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Volumn 7, Issue 1, 2012, Pages

A novel, "double-clamp" binding mode for human heme oxygenase-1 inhibition

Author keywords

[No Author keywords available]

Indexed keywords

1 (1H IMIDAZOL 1 YL) 4,4 DIPHENYL 2 BUTANONE; 1 (ADAMANTAN 1 YL) 2 (1H IMIDAZOL 1 YL)ETHANONE; 2 (2 PHENYLETHYL) 2 [(1H IMIDAZOL 1 YL)METHYL] 1,3 DIOXOLANE; 2 [2 (4 CHLOROPHENYL)ETHYL] 2 [(1H IMIDAZOL 1 YL)METHYL] 1,3 DIOXOLANE; 2 [2 (4 CHLOROPHENYL)ETHYL] 2 [(1H IMIDAZOL 1 YL)METHYL] 4 [[(5 TRIFLUOROMETHYLPYRIDIN 2 YL)THIO]METHYL] 1,3 DIOXOLANE; 4 PHENYL 1 (1,2,4 1H TRIAZOL 1 YL) 2 BUTANONE; 4 PHENYL 1 (1H IMIDAZOL 1 YL) 2 BUTANONE; AZALANSTAT; CARBON MONOXIDE; HEME OXYGENASE 1; HEME OXYGENASE INHIBITOR; PHENYL GROUP; QC 15; QC 308; QC 57; QC 65; QC 80; QC 82; QC 86; UNCLASSIFIED DRUG; ENZYME INHIBITOR;

EID: 84855998406     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0029514     Document Type: Article
Times cited : (29)

References (60)
  • 1
    • 0014670945 scopus 로고
    • Microsomal heme oxygenase. Characterization of the enzyme
    • Tenhunen R, Marver HS, Schmid R, (1969) Microsomal heme oxygenase. Characterization of the enzyme. J Biol Chem 244: 6388-6394.
    • (1969) J Biol Chem , vol.244 , pp. 6388-6394
    • Tenhunen, R.1    Marver, H.S.2    Schmid, R.3
  • 3
    • 0030923630 scopus 로고    scopus 로고
    • The heme oxygenase system: a regulator of second messenger gases
    • Maines MD, (1997) The heme oxygenase system: a regulator of second messenger gases. Annu Rev Pharmacol Toxicol 37: 517-554.
    • (1997) Annu Rev Pharmacol Toxicol , vol.37 , pp. 517-554
    • Maines, M.D.1
  • 4
    • 3042799349 scopus 로고    scopus 로고
    • Characterization of rat heme oxygenase-3 gene. Implication of processed pseudogenes derived from heme oxygenase-2 gene
    • Hayashi S, Omata Y, Sakamoto H, Higashimoto Y, Hara T, et al. (2004) Characterization of rat heme oxygenase-3 gene. Implication of processed pseudogenes derived from heme oxygenase-2 gene. Gene 336: 241-250.
    • (2004) Gene , vol.336 , pp. 241-250
    • Hayashi, S.1    Omata, Y.2    Sakamoto, H.3    Higashimoto, Y.4    Hara, T.5
  • 5
    • 33645945014 scopus 로고    scopus 로고
    • Heme oxygenase-1/carbon monoxide: from basic science to therapeutic applications
    • Ryter SW, Alam J, Choi AM, (2006) Heme oxygenase-1/carbon monoxide: from basic science to therapeutic applications. Physiol Rev 86: 583-650.
    • (2006) Physiol Rev , vol.86 , pp. 583-650
    • Ryter, S.W.1    Alam, J.2    Choi, A.M.3
  • 6
    • 0036127426 scopus 로고    scopus 로고
    • Heme oxygenase-1 mediates the anti-inflammatory effect of interleukin-10 in mice
    • Lee TS, Chau LY, (2002) Heme oxygenase-1 mediates the anti-inflammatory effect of interleukin-10 in mice. Nat Med 8: 240-246.
