메뉴 건너뛰기




Volumn 41, Issue 47, 2002, Pages 13915-13925

Conformational changes in nitric oxide synthases induced by chlorzoxazone and nitroindazoles: Crystallographic and computational analyses of inhibitor potency

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITES;

EID: 18744380020     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi026313j     Document Type: Article
Times cited : (62)

References (56)
  • 1
    • 0028026868 scopus 로고
    • Nitric oxide synthase: Aspects concerning structure and catalysis
    • Marietta, M. A. (1994) Nitric oxide synthase: Aspects concerning structure and catalysis, Cell 78, 927-930.
    • (1994) Cell , vol.78 , pp. 927-930
    • Marietta, M.A.1
  • 2
    • 0028902552 scopus 로고
    • Nitric oxide synthases: Properties and catalytic mechanism
    • Griffith, O. W., and Stuehr, D. J. (1995) Nitric oxide synthases: Properties and catalytic mechanism, Annu. Rev. Physiol. 57, 707-736.
    • (1995) Annu. Rev. Physiol. , vol.57 , pp. 707-736
    • Griffith, O.W.1    Stuehr, D.J.2
  • 3
    • 0029776782 scopus 로고    scopus 로고
    • Understanding the structural aspects of neuronal nitric oxide synthase (NOS) using microdissection by molecular cloning techniques: Molecular dissection of neuronal NOS
    • Masters, B. S., McMillan, K., Nishimura, J., Martasek, P., Roman, L. J., Sheta, E., Gross, S. S., and Salerno, J. (1996) Understanding the structural aspects of neuronal nitric oxide synthase (NOS) using microdissection by molecular cloning techniques: Molecular dissection of neuronal NOS, Adv. Exp. Med. Biol. 387, 163-169.
    • (1996) Adv. Exp. Med. Biol. , vol.387 , pp. 163-169
    • Masters, B.S.1    McMillan, K.2    Nishimura, J.3    Martasek, P.4    Roman, L.J.5    Sheta, E.6    Gross, S.S.7    Salerno, J.8
  • 4
    • 0032789444 scopus 로고    scopus 로고
    • Nitric oxide: A unique endogenous signaling molecule in vascular biology
    • Ignarro, L. J. (1999) Nitric oxide: A unique endogenous signaling molecule in vascular biology, Biosci. Rep. 19, 51-71.
    • (1999) Biosci. Rep. , vol.19 , pp. 51-71
    • Ignarro, L.J.1
  • 5
    • 0033219947 scopus 로고    scopus 로고
    • Cellular signaling with nitric oxide and cyclic GMP
    • Murad, F. (1999) Cellular signaling with nitric oxide and cyclic GMP, Braz. J. Med. Biol. Res. 32, 1317-1327.
    • (1999) Braz. J. Med. Biol. Res. , vol.32 , pp. 1317-1327
    • Murad, F.1
  • 6
    • 0027202456 scopus 로고
    • Molecular mechanisms of nitric oxide regulation. Potential relevance to cardiovascular disease
    • Dinerman, J. L., Lowenstein, C. J., and Snyder, S. H. (1993) Molecular mechanisms of nitric oxide regulation. Potential relevance to cardiovascular disease, Circ. Res. 73, 217-222.
    • (1993) Circ. Res. , vol.73 , pp. 217-222
    • Dinerman, J.L.1    Lowenstein, C.J.2    Snyder, S.H.3
  • 7
    • 0028128416 scopus 로고
    • NO at work
    • Schmidt, H. H., and Walter, U. (1994) NO at work, Cell 78, 919-925.
    • (1994) Cell , vol.78 , pp. 919-925
    • Schmidt, H.H.1    Walter, U.2
  • 8
    • 0030752552 scopus 로고    scopus 로고
    • Design of nitric oxide synthase inhibitors and their use to reverse hypotension associated with cancer immunotherapy
    • Griffith, O. W., and Kilbourn, R. G. (1997) Design of nitric oxide synthase inhibitors and their use to reverse hypotension associated with cancer immunotherapy, Adv. Enzyme Regul. 37, 171-194.
