메뉴 건너뛰기




Volumn 7, Issue 6, 2012, Pages

Lobe-specific calcium binding in calmodulin regulates endothelial nitric oxide synthase activation

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; ASPARAGINE; CALMODULIN; CITRULLINE; ENDOTHELIAL NITRIC OXIDE SYNTHASE; GLUTAMIC ACID; GLUTAMINE; INDUCIBLE NITRIC OXIDE SYNTHASE; METHIONINE; MUTANT PROTEIN; NEURONAL NITRIC OXIDE SYNTHASE; PHENYLALANINE; QUERCETIN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE;

EID: 84863088955     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0039851     Document Type: Article
Times cited : (8)

References (50)
  • 1
    • 80052758036 scopus 로고    scopus 로고
    • eNOS activation and NO function: structural motifs responsible for the posttranslational control of endothelial nitric oxide synthase activity
    • Rafikov R, Fonseca FV, Kumar S, Pardo D, Darragh C, et al. (2011) eNOS activation and NO function: structural motifs responsible for the posttranslational control of endothelial nitric oxide synthase activity. J Endocrinol 210: 271-284.
    • (2011) J Endocrinol , vol.210 , pp. 271-284
    • Rafikov, R.1    Fonseca, F.V.2    Kumar, S.3    Pardo, D.4    Darragh, C.5
  • 2
    • 34250731849 scopus 로고    scopus 로고
    • Life history of eNOS: partners and pathways
    • Dudzinski DM, Michel T, (2007) Life history of eNOS: partners and pathways. Cardiovascular Research 75: 247-260.
    • (2007) Cardiovascular Research , vol.75 , pp. 247-260
    • Dudzinski, D.M.1    Michel, T.2
  • 3
    • 0024391109 scopus 로고
    • Enzymatic formation of nitrogen oxides from L-arginine in bovine brain cytosol
    • Schmidt HH, Wilke P, Evers B, Bohme E, (1989) Enzymatic formation of nitrogen oxides from L-arginine in bovine brain cytosol. Biochem Biophys Res Commun 165: 813-819.
    • (1989) Biochem Biophys Res Commun , vol.165 , pp. 813-819
    • Schmidt, H.H.1    Wilke, P.2    Evers, B.3    Bohme, E.4
  • 4
    • 0025802065 scopus 로고
    • Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase
    • Bredt DS, Hwang PM, Glatt CE, Lowenstein C, Reed RR, et al. (1991) Cloned and expressed nitric oxide synthase structurally resembles cytochrome P-450 reductase. Nature 351: 714-718.
    • (1991) Nature , vol.351 , pp. 714-718
    • Bredt, D.S.1    Hwang, P.M.2    Glatt, C.E.3    Lowenstein, C.4    Reed, R.R.5
  • 5
    • 0025787205 scopus 로고
    • Purification and characterization of the cytokine-induced macrophage nitric oxide synthase: an FAD- and FMN-containing flavoprotein
    • Stuehr DJ, Cho HJ, Kwon NS, Weise M, Nathan C, (1991) Purification and characterization of the cytokine-induced macrophage nitric oxide synthase: an FAD- and FMN-containing flavoprotein. Proc Natl Acad Sci U S A 88: 7773-7777.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 7773-7777
    • Stuehr, D.J.1    Cho, H.J.2    Kwon, N.S.3    Weise, M.4    Nathan, C.5
  • 6
    • 0026569273 scopus 로고
    • Cloning and characterization of inducible nitric oxide synthase from mouse macrophages
    • Xie QW, Cho HJ, Calaycay J, Mumford RA, Swiderek KM, et al. (1992) Cloning and characterization of inducible nitric oxide synthase from mouse macrophages. Science 256: 225-228.