    • (2002) Nat Med , vol.8 , pp. 240-246
    • Lee, T.S.1    Chau, L.Y.2
  • 7
    • 0038143233 scopus 로고    scopus 로고
    • Induction of heme oxygenase-1 expression in murine macrophages is essential for the anti-inflammatory effect of low dose 15-deoxy-Delta 12,14-prostaglandin J2
    • Lee TS, Tsai HL, Chau LY, (2003) Induction of heme oxygenase-1 expression in murine macrophages is essential for the anti-inflammatory effect of low dose 15-deoxy-Delta 12,14-prostaglandin J2. J Biol Chem 278: 19325-19330.
    • (2003) J Biol Chem , vol.278 , pp. 19325-19330
    • Lee, T.S.1    Tsai, H.L.2    Chau, L.Y.3
  • 8
    • 34247171289 scopus 로고    scopus 로고
    • Hypoxia-mediated induction of heme oxygenase type I and carbon monoxide release from astrocytes protects nearby cerebral neurons from hypoxia-mediated apoptosis
    • Imuta N, Hori O, Kitao Y, Tabata Y, Yoshimoto T, et al. (2007) Hypoxia-mediated induction of heme oxygenase type I and carbon monoxide release from astrocytes protects nearby cerebral neurons from hypoxia-mediated apoptosis. Antioxid Redox Signal 9: 543-552.
    • (2007) Antioxid Redox Signal , vol.9 , pp. 543-552
    • Imuta, N.1    Hori, O.2    Kitao, Y.3    Tabata, Y.4    Yoshimoto, T.5
  • 10
    • 0035979281 scopus 로고    scopus 로고
    • Prooxidant and antioxidant activities of bilirubin and its metabolic precursor biliverdin: a structure-activity study
    • S0009279701002095 [pii]
    • Asad SF, Singh S, Ahmad A, Khan NU, Hadi SM, (2001) Prooxidant and antioxidant activities of bilirubin and its metabolic precursor biliverdin: a structure-activity study. Chem Biol Interact 137: 59-74 S0009279701002095 [pii].
    • (2001) Chem Biol Interact , vol.137 , pp. 59-74
    • Asad, S.F.1    Singh, S.2    Ahmad, A.3    Khan, N.U.4    Hadi, S.M.5
  • 11
    • 0032522255 scopus 로고    scopus 로고
    • Bilirubin is an effective antioxidant of peroxynitrite-mediated protein oxidation in human blood plasma
    • S0003-9861(98)90584-7 [pii];10.1006/abbi.1998.0584 [doi]
    • Minetti M, Mallozzi C, Di Stasi AM, Pietraforte D, (1998) Bilirubin is an effective antioxidant of peroxynitrite-mediated protein oxidation in human blood plasma. Arch Biochem Biophys 352: 165-174 S0003-9861(98)90584-7 [pii];10.1006/abbi.1998.0584 [doi].
    • (1998) Arch Biochem Biophys , vol.352 , pp. 165-174
    • Minetti, M.1    Mallozzi, C.2    Di Stasi, A.M.3    Pietraforte, D.4
  • 12
    • 77949525185 scopus 로고    scopus 로고
    • Mechanisms of cell protection by heme oxygenase-1
    • 10.1146/annurev.pharmtox.010909.105600 [doi]
    • Gozzelino R, Jeney V, Soares MP, (2010) Mechanisms of cell protection by heme oxygenase-1. Annu Rev Pharmacol Toxicol 50: 323-354 10.1146/annurev.pharmtox.010909.105600 [doi].
    • (2010) Annu Rev Pharmacol Toxicol , vol.50 , pp. 323-354
    • Gozzelino, R.1    Jeney, V.2    Soares, M.P.3
  • 13
    • 0030003896 scopus 로고    scopus 로고
    • Expression of heme oxygenase-1 (HSP32) in human prostate: normal, hyperplastic, and tumor tissue distribution
    • S0090-4295(96)00010-6 [pii]
    • Maines MD, Abrahamsson PA, (1996) Expression of heme oxygenase-1 (HSP32) in human prostate: normal, hyperplastic, and tumor tissue distribution. Urology 47: 727-733 S0090-4295(96)00010-6 [pii].