    • (1997) Adv. Enzyme Regul. , vol.37 , pp. 171-194
    • Griffith, O.W.1    Kilbourn, R.G.2
  • 10
    • 0032571411 scopus 로고    scopus 로고
    • Structure of nitric oxide synthase oxygenase dimer with pterin and substrate
    • Crane, B. R., Arvai, A. S., Ghosh, D. K., Wu, C., Getzoff, E. D., Stuehr, D. J., and Tainer, J. A. (1998) Structure of nitric oxide synthase oxygenase dimer with pterin and substrate, Science 279, 2121-2126.
    • (1998) Science , vol.279 , pp. 2121-2126
    • Crane, B.R.1    Arvai, A.S.2    Ghosh, D.K.3    Wu, C.4    Getzoff, E.D.5    Stuehr, D.J.6    Tainer, J.A.7
  • 11
    • 0032416666 scopus 로고    scopus 로고
    • Crystal structure of constitutive endothelial nitric oxide synthase: A paradigm for pterin function involving a novel metal center
    • Raman, C. S., Li, H., Martasek, P., Kral, V., Masters, B. S., and Poulos, T. L. (1998) Crystal structure of constitutive endothelial nitric oxide synthase: A paradigm for pterin function involving a novel metal center, Cell 95, 939-950.
    • (1998) Cell , vol.95 , pp. 939-950
    • Raman, C.S.1    Li, H.2    Martasek, P.3    Kral, V.4    Masters, B.S.5    Poulos, T.L.6
  • 13
    • 0030917621 scopus 로고    scopus 로고
    • Mutagenesis of acidic residues in the oxygenase domain of inducible nitric-oxide synthase identifies a glutamate involved in arginine binding
    • Gachhui, R., Ghosh, D. K., Wu, C., Parkinson, J., Crane, B. R., and Stuehr, D. J. (1997) Mutagenesis of acidic residues in the oxygenase domain of inducible nitric-oxide synthase identifies a glutamate involved in arginine binding, Biochemistry 36, 5097-5103.
    • (1997) Biochemistry , vol.36 , pp. 5097-5103
    • Gachhui, R.1    Ghosh, D.K.2    Wu, C.3    Parkinson, J.4    Crane, B.R.5    Stuehr, D.J.6
  • 14
    • 0030889046 scopus 로고    scopus 로고
    • Mutation of Glu-361 in human endothelial nitric-oxide synthase selectively abolishes L-arginine binding without perturbing the behavior of heme and other redox centers
    • Chen, P. F., Tsai, A. L., Berka, V., and Wu, K. K. (1997) Mutation of Glu-361 in human endothelial nitric-oxide synthase selectively abolishes L-arginine binding without perturbing the behavior of heme and other redox centers, J. Biol. Chem. 272, 6114-6118.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6114-6118
    • Chen, P.F.1    Tsai, A.L.2    Berka, V.3    Wu, K.K.4
  • 15
    • 0034712677 scopus 로고    scopus 로고
    • Structures of the Nω-hydroxy-L-arginine complex of inducible nitric oxide synthase oxygenase dimer with active and inactive pterins
    • Crane, B. R., Arvai, A. S., Ghosh, S., Getzoff, E. D., Stuehr, D. J., and Tainer, J. A. (2000) Structures of the Nω-hydroxy-L-arginine complex of inducible nitric oxide synthase oxygenase dimer with active and inactive pterins, Biochemistry 39, 4608-4621.
    • (2000) Biochemistry , vol.39 , pp. 4608-4621
    • Crane, B.R.1    Arvai, A.S.2    Ghosh, S.3    Getzoff, E.D.4    Stuehr, D.J.5    Tainer, J.A.6
  • 16
    • 0033520402 scopus 로고    scopus 로고
    • L-Arginine binding to nitric oxide synthase: The role of H-bonds to the nonreactive guanidinium nitrogens
    • Babu, B., Frey, C., and Griffith, O. (1999) L-Arginine binding to nitric oxide synthase: The role of H-bonds to the nonreactive guanidinium nitrogens, J. Biol. Chem. 274, 25218-25226.
