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Volumn 7, Issue 6, 2011, Pages 375-383

A yeast-based screen reveals that sulfasalazine inhibits tetrahydrobiopterin biosynthesis

Author keywords

[No Author keywords available]

Indexed keywords

ATORVASTATIN; DIHYDROFOLATE REDUCTASE; ERLOTINIB; FUROSEMIDE; INDOMETACIN; MESALAZINE; METHOTREXATE; PHOSPHODIESTERASE; PURVALANOL B; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) DEHYDROGENASE (QUINONE); SALAZOSULFAPYRIDINE; SEPIAPTERIN REDUCTASE; SULFAPYRIDINE; TETRAHYDROBIOPTERIN;

EID: 85027931231     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.557     Document Type: Article
Times cited : (111)

References (50)
  • 2
    • 75149125686 scopus 로고    scopus 로고
    • Recent advances and method development for drug target identification
    • Chan, J.N., Nislow, C. & Emili, A. Recent advances and method development for drug target identification. Trends Pharmacol. Sci. 31, 82-88 (2010).
    • (2010) Trends Pharmacol. Sci. , vol.31 , pp. 82-88
    • Chan, J.N.1    Nislow, C.2    Emili, A.3
  • 3
    • 69249136243 scopus 로고    scopus 로고
    • Target profiling of small molecules by chemical proteomics
    • Rix, U. & Superti-Furga, G. Target profiling of small molecules by chemical proteomics. Nat. Chem. Biol. 5, 616-624 (2009).
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 616-624
    • Rix, U.1    Superti-Furga, G.2
  • 7
    • 0031796062 scopus 로고    scopus 로고
    • In vivo characterization of the drug resistance profile of the major ABC transporters and other components of the yeast pleiotropic drug resistance network
    • Kolaczkowski, M., Kolaczowska, A., Luczynski, J., Witek, S. & Goffeau, A. In vivo characterization of the drug resistance profile of the major ABC transporters and other components of the yeast pleiotropic drug resistance network. Microb. Drug Resist. 4, 143-158 (1998). (Pubitemid 28500712)
    • (1998) Microbial Drug Resistance , vol.4 , Issue.3 , pp. 143-158
    • Kolaczkowski, M.1    Kolaczkowska, A.2    Luczynski, J.3    Witek, S.4    Goffeau, A.5
  • 8
    • 49649105136 scopus 로고    scopus 로고
    • Septin stability and recycling during dynamic structural transitions in cell division and development
    • McMurray, M.A. & Thorner, J. Septin stability and recycling during dynamic structural transitions in cell division and development. Curr. Biol. 18, 1203-1208 (2008).
    • (2008) Curr. Biol. , vol.18 , pp. 1203-1208
    • McMurray, M.A.1    Thorner, J.2
  • 9
    • 0020441466 scopus 로고
    • Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 Aθ resolution. I. General features and binding of methotrexate
    • Bolin, J.T., Filman, D.J., Matthews, D.A., Hamlin, R.C. & Kraut, J. Crystal structures of Escherichia coli and Lactobacillus casei dihydrofolate reductase refined at 1.7 A resolution. I. General features and binding of methotrexate. J. Biol. Chem. 257, 13650-13662 (1982). (Pubitemid 13187127)
    • (1982) Journal of Biological Chemistry , vol.257 , Issue.22 , pp. 13650-13662
    • Bolin, J.T.1    Filman, D.J.2    Matthews, D.A.3
  • 12
    • 0024512066 scopus 로고
    • Hydrophobic interactions via mutants of Escherichia coli dihydrofolate reductase: Separation of binding and catalysis
    • DOI 10.1021/bi00433a043
    • Murphy, D.J. & Benkovic, S.J. Hydrophobic interactions via mutants of Escherichia coli dihydrofolate reductase: Separation of binding and catalysis. Biochemistry 28, 3025-3031 (1989). (Pubitemid 19099486)
    • (1989) Biochemistry , vol.28 , Issue.7 , pp. 3025-3031
    • Murphy, D.J.1    Benkovic, S.J.2
  • 13
    • 45949100254 scopus 로고    scopus 로고
    • Improving yeast two-hybrid screening systems
    • Koegl, M. & Uetz, P. Improving yeast two-hybrid screening systems. Brief. Funct. Genomics Proteomics 6, 302-312 (2008).