    • (1996) Urology , vol.47 , pp. 727-733
    • Maines, M.D.1    Abrahamsson, P.A.2
  • 14
    • 21044452445 scopus 로고    scopus 로고
    • Inhibition of heme oxygenase-1 increases responsiveness of pancreatic cancer cells to anticancer treatment
    • 11/10/3790 [pii];10.1158/1078-0432.CCR-04-2159 [doi]
    • Berberat PO, Dambrauskas Z, Gulbinas A, Giese T, Giese N, et al. (2005) Inhibition of heme oxygenase-1 increases responsiveness of pancreatic cancer cells to anticancer treatment. Clin Cancer Res 11: 3790-3798 11/10/3790 [pii];10.1158/1078-0432.CCR-04-2159 [doi].
    • (2005) Clin Cancer Res , vol.11 , pp. 3790-3798
    • Berberat, P.O.1    Dambrauskas, Z.2    Gulbinas, A.3    Giese, T.4    Giese, N.5
  • 15
    • 33745074201 scopus 로고    scopus 로고
    • Heme oxygenase-1 protects tumor cells against photodynamic therapy-mediated cytotoxicity
    • 1209378 [pii];10.1038/sj.onc.1209378 [doi]
    • Nowis D, Legat M, Grzela T, Niderla J, Wilczek E, et al. (2006) Heme oxygenase-1 protects tumor cells against photodynamic therapy-mediated cytotoxicity. Oncogene 25: 3365-3374 1209378 [pii];10.1038/sj.onc.1209378 [doi].
    • (2006) Oncogene , vol.25 , pp. 3365-3374
    • Nowis, D.1    Legat, M.2    Grzela, T.3    Niderla, J.4    Wilczek, E.5
  • 16
    • 0028176233 scopus 로고
    • Metalloporphyrins inhibit nitric oxide-dependent cGMP formation in vivo
    • Luo D, Vincent SR, (1994) Metalloporphyrins inhibit nitric oxide-dependent cGMP formation in vivo. Eur J Pharmacol 267: 263-267.
    • (1994) Eur J Pharmacol , vol.267 , pp. 263-267
    • Luo, D.1    Vincent, S.R.2
  • 17
    • 0028067882 scopus 로고
    • Inhibition of hippocampal heme oxygenase, nitric oxide synthase, and long-term potentiation by metalloporphyrins
    • Meffert MK, Haley JE, Schuman EM, Schulman H, Madison DV, (1994) Inhibition of hippocampal heme oxygenase, nitric oxide synthase, and long-term potentiation by metalloporphyrins. Neuron 13: 1225-1233.
    • (1994) Neuron , vol.13 , pp. 1225-1233
    • Meffert, M.K.1    Haley, J.E.2    Schuman, E.M.3    Schulman, H.4    Madison, D.V.5
  • 18
    • 0030834118 scopus 로고    scopus 로고
    • Pitfalls using metalloporphyrins in carbon monoxide research
    • Grundemar L, Ny L, (1997) Pitfalls using metalloporphyrins in carbon monoxide research. Trends Pharmacol Sci 18: 193-195.
    • (1997) Trends Pharmacol Sci , vol.18 , pp. 193-195
    • Grundemar, L.1    Ny, L.2
  • 19
    • 0032876719 scopus 로고    scopus 로고
    • Selective inhibition of heme oxygenase, without inhibition of nitric oxide synthase or soluble guanylyl cyclase, by metalloporphyrins at low concentrations
    • Appleton SD, Chretien ML, McLaughlin BE, Vreman HJ, Stevenson DK, et al. (1999) Selective inhibition of heme oxygenase, without inhibition of nitric oxide synthase or soluble guanylyl cyclase, by metalloporphyrins at low concentrations. Drug Metab Dispos 27: 1214-1219.
    • (1999) Drug Metab Dispos , vol.27 , pp. 1214-1219
    • Appleton, S.D.1    Chretien, M.L.2    McLaughlin, B.E.3    Vreman, H.J.4    Stevenson, D.K.5
  • 21
    • 32244436212 scopus 로고    scopus 로고
    • Selectivity of imidazole-dioxolane compounds for in vitro inhibition of microsomal haem oxygenase isoforms
    • Kinobe RT, Vlahakis JZ, Vreman HJ, Stevenson DK, Brien JF, et al. (2006) Selectivity of imidazole-dioxolane compounds for in vitro inhibition of microsomal haem oxygenase isoforms. Br J Pharmacol 147: 307-315.