    • (1999) J. Biol. Chem. , vol.274 , pp. 25218-25226
    • Babu, B.1    Frey, C.2    Griffith, O.3
  • 17
    • 0034738986 scopus 로고    scopus 로고
    • Mapping the active site polarity in structures of endothelial nitric oxide synthase heme domain complexed with isothioureas
    • Li, H., Raman, C. S., Martasek, P., Kral, V., Masters, B. S., and Poulos, T. L. (2000) Mapping the active site polarity in structures of endothelial nitric oxide synthase heme domain complexed with isothioureas, J. Inorg. Biochem. 81, 133-139.
    • (2000) J. Inorg. Biochem. , vol.81 , pp. 133-139
    • Li, H.1    Raman, C.S.2    Martasek, P.3    Kral, V.4    Masters, B.S.5    Poulos, T.L.6
  • 18
    • 0032133353 scopus 로고    scopus 로고
    • Design of isoform-selective inhibitors of nitric oxide synthase
    • Babu, B. R., and Griffith, O. W. (1998) Design of isoform-selective inhibitors of nitric oxide synthase, Curr. Opin. Chem. Biol. 2, 491-500.
    • (1998) Curr. Opin. Chem. Biol. , vol.2 , pp. 491-500
    • Babu, B.R.1    Griffith, O.W.2
  • 19
    • 0030040255 scopus 로고    scopus 로고
    • Selective pharmacological inhibition of distinct nitric oxide synthase isoforms
    • Southan, G. J., and Szabo, C. (1996) Selective pharmacological inhibition of distinct nitric oxide synthase isoforms, Biochem. Pharmacol. 51, 383-394.
    • (1996) Biochem. Pharmacol. , vol.51 , pp. 383-394
    • Southan, G.J.1    Szabo, C.2
  • 20
    • 0027404419 scopus 로고
    • 7-Nitro indazole, an inhibitor of nitric oxide synthase, exhibits anti-nociceptive activity in the mouse without increasing blood pressure
    • Moore, P. K., Babbedge, R. C., Wallace, P., Gaffen, Z. A., and Hart, S. L. (1993) 7-Nitro indazole, an inhibitor of nitric oxide synthase, exhibits anti-nociceptive activity in the mouse without increasing blood pressure, Br. J. Pharmacol. 108, 296-297.
    • (1993) Br. J. Pharmacol. , vol.108 , pp. 296-297
    • Moore, P.K.1    Babbedge, R.C.2    Wallace, P.3    Gaffen, Z.A.4    Hart, S.L.5
  • 21
    • 0031021805 scopus 로고    scopus 로고
    • Characterization of inducible nitric-oxide synthase by cytochrome P-450 substrates and inhibitors. Inhibition by chlorzoxazone
    • Grant, S. K., Green, B. G., Wang, R., Pacholok, S. G., and Kozarich, J. W. (1997) Characterization of inducible nitric-oxide synthase by cytochrome P-450 substrates and inhibitors. Inhibition by chlorzoxazone, J. Biol. Chem. 272, 977-983.
    • (1997) J. Biol. Chem. , vol.272 , pp. 977-983
    • Grant, S.K.1    Green, B.G.2    Wang, R.3    Pacholok, S.G.4    Kozarich, J.W.5
  • 22
  • 23
    • 0027159323 scopus 로고
    • Single-dose disulfiram inhibition of chlorzoxazone metabolism: A clinical probe for P450 2E1
    • Kharasch, E. D., Thummel, K. E., Mhyre, J., and Lillibridge, J. H. (1993) Single-dose disulfiram inhibition of chlorzoxazone metabolism: A clinical probe for P450 2E1, Clin. Pharmacol. Ther. 53, 643-650.
