 scopus 로고    scopus 로고
    • Inhibition of the CYP3A4-mediated metabolism and P-glycoprotein-mediated transport of the HIV-1 protease inhibitor saquinavir by grapefruit juice components
    • Eagling, V. A.; Profit, L.; Back, D. J. Inhibition of the CYP3A4-mediated metabolism and P-glycoprotein-mediated transport of the HIV-1 protease inhibitor saquinavir by grapefruit juice components Br. J. Clin. Pharmacol. 1999, 48, 543-552
    • (1999) Br. J. Clin. Pharmacol. , vol.48 , pp. 543-552
    • Eagling, V.A.1    Profit, L.2    Back, D.J.3
  • 21
    • 0033371825 scopus 로고    scopus 로고
    • Modulation of P-glycoprotein function in human lymphocytes and Caco-2 cell monolayers by HIV-1 protease inhibitors
    • Profit, L.; Eagling, V. A.; Back, D. J. Modulation of P-glycoprotein function in human lymphocytes and Caco-2 cell monolayers by HIV-1 protease inhibitors AIDS 1999, 13, 1623-1627
    • (1999) AIDS , vol.13 , pp. 1623-1627
    • Profit, L.1    Eagling, V.A.2    Back, D.J.3
  • 22
    • 0030792730 scopus 로고    scopus 로고
    • Estimation of the relative contribution of the transcellular and paracellular pathway to the transport of passively absorbed drugs in the Caco-2 cell culture model
    • Pade, V.; Stavchansky, S. Estimation of the relative contribution of the transcellular and paracellular pathway to the transport of passively absorbed drugs in the Caco-2 cell culture model Pharm. Res. 1997, 14, 1210-1215
    • (1997) Pharm. Res. , vol.14 , pp. 1210-1215
    • Pade, V.1    Stavchansky, S.2
  • 23
    • 0035662950 scopus 로고    scopus 로고
    • In vitro intestinal permeability of factor Xa inhibitors: Influence of chemical structure on passive transport and susceptibility to efflux
    • Schipper, N. G.; Osterberg, T.; Wrange, U.; Westberg, C.; Sokolowski, A.; Rai, R.; Young, W.; Sjostrom, B. In vitro intestinal permeability of factor Xa inhibitors: influence of chemical structure on passive transport and susceptibility to efflux Pharm. Res. 2001, 18, 1735-1741
    • (2001) Pharm. Res. , vol.18 , pp. 1735-1741
    • Schipper, N.G.1    Osterberg, T.2    Wrange, U.3    Westberg, C.4    Sokolowski, A.5    Rai, R.6    Young, W.7    Sjostrom, B.8
  • 24
    • 0141567449 scopus 로고    scopus 로고
    • Preliminary investigation of proton-coupled oligopeptide transporters in neural retina pigment epithelium (RPE): Lack of functional activity in RPE plasma membranes
    • Ocheltree, S. M.; Keep, R. F.; Shen, H.; Yang, D.; Hughes, B. A.; Smith, D. E. Preliminary investigation of proton-coupled oligopeptide transporters in neural retina pigment epithelium (RPE): lack of functional activity in RPE plasma membranes Pharm. Res. 2003, 20, 1364-1372
    • (2003) Pharm. Res. , vol.20 , pp. 1364-1372
    • Ocheltree, S.M.1    Keep, R.F.2    Shen, H.3    Yang, D.4    Hughes, B.A.5    Smith, D.E.6
  • 25
    • 0034807802 scopus 로고    scopus 로고
    • Characterizing the expression of CYP3A4 and efflux transporters (P-gp, MRP1, and MRP2) in CYP3A4-transfected Caco-2 cells after induction with sodium butyrate and the phorbol ester 12-o-tetradecanoylphorbol-13-acetate