    • (2006) Br J Pharmacol , vol.147 , pp. 307-315
    • Kinobe, R.T.1    Vlahakis, J.Z.2    Vreman, H.J.3    Stevenson, D.K.4    Brien, J.F.5
  • 22
    • 77956253388 scopus 로고    scopus 로고
    • The effects of azole-based heme oxygenase inhibitors on rat cytochromes P450 2E1 and 3A1/2 and human cytochromes P450 3A4 and 2D6
    • jpet.110.168492 [pii];10.1124/jpet.110.168492 [doi]
    • Hum M, McLaughlin BE, Roman G, Vlahakis JZ, Szarek WA, et al. (2010) The effects of azole-based heme oxygenase inhibitors on rat cytochromes P450 2E1 and 3A1/2 and human cytochromes P450 3A4 and 2D6. J Pharmacol Exp Ther 334: 981-987 jpet.110.168492 [pii];10.1124/jpet.110.168492 [doi].
    • (2010) J Pharmacol Exp Ther , vol.334 , pp. 981-987
    • Hum, M.1    McLaughlin, B.E.2    Roman, G.3    Vlahakis, J.Z.4    Szarek, W.A.5
  • 23
    • 33947609736 scopus 로고    scopus 로고
    • Heme oxygenase inhibition by 2-oxy-substituted 1-(1H-imidazol-1-yl)-4-phenylbutanes: effect of halogen substitution in the phenyl ring
    • Roman G, Riley JG, Vlahakis JZ, Kinobe RT, Brien JF, et al. (2007) Heme oxygenase inhibition by 2-oxy-substituted 1-(1H-imidazol-1-yl)-4-phenylbutanes: effect of halogen substitution in the phenyl ring. Bioorg Med Chem 15: 3225-3234.
    • (2007) Bioorg Med Chem , vol.15 , pp. 3225-3234
    • Roman, G.1    Riley, J.G.2    Vlahakis, J.Z.3    Kinobe, R.T.4    Brien, J.F.5
  • 24
    • 33745845157 scopus 로고    scopus 로고
    • Imidazole-dioxolane compounds as isozyme-selective heme oxygenase inhibitors
    • Vlahakis JZ, Kinobe RT, Bowers RJ, Brien JF, Nakatsu K, et al. (2006) Imidazole-dioxolane compounds as isozyme-selective heme oxygenase inhibitors. J Med Chem 49: 4437-4441.
    • (2006) J Med Chem , vol.49 , pp. 4437-4441
    • Vlahakis, J.Z.1    Kinobe, R.T.2    Bowers, R.J.3    Brien, J.F.4    Nakatsu, K.5
  • 26
    • 62149141367 scopus 로고    scopus 로고
    • Synthesis and evaluation of imidazole-dioxolane compounds as selective heme oxygenase inhibitors: effect of substituents at the 4-position of the dioxolane ring
    • Vlahakis JZ, Hum M, Rahman MN, Jia Z, Nakatsu K, et al. (2009) Synthesis and evaluation of imidazole-dioxolane compounds as selective heme oxygenase inhibitors: effect of substituents at the 4-position of the dioxolane ring. Bioorg Med Chem 17: 2461-2475.
    • (2009) Bioorg Med Chem , vol.17 , pp. 2461-2475
    • Vlahakis, J.Z.1    Hum, M.2    Rahman, M.N.3    Jia, Z.4    Nakatsu, K.5
  • 27
    • 71449115481 scopus 로고    scopus 로고
    • Heme oxygenase inhibition by 2-oxy-substituted 1-azolyl-4-phenylbutanes: effect of variation of the azole moiety. X-ray crystal structure of human heme oxygenase-1 in complex with 4-phenyl-1-(1H-1,2,4-triazol-1-yl)-2-butanone
    • JPP909 [pii];10.1111/j.1747-0285.2009.00909.x [doi]
    • Roman G, Rahman MN, Vukomanovic D, Jia Z, Nakatsu K, et al. (2010) Heme oxygenase inhibition by 2-oxy-substituted 1-azolyl-4-phenylbutanes: effect of variation of the azole moiety. X-ray crystal structure of human heme oxygenase-1 in complex with 4-phenyl-1-(1H-1,2,4-triazol-1-yl)-2-butanone. Chem Biol Drug Des 75: 68-90 JPP909 [pii];10.1111/j.1747-0285.2009.00909.x [doi].