    • (1993) Clin. Pharmacol. Ther. , vol.53 , pp. 643-650
    • Kharasch, E.D.1    Thummel, K.E.2    Mhyre, J.3    Lillibridge, J.H.4
  • 24
    • 0035856516 scopus 로고    scopus 로고
    • Crystal structure of nitric oxide synthase bound to nitro indazole reveals a novel inactivation mechanism
    • Raman, C. S., Li, H., Martasek, P., Southan, G., Masters, B. S. S., and Poulos, T. L. (2001) Crystal structure of Nitric Oxide Synthase Bound to Nitro Indazole Reveals a Novel Inactivation Mechanism, Biochemistry 40, 13448-13455.
    • (2001) Biochemistry , vol.40 , pp. 13448-13455
    • Raman, C.S.1    Li, H.2    Martasek, P.3    Southan, G.4    Masters, B.S.S.5    Poulos, T.L.6
  • 27
    • 0030758321 scopus 로고    scopus 로고
    • Characterization of the inducible nitric oxide synthase oxygenase domain identifies a 49 amino acid segment required for subunit dimerization and tetrahydrobiopterin interaction
    • Ghosh, D. K., Wu, C., Pitters, E., Moloney, M., Werner, E. R., Mayer, B., and Stuehr, D. J. (1997) Characterization of the inducible nitric oxide synthase oxygenase domain identifies a 49 amino acid segment required for subunit dimerization and tetrahydrobiopterin interaction, Biochemistry 36, 10609-10619.
    • (1997) Biochemistry , vol.36 , pp. 10609-10619
    • Ghosh, D.K.1    Wu, C.2    Pitters, E.3    Moloney, M.4    Werner, E.R.5    Mayer, B.6    Stuehr, D.J.7
  • 28
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode, Methods Enzymol. 276, 307-336.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-336
    • Otwinowski, Z.1    Minor, W.2
  • 30
    • 0032790081 scopus 로고    scopus 로고
    • XtalView/Xfit: A versatile program for manipulating atomic coordinates and electron density
    • McRee, D. (1999) XtalView/Xfit: A versatile program for manipulating atomic coordinates and electron density, J. Struct. Biol. 125, 156-165.
    • (1999) J. Struct. Biol. , vol.125 , pp. 156-165
    • McRee, D.1
  • 31
    • 0033529670 scopus 로고    scopus 로고
    • Role of reductase domain cluster 1 acidic residues in neuronal nitric-oxide synthase. Characterization of the FMN-free enzyme
    • Adak, S., Ghosh, S., Abu-Soud, H. M., and Stuehr, D. J. (1999) Role of reductase domain cluster 1 acidic residues in neuronal nitric-oxide synthase. Characterization of the FMN-free enzyme, J. Biol. Chem. 274, 22313-22320.
    • (1999) J. Biol. Chem. , vol.274 , pp. 22313-22320
    • Adak, S.1    Ghosh, S.2    Abu-Soud, H.M.3    Stuehr, D.J.4
  • 32
    • 0030585351 scopus 로고    scopus 로고
    • High-level expression of mouse inducible nitric oxide synthase in Escherichia coli requires coexpression with calmodulin
    • Wu, C., Zhang, J., Abu-Soud, H., Ghosh, D. K., and Stuehr, D. J. (1996) High-level expression of mouse inducible nitric oxide synthase in Escherichia coli requires coexpression with calmodulin, Biochem. Biophys. Res. Commun. 222, 439-444.