    • (2008) Brief. Funct. Genomics Proteomics , vol.6 , pp. 302-312
    • Koegl, M.1    Uetz, P.2
  • 14
    • 1542345539 scopus 로고    scopus 로고
    • Increasing specificity in high-throughput yeast two-hybrid experiments
    • DOI 10.1016/j.ymeth.2003.10.001, PII S1046202303002652
    • Vidalain, P.O., Boxem, M., Ge, H., Li, S. & Vidal, M. Increasing specificity in high-throughput yeast two-hybrid experiments. Methods 32, 363-370 (2004). (Pubitemid 38299327)
    • (2004) Methods , vol.32 , Issue.4 , pp. 363-370
    • Vidalain, P.-O.1    Boxem, M.2    Ge, H.3    Li, S.4    Vidal, M.5
  • 15
    • 0030963019 scopus 로고    scopus 로고
    • Toward a functional analysis of the yeast genome through exhaustive two- hybrid screens
    • DOI 10.1038/ng0797-277
    • Fromont-Racine, M., Rain, J.C. & Legrain, P. Toward a functional analysis of the yeast genome through exhaustive two-hybrid screens. Nat. Genet. 16, 277-282 (1997). (Pubitemid 27280212)
    • (1997) Nature Genetics , vol.16 , Issue.3 , pp. 277-282
    • Fromont-Racine, M.1    Rain, J.-C.2    Legrain, P.3
  • 16
    • 38049018155 scopus 로고    scopus 로고
    • A quantitative analysis of kinase inhibitor selectivity
    • Karaman, M.W. et al. A quantitative analysis of kinase inhibitor selectivity. Nat. Biotechnol. 26, 127-132 (2008).
    • (2008) Nat. Biotechnol. , vol.26 , pp. 127-132
    • Karaman, M.W.1
  • 19
    • 0141599428 scopus 로고    scopus 로고
    • Structure of the epidermal growth factor receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor
    • DOI 10.1074/jbc.M207135200
    • Stamos, J., Sliwkowski, M.X. & Eigenbrot, C. Structure of the epidermal growth factor receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor. J. Biol. Chem. 277, 46265-46272 (2002). (Pubitemid 35417619)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.48 , pp. 46265-46272
    • Stamos, J.1    Sliwkowski, M.X.2    Eigenbrot, C.3
  • 20
    • 38549169589 scopus 로고    scopus 로고
    • Emerging roles of the oxysterol-binding protein family in metabolism, transport, and signaling
    • DOI 10.1007/s00018-007-7325-2
    • Fairn, G.D. & McMaster, C.R. Emerging roles of the oxysterol-binding protein family in metabolism, transport, and signaling. Cell. Mol. Life Sci. 65, 228-236 (2008). (Pubitemid 351161484)
    • (2008) Cellular and Molecular Life Sciences , vol.65 , Issue.2 , pp. 228-236
    • Fairn, G.D.1    McMaster, C.R.2
  • 21
    • 0035843962 scopus 로고    scopus 로고
    • Structural mechanism for statin inhibition of HMG-CoA reductase
    • DOI 10.1126/science.1059344
    • Istvan, E.S. & Deisenhofer, J. Structural mechanism for statin inhibition of HMG-CoA reductase. Science 292, 1160-1164 (2001). (Pubitemid 32440937)
    • (2001) Science , vol.292 , Issue.5519 , pp. 1160-1164
    • Istvan, E.S.1    Deisenhofer, J.2
  • 23
    • 33744962184 scopus 로고    scopus 로고
    • Internalization and recycling of the human prostacyclin receptor is modulated through its isoprenylation-dependent interaction with the δ subunit of cGMP phosphodiesterase 6
    • DOI 10.1074/jbc.M513110200
    • Wilson, S.J. & Smyth, E.M. Internalization and recycling of the human prostacyclin receptor is modulated through its isoprenylation-dependent interaction with the delta subunit of cGMP phosphodiesterase 6. J. Biol. Chem. 281, 11780-11786 (2006). (Pubitemid 43855437)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.17 , pp. 11780-11786
    • Wilson, S.J.1    Smyth, E.M.2
  • 25
    • 62449337409 scopus 로고    scopus 로고
    • The structure of the leukemia drug imatinib bound to human quinone reductase 2 (NQO2)
    • Winger, J.A., Hantschel, O., Superti-Furga, G. & Kuriyan, J. The structure of the leukemia drug imatinib bound to human quinone reductase 2 (NQO2). BMC Struct. Biol. 9, 7 (2009).