    • (2010) Chem Biol Drug Des , vol.75 , pp. 68-90
    • Roman, G.1    Rahman, M.N.2    Vukomanovic, D.3    Jia, Z.4    Nakatsu, K.5
  • 28
    • 61949241329 scopus 로고    scopus 로고
    • Induction of prostacyclin by steady laminar shear stress suppresses tumor necrosis factor-alpha biosynthesis via heme oxygenase-1 in human endothelial cells
    • CIRCRESAHA.108.191114 [pii];10.1161/CIRCRESAHA.108.191114 [doi]
    • Di FL, Totani L, Dovizio M, Piccoli A, Di FA, et al. (2009) Induction of prostacyclin by steady laminar shear stress suppresses tumor necrosis factor-alpha biosynthesis via heme oxygenase-1 in human endothelial cells. Circ Res 104: 506-513 CIRCRESAHA.108.191114 [pii];10.1161/CIRCRESAHA.108.191114 [doi].
    • (2009) Circ Res , vol.104 , pp. 506-513
    • Di, F.L.1    Totani, L.2    Dovizio, M.3    Piccoli, A.4    Di, F.A.5
  • 29
    • 77149138802 scopus 로고    scopus 로고
    • Structural characterization of human heme oxygenase-1 in complex with azole-based inhibitors
    • S0162-0134(09)00259-1 [pii];10.1016/j.jinorgbio.2009.10.011 [doi]
    • Rahman MN, Vlahakis JZ, Roman G, Vukomanovic D, Szarek WA, et al. (2010) Structural characterization of human heme oxygenase-1 in complex with azole-based inhibitors. J Inorg Biochem 104: 324-330 S0162-0134(09)00259-1 [pii];10.1016/j.jinorgbio.2009.10.011 [doi].
    • (2010) J Inorg Biochem , vol.104 , pp. 324-330
    • Rahman, M.N.1    Vlahakis, J.Z.2    Roman, G.3    Vukomanovic, D.4    Szarek, W.A.5
  • 30
    • 53549129271 scopus 로고    scopus 로고
    • X-ray crystal structure of human heme oxygenase-1 in complex with 1-(adamantan-1-yl)-2-(1H-imidazol-1-yl)ethanone: a common binding mode for imidazole-based heme oxygenase-1 inhibitors
    • Rahman MN, Vlahakis JZ, Szarek WA, Nakatsu K, Jia Z, (2008) X-ray crystal structure of human heme oxygenase-1 in complex with 1-(adamantan-1-yl)-2-(1H-imidazol-1-yl)ethanone: a common binding mode for imidazole-based heme oxygenase-1 inhibitors. J Med Chem 51: 5943-5952.
    • (2008) J Med Chem , vol.51 , pp. 5943-5952
    • Rahman, M.N.1    Vlahakis, J.Z.2    Szarek, W.A.3    Nakatsu, K.4    Jia, Z.5
  • 31
    • 68549120921 scopus 로고    scopus 로고
    • X-ray crystal structure of human heme oxygenase-1 with (2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4[((5-tri fluoromethylpyridin-2-yl)thio)methyl]-1,3-dioxolane: a novel, inducible binding mode
    • Rahman MN, Vlahakis JZ, Vukomanovic D, Szarek WA, Nakatsu K, et al. (2009) X-ray crystal structure of human heme oxygenase-1 with (2R,4S)-2-[2-(4-chlorophenyl)ethyl]-2-[(1H-imidazol-1-yl)methyl]-4[((5-tri fluoromethylpyridin-2-yl)thio)methyl]-1,3-dioxolane: a novel, inducible binding mode. J Med Chem 52: 4946-4950.
    • (2009) J Med Chem , vol.52 , pp. 4946-4950
    • Rahman, M.N.1    Vlahakis, J.Z.2    Vukomanovic, D.3    Szarek, W.A.4    Nakatsu, K.5
  • 32
    • 33847033375 scopus 로고    scopus 로고
    • X-ray crystallographic and biochemical characterization of the inhibitory action of an imidazole-dioxolane compound on heme oxygenase
    • Sugishima M, Higashimoto Y, Oishi T, Takahashi H, Sakamoto H, et al. (2007) X-ray crystallographic and biochemical characterization of the inhibitory action of an imidazole-dioxolane compound on heme oxygenase. Biochemistry 46: 1860-1867.