    • (1996) Biochem. Biophys. Res. Commun. , vol.222 , pp. 439-444
    • Wu, C.1    Zhang, J.2    Abu-Soud, H.3    Ghosh, D.K.4    Stuehr, D.J.5
  • 33
    • 0028170425 scopus 로고
    • L-Arginine and calmodulin regulation of the heme iron reactivity in neuronal nitric oxide synthase
    • Matsuoka, A., Stuehr, D. J., Olson, J. S., Clark, P., and Ikeda-Saito, M. (1994) L-Arginine and calmodulin regulation of the heme iron reactivity in neuronal nitric oxide synthase, J. Biol. Chem. 269, 20335-20339.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20335-20339
    • Matsuoka, A.1    Stuehr, D.J.2    Olson, J.S.3    Clark, P.4    Ikeda-Saito, M.5
  • 34
    • 0015861774 scopus 로고
    • Relationship between the inhibition constant (Ki) and the concentration of inhibitor which causes 50% inhibition (IC50) of an enzymatic reaction
    • Cheng, Y., and Prusoff, W. (1973) Relationship between the inhibition constant (Ki) and the concentration of inhibitor which causes 50% inhibition (IC50) of an enzymatic reaction, Biochem. Pharmacol. 22, 3099-3108.
    • (1973) Biochem. Pharmacol. , vol.22 , pp. 3099-3108
    • Cheng, Y.1    Prusoff, W.2
  • 35
    • 84986468608 scopus 로고
    • An approach to computing electrostatic charges for molecules
    • Singh, U. C., and Kollman, P. A. (1984) An approach to computing electrostatic charges for molecules, J. Comput. Chem. 5, 145-159.
    • (1984) J. Comput. Chem. , vol.5 , pp. 145-159
    • Singh, U.C.1    Kollman, P.A.2
  • 36
    • 84986492477 scopus 로고
    • Atomic charges derived from semiempirical methods
    • Bessler, B. H., Merz, K. M., Jr., and Kollman, P. A. (1990) Atomic charges derived from semiempirical methods, J. Comput. Chem. 11, 431-439.
    • (1990) J. Comput. Chem. , vol.11 , pp. 431-439
    • Bessler, B.H.1    Merz K.M., Jr.2    Kollman, P.A.3
  • 37
    • 11644261806 scopus 로고    scopus 로고
    • AutoDock 3.0: Automated Docking using a Lamarckian genetic algorithm and an empirical free energy function
    • Morris, G. M., Goodsell, D. S., Halliday, S., Huey, R., Hart, W. E., Belew, R. K., and Olson, A. J. (1998) AutoDock 3.0: Automated Docking using a Lamarckian genetic algorithm and an empirical free energy function, J. Comput. Chem. 19, 1639-1662.
    • (1998) J. Comput. Chem. , vol.19 , pp. 1639-1662
    • Morris, G.M.1    Goodsell, D.S.2    Halliday, S.3    Huey, R.4    Hart, W.E.5    Belew, R.K.6    Olson, A.J.7
  • 38
    • 0032605099 scopus 로고    scopus 로고
    • Altman, R. B., Lauderdale, K., Dunker, A. K., Hunter, L., and Klein, T. E., Eds., World Scientific Press, Mauna Lani, HI
    • Sanner, M. F., Duncan, B. S., Carrillo, C. J., and Olson, A. J. (1999) in Biocomputing '99: Proceedings of the Pacific Symposium (Altman, R. B., Lauderdale, K., Dunker, A. K., Hunter, L., and Klein, T. E., Eds.) pp 401-412, World Scientific Press, Mauna Lani, HI.
    • (1999) Biocomputing '99: Proceedings of the Pacific Symposium , pp. 401-412
    • Sanner, M.F.1    Duncan, B.S.2    Carrillo, C.J.3    Olson, A.J.4
  • 39
  • 40
    • 21844506602 scopus 로고
    • Synthesis, characterization, and structure of lanthanide picrate complexes with tetramethylene-sulfoxide (TMSO)
    • Zinner, L. B., Ayala, J. D., Andrade de Silva, M. A., Bombieri, G., and Del Pra, A. (1994) Synthesis, characterization, and structure of lanthanide picrate complexes with tetramethylene-sulfoxide (TMSO), J. Chem. Crystallogr. 24, 445-450.