    • (1992) Science , vol.256 , pp. 225-228
    • Xie, Q.W.1    Cho, H.J.2    Calaycay, J.3    Mumford, R.A.4    Swiderek, K.M.5
  • 7
    • 0025750850 scopus 로고
    • Purification and characterization of particulate endothelium-derived relaxing factor synthase from cultured and native bovine aortic endothelial cells
    • Pollock JS, Förstermann U, Mitchell JA, Warner TD, Schmidt HH, et al. (1991) Purification and characterization of particulate endothelium-derived relaxing factor synthase from cultured and native bovine aortic endothelial cells. Proc Natl Acad Sci U S A 88: 10480-10484.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 10480-10484
    • Pollock, J.S.1    Förstermann, U.2    Mitchell, J.A.3    Warner, T.D.4    Schmidt, H.H.5
  • 8
    • 0028276990 scopus 로고
    • Evidence for a bidomain structure of constitutive cerebellar nitric oxide synthase
    • Sheta EA, McMillan K, Masters BS, (1994) Evidence for a bidomain structure of constitutive cerebellar nitric oxide synthase. J Biol Chem 269: 15147-15153.
    • (1994) J Biol Chem , vol.269 , pp. 15147-15153
    • Sheta, E.A.1    McMillan, K.2    Masters, B.S.3
  • 9
    • 0028911054 scopus 로고
    • Macrophage NO synthase: characterization of isolated oxygenase and reductase domains reveals a head-to-head subunit interaction
    • Ghosh DK, Stuehr DJ, (1995) Macrophage NO synthase: characterization of isolated oxygenase and reductase domains reveals a head-to-head subunit interaction. Biochemistry 34: 801-807.
    • (1995) Biochemistry , vol.34 , pp. 801-807
    • Ghosh, D.K.1    Stuehr, D.J.2
  • 10
    • 0030007024 scopus 로고    scopus 로고
    • Endothelial nitric-oxide synthase. Evidence for bidomain structure and successful reconstitution of catalytic activity from two separate domains generated by a baculovirus expression system
    • Chen PF, Tsai AL, Berka V, Wu KK, (1996) Endothelial nitric-oxide synthase. Evidence for bidomain structure and successful reconstitution of catalytic activity from two separate domains generated by a baculovirus expression system. J Biol Chem 271: 14631-14635.
    • (1996) J Biol Chem , vol.271 , pp. 14631-14635
    • Chen, P.F.1    Tsai, A.L.2    Berka, V.3    Wu, K.K.4
  • 11
    • 0028582164 scopus 로고
    • Calmodulin controls neuronal nitric-oxide synthase by a dual mechanism. Activation of intra- and interdomain electron transfer
    • Abu-Soud HM, Yoho LL, Stuehr DJ, (1994) Calmodulin controls neuronal nitric-oxide synthase by a dual mechanism. Activation of intra- and interdomain electron transfer. J Biol Chem 269: 32047-32050.
    • (1994) J Biol Chem , vol.269 , pp. 32047-32050
    • Abu-Soud, H.M.1    Yoho, L.L.2    Stuehr, D.J.3
  • 12
    • 0032563106 scopus 로고    scopus 로고
    • Domain swapping in inducible nitric-oxide synthase. Electron transfer occurs between flavin and heme groups located on adjacent subunits in the dimer
    • Siddhanta U, Presta A, Fan BC, Wolan D, Rousseau DL, et al. (1998) Domain swapping in inducible nitric-oxide synthase. Electron transfer occurs between flavin and heme groups located on adjacent subunits in the dimer. J Biol Chem 273: 18950-18958.
    • (1998) J Biol Chem , vol.273 , pp. 18950-18958
    • Siddhanta, U.1    Presta, A.2    Fan, B.C.3    Wolan, D.4    Rousseau, D.L.5
  • 13
    • 0035839435 scopus 로고    scopus 로고
    • Intra-subunit and inter-subunit electron transfer in neuronal nitric-oxide synthase: effect of calmodulin on heterodimer catalysis
    • Sagami I, Daff S, Shimizu T, (2001) Intra-subunit and inter-subunit electron transfer in neuronal nitric-oxide synthase: effect of calmodulin on heterodimer catalysis. J Biol Chem 276: 30036-30042.
    • (2001) J Biol Chem , vol.276 , pp. 30036-30042
    • Sagami, I.1    Daff, S.2    Shimizu, T.3
  • 14
    • 0037450635 scopus 로고    scopus 로고
    • Structural basis for endothelial nitric oxide synthase binding to calmodulin
    • Aoyagi M, Arvai AS, Tainer JA, Getzoff ED, (2003) Structural basis for endothelial nitric oxide synthase binding to calmodulin. Embo J 22: 766-775.
