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Volumn 111, Issue 35, 2014, Pages

Molecular architecture of mammalian nitric oxide synthases

Author keywords

Conformational heterogeneity; Electron microscopy; Flavin; Heme

Indexed keywords

CALMODULIN; INDUCIBLE NITRIC OXIDE SYNTHASE; NITRIC OXIDE SYNTHASE;

EID: 84907227897     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1413763111     Document Type: Article
Times cited : (87)

References (63)
  • 1
    • 84879496815 scopus 로고    scopus 로고
    • Vascular regenerative therapies for the treatment of erectile dysfunction: Current approaches
    • Condorelli RA, et al. (2013) Vascular regenerative therapies for the treatment of erectile dysfunction: current approaches. Andrology 1(4):533-540.
    • (2013) Andrology , vol.1 , Issue.4 , pp. 533-540
    • Condorelli, R.A.1
  • 3
    • 84859921204 scopus 로고    scopus 로고
    • Current therapeutic strategies to mitigate the eNOS dysfunction in ischaemic stroke
    • Srivastava K, Bath PMW, Bayraktutan U (2012) Current therapeutic strategies to mitigate the eNOS dysfunction in ischaemic stroke. Cell Mol Neurobiol 32(3):319-336.
    • (2012) Cell Mol Neurobiol , vol.32 , Issue.3 , pp. 319-336
    • Srivastava, K.1    Bath, P.M.W.2    Bayraktutan, U.3
  • 4
    • 84859487532 scopus 로고    scopus 로고
    • Nitric oxide synthases: Regulation and function
    • Förstermann U, Sessa WC (2012) Nitric oxide synthases: Regulation and function. Eur Heart J 33(7):829-837.
    • (2012) Eur Heart J , vol.33 , Issue.7 , pp. 829-837
    • Förstermann, U.1    Sessa, W.C.2
  • 5
    • 0035425503 scopus 로고    scopus 로고
    • Nitric oxide synthases: Structure, function and inhibition
    • DOI 10.1042/0264-6021:3570593
    • Alderton WK, Cooper CE, Knowles RG (2001) Nitric oxide synthases: Structure, function and inhibition. Biochem J 357(pt 3):593-615. (Pubitemid 32735142)
    • (2001) Biochemical Journal , vol.357 , Issue.3 , pp. 593-615
    • Alderton, W.K.1    Cooper, C.E.2    Knowles, R.G.3
  • 6
    • 84867121243 scopus 로고    scopus 로고
    • NADPH-cytochrome P450 oxidoreductase: Prototypic member of the diflavin reductase family
    • Iyanagi T, Xia C, Kim J-JP (2012) NADPH-cytochrome P450 oxidoreductase: Prototypic member of the diflavin reductase family. Arch Biochem Biophys 528(1):72-89.
    • (2012) Arch Biochem Biophys , vol.528 , Issue.1 , pp. 72-89
    • Iyanagi, T.1    Xia, C.2    Kim, J.-J.P.3
  • 7
  • 9
    • 77956070332 scopus 로고    scopus 로고
    • Surface charges and regulation of FMN to heme electron transfer in nitric-oxide synthase
    • Tejero J, Hannibal L, Mustovich A, Stuehr DJ (2010) Surface charges and regulation of FMN to heme electron transfer in nitric-oxide synthase. J Biol Chem 285(35): 27232-27240.
    • (2010) J Biol Chem , vol.285 , Issue.35 , pp. 27232-27240
    • Tejero, J.1    Hannibal, L.2    Mustovich, A.3    Stuehr, D.J.4
  • 10
    • 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 HM, Stuehr DJ (1999) Role of reductase domain cluster 1 acidic residues in neuronal nitric-oxide synthase. Characterization of the FMN-FREE enzyme. J Biol Chem 274(32):22313-22320.