    • (1994) J. Chem. Crystallogr. , vol.24 , pp. 445-450
    • Zinner, L.B.1    Ayala, J.D.2    Andrade de Silva, M.A.3    Bombieri, G.4    Del Pra, A.5
  • 41
    • 0029797753 scopus 로고    scopus 로고
    • 7-Nitroindazole: An inhibitor of nitric oxide synthase
    • Moore, P. K., and Bland-Ward, P. A. (1996) 7-Nitroindazole: An inhibitor of nitric oxide synthase, Methods Enzymol. 268, 393-398.
    • (1996) Methods Enzymol. , vol.268 , pp. 393-398
    • Moore, P.K.1    Bland-Ward, P.A.2
  • 42
    • 0001227655 scopus 로고
    • The nature of pi-pi interactions
    • Hunter, C. A., and Sanders, J. K. M. (1990) The nature of pi-pi interactions, J. Am. Chem. Soc. 112, 5525-5534.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 5525-5534
    • Hunter, C.A.1    Sanders, J.K.M.2
  • 43
    • 0002462375 scopus 로고    scopus 로고
    • A critical account on pi-pi stacking in metal complexes with aromatic nitrogen-containing ligands
    • Janiak, C. (2000) A critical account on pi-pi stacking in metal complexes with aromatic nitrogen-containing ligands, J. Chem. Soc., Dalton Trans., 3885-3869.
    • (2000) J. Chem. Soc., Dalton Trans. , pp. 3885-3869
    • Janiak, C.1
  • 44
    • 0000299809 scopus 로고
    • Aromatic - Aromatic interactions: Free energy profiles for the benzene dimer in water, chloroform, and liquid benzene
    • Jorgensen, W. L., and Severance, D. L. (1990) Aromatic - Aromatic interactions: Free energy profiles for the benzene dimer in water, chloroform, and liquid benzene, J. Am. Chem. Soc. 112, 4768-4774.
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 4768-4774
    • Jorgensen, W.L.1    Severance, D.L.2
  • 45
    • 0027515708 scopus 로고
    • Identification of cytochrome P450 2E1 as the predominant enzyme catalyzing human liver microsomal defluorination of sevoflurane, isoflurane, and methoxyflurane
    • Kharasch, E. D., and Thummel, K. E. (1993) Identification of cytochrome P450 2E1 as the predominant enzyme catalyzing human liver microsomal defluorination of sevoflurane, isoflurane, and methoxyflurane, Anesthesiology 79, 795-807.
    • (1993) Anesthesiology , vol.79 , pp. 795-807
    • Kharasch, E.D.1    Thummel, K.E.2
  • 48
    • 0035980234 scopus 로고    scopus 로고
    • Structures of tetrahydrobiopterin binding-site mutants of inducible nitric oxide synthase dimer and implicated roles of Trp457
    • Aoyagi, M., Arvai, A. S., Ghosh, S., Stuehr, D. J., Tainer, J. A., and Getzoff, E. D. (2001) Structures of tetrahydrobiopterin binding-site mutants of inducible nitric oxide synthase dimer and implicated roles of Trp457, Biochemistry 40, 12826-12832.
    • (2001) Biochemistry , vol.40 , pp. 12826-12832
    • Aoyagi, M.1    Arvai, A.S.2    Ghosh, S.3    Stuehr, D.J.4    Tainer, J.A.5    Getzoff, E.D.6
  • 49
    • 0033597930 scopus 로고    scopus 로고
    • Crystal structures of zinc-free and -bound heme domain of human inducible nitric-oxide synthase. Implications for dimer stability and comparison with endothelial nitric-oxide synthase
    • Li, H., Raman, C. S., Glaser, C. B., Blasko, E., Young, T. A., Parkinson, J. F., Whitlow, M., and Poulos, T. L. (1999) Crystal structures of zinc-free and -bound heme domain of human inducible nitric-oxide synthase. Implications for dimer stability and comparison with endothelial nitric-oxide synthase, J. Biol. Chem. 274, 21276-21284.