    • (2003) Embo J , vol.22 , pp. 766-775
    • Aoyagi, M.1    Arvai, A.S.2    Tainer, J.A.3    Getzoff, E.D.4
  • 15
    • 67349214590 scopus 로고    scopus 로고
    • Two synthetic peptides corresponding to the proximal heme-binding domain and CD1 domain of human endothelial nitric-oxide synthase inhibit the oxygenase activity by interacting with CaM
    • Chen PF, Wu KK, (2009) Two synthetic peptides corresponding to the proximal heme-binding domain and CD1 domain of human endothelial nitric-oxide synthase inhibit the oxygenase activity by interacting with CaM. Arch Biochem Biophys 486: 132-140.
    • (2009) Arch Biochem Biophys , vol.486 , pp. 132-140
    • Chen, P.F.1    Wu, K.K.2
  • 16
    • 0024213513 scopus 로고
    • Structure of calmodulin refined at 2.2 A resolution
    • Babu YS, Bugg CE, Cook WJ, (1988) Structure of calmodulin refined at 2.2 A resolution. J Mol Biol 204: 191-204.
    • (1988) J Mol Biol , vol.204 , pp. 191-204
    • Babu, Y.S.1    Bugg, C.E.2    Cook, W.J.3
  • 17
    • 0022271372 scopus 로고
    • A note on calcium binding to calmodulin
    • Wang CL, (1985) A note on calcium binding to calmodulin. Biochem Biophys Res Commun 130: 426-430.
    • (1985) Biochem Biophys Res Commun , vol.130 , pp. 426-430
    • Wang, C.L.1
  • 18
    • 0026794065 scopus 로고
    • Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex
    • Meador WE, Means AR, Quiocho FA, (1992) Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex. Science 257: 1251-1255.
    • (1992) Science , vol.257 , pp. 1251-1255
    • Meador, W.E.1    Means, A.R.2    Quiocho, F.A.3
  • 19
    • 0026724223 scopus 로고
    • Calmodulin is a subunit of nitric oxide synthase from macrophages
    • Cho HJ, Xie QW, Calaycay J, Mumford RA, Swiderek KM, et al. (1992) Calmodulin is a subunit of nitric oxide synthase from macrophages. J Exp Med 176: 599-604.
    • (1992) J Exp Med , vol.176 , pp. 599-604
    • Cho, H.J.1    Xie, Q.W.2    Calaycay, J.3    Mumford, R.A.4    Swiderek, K.M.5
  • 20
    • 0025191219 scopus 로고
    • Isolation of nitric oxide synthetase, a calmodulin-requiring enzyme
    • Bredt DS, Snyder SH, (1990) Isolation of nitric oxide synthetase, a calmodulin-requiring enzyme. Proc Natl Acad Sci U S A 87: 682-685.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 682-685
    • Bredt, D.S.1    Snyder, S.H.2
  • 21
    • 0030856718 scopus 로고    scopus 로고
    • Calcium binding sites of calmodulin and electron transfer by neuronal nitric oxide synthase
    • Stevens-Truss R, Beckingham K, Marletta MA, (1997) Calcium binding sites of calmodulin and electron transfer by neuronal nitric oxide synthase. Biochemistry 36: 12337-12345.
    • (1997) Biochemistry , vol.36 , pp. 12337-12345
    • Stevens-Truss, R.1    Beckingham, K.2    Marletta, M.A.3
  • 22
    • 18844460212 scopus 로고    scopus 로고
    • Calcium-binding sites of calmodulin and electron transfer by inducible nitric oxide synthase
    • Gribovskaja I, Brownlow KC, Dennis SJ, Rosko AJ, Marletta MA, et al. (2005) Calcium-binding sites of calmodulin and electron transfer by inducible nitric oxide synthase. Biochemistry 44: 7593-7601.
    • (2005) Biochemistry , vol.44 , pp. 7593-7601
    • Gribovskaja, I.1    Brownlow, K.C.2    Dennis, S.J.3    Rosko, A.J.4    Marletta, M.A.5
  • 23
    • 34748888339 scopus 로고    scopus 로고
    • Calcium-deficient calmodulin binding and activation of neuronal and inducible nitric oxide synthases
    • Spratt DE, Taiakina V, Guillemette JG, (2007) Calcium-deficient calmodulin binding and activation of neuronal and inducible nitric oxide synthases. Biochim Biophys Acta 1774: 1351-1358.