    • (1999) J Biol Chem , vol.274 , Issue.32 , pp. 22313-22320
    • Adak, S.1    Ghosh, S.2    Abu-Soud, H.M.3    Stuehr, D.J.4
  • 12
    • 67749124524 scopus 로고    scopus 로고
    • Neutralizing a surface charge on the FMN subdomain increases the activity of neuronal nitric-oxide synthase by enhancing the oxygen reactivity of the enzyme heme-nitric oxide complex
    • Haque MM, et al. (2009) Neutralizing a surface charge on the FMN subdomain increases the activity of neuronal nitric-oxide synthase by enhancing the oxygen reactivity of the enzyme heme-nitric oxide complex. J Biol Chem 284(29):19237-19247.
    • (2009) J Biol Chem , vol.284 , Issue.29 , pp. 19237-19247
    • Haque, M.M.1
  • 13
    • 84902438336 scopus 로고    scopus 로고
    • Architecture of the nitric-oxide synthase holoenzyme reveals large conformational changes and a calmodulin-driven release of the FMN domain
    • Yokom AL, et al. (2014) Architecture of the nitric-oxide synthase holoenzyme reveals large conformational changes and a calmodulin-driven release of the FMN domain. J Biol Chem 289(24):16855-16865.
    • (2014) J Biol Chem , vol.289 , Issue.24 , pp. 16855-16865
    • Yokom, A.L.1
  • 14
    • 79959898633 scopus 로고    scopus 로고
    • Novel nanomolar imidazo[4,5-b]pyridines as selective nitric oxide synthase (iNOS) inhibitors: SAR and structural insights
    • Grädler U, et al. (2011) Novel nanomolar imidazo[4,5-b]pyridines as selective nitric oxide synthase (iNOS) inhibitors: SAR and structural insights. Bioorg Med Chem Lett 21(14):4228-4232.
    • (2011) Bioorg Med Chem Lett , vol.21 , Issue.14 , pp. 4228-4232
    • Grädler, U.1
  • 15
    • 0034738986 scopus 로고    scopus 로고
    • Mapping the active site polarity in structures of endothelial nitric oxide synthase heme domain complexed with isothioureas
    • Li H, et al. (2000) Mapping the active site polarity in structures of endothelial nitric oxide synthase heme domain complexed with isothioureas. J Inorg Biochem 81(3): 133-139.
    • (2000) J Inorg Biochem , vol.81 , Issue.3 , pp. 133-139
    • Li, H.1
  • 16
    • 0035813091 scopus 로고    scopus 로고
    • Crystal structure of the FAD/NADPH-binding domain of rat neuronal nitric-oxide synthase. Comparisons with NADPH-cytochrome P450 oxidoreductase
    • Zhang J, et al. (2001) Crystal structure of the FAD/NADPH-binding domain of rat neuronal nitric-oxide synthase. Comparisons with NADPH-cytochrome P450 oxidoreductase. J Biol Chem 276(40):37506-37513.
    • (2001) J Biol Chem , vol.276 , Issue.40 , pp. 37506-37513
    • Zhang, J.1
  • 17
    • 71049135329 scopus 로고    scopus 로고
    • Regulation of interdomain interactions by calmodulin in inducible nitric-oxide synthase
    • Xia C, Misra I, Iyanagi T, Kim J-JP (2009) Regulation of interdomain interactions by calmodulin in inducible nitric-oxide synthase. J Biol Chem 284(44):30708-30717.
    • (2009) J Biol Chem , vol.284 , Issue.44 , pp. 30708-30717
    • Xia, C.1    Misra, I.2    Iyanagi, T.3    Kim, J.-J.P.4
  • 18
    • 77956087963 scopus 로고    scopus 로고
    • Pulsed EPR determination of the distance between heme iron and FMN centers in a human inducible nitric oxide synthase
    • Astashkin AV, Elmore BO, Fan W, Guillemette JG, Feng C (2010) Pulsed EPR determination of the distance between heme iron and FMN centers in a human inducible nitric oxide synthase. J Am Chem Soc 132(34):12059-12067.
    • (2010) J Am Chem Soc , vol.132 , Issue.34 , pp. 12059-12067
    • Astashkin, A.V.1    Elmore, B.O.2    Fan, W.3    Guillemette, J.G.4    Feng, C.5
  • 19
    • 77952240774 scopus 로고    scopus 로고
    • NO synthase: Structures and mechanisms
    • Daff S (2010) NO synthase: Structures and mechanisms. Nitric Oxide 23(1):1-11.