    • (1999) J. Biol. Chem. , vol.274 , pp. 21276-21284
    • Li, H.1    Raman, C.S.2    Glaser, C.B.3    Blasko, E.4    Young, T.A.5    Parkinson, J.F.6    Whitlow, M.7    Poulos, T.L.8
  • 50
    • 0030948345 scopus 로고    scopus 로고
    • Characterization of bovine endothelial nitric oxide synthase as a homodimer with downregulated uncoupled NADPH oxidase activity: Tetrahydrobiopterin binding kinetics and role of haem in dimerization
    • List, B. M., Klosch, B., Volker, C., Gorren, A. C., Sessa, W. C., Werner, E. R., Kukovetz, W. R., Schmidt, K., and Mayer, B. (1997) Characterization of bovine endothelial nitric oxide synthase as a homodimer with downregulated uncoupled NADPH oxidase activity: Tetrahydrobiopterin binding kinetics and role of haem in dimerization, Biochem. J. 323, 159-165.
    • (1997) Biochem. J. , vol.323 , pp. 159-165
    • List, B.M.1    Klosch, B.2    Volker, C.3    Gorren, A.C.4    Sessa, W.C.5    Werner, E.R.6    Kukovetz, W.R.7    Schmidt, K.8    Mayer, B.9
  • 51
    • 0030793667 scopus 로고    scopus 로고
    • Tetrahydrobiopterin binding to macrophage inducible nitric oxide synthase: Heme spin shift and dimer stabilization by the potent pterin antagonist 4-amino-tetrahydrobiopterin
    • Mayer, B., Wu, C., Gorren, A. C., Pfeiffer, S., Schmidt, K., Clark, P., Stuehr, D. J., and Werner, E. R. (1997) Tetrahydrobiopterin binding to macrophage inducible nitric oxide synthase: Heme spin shift and dimer stabilization by the potent pterin antagonist 4-amino-tetrahydrobiopterin, Biochemistry 36, 8422-8427.
    • (1997) Biochemistry , vol.36 , pp. 8422-8427
    • Mayer, B.1    Wu, C.2    Gorren, A.C.3    Pfeiffer, S.4    Schmidt, K.5    Clark, P.6    Stuehr, D.J.7    Werner, E.R.8
  • 52
    • 0017115998 scopus 로고
    • The role of tetrahydrofolate dehydrogenase in the hepatic supply of tetrahydrobiopterin in rats
    • Stone, K. J. (1976) The role of tetrahydrofolate dehydrogenase in the hepatic supply of tetrahydrobiopterin in rats, Biochem, J. 157, 105-109.
    • (1976) Biochem, J. , vol.157 , pp. 105-109
    • Stone, K.J.1
  • 53
    • 0014198950 scopus 로고
    • Metabolism of the phenylalanine hydroxylation cofactor
    • Kaufman, S. (1967) Metabolism of the phenylalanine hydroxylation cofactor, J. Biol. Chem. 242, 3934-3943.
    • (1967) J. Biol. Chem. , vol.242 , pp. 3934-3943
    • Kaufman, S.1
  • 54
    • 0037163086 scopus 로고    scopus 로고
    • Distinct dimer interaction and regulation in nitric oxide synthase types I, II, and III
    • Panda, K., Rosenfeld, R. J., Ghosh, S., Meade, A. L., Getzoff, E. D., and Stuehr, D. J. (2002) Distinct dimer interaction and regulation in nitric oxide synthase types I, II, and III, J. Biol. Chem. 277, 31020-31030.
    • (2002) J. Biol. Chem. , vol.277 , pp. 31020-31030
    • Panda, K.1    Rosenfeld, R.J.2    Ghosh, S.3    Meade, A.L.4    Getzoff, E.D.5    Stuehr, D.J.6
  • 55
    • 0031874893 scopus 로고    scopus 로고
    • Tetrahydrobiopterin and endothelial function
    • Cosentino, F., and Luscher, T. F. (1998) Tetrahydrobiopterin and endothelial function. Eur. Heart J. 19, G3-G8.
    • (1998) Eur. Heart J. , vol.19
    • Cosentino, F.1    Luscher, T.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.