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Volumn 346, Issue 5, 2005, Pages 1423-1440

Mechanism of free radical nitric oxide-mediated Ras guanine nucleotide dissociation

Author keywords

5 Guanidino 4 nitroimidazole diphosphate (NIm DP); Guanine nucleotide exchange; Nitric oxide; NKCD motif; Ras

Indexed keywords

5 GUANIDINO 4 NITROIMIDAZOLE DIPHOSPHATE; CATION; CYSTEINE DERIVATIVE; FREE RADICAL; GUANIDINE; GUANINE NUCLEOTIDE; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATASE; NITRIC OXIDE; NITROGEN DIOXIDE; NITROIMIDAZOLE; PHENYL GROUP; PYROPHOSPHATE; RAB PROTEIN; RAP PROTEIN; RAS PROTEIN; UNCLASSIFIED DRUG;

EID: 13844298143     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.12.050     Document Type: Article
Times cited : (64)

References (80)
  • 2
    • 0028982274 scopus 로고
    • ras as a common signaling target of reactive free radicals and cellular redox stress
    • ras as a common signaling target of reactive free radicals and cellular redox stress J. Biol. Chem. 270 1995 21195 21198
    • (1995) J. Biol. Chem. , vol.270 , pp. 21195-21198
    • Lander, H.M.1    Ogiste, J.S.2    Teng, K.K.3    Novogrodsky, A.4
  • 6
    • 0035920116 scopus 로고    scopus 로고
    • Structure-based mutagenesis reveals distinct functions for Ras switch 1 and switch 2 in Sos-catalyzed guanine nucleotide exchange
    • B.E. Hall, S.S. Yang, P.A. Boriack-Sjodin, J. Kuriyan, and D. Bar-Sagi Structure-based mutagenesis reveals distinct functions for Ras switch 1 and switch 2 in Sos-catalyzed guanine nucleotide exchange J. Biol. Chem. 276 2001 27629 27637
    • (2001) J. Biol. Chem. , vol.276 , pp. 27629-27637
    • Hall, B.E.1    Yang, S.S.2    Boriack-Sjodin, P.A.3    Kuriyan, J.4    Bar-Sagi, D.5
  • 7
    • 0029829561 scopus 로고    scopus 로고
    • Crystal structure of the GTPase-activating domain of human p120GAP and implications for the interaction with Ras
    • K. Scheffzek, A. Lautwein, W. Kabsch, M.R. Ahmadian, and A. Wittinghofer Crystal structure of the GTPase-activating domain of human p120GAP and implications for the interaction with Ras Nature 384 1996 591 596
    • (1996) Nature , vol.384 , pp. 591-596
    • Scheffzek, K.1    Lautwein, A.2    Kabsch, W.3    Ahmadian, M.R.4    Wittinghofer, A.5
  • 9
    • 0031740429 scopus 로고    scopus 로고
    • Regulation of neuronal nitric oxide synthase and identification of novel nitric oxide signaling pathways
    • T.M. Dawson, M. Sasaki, M. Gonzalez-Zulueta, and V.L. Dawson Regulation of neuronal nitric oxide synthase and identification of novel nitric oxide signaling pathways Prog. Brain Res. 118 1998 3 11
    • (1998) Prog. Brain Res. , vol.118 , pp. 3-11
    • Dawson, T.M.1    Sasaki, M.2    Gonzalez-Zulueta, M.3    Dawson, V.L.4
  • 10
  • 11
    • 1442300935 scopus 로고    scopus 로고
    • Ras S-nitrosylation and kinetics of nitric oxide-mediated guanine nucleotide exchange
    • Ras S-nitrosylation and kinetics of nitric oxide-mediated guanine nucleotide exchange Biochemistry 43 2004 2314 2322
    • (2004) Biochemistry , vol.43 , pp. 2314-2322
    • Heo, J.1    Campbell, S.L.2
  • 12
    • 0037096198 scopus 로고    scopus 로고
    • Kinetics of the reactions of nitrogen dioxide with glutathione, cysteine, and uric acid at physiological pH
    • E. Ford, M. Hughes, and P. Wardman Kinetics of the reactions of nitrogen dioxide with glutathione, cysteine, and uric acid at physiological pH Free Radic. Biol. Med. 32 2002 1314 1323
    • (2002) Free Radic. Biol. Med. , vol.32 , pp. 1314-1323
    • Ford, E.1    Hughes, M.2    Wardman, P.3
  • 13
    • 0038182543 scopus 로고    scopus 로고
    • Oxidation and nitrosation of thiols at low micromolar exposure to nitric oxide. Evidence for a free radical mechanism
    • D. Jourd'heuil, F. Jourd'heuil, and M. Feelisch Oxidation and nitrosation of thiols at low micromolar exposure to nitric oxide. Evidence for a free radical mechanism J. Biol. Chem. 278 2003 15720 15726
    • (2003) J. Biol. Chem. , vol.278 , pp. 15720-15726
    • Jourd'Heuil, D.1    Jourd'Heuil, F.2    Feelisch, M.3
  • 15
    • 0024463212 scopus 로고
    • Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation
    • E.F. Pai, W. Kabsch, U. Krengel, K.C. Holmes, J. John, and A. Wittinghofer Structure of the guanine-nucleotide-binding domain of the Ha-ras oncogene product p21 in the triphosphate conformation Nature 341 1989 209 214
    • (1989) Nature , vol.341 , pp. 209-214
    • Pai, E.F.1    Kabsch, W.2    Krengel, U.3    Holmes, K.C.4    John, J.5    Wittinghofer, A.6
  • 16