    • (2009) BMC Struct. Biol. , vol.9 , pp. 7
    • Winger, J.A.1    Hantschel, O.2    Superti-Furga, G.3    Kuriyan, J.4
  • 26
    • 67651087175 scopus 로고    scopus 로고
    • The long journey of salicylates in ulcerative colitis: The past and the future
    • Caprilli, R., Cesarini, M., Angelucci, E. & Frieri, G. The long journey of salicylates in ulcerative colitis: The past and the future. J. Crohn's Colitis 3, 149-156 (2009).
    • (2009) J. Crohn's Colitis , vol.3 , pp. 149-156
    • Caprilli, R.1    Cesarini, M.2    Angelucci, E.3    Frieri, G.4
  • 28
    • 33745013901 scopus 로고    scopus 로고
    • Oral 5-aminosalicylic acid for maintenance of remission in ulcerative colitis
    • Sutherland, L. & Macdonald, J.K. Oral 5-aminosalicylic acid for maintenance of remission in ulcerative colitis. Cochrane Database Syst. Rev. CD000544 (2006).
    • (2006) Cochrane Database Syst. Rev.
    • Sutherland, L.1    Macdonald, J.K.2
  • 29
    • 0026551768 scopus 로고
    • Inhibition of folate-dependent enzymes by non-steroidal anti-inflammatory drugs
    • Baggott, J.E., Morgan, S.L., Ha, T., Vaughn, W.H. & Hine, R.J. Inhibition of folate-dependent enzymes by non-steroidal anti-inflammatory drugs. Biochem. J. 282, 197-202 (1992).
    • (1992) Biochem. J. , vol.282 , pp. 197-202
    • Baggott, J.E.1    Morgan, S.L.2    Ha, T.3    Vaughn, W.H.4    Hine, R.J.5
  • 30
    • 0032032469 scopus 로고    scopus 로고
    • Sulfasalazine: A potent and specific inhibitor of nuclear factor kappa B
    • Wahl, C., Liptay, S., Adler, G. & Schmid, R.M. Sulfasalazine: A potent and specific inhibitor of nuclear factor kappa B. J. Clin. Invest. 101, 1163-1174 (1998). (Pubitemid 28125296)
    • (1998) Journal of Clinical Investigation , vol.101 , Issue.5 , pp. 1163-1174
    • Wahl, C.1    Liptay, S.2    Adler, G.3    Schmid, R.M.4
  • 31
    • 0034176921 scopus 로고    scopus 로고
    • Tetrahydrobiopterin biosynthesis, regeneration and functions
    • DOI 10.1042/0264-6021:3470001
    • Thöny, B., Auerbach, G. & Blau, N. Tetrahydrobiopterin biosynthesis, regeneration and functions. Biochem. J. 347, 1-16 (2000). (Pubitemid 30199034)
    • (2000) Biochemical Journal , vol.347 , Issue.1 , pp. 1-16
    • Thony, B.1    Auerbach, G.2    Blau, N.3
  • 32
    • 0026733592 scopus 로고
    • New inhibitors of sepiapterin reductase. Lack of an effect of intracellular tetrahydrobiopterin depletion upon in vitro proliferation of two human cell lines
    • Smith, G.K., Duch, D.S., Edelstein, M.P. & Bigham, E.C. New inhibitors of sepiapterin reductase. Lack of an effect of intracellular tetrahydrobiopterin depletion upon in vitro proliferation of two human cell lines. J. Biol. Chem. 267, 5599-5607 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 5599-5607
    • Smith, G.K.1    Duch, D.S.2    Edelstein, M.P.3    Bigham, E.C.4
  • 33
    • 74149085130 scopus 로고    scopus 로고
    • MRP2 mediated drug-drug interaction: Indomethacin increases sulfasalazine absorption in the small intestine, potentially decreasing its colonic targeting
    • Dahan, A. & Amidon, G.L. MRP2 mediated drug-drug interaction: Indomethacin increases sulfasalazine absorption in the small intestine, potentially decreasing its colonic targeting. Int. J. Pharm. 386, 216-220 (2010).