    • Cummins, C. L.; Mangravite, L. M.; Benet, L. Z. Characterizing the expression of CYP3A4 and efflux transporters (P-gp, MRP1, and MRP2) in CYP3A4-transfected Caco-2 cells after induction with sodium butyrate and the phorbol ester 12-o-tetradecanoylphorbol-13-acetate Pharm. Res. 2001, 18, 1102-1109
    • (2001) Pharm. Res. , vol.18 , pp. 1102-1109
    • Cummins, C.L.1    Mangravite, L.M.2    Benet, L.Z.3
  • 26
    • 0029896241 scopus 로고    scopus 로고
    • Age-dependent expression of P-glycoprotein gp170 in Caco-2 cell monolayers
    • Hosoya, K. I.; Kim, K. J.; Lee, V. H. Age-dependent expression of P-glycoprotein gp170 in Caco-2 cell monolayers Pharm. Res. 1996, 13, 885-890
    • (1996) Pharm. Res. , vol.13 , pp. 885-890
    • Hosoya, K.I.1    Kim, K.J.2    Lee, V.H.3
  • 28
    • 0027987417 scopus 로고
    • Mechanism and kinetics of transcellular transport of a new beta-lactam antibiotic loracarbef across an intestinal epithelial membrane model system (Caco-2)
    • Hu, M.; Chen, J.; Zhu, Y.; Dantzig, A. H.; Stratford, R. E., Jr.; Kuhfeld, M. T. Mechanism and kinetics of transcellular transport of a new beta-lactam antibiotic loracarbef across an intestinal epithelial membrane model system (Caco-2) Pharm. Res. 1994, 11, 1405-1413
    • (1994) Pharm. Res. , vol.11 , pp. 1405-1413
    • Hu, M.1    Chen, J.2    Zhu, Y.3    Dantzig, A.H.4    Stratford Jr., R.E.5    Kuhfeld, M.T.6
  • 29
    • 0031941789 scopus 로고    scopus 로고
    • Taxol transport by human intestinal epithelial Caco-2 cells
    • Walle, U. K.; Walle, T. Taxol transport by human intestinal epithelial Caco-2 cells Drug Metab. Dispos. 1998, 26, 343-346
    • (1998) Drug Metab. Dispos. , vol.26 , pp. 343-346
    • Walle, U.K.1    Walle, T.2
  • 30
    • 0034059327 scopus 로고    scopus 로고
    • Atorvastatin transport in the Caco-2 cell model: Contributions of P-glycoprotein and the proton-monocarboxylic acid co-transporter
    • Wu, X.; Whitfield, L. R.; Stewart, B. H. Atorvastatin transport in the Caco-2 cell model: contributions of P-glycoprotein and the proton-monocarboxylic acid co-transporter Pharm. Res. 2000, 17, 209-215
    • (2000) Pharm. Res. , vol.17 , pp. 209-215
    • Wu, X.1    Whitfield, L.R.2    Stewart, B.H.3
  • 31
    • 0034870523 scopus 로고    scopus 로고
    • Transport characteristics of ebastine and its metabolites across human intestinal epithelial Caco-2 cell monolayers
    • Imamura, Y.; Shimizu, K.; Yamashita, M.; Yamaoka, K.; Takakura, Y.; Hashida, M. Transport characteristics of ebastine and its metabolites across human intestinal epithelial Caco-2 cell monolayers Bio. Pharmacol. Bull. 2001, 24, 930-934
    • (2001) Bio. Pharmacol. Bull. , vol.24 , pp. 930-934
    • Imamura, Y.1    Shimizu, K.2    Yamashita, M.3    Yamaoka, K.4    Takakura, Y.5    Hashida, M.6
  • 32
    • 0036298317 scopus 로고    scopus 로고
    • Are MDCK cells transfected with the human MRP2 gene a good model of the human intestinal mucosa?