    • (2007) Biochim Biophys Acta , vol.1774 , pp. 1351-1358
    • Spratt, D.E.1    Taiakina, V.2    Guillemette, J.G.3
  • 24
    • 0035018871 scopus 로고    scopus 로고
    • Cellular regulation of endothelial nitric oxide synthase
    • Govers R, Rabelink TJ, (2001) Cellular regulation of endothelial nitric oxide synthase. Am J Physiol Renal Physiol 280: F193-F206.
    • (2001) Am J Physiol Renal Physiol , vol.280
    • Govers, R.1    Rabelink, T.J.2
  • 25
    • 33749343007 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent protein kinase II (CaMKII) is activated by calmodulin with two bound calciums
    • Shifman JM, Choi MH, Mihalas S, Mayo SL, Kennedy MB, (2006) Calcium/calmodulin-dependent protein kinase II (CaMKII) is activated by calmodulin with two bound calciums. Proc Natl Acad Sci USA. 103: 13968-13973.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 13968-13973
    • Shifman, J.M.1    Choi, M.H.2    Mihalas, S.3    Mayo, S.L.4    Kennedy, M.B.5
  • 26
    • 0037072782 scopus 로고    scopus 로고
    • Calmodulin activates electron transfer through neuronal nitric-oxide synthase reductase domain by releasing an NADPH-dependent conformational lock
    • Craig DH, Chapman SK, Daff S, (2002) Calmodulin activates electron transfer through neuronal nitric-oxide synthase reductase domain by releasing an NADPH-dependent conformational lock. J Biol Chem 277: 33987-33994.
    • (2002) J Biol Chem , vol.277 , pp. 33987-33994
    • Craig, D.H.1    Chapman, S.K.2    Daff, S.3
  • 27
    • 0043154640 scopus 로고    scopus 로고
    • Nitric oxide synthases: domain structure and alignment in enzyme function and control
    • Ghosh DK, Salerno JC, (2003) Nitric oxide synthases: domain structure and alignment in enzyme function and control. Front Biosci 8: 193-209.
    • (2003) Front Biosci , vol.8 , pp. 193-209
    • Ghosh, D.K.1    Salerno, J.C.2
  • 28
    • 4444354274 scopus 로고    scopus 로고
    • Structural basis for isozyme-specific regulation of electron transfer in nitric-oxide synthase
    • Garcin ED, Bruns CM, Lloyd SJ, Hosfield DJ, Tiso M, et al. (2004) Structural basis for isozyme-specific regulation of electron transfer in nitric-oxide synthase. J Biol Chem 279: 37918-37927.
    • (2004) J Biol Chem , vol.279 , pp. 37918-37927
    • Garcin, E.D.1    Bruns, C.M.2    Lloyd, S.J.3    Hosfield, D.J.4    Tiso, M.5
  • 29
    • 33747335659 scopus 로고    scopus 로고
    • Electron transfer by neuronal nitric-oxide synthase is regulated by concerted interaction of calmodulin and two intrinsic regulatory elements
    • Roman LJ, Masters BS, (2006) Electron transfer by neuronal nitric-oxide synthase is regulated by concerted interaction of calmodulin and two intrinsic regulatory elements. J Biol Chem 281: 23111-23118.
    • (2006) J Biol Chem , vol.281 , pp. 23111-23118
    • Roman, L.J.1    Masters, B.S.2
  • 30
    • 58049199399 scopus 로고    scopus 로고
    • Exploring the electron transfer properties of neuronal nitric-oxide synthase by reversal of the FMN redox potential
    • Li H, Das A, Sibhatu H, Jamal J, Sligar SG, et al. (2008) Exploring the electron transfer properties of neuronal nitric-oxide synthase by reversal of the FMN redox potential. J Biol Chem 283: 34762-34772.
    • (2008) J Biol Chem , vol.283 , pp. 34762-34772
    • Li, H.1    Das, A.2    Sibhatu, H.3    Jamal, J.4    Sligar, S.G.5
  • 31
    • 50349102696 scopus 로고    scopus 로고
    • Differences in a conformational equilibrium distinguish catalysis by the endothelial and neuronal nitric-oxide synthase flavoproteins
    • Ilagan RP, Tiso M, Konas DW, Hemann C, Durra D, et al. (2008) Differences in a conformational equilibrium distinguish catalysis by the endothelial and neuronal nitric-oxide synthase flavoproteins. J Biol Chem 283: 19603-19615.