    • (2007) Biochemistry , vol.46 , pp. 1860-1867
    • Sugishima, M.1    Higashimoto, Y.2    Oishi, T.3    Takahashi, H.4    Sakamoto, H.5
  • 33
    • 78650763939 scopus 로고    scopus 로고
    • Rapid, convenient method for screening imidazole-containing compounds for heme oxygenase inhibition
    • S1056-8719(10)00088-2 [pii];10.1016/j.vascn.2010.05.015 [doi]
    • Vlahakis JZ, Rahman MN, Roman G, Jia Z, Nakatsu K, et al. (2010) Rapid, convenient method for screening imidazole-containing compounds for heme oxygenase inhibition. J Pharmacol Toxicol Methods S1056-8719(10)00088-2 [pii];10.1016/j.vascn.2010.05.015 [doi].
    • (2010) J Pharmacol Toxicol Methods
    • Vlahakis, J.Z.1    Rahman, M.N.2    Roman, G.3    Jia, Z.4    Nakatsu, K.5
  • 34
    • 77952028218 scopus 로고    scopus 로고
    • Recombinant truncated and microsomal heme oxygenase-1 and -2: differential sensitivity to inhibitors
    • y10-004 [pii];10.1139/y10-004 [doi]
    • Vukomanovic D, McLaughlin B, Rahman MN, Vlahakis JZ, Roman G, et al. (2010) Recombinant truncated and microsomal heme oxygenase-1 and-2: differential sensitivity to inhibitors. Can J Physiol Pharmacol 88: 480-486 y10-004 [pii];10.1139/y10-004 [doi].
    • (2010) Can J Physiol Pharmacol , vol.88 , pp. 480-486
    • Vukomanovic, D.1    McLaughlin, B.2    Rahman, M.N.3    Vlahakis, J.Z.4    Roman, G.5
  • 35
    • 0037424264 scopus 로고    scopus 로고
    • Comparison of the heme-free and -bound crystal structures of human heme oxygenase-1
    • Lad L, Schuller DJ, Shimizu H, Friedman J, Li H, et al. (2003) Comparison of the heme-free and-bound crystal structures of human heme oxygenase-1. J Biol Chem 278: 7834-7843.
    • (2003) J Biol Chem , vol.278 , pp. 7834-7843
    • Lad, L.1    Schuller, D.J.2    Shimizu, H.3    Friedman, J.4    Li, H.5
  • 38
    • 38049144525 scopus 로고    scopus 로고
    • Comparison of apo- and heme-bound crystal structures of a truncated human heme oxygenase-2
    • Bianchetti CM, Yi L, Ragsdale SW, Phillips GN Jr, (2007) Comparison of apo- and heme-bound crystal structures of a truncated human heme oxygenase-2. J Biol Chem 282: 37624-37631.
    • (2007) J Biol Chem , vol.282 , pp. 37624-37631
    • Bianchetti, C.M.1    Yi, L.2    Ragsdale, S.W.3    Phillips Jr., G.N.4
  • 39
    • 35648992389 scopus 로고    scopus 로고
    • Expression and characterization of full-length human heme oxygenase-1: the presence of intact membrane-binding region leads to increased binding affinity for NADPH cytochrome P450 reductase
    • Huber WJ III, Backes WL, (2007) Expression and characterization of full-length human heme oxygenase-1: the presence of intact membrane-binding region leads to increased binding affinity for NADPH cytochrome P450 reductase. Biochemistry 46: 12212-12219.
    • (2007) Biochemistry , vol.46 , pp. 12212-12219
    • Huber III, W.J.1    Backes, W.L.2
  • 40
    • 63849254891 scopus 로고    scopus 로고
    • Measurement of membrane-bound human heme oxygenase-1 activity using a chemically defined assay system
    • Huber WJ III, Marohnic CC, Peters M, Alam J, Reed JR, et al. (2009) Measurement of membrane-bound human heme oxygenase-1 activity using a chemically defined assay system. Drug Metab Dispos 37: 857-864.