    • (2010) Nitric Oxide , vol.23 , Issue.1 , pp. 1-11
    • Daff, S.1
  • 21
    • 77954173548 scopus 로고    scopus 로고
    • Identification of a flavin mononucleotide module residue critical for activity of inducible nitrite oxide synthase
    • Liu X-D, Mazumdar T, Xu Y, Getzoff ED, Eissa NT (2009) Identification of a flavin mononucleotide module residue critical for activity of inducible nitrite oxide synthase. J Immunol 183(9):5977-5982.
    • (2009) J Immunol , vol.183 , Issue.9 , pp. 5977-5982
    • Liu, X.-D.1    Mazumdar, T.2    Xu, Y.3    Getzoff, E.D.4    Eissa, N.T.5
  • 22
    • 84985231782 scopus 로고
    • Three-dimensional reconstruction from a single-exposure, random conical tilt series applied to the 50S ribosomal subunit of Escherichia coli
    • Radermacher M, Wagenknecht T, Verschoor A, Frank J (1987) Three-dimensional reconstruction from a single-exposure, random conical tilt series applied to the 50S ribosomal subunit of Escherichia coli. J Microsc 146(pt 2):113-136.
    • (1987) J Microsc , vol.146 , Issue.PART 2 , pp. 113-136
    • Radermacher, M.1    Wagenknecht, T.2    Verschoor, A.3    Frank, J.4
  • 23
    • 76749168960 scopus 로고    scopus 로고
    • A toolbox for ab initio 3-D reconstructions in single-particle electron microscopy
    • Voss NR, et al. (2010) A toolbox for ab initio 3-D reconstructions in single-particle electron microscopy. J Struct Biol 169(3):389-398.
    • (2010) J Struct Biol , vol.169 , Issue.3 , pp. 389-398
    • Voss, N.R.1
  • 24
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera - A visualization system for exploratory research and analysis
    • Pettersen EF, et al. (2004) UCSF Chimera- a visualization system for exploratory research and analysis. J Comput Chem 25(13):1605-1612.
    • (2004) J Comput Chem , vol.25 , Issue.13 , pp. 1605-1612
    • Pettersen, E.F.1
  • 25
    • 0034712677 scopus 로고    scopus 로고
    • Structures of the N(omega)-hydroxy-L-arginine complex of inducible nitric oxide synthase oxygenase dimer with active and inactive pterins
    • DOI 10.1021/bi992409a
    • Crane BR, et al. (2000) Structures of the N(omega)-hydroxy-L-arginine complex of inducible nitric oxide synthase oxygenase dimer with active and inactive pterins. Biochemistry 39(16):4608-4621. (Pubitemid 30225324)
    • (2000) Biochemistry , vol.39 , Issue.16 , 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
  • 27
    • 84872912958 scopus 로고    scopus 로고
    • Calmodulin-induced structural changes in endothelial nitric oxide synthase
    • Persechini A, Tran Q-K, Black DJ, Gogol EP (2013) Calmodulin-induced structural changes in endothelial nitric oxide synthase. FEBS Lett 587(3):297-301.
    • (2013) FEBS Lett , vol.587 , Issue.3 , pp. 297-301
    • Persechini, A.1    Tran, Q.-K.2    Black, D.J.3    Gogol, E.P.4
  • 28
    • 0028805425 scopus 로고
    • Role of acidic residues in the interaction of NADPH-cytochrome P450 oxidoreductase with cytochrome P450 and cytochrome c
    • Shen AL, Kasper CB (1995) Role of acidic residues in the interaction of NADPH-cytochrome P450 oxidoreductase with cytochrome P450 and cytochrome c. J Biol Chem 270(46):27475-27480.