    • (2008) J Biol Chem , vol.283 , pp. 19603-19615
    • Ilagan, R.P.1    Tiso, M.2    Konas, D.W.3    Hemann, C.4    Durra, D.5
  • 32
    • 0347994887 scopus 로고    scopus 로고
    • Molecular determinants of Ca(2+)/calmodulin-dependent regulation of Ca(v)2.1 channels
    • Lee A, Zhou H, Scheuer T, Catterall WA, (2003) Molecular determinants of Ca(2+)/calmodulin-dependent regulation of Ca(v)2.1 channels. Proc Natl Acad Sci USA 100: 16059-16064.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 16059-16064
    • Lee, A.1    Zhou, H.2    Scheuer, T.3    Catterall, W.A.4
  • 33
    • 84872366408 scopus 로고    scopus 로고
    • Lobe-specific functions of calcium calmodulin in α calcium calmodulin-dependent protein kinase II activation
    • Jama AM, Gabriel J, Al-Nagar AJ, Martin S, Baig SZ, et al. (2011) Lobe-specific functions of calcium calmodulin in α calcium calmodulin-dependent protein kinase II activation. J Biol Chem 276: 30794-30802.
    • (2011) J Biol Chem , vol.276 , pp. 30794-30802
    • Jama, A.M.1    Gabriel, J.2    Al-Nagar, A.J.3    Martin, S.4    Baig, S.Z.5
  • 35
    • 0042823613 scopus 로고    scopus 로고
    • Apocalmodulin and calcium calmodulin-binding sites on the CaV1.2 channel
    • Tang W, Halling DB, Black DJ, Pate P, Zhang JZ, et al. (2003) Apocalmodulin and calcium calmodulin-binding sites on the CaV1.2 channel. Biophys J 85: 1538-1547.
    • (2003) Biophys J , vol.85 , pp. 1538-1547
    • Tang, W.1    Halling, D.B.2    Black, D.J.3    Pate, P.4    Zhang, J.Z.5
  • 36
    • 0028305218 scopus 로고
    • Activation of myosin light chain kinase and nitric oxide synthase activities by calmodulin fragments
    • Persechini A, McMillans K, Leakey P, (1994) Activation of myosin light chain kinase and nitric oxide synthase activities by calmodulin fragments. J Biol Chem 269: 16148-16154.
    • (1994) J Biol Chem , vol.269 , pp. 16148-16154
    • Persechini, A.1    McMillans, K.2    Leakey, P.3
  • 37
    • 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: 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
  • 38
    • 0030715301 scopus 로고    scopus 로고
    • An autoinhibitory control element defines calcium-regulated isoforms of nitric oxide synthase
    • Salerno JC, Harris DE, Irizarry K, Patel B, Morales AJ, et al. (1997) An autoinhibitory control element defines calcium-regulated isoforms of nitric oxide synthase. J Biol Chem 272: 29769-29777.
    • (1997) J Biol Chem , vol.272 , pp. 29769-29777
    • Salerno, J.C.1    Harris, D.E.2    Irizarry, K.3    Patel, B.4    Morales, A.J.5
  • 39
    • 0028361984 scopus 로고
    • Identification of covalently bound amino-terminal myristic acid in endothelial nitric oxide synthase
    • Liu J, Sessa WC, (1994) Identification of covalently bound amino-terminal myristic acid in endothelial nitric oxide synthase. J Biol Chem 269: 11691-11694.
    • (1994) J Biol Chem , vol.269 , pp. 11691-11694
    • Liu, J.1    Sessa, W.C.2
  • 40
    • 0029084761 scopus 로고
    • Biosynthesis and palmitoylation of endothelial nitric oxide synthase: mutagenesis of palmitoylation sites, cysteines-15 and/or -26, argues against depalmitoylation-induced translocation of the enzyme
    • Liu J, Garcia-Cardeiia G, Sessa WC, (1995) Biosynthesis and palmitoylation of endothelial nitric oxide synthase: mutagenesis of palmitoylation sites, cysteines-15 and/or-26, argues against depalmitoylation-induced translocation of the enzyme. Biochemistry 34: 12333-12340.