    • (2009) Drug Metab Dispos , vol.37 , pp. 857-864
    • Huber III, W.J.1    Marohnic, C.C.2    Peters, M.3    Alam, J.4    Reed, J.R.5
  • 41
    • 58549118279 scopus 로고    scopus 로고
    • C-Terminal membrane spanning region of human heme oxygenase-1 mediates a time-dependent complex formation with cytochrome P450 reductase
    • Huber WJ III, Scruggs BA, Backes WL, (2009) C-Terminal membrane spanning region of human heme oxygenase-1 mediates a time-dependent complex formation with cytochrome P450 reductase. Biochemistry 48: 190-197.
    • (2009) Biochemistry , vol.48 , pp. 190-197
    • Huber III, W.J.1    Scruggs, B.A.2    Backes, W.L.3
  • 42
    • 34547135735 scopus 로고    scopus 로고
    • Heme oxygenase-1 protein localizes to the nucleus and activates transcription factors important in oxidative stress
    • M607954200 [pii];10.1074/jbc.M607954200 [doi]
    • Lin Q, Weis S, Yang G, Weng YH, Helston R, et al. (2007) Heme oxygenase-1 protein localizes to the nucleus and activates transcription factors important in oxidative stress. J Biol Chem 282: 20621-20633 M607954200 [pii];10.1074/jbc.M607954200 [doi].
    • (2007) J Biol Chem , vol.282 , pp. 20621-20633
    • Lin, Q.1    Weis, S.2    Yang, G.3    Weng, Y.H.4    Helston, R.5
  • 43
    • 0034871085 scopus 로고    scopus 로고
    • Heme oxygenase-2 interaction with metalloporphyrins: function of heme regulatory motifs
    • 10.1089/15230860152543023 [doi]
    • Huang TJ, McCoubrey WK Jr, Maines MD, (2001) Heme oxygenase-2 interaction with metalloporphyrins: function of heme regulatory motifs. Antioxid Redox Signal 3: 685-696 10.1089/15230860152543023 [doi].
    • (2001) Antioxid Redox Signal , vol.3 , pp. 685-696
    • Huang, T.J.1    McCoubrey Jr., W.K.2    Maines, M.D.3
  • 44
    • 1842330947 scopus 로고    scopus 로고
    • Heme oxygenase-2 is a hemoprotein and binds heme through heme regulatory motifs that are not involved in heme catalysis
    • McCoubrey WK Jr, Huang TJ, Maines MD, (1997) Heme oxygenase-2 is a hemoprotein and binds heme through heme regulatory motifs that are not involved in heme catalysis. J Biol Chem 272: 12568-12574.
    • (1997) J Biol Chem , vol.272 , pp. 12568-12574
    • McCoubrey Jr., W.K.1    Huang, T.J.2    Maines, M.D.3
  • 45
    • 0033539642 scopus 로고    scopus 로고
    • Heme is an effector molecule for iron-dependent degradation of the bacterial iron response regulator (Irr) protein
    • Qi Z, Hamza I, O'Brian MR, (1999) Heme is an effector molecule for iron-dependent degradation of the bacterial iron response regulator (Irr) protein. Proc Natl Acad Sci U S A 96: 13056-13061.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 13056-13061
    • Qi, Z.1    Hamza, I.2    O'Brian, M.R.3
  • 46
    • 34547121697 scopus 로고    scopus 로고
    • Evidence that the heme regulatory motifs in heme oxygenase-2 serve as a thiol/disulfide redox switch regulating heme binding
    • Yi L, Ragsdale SW, (2007) Evidence that the heme regulatory motifs in heme oxygenase-2 serve as a thiol/disulfide redox switch regulating heme binding. J Biol Chem 282: 21056-21067.
    • (2007) J Biol Chem , vol.282 , pp. 21056-21067
    • Yi, L.1    Ragsdale, S.W.2
  • 47
    • 68949122857 scopus 로고    scopus 로고
    • Heme regulatory motifs in heme oxygenase-2 form a thiol/disulfide redox switch that responds to the cellular redox state
    • M109.015651 [pii];10.1074/jbc.M109.015651 [doi]
    • Yi L, Jenkins PM, Leichert LI, Jakob U, Martens JR, et al. (2009) Heme regulatory motifs in heme oxygenase-2 form a thiol/disulfide redox switch that responds to the cellular redox state. J Biol Chem 284: 20556-20561 M109.015651 [pii];10.1074/jbc.M109.015651 [doi].