    • (2010) Int. J. Pharm. , vol.386 , pp. 216-220
    • Dahan, A.1    Amidon, G.L.2
  • 34
    • 0027101755 scopus 로고
    • Tetrahydrobiopterin synthesis. An absolute requirement for cytokine- induced nitric oxide generation by vascular smooth muscle
    • Gross, S.S. & Levi, R. Tetrahydrobiopterin synthesis. An absolute requirement for cytokine-induced nitric oxide generation by vascular smooth muscle. J. Biol. Chem. 267, 25722-25729 (1992). (Pubitemid 23013967)
    • (1992) Journal of Biological Chemistry , vol.267 , Issue.36 , pp. 25722-25729
    • Gross, S.S.1    Levi, R.2
  • 36
    • 0026467074 scopus 로고
    • Increased concentrations of nitrite in synovial fluid and serum samples suggest increased nitric oxide synthesis in rheumatic diseases
    • Farrell, A.J., Blake, D.R., Palmer, R.M. & Moncada, S. Increased concentrations of nitrite in synovial fluid and serum samples suggest increased nitric oxide synthesis in rheumatic diseases. Ann. Rheum. Dis. 51, 1219-1222 (1992).
    • (1992) Ann. Rheum. Dis. , vol.51 , pp. 1219-1222
    • Farrell, A.J.1    Blake, D.R.2    Palmer, R.M.3    Moncada, S.4
  • 38
    • 0028959180 scopus 로고
    • Suppression of adjuvant-induced arthritis by selective inhibition of inducible nitric oxide synthase
    • Connor, J.R. et al. Suppression of adjuvant-induced arthritis by selective inhibition of inducible nitric oxide synthase. Eur. J. Pharmacol. 273, 15-24 (1995).
    • (1995) Eur. J. Pharmacol. , vol.273 , pp. 15-24
    • Connor, J.R.1
  • 40
    • 0022343103 scopus 로고
    • Plasma and synovial fluid concentrations of sulphasalazine and two of its metabolites in rheumatoid arthritis
    • DOI 10.1007/BF00541351
    • Farr, M., Brodrick, A. & Bacon, P.A. Plasma and synovial fluid concentrations of sulphasalazine and two of its metabolites in rheumatoid arthritis. Rheumatol. Int. 5, 247-251 (1985). (Pubitemid 16232307)
    • (1985) Rheumatology International , vol.5 , Issue.6 , pp. 247-251
    • Farr, M.1    Brodrick, A.2    Bacon, P.A.3
  • 41
    • 0021989128 scopus 로고
    • Which component of sulphasalazine is active in rheumatoid arthritis?
    • Pullar, T., Hunter, J.A. & Capell, H.A. Which component of sulphasalazine is active in rheumatoid arthritis? Br. Med. J. (Clin. Res. Ed.) 290, 1535-1538 (1985). (Pubitemid 15094508)
    • (1985) British Medical Journal , vol.290 , Issue.6481 , pp. 1535-1538
    • Pullar, T.1    Hunter, J.A.2    Capell, H.A.3
  • 42
    • 0021337576 scopus 로고
    • Colonic azodisalicylate metabolism determined by in vivo dialysis in healthy volunteers and patients with ulcerative colitis
    • Lauritsen, K., Hansen, J., Ryde, M. & Rask-Madsen, J. Colonic azodisalicylate metabolism determined by in vivo dialysis in healthy volunteers and patients with ulcerative colitis. Gastroenterology 86, 1496-1500 (1984). (Pubitemid 14147943)
    • (1984) Gastroenterology , vol.86 , Issue.6 , pp. 1496-1500
    • Lauritsen, K.1    Hansen, J.2    Ryde, M.3    Rask-Madsen, J.4
  • 43
    • 26944479743 scopus 로고    scopus 로고
    • Colonic targeting of aminosalicylates for the treatment of ulcerative colitis
    • DOI 10.1016/j.dld.2004.12.011, PII S159086580500040X
    • Klotz, U. Colonic targeting of aminosalicylates for the treatment of ulcerative colitis. Dig. Liver Dis. 37, 381-388 (2005). (Pubitemid 44356040)
    • (2005) Digestive and Liver Disease , vol.37 , Issue.6 , pp. 381-388
    • Klotz, U.1
  • 44
    • 58949083662 scopus 로고    scopus 로고
    • Carbonic anhydrase inhibitors. Comparison of chlorthalidone, indapamide, trichloromethiazide, and furosemide X-ray crystal structures in adducts with isozyme II, when several water molecules make the difference
    • Temperini, C., Cecchi, A., Scozzafava, A. & Supuran, C.T. Carbonic anhydrase inhibitors. Comparison of chlorthalidone, indapamide, trichloromethiazide, and furosemide X-ray crystal structures in adducts with isozyme II, when several water molecules make the difference. Bioorg. Med. Chem. 17, 1214-1221 (2009).