    • (1995) J Biol Chem , vol.270 , Issue.46 , pp. 27475-27480
    • Shen, A.L.1    Kasper, C.B.2
  • 29
    • 0032916127 scopus 로고    scopus 로고
    • Solution structure of the extended neuronal nitric oxide synthase PDZ domain complexed with an associated peptide
    • DOI 10.1038/8216
    • Tochio H, Zhang Q, Mandal P, Li M, Zhang M (1999) Solution structure of the extended neuronal nitric oxide synthase PDZ domain complexed with an associated peptide. Nat Struct Biol 6(5):417-421. (Pubitemid 29218008)
    • (1999) Nature Structural Biology , vol.6 , Issue.5 , pp. 417-421
    • Tochio, H.1    Zhang, Q.2    Mandal, P.3    Li, M.4    Zhang, M.5
  • 30
    • 60649103238 scopus 로고    scopus 로고
    • Appion: An integrated, database-driven pipeline to facilitate EM image processing
    • Lander GC, et al. (2009) Appion: an integrated, database-driven pipeline to facilitate EM image processing. J Struct Biol 166(1):95-102.
    • (2009) J Struct Biol , vol.166 , Issue.1 , pp. 95-102
    • Lander, G.C.1
  • 33
    • 84873130995 scopus 로고    scopus 로고
    • Single-particle EM reveals extensive conformational variability of the Ltn1 E3 ligase
    • Lyumkis D, et al. (2013) Single-particle EM reveals extensive conformational variability of the Ltn1 E3 ligase. Proc Natl Acad Sci USA 110(5):1702-1707.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.5 , pp. 1702-1707
    • Lyumkis, D.1
  • 34
    • 0035968276 scopus 로고    scopus 로고
    • Chimeras of nitric-oxide synthase types I and III establish fundamental correlates between heme reduction, heme-NO complex formation, and catalytic activity
    • Adak S, Aulak KS, Stuehr DJ (2001) Chimeras of nitric-oxide synthase types I and III establish fundamental correlates between heme reduction, heme-NO complex formation, and catalytic activity. J Biol Chem 276(26):23246-23252.
    • (2001) J Biol Chem , vol.276 , Issue.26 , pp. 23246-23252
    • Adak, S.1    Aulak, K.S.2    Stuehr, D.J.3
  • 35
    • 50349102696 scopus 로고    scopus 로고
    • Differences in a conformational equilibrium distinguish catalysis by the endothelial and neuronal nitric-oxide synthase flavoproteins
    • Ilagan RP, et al. (2008) Differences in a conformational equilibrium distinguish catalysis by the endothelial and neuronal nitric-oxide synthase flavoproteins. J Biol Chem 283(28):19603-19615.
    • (2008) J Biol Chem , vol.283 , Issue.28 , pp. 19603-19615
    • Ilagan, R.P.1
  • 37
    • 0032489512 scopus 로고    scopus 로고
    • Electron transfer and catalytic activity of nitric oxide synthases. Chimeric constructs of the neuronal, inducible, and endothelial isoforms
    • DOI 10.1074/jbc.273.10.5566
    • Nishida CR, Ortiz de Montellano PR (1998) Electron transfer and catalytic activity of nitric oxide synthases. Chimeric constructs of the neuronal, inducible, and endothelial isoforms. J Biol Chem 273(10):5566-5571. (Pubitemid 28124023)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.10 , pp. 5566-5571
    • Nishida, C.R.1    Ortiz, D.M.P.R.2
  • 38
    • 0029943630 scopus 로고    scopus 로고
    • Characterization of C415 mutants of neuronal nitric oxide synthase
    • DOI 10.1021/bi952582g
    • Richards MK, Clague MJ, Marletta MA (1996) Characterization of C415 mutants of neuronal nitric oxide synthase. Biochemistry 35(24):7772-7780. (Pubitemid 26202516)