    • (2009) J Biol Chem , vol.284 , pp. 20556-20561
    • Yi, L.1    Jenkins, P.M.2    Leichert, L.I.3    Jakob, U.4    Martens, J.R.5
  • 48
    • 77956909582 scopus 로고    scopus 로고
    • Spectroscopic insights into axial ligation and active-site H-bonding in substrate-bound human heme oxygenase-2
    • 10.1007/s00775-010-0672-8 [doi]
    • Gardner JD, Yi L, Ragsdale SW, Brunold TC, (2010) Spectroscopic insights into axial ligation and active-site H-bonding in substrate-bound human heme oxygenase-2. J Biol Inorg Chem 15: 1117-1127 10.1007/s00775-010-0672-8 [doi].
    • (2010) J Biol Inorg Chem , vol.15 , pp. 1117-1127
    • Gardner, J.D.1    Yi, L.2    Ragsdale, S.W.3    Brunold, T.C.4
  • 49
    • 84889582115 scopus 로고    scopus 로고
    • NMR Chemical Shifts of Common Laboratory Solvents as Trace Impurities
    • Gottlieb HE, Kotlyar V, Nudelman A, (1997) NMR Chemical Shifts of Common Laboratory Solvents as Trace Impurities. J Org Chem 62: 7512-7515.
    • (1997) J Org Chem , vol.62 , pp. 7512-7515
    • Gottlieb, H.E.1    Kotlyar, V.2    Nudelman, A.3
  • 50
    • 0023837193 scopus 로고
    • Heme oxygenase activity as measured by carbon monoxide production
    • Vreman HJ, Stevenson DK, (1988) Heme oxygenase activity as measured by carbon monoxide production. Anal Biochem 168: 31-38.
    • (1988) Anal Biochem , vol.168 , pp. 31-38
    • Vreman, H.J.1    Stevenson, D.K.2
  • 51
    • 0029015225 scopus 로고
    • Heme oxygenase activity in the adult rat aorta and liver as measured by carbon monoxide formation
    • Cook MN, Nakatsu K, Marks GS, McLaughlin BE, Vreman HJ, et al. (1995) Heme oxygenase activity in the adult rat aorta and liver as measured by carbon monoxide formation. Can J Physiol Pharmacol 73: 515-518.
    • (1995) Can J Physiol Pharmacol , vol.73 , pp. 515-518
    • Cook, M.N.1    Nakatsu, K.2    Marks, G.S.3    McLaughlin, B.E.4    Vreman, H.J.5
  • 52
    • 76449099287 scopus 로고    scopus 로고
    • XDS
    • S0907444909047337 [pii];10.1107/S0907444909047337 [doi]
    • Kabsch W, (2010) XDS. Acta Crystallogr D Biol Crystallogr 66: 125-132 S0907444909047337 [pii];10.1107/S0907444909047337 [doi].
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 125-132
    • Kabsch, W.1
  • 54
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • Collaborative Computational Project N4
    • Collaborative Computational Project N4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50: 760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 55
    • 7544226311 scopus 로고    scopus 로고
    • PRODRG: a tool for high-throughput crystallography of protein-ligand complexes
    • Schuttelkopf AW, van Aalten DM, (2004) PRODRG: a tool for high-throughput crystallography of protein-ligand complexes. Acta Crystallogr D Biol Crystallogr 60: 1355-1363.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 1355-1363
    • Schuttelkopf, A.W.1    van Aalten, D.M.2
  • 56
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P, Cowtan K, (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60: 2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 57
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • 10.1107/S0907444996012255 [doi];S0907444996012255 [pii]
    • Murshudov GN, Vagin AA, Dodson EJ, (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D Biol Crystallogr 53: 240-255 10.1107/S0907444996012255 [doi];S0907444996012255 [pii].
    • (1997) Acta Crystallogr D Biol Crystallogr , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 58
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • S0907444904026460 [pii];10.1107/S0907444904026460 [doi]
    • Krissinel E, Henrick K, (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr D Biol Crystallogr 60: 2256-2268 S0907444904026460 [pii];10.1107/S0907444904026460 [doi].
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 59


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