    • (2009) Bioorg. Med. Chem. , vol.17 , pp. 1214-1221
    • Temperini, C.1    Cecchi, A.2    Scozzafava, A.3    Supuran, C.T.4
  • 45
    • 0033136768 scopus 로고    scopus 로고
    • Kinetic basis for selective inhibition of cyclo-oxygenases
    • DOI 10.1042/0264-6021:3390607
    • Gierse, J.K., Koboldt, C.M., Walker, M.C., Seibert, K. & Isakson, P.C. Kinetic basis for selective inhibition of cyclo-oxygenases. Biochem. J. 339, 607-614 (1999). (Pubitemid 29243524)
    • (1999) Biochemical Journal , vol.339 , Issue.3 , pp. 607-614
    • Gierse, J.K.1    Koboldt, C.M.2    Walker, M.C.3    Seibert, K.4    Isakson, P.C.5
  • 46
    • 33750682661 scopus 로고    scopus 로고
    • 4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase complex reveals the structural basis of broad spectrum indomethacin efficacy
    • DOI 10.1093/jb/mvj176
    • Hori, T. et al. Crystal structure of anti-configuration of indomethacin and leukotriene B4 12-hydroxydehydrogenase/15-oxo-prostaglandin 13-reductase complex reveals the structural basis of broad spectrum indomethacin efficacy. J. Biochem. 140, 457-466 (2006). (Pubitemid 44703165)
    • (2006) Journal of Biochemistry , vol.140 , Issue.3 , pp. 457-466
    • Hori, T.1    Ishijima, J.2    Yokomizo, T.3    Ago, H.4    Shimizu, T.5    Miyano, M.6
  • 48
    • 72149092233 scopus 로고    scopus 로고
    • GTP cyclohydrolase 1 genetic variant delays cancer pain
    • Lötsch, J., Klepstad, P., Doehring, A. & Dale, O.A. GTP cyclohydrolase 1 genetic variant delays cancer pain. Pain 148, 103-106 (2010).
    • (2010) Pain , vol.148 , pp. 103-106
    • Lötsch, J.1    Klepstad, P.2    Doehring, A.3    Dale, O.A.4
  • 49
    • 58149335418 scopus 로고    scopus 로고
    • Sulfasalazine blocks the development of tactile allodynia in diabetic rats
    • Berti-Mattera, L.N., Kern, T.S., Siegel, R.E., Nemet, I. & Mitchell, R. Sulfasalazine blocks the development of tactile allodynia in diabetic rats. Diabetes 57, 2801-2808 (2008).
    • (2008) Diabetes , vol.57 , pp. 2801-2808
    • Berti-Mattera, L.N.1    Kern, T.S.2    Siegel, R.E.3    Nemet, I.4    Mitchell, R.5
  • 50
    • 0034788778 scopus 로고    scopus 로고
    • Tetrahydrobiopterin deficiencies without hyperphenylalaninemia: Diagnosis and genetics of DOPA-responsive dystonia and sepiapterin reductase deficiency
    • DOI 10.1006/mgme.2001.3213
    • Blau, N., Bonafe, L. & Thony, B. Tetrahydrobiopterin deficiencies without hyperphenylalaninemia: Diagnosis and genetics of dopa-responsive dystonia and sepiapterin reductase deficiency. Mol. Genet. Metab. 74, 172-185 (2001). (Pubitemid 32955158)
    • (2001) Molecular Genetics and Metabolism , vol.74 , Issue.1-2 , pp. 172-185
    • Blau, N.1    Bonafe, L.2    Thony, B.3


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