    • DOI 10.1023/A:1016192413308
    • Tang, F.; Horie, K.; Borchardt, R. T. Are MDCK cells transfected with the human MRP2 gene a good model of the human intestinal mucosa Pharm. Res. 2002, 19, 773-779 (Pubitemid 34686735)
    • (2002) Pharmaceutical Research , vol.19 , Issue.6 , pp. 773-779
    • Tang, F.1    Horie, K.2    Borchardt, R.T.3
  • 33
    • 16644374851 scopus 로고    scopus 로고
    • Cotransport of macrolide and fluoroquinolones, a beneficial interaction reversing P-glycoprotein efflux
    • Sikri, V.; Pal, D.; Jain, R.; Kalyani, D.; Mitra, A. K. Cotransport of macrolide and fluoroquinolones, a beneficial interaction reversing P-glycoprotein efflux Am. J. Ther. 2004, 11, 433-442
    • (2004) Am. J. Ther. , vol.11 , pp. 433-442
    • Sikri, V.1    Pal, D.2    Jain, R.3    Kalyani, D.4    Mitra, A.K.5
  • 34
    • 0031834404 scopus 로고    scopus 로고
    • P-Glycoprotein (P-gp) mediated efflux in Caco-2 cell monolayers: The influence of culturing conditions and drug exposure on P-gp expression levels
    • Anderle, P.; Niederer, E.; Rubas, W.; Hilgendorf, C.; Spahn-Langguth, H.; Wunderli-Allenspach, H.; Merkle, H. P.; Langguth, P. P-Glycoprotein (P-gp) mediated efflux in Caco-2 cell monolayers: the influence of culturing conditions and drug exposure on P-gp expression levels J. Pharm. Sci. 1998, 87, 757-762
    • (1998) J. Pharm. Sci. , vol.87 , pp. 757-762
    • Anderle, P.1    Niederer, E.2    Rubas, W.3    Hilgendorf, C.4    Spahn-Langguth, H.5    Wunderli-Allenspach, H.6    Merkle, H.P.7    Langguth, P.8
  • 35
    • 0034646468 scopus 로고    scopus 로고
    • Evidence for a requirement for ATP hydrolysis at two distinct steps during a single turnover of the catalytic cycle of human P-glycoprotein
    • Sauna, Z. E.; Ambudkar, S. V. Evidence for a requirement for ATP hydrolysis at two distinct steps during a single turnover of the catalytic cycle of human P-glycoprotein Proc. Natl. Acad. Sci. U.S.A. 2000, 97, 2515-2520
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 2515-2520
    • Sauna, Z.E.1    Ambudkar, S.V.2
  • 36
    • 0026756347 scopus 로고
    • P-glycoprotein. ATP hydrolysis by the N-terminal nucleotide-binding domain
    • Shimabuku, A. M.; Nishimoto, T.; Ueda, K.; Komano, T. P-glycoprotein. ATP hydrolysis by the N-terminal nucleotide-binding domain J. Biol. Chem. 1992, 267, 4308-4311
    • (1992) J. Biol. Chem. , vol.267 , pp. 4308-4311
    • Shimabuku, A.M.1    Nishimoto, T.2    Ueda, K.3    Komano, T.4
  • 37
    • 0029824820 scopus 로고    scopus 로고
    • The mechanism of proline/glutamate antiport in rat kidney mitochondria Energy dependence and glutamate-carrier involvement
    • Atlante, A.; Passarella, S.; Pierro, P.; Di Martino, C.; Quagliariello, E. The mechanism of proline/glutamate antiport in rat kidney mitochondria Energy dependence and glutamate-carrier involvement Eur. J. Biochem. 1996, 241, 171-177
    • (1996) Eur. J. Biochem. , vol.241 , pp. 171-177
    • Atlante, A.1    Passarella, S.2    Pierro, P.3    Di Martino, C.4    Quagliariello, E.5
  • 38
    • 0023715532 scopus 로고
    • Glutamate uptake by brain synaptic vesicles. Energy dependence of transport and functional reconstitution in proteoliposomes
    • Maycox, P. R.; Deckwerth, T.; Hell, J. W.; Jahn, R. Glutamate uptake by brain synaptic vesicles. Energy dependence of transport and functional reconstitution in proteoliposomes J. Biol. Chem. 1988, 263, 15423-15428
    • (1988) J. Biol. Chem. , vol.263 , pp. 15423-15428
    • Maycox, P.R.1    Deckwerth, T.2    Hell, J.W.3    Jahn, R.4
  • 39