    • (1996) Biochemistry , vol.35 , Issue.24 , pp. 7772-7780
    • Richards, M.K.1    Clague, M.J.2    Marietta, M.A.3
  • 39
    • 0035901473 scopus 로고    scopus 로고
    • 2+-activated calmodulin on the kinetic mechanism
    • DOI 10.1021/bi0023495
    • Wolthers KR, Schimerlik MI (2001) Reaction of neuronal nitric-oxide synthase with 2,6-dichloroindolphenol and cytochrome c3+: Influence of the electron acceptor and binding of Ca2+-activated calmodulin on the kinetic mechanism. Biochemistry 40(15): 4722-4737. (Pubitemid 32377289)
    • (2001) Biochemistry , vol.40 , Issue.15 , pp. 4722-4737
    • Wolthers, K.R.1    Schimerlik, M.I.2
  • 40
    • 0029786411 scopus 로고    scopus 로고
    • Characterization of the reductase domain of rat neuronal nitric oxide synthase generated in the methylotrophic yeast Pichia pastoris. Calmodulin response is complete within the reductase domain itself
    • DOI 10.1074/jbc.271.34.20594
    • Gachhui R, et al. (1996) Characterization of the reductase domain of rat neuronal nitric oxide synthase generated in the methylotrophic yeast Pichia pastoris. Calmodulin response is complete within the reductase domain itself. J Biol Chem 271(34): 20594-20602. (Pubitemid 26281837)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.34 , pp. 20594-20602
    • Gachhui, R.1    Presta, A.2    Bentley, D.F.3    Abu-Soud, H.M.4    McArthur, R.5    Brudvig, G.6    Ghosh, D.K.7    Stuehr, D.J.8
  • 41
    • 0034681382 scopus 로고    scopus 로고
    • Removal of a putative inhibitory element reduces the calcium-dependent calmodulin activation of neuronal nitricoxide synthase
    • Montgomery HJ, Romanov V, Guillemette JG (2000) Removal of a putative inhibitory element reduces the calcium-dependent calmodulin activation of neuronal nitricoxide synthase. J Biol Chem 275(7):5052-5058.
    • (2000) J Biol Chem , vol.275 , Issue.7 , pp. 5052-5058
    • Montgomery, H.J.1    Romanov, V.2    Guillemette, J.G.3
  • 42
    • 0032533679 scopus 로고    scopus 로고
    • The reductase domain of the human inducible nitric oxide synthase is fully active in the absence of bound calmodulin
    • DOI 10.1006/abbi.1998.0917
    • Newton DC, Montgomery HJ, Guillemette JG (1998) The reductase domain of the human inducible nitric oxide synthase is fully active in the absence of bound calmodulin. Arch Biochem Biophys 359(2):249-257. (Pubitemid 28525240)
    • (1998) Archives of Biochemistry and Biophysics , vol.359 , Issue.2 , pp. 249-257
    • Newton, D.C.1    Montgomery, H.J.2    Guy, G.J.3
  • 43
    • 0028829396 scopus 로고
    • The calmodulinbinding domain of the inducible (macrophage) nitric oxide synthase
    • Anagli J, Hofmann F, Quadroni M, Vorherr T, Carafoli E (1995) The calmodulinbinding domain of the inducible (macrophage) nitric oxide synthase. Eur J Biochem 233(3):701-708.
    • (1995) Eur J Biochem , vol.233 , Issue.3 , pp. 701-708
    • Anagli, J.1    Hofmann, F.2    Quadroni, M.3    Vorherr, T.4    Carafoli, E.5
  • 44
    • 79960340323 scopus 로고    scopus 로고
    • Binding kinetics of calmodulin with target peptides of three nitric oxide synthase isozymes
    • Wu G, Berka V, Tsai A-LA (2011) Binding kinetics of calmodulin with target peptides of three nitric oxide synthase isozymes. J Inorg Biochem 105(9):1226-1237.