    • (1995) Biochemistry , vol.34 , pp. 12333-12340
    • Liu, J.1    Garcia-Cardeiia, G.2    Sessa, W.C.3
  • 42
    • 71049135329 scopus 로고    scopus 로고
    • Regulation of interdomain interactions by calmodulin in inducible nitric-oxide synthase
    • Xia C, Misra I, Iyanagi T, Kim JJ, (2009) Regulation of interdomain interactions by calmodulin in inducible nitric-oxide synthase. J Biol Chem 284: 30708-30717.
    • (2009) J Biol Chem , vol.284 , pp. 30708-30717
    • Xia, C.1    Misra, I.2    Iyanagi, T.3    Kim, J.J.4
  • 43
    • 77956221747 scopus 로고    scopus 로고
    • A bridging interaction allows calmodulin to activate NO synthase through a bi-modal mechanism
    • Tejero J, Haque1 MM, Durra D, Stuehr DJ
    • Tejero J, Haque1 MM, Durra D, Stuehr DJ (2010) A bridging interaction allows calmodulin to activate NO synthase through a bi-modal mechanism. J Biol Chem 285: 25941-25949.
    • (2010) J Biol Chem , vol.285 , pp. 25941-25949
  • 44
    • 77952240774 scopus 로고    scopus 로고
    • NO synthase: structures and mechanisms
    • Daff S, (2010) NO synthase: structures and mechanisms. Nitric Oxide 23: 1-11.
    • (2010) Nitric Oxide , vol.23 , pp. 1-11
    • Daff, S.1
  • 45
    • 0035900010 scopus 로고    scopus 로고
    • The carboxy-terminal calcium binding sites of calmodulin control calmodulin's Switch from an Activator to an Inhibitor of RYR1
    • Rodney GG, Krol J, Williams B, Beckingham K, Hamilton SL, (2001) The carboxy-terminal calcium binding sites of calmodulin control calmodulin's Switch from an Activator to an Inhibitor of RYR1. Biochemistry 40: 12430-12435.
    • (2001) Biochemistry , vol.40 , pp. 12430-12435
    • Rodney, G.G.1    Krol, J.2    Williams, B.3    Beckingham, K.4    Hamilton, S.L.5
  • 46
    • 4043170593 scopus 로고    scopus 로고
    • Differential activation of nitric-oxide synthase isozymes by calmodulin-troponin C chimeras
    • Newman E, Spratt DE, Mosher J, Cheyne B, Montgomery HJ, et al. (2004) Differential activation of nitric-oxide synthase isozymes by calmodulin-troponin C chimeras. J Biol Chem 279: 33547-33557.
    • (2004) J Biol Chem , vol.279 , pp. 33547-33557
    • Newman, E.1    Spratt, D.E.2    Mosher, J.3    Cheyne, B.4    Montgomery, H.J.5
  • 47
    • 0028043460 scopus 로고
    • Cysteine 184 of endothelial nitric oxide synthase is involved in heme coordination and catalytic activity
    • Chen PF, Tsai AL, Wu KK, (1994) Cysteine 184 of endothelial nitric oxide synthase is involved in heme coordination and catalytic activity. J Biol Chem 269: 25062-25066.
    • (1994) J Biol Chem , vol.269 , pp. 25062-25066
    • Chen, P.F.1    Tsai, A.L.2    Wu, K.K.3
  • 48
    • 0035903175 scopus 로고    scopus 로고
    • Molecular basis of calmodulin tethering and calcium-dependent inactivation of L-type calcium channels
    • Pitt GS, Zu{double acute}hlke RD, Hudmon A, Schlman H, Reuter H, et al. (2001) Molecular basis of calmodulin tethering and calcium-dependent inactivation of L-type calcium channels. J Biol Chem 276: 30794-30802.
    • (2001) J Biol Chem , vol.276 , pp. 30794-30802
    • Pitt, G.S.1    Zuhlke, R.D.2    Hudmon, A.3    Schlman, H.4    Reuter, H.5
  • 49
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM, (1976) A 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
  • 50
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK, (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.