    • 0018638719 scopus 로고
    • Uptake of glutamate into synaptic vesicles: Dependence on vesicle treatment, ions, temperature and energy supply
    • Karppinen, A.; Lahdesmaki, P. Uptake of glutamate into synaptic vesicles: dependence on vesicle treatment, ions, temperature and energy supply Cell. Mol. Biol. Incl. Cyto Enzymol. 1979, 25, 195-202
    • (1979) Cell. Mol. Biol. Incl. Cyto Enzymol. , vol.25 , pp. 195-202
    • Karppinen, A.1    Lahdesmaki, P.2
  • 40
    • 1842789741 scopus 로고    scopus 로고
    • Identification and functional characterization of a Na(+)-independent large neutral amino acid transporter (LAT2) on ARPE-19 cells
    • Gandhi, M. D.; Pal, D.; Mitra, A. K. Identification and functional characterization of a Na(+)-independent large neutral amino acid transporter (LAT2) on ARPE-19 cells Int. J. Pharm. 2004, 275, 189-200
    • (2004) Int. J. Pharm. , vol.275 , pp. 189-200
    • Gandhi, M.D.1    Pal, D.2    Mitra, A.K.3
  • 41
    • 0036891989 scopus 로고    scopus 로고
    • Functional characterization of monocarboxylic acid, large neutral amino acid, bile acid and peptide transporters, and P-glycoprotein in MDCK and Caco-2 cells
    • Putnam, W. S.; Ramanathan, S.; Pan, L.; Takahashi, L. H.; Benet, L. Z. Functional characterization of monocarboxylic acid, large neutral amino acid, bile acid and peptide transporters, and P-glycoprotein in MDCK and Caco-2 cells J. Pharm. Sci. 2002, 91, 2622-2635
    • (2002) J. Pharm. Sci. , vol.91 , pp. 2622-2635
    • Putnam, W.S.1    Ramanathan, S.2    Pan, L.3    Takahashi, L.H.4    Benet, L.Z.5
  • 42
    • 0036432807 scopus 로고    scopus 로고
    • 1-like receptor function in two opossum kidney cell clonal sublines
    • DOI 10.1159/000067896
    • Gomes, P.; Soares-da-Silva, P. Na(+)/H(+) exchanger activity and dopamine D(1)-like receptor function in two opossum kidney cell clonal sublines Cell. Physiol. Biochem. 2002, 12, 259-268 (Pubitemid 35356701)
    • (2002) Cellular Physiology and Biochemistry , vol.12 , Issue.5-6 , pp. 259-268
    • Gomes, P.1    Soares-Da-Silva, P.2
  • 43
    • 0030035535 scopus 로고    scopus 로고
    • Effects of steroids and verapamil on P-glycoprotein ATPase activity: Progesterone, desoxycorticosterone, corticosterone and verapamil are mutually non-exclusive modulators
    • Orlowski, S.; Mir, L. M.; Belehradek, J., Jr.; Garrigos, M. Effects of steroids and verapamil on P-glycoprotein ATPase activity: progesterone, desoxycorticosterone, corticosterone and verapamil are mutually non-exclusive modulators Biochem. J. 1996, 317, 515 - 522
    • (1996) Biochem. J. , vol.317 , pp. 515-522
    • Orlowski, S.1    Mir, L.M.2    Belehradek Jr., J.3    Garrigos, M.4
  • 46
    • 0032533542 scopus 로고    scopus 로고
    • Firefly luciferase has two nucleotide binding sites: Effect of nucleoside monophosphate and CoA on the light-emission spectra
    • Steghens, J. P.; Min, K. L.; Bernengo, J. C. Firefly luciferase has two nucleotide binding sites: effect of nucleoside monophosphate and CoA on the light-emission spectra Biochem. J. 1998, 336, 109-113
    • (1998) Biochem. J. , vol.336 , pp. 109-113
    • Steghens, J.P.1    Min, K.L.2    Bernengo, J.C.3
  • 47
    • 0028924829 scopus 로고
    • Regulatory effects of ATP and luciferin on firefly luciferase activity
    • Lembert, N.; Idahl, L. A. Regulatory effects of ATP and luciferin on firefly luciferase activity Biochem. J. 1995, 305, 929-933
    • (1995) Biochem. J. , vol.305 , pp. 929-933
    • Lembert, N.1    Idahl, L.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.