    • (2011) J Inorg Biochem , vol.105 , Issue.9 , pp. 1226-1237
    • Wu, G.1    Berka, V.2    Tsai, A.-L.A.3
  • 45
    • 0032540754 scopus 로고    scopus 로고
    • 2+-dependent and -independent interactions between calmodulin and its binding domain of inducible nitric oxide synthase
    • DOI 10.1016/S0014-5793(98)00750-9, PII S0014579398007509
    • Yuan T, Vogel HJ, Sutherland C, Walsh MP (1998) Characterization of the Ca2+ -dependent and -independent interactions between calmodulin and its binding domain of inducible nitric oxide synthase. FEBS Lett 431(2):210-214. (Pubitemid 28334218)
    • (1998) FEBS Letters , vol.431 , Issue.2 , pp. 210-214
    • Yuan, T.1    Vogel, H.J.2    Sutherland, C.3    Walsh, M.P.4
  • 46
    • 0037331863 scopus 로고    scopus 로고
    • Functional characterization of Glu298Asp mutant human endothelial nitric oxide synthase purified from a yeast expression system
    • DOI 10.1016/S1089-8603(02)00131-3, PII S1089860302001313
    • Golser R, Gorren ACFA, Mayer B, Schmidt K (2003) Functional characterization of Glu298Asp mutant human endothelial nitric oxide synthase purified from a yeast expression system. Nitric Oxide 8(1):7-14. (Pubitemid 36263427)
    • (2003) Nitric Oxide - Biology and Chemistry , vol.8 , Issue.1 , pp. 7-14
    • Golser, R.1    Gorren, A.C.F.2    Mayer, B.3    Schmidt, K.4
  • 47
    • 0029983264 scopus 로고    scopus 로고
    • Identification, characterization, and comparison of the calmodulin-binding domains of the endothelial and inducible nitric oxide synthases
    • Venema RC, Sayegh HS, Kent JD, Harrison DG (1996) Identification, characterization, and comparison of the calmodulin-binding domains of the endothelial and inducible nitric oxide synthases. J Biol Chem 271(11):6435-6440.
    • (1996) J Biol Chem , vol.271 , Issue.11 , pp. 6435-6440
    • Venema, R.C.1    Sayegh, H.S.2    Kent, J.D.3    Harrison, D.G.4
  • 49
    • 0037126968 scopus 로고    scopus 로고
    • 125I]Calmodulin binding
    • DOI 10.1016/S0014-2999(01)01560-6, PII S0014299901015606
    • Weissman BA, Jones CL, Liu Q, Gross SS (2002) Activation and inactivation of neuronal nitric oxide synthase: Characterization of Ca(2+)-dependent [125I]Calmodulin binding. Eur J Pharmacol 435(1):9-18. (Pubitemid 34094970)
    • (2002) European Journal of Pharmacology , vol.435 , Issue.1 , pp. 9-18
    • Weissman, B.A.1    Jones, C.L.2    Liu, Q.3    Gross, S.S.4
  • 50
    • 0028882828 scopus 로고
    • Interaction of calmodulin with the inducible murine macrophage nitric oxide synthase
    • Stevens-Truss R, Marletta MA (1995) Interaction of calmodulin with the inducible murine macrophage nitric oxide synthase. Biochemistry 34(48):15638-15645.
    • (1995) Biochemistry , vol.34 , Issue.48 , pp. 15638-15645
    • Stevens-Truss, R.1    Marletta, M.A.2
  • 51
    • 0029891615 scopus 로고    scopus 로고
    • High reductase activity of recombinant NOS2 flavoprotein domain lacking the calmodulin binding regulatory sequence
    • Rafferty S, Malech HL (1996) High reductase activity of recombinant NOS2 flavoprotein domain lacking the calmodulin binding regulatory sequence. Biochem Biophys Res Commun 220(3):1002- 1007.
    • (1996) Biochem Biophys Res Commun , vol.220 , Issue.3 , pp. 1002-1007
    • Rafferty, S.1    Malech, H.L.2
  • 52
    • 15444379675 scopus 로고    scopus 로고
    • S-nitrosation and regulation of inducible nitric oxide synthase
    • DOI 10.1021/bi0474463
    • Mitchell DA, Erwin PA, Michel T, Marletta MA (2005) S-nitrosation and regulation of inducible nitric oxide synthase. Biochemistry 44(12):4636-4647. (Pubitemid 40396742)
    • (2005) Biochemistry , vol.44 , Issue.12 , pp. 4636-4647
    • Mitchell, D.A.1    Erwin, P.A.2    Michel, T.3    Marletta, M.A.4
  • 53
    • 0032480754 scopus 로고    scopus 로고
    • Reactions catalyzed by tetrahy-drobiopterin- free nitric oxide synthase
    • Rusche KM, Spiering MM, Marletta MA (1998) Reactions catalyzed by tetrahy-drobiopterin- free nitric oxide synthase. Biochemistry 37(44):15503- 15512.
    • (1998) Biochemistry , vol.37 , Issue.44 , pp. 15503-15512
    • Rusche, K.M.1    Spiering, M.M.2    Marletta, M.A.3
  • 54
    • 0030446051 scopus 로고    scopus 로고
    • Human endothelial nitric oxide synthase: Expression in Escherichia coli, coexpression with calmodulin, and characterization
    • DOI 10.1006/abbi.1996.0543
    • Rodríguez-Crespo I, Ortiz de Montellano PR (1996) Human endothelial nitric oxide synthase: Expression in Escherichia coli, coexpression with calmodulin, and characterization. Arch Biochem Biophys 336(1):151-156. (Pubitemid 26423761)
    • (1996) Archives of Biochemistry and Biophysics , vol.336 , Issue.1 , pp. 151-156
    • Rodriguez-Crespo, I.1    Ortiz, D.M.P.R.2
  • 55
    • 0029048347 scopus 로고
    • Neuronal nitric oxide synthase. Expression in Escherichia coli, irreversible inhibition by phenyldiazene, and active site topology
    • Gerber NC, Ortiz de Montellano PR (1995) Neuronal nitric oxide synthase. Expression in Escherichia coli, irreversible inhibition by phenyldiazene, and active site topology. J Biol Chem 270(30):17791-17796.
    • (1995) J Biol Chem , vol.270 , Issue.30 , pp. 17791-17796
    • Gerber, N.C.1    Ortiz De Montellano, P.R.2
  • 56
    • 0029114645 scopus 로고
    • High-level expression of functional rat neuronal nitric oxide synthase in Escherichia coli
    • Roman LJL, et al. (1995) High-level expression of functional rat neuronal nitric oxide synthase in Escherichia coli. Proc Natl Acad Sci USA 92(18):8428-8432.
    • (1995) Proc Natl Acad Sci USA , vol.92 , Issue.18 , pp. 8428-8432
    • Roman, L.J.L.1
  • 57
    • 0017184389 scopus 로고
    • Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) Rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 58
    • 2342662152 scopus 로고    scopus 로고
    • Negative staining and image classification - Powerful tools in modern electron microscopy
    • DOI 10.1251/bpo70
    • Ohi M, Li Y, Cheng Y, Walz T (2004) Negative staining and image classification - powerful tools in modern electron microscopy. Biol Proced Online 6:23-34. (Pubitemid 38597695)
    • (2004) Biological Procedures Online , vol.6 , Issue.1 , pp. 23-34
    • Ohi, M.1    Li, Y.2    Cheng, Y.3    Walz, T.4
  • 59
    • 0038441501 scopus 로고    scopus 로고
    • Accurate determination of local defocus and specimen tilt in electron microscopy
    • DOI 10.1016/S1047-8477(03)00069-8
    • Mindell JA, Grigorieff N (2003) Accurate determination of local defocus and specimen tilt in electron microscopy. J Struct Biol 142(3):334-347. (Pubitemid 36638267)
    • (2003) Journal of Structural Biology , vol.142 , Issue.3 , pp. 334-347
    • Mindell, J.A.1    Grigorieff, N.2
  • 60
    • 63649113687 scopus 로고    scopus 로고
    • DoG Picker and TiltPicker: Software tools to facilitate particle selection in single particle electron microscopy
    • Voss NR, Yoshioka CK, Radermacher M, Potter CS, Carragher B (2009) DoG Picker and TiltPicker: Software tools to facilitate particle selection in single particle electron microscopy. J Struct Biol 166(2):205-213.
    • (2009) J Struct Biol , vol.166 , Issue.2 , pp. 205-213
    • Voss, N.R.1    Yoshioka, C.K.2    Radermacher, M.3    Potter, C.S.4    Carragher, B.5
  • 61
    • 77953710827 scopus 로고    scopus 로고
    • A clustering approach to multireference alignment of single-particle projections in electron microscopy
    • Sorzano COS, et al. (2010) A clustering approach to multireference alignment of single-particle projections in electron microscopy. J Struct Biol 171(2):197-206.
    • (2010) J Struct Biol , vol.171 , Issue.2 , pp. 197-206
    • Sorzano, C.O.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.