    • 0025327522 scopus 로고
    • Crystal structure of an active form of RAS protein, a complex of a GTP analog and the HRAS p21 catalytic domain
    • A.T. Brunger, M.V. Milburn, L. Tong, A.M. deVos, J. Jancarik, and Z. Yamaizumi Crystal structure of an active form of RAS protein, a complex of a GTP analog and the HRAS p21 catalytic domain Proc. Natl Acad. Sci. USA 87 1990 4849 4853
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 4849-4853
    • Brunger, A.T.1    Milburn, M.V.2    Tong, L.3    Devos, A.M.4    Jancarik, J.5    Yamaizumi, Z.6
  • 17
    • 0028204451 scopus 로고
    • Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy
    • P.J. Kraulis, P.J. Domaille, S.L. Campbell-Burk, T. Van Aken, and E.D. Laue Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy Biochemistry 33 1994 3515 3531
    • (1994) Biochemistry , vol.33 , pp. 3515-3531
    • Kraulis, P.J.1    Domaille, P.J.2    Campbell-Burk, S.L.3    Van Aken, T.4    Laue, E.D.5
  • 18
    • 0026086679 scopus 로고
    • Crystal structures at 2.2 a resolution of the catalytic domains of normal ras protein and an oncogenic mutant complexed with GDP
    • L.A. Tong, A.M. de Vos, M.V. Milburn, and S.H. Kim Crystal structures at 2.2 A resolution of the catalytic domains of normal ras protein and an oncogenic mutant complexed with GDP J. Mol. Biol. 217 1991 503 516
    • (1991) J. Mol. Biol. , vol.217 , pp. 503-516
    • Tong, L.A.1    De Vos, A.M.2    Milburn, M.V.3    Kim, S.H.4
  • 19
    • 0030818825 scopus 로고    scopus 로고
    • Regional polysterism in the GTP-bound form of the human c-Ha-Ras protein
    • Y. Ito, K. Yamasaki, J. Iwahara, T. Terada, A. Kamiya, and M. Shirouzu Regional polysterism in the GTP-bound form of the human c-Ha-Ras protein Biochemistry 36 1997 9109 9119
    • (1997) Biochemistry , vol.36 , pp. 9109-9119
    • Ito, Y.1    Yamasaki, K.2    Iwahara, J.3    Terada, T.4    Kamiya, A.5    Shirouzu, M.6
  • 20
    • 0033571343 scopus 로고    scopus 로고
    • The pre-hydrolysis state of p21(ras) in complex with GTP: New insights into the role of water molecules in the GTP hydrolysis reaction of ras-like proteins
    • A.J. Scheidig, C. Burmester, and R.S. Goody The pre-hydrolysis state of p21(ras) in complex with GTP: new insights into the role of water molecules in the GTP hydrolysis reaction of ras-like proteins Structure 7 1999 1311 1324
    • (1999) Structure , vol.7 , pp. 1311-1324
    • Scheidig, A.J.1    Burmester, C.2    Goody, R.S.3
  • 21
    • 1842301722 scopus 로고    scopus 로고
    • Crystal structures of the small G protein Rap2A in complex with its substrate GTP, with GDP and with GTPγS
    • J. Cherfils, J. Menetrey, G. Le Bras, I. Janoueix-Lerosey, J. de Gunzburg, J.R. Garel, and I. Auzat Crystal structures of the small G protein Rap2A in complex with its substrate GTP, with GDP and with GTPγS EMBO J. 16 1997 5582 5591
    • (1997) EMBO J. , vol.16 , pp. 5582-5591
    • Cherfils, J.1    Menetrey, J.2    Le Bras, G.3    Janoueix-Lerosey, I.4    De Gunzburg, J.5    Garel, J.R.6    Auzat, I.7
  • 22
    • 0035958009 scopus 로고    scopus 로고
    • Structural plasticity of an invariant hydrophobic triad in the switch regions of Rab GTPases is a determinant of effector recognition
    • E. Merithew, S. Hatherly, J.J. Dumas, D.C. Lawe, R. Heller-Harrison, and D.G. Lambright Structural plasticity of an invariant hydrophobic triad in the switch regions of Rab GTPases is a determinant of effector recognition J. Biol. Chem. 276 2001 13982 13988
    • (2001) J. Biol. Chem. , vol.276 , pp. 13982-13988
    • Merithew, E.1    Hatherly, S.2    Dumas, J.J.3    Lawe, D.C.4    Heller-Harrison, R.5    Lambright, D.G.6
  • 23
    • 0037462808 scopus 로고    scopus 로고
    • High resolution crystal structures of human Rab5a and five mutants with substitutions in the catalytically important phosphate-binding loop
    • G. Zhu, J. Liu, S. Terzyan, P. Zhai, G. Li, and X.C. Zhang High resolution crystal structures of human Rab5a and five mutants with substitutions in the catalytically important phosphate-binding loop J. Biol. Chem. 278 2003 2452 2460
    • (2003) J. Biol. Chem. , vol.278 , pp. 2452-2460
    • Zhu, G.1    Liu, J.2    Terzyan, S.3    Zhai, P.4    Li, G.5    Zhang, X.C.6
  • 24
    • 0033523919 scopus 로고    scopus 로고
    • Natural engineering principles of electron tunnelling in biological oxidation-reduction
    • C.C. Page, C.C. Moser, X. Chen, and P.L. Dutton Natural engineering principles of electron tunnelling in biological oxidation-reduction Nature 402 1999 47 52
    • (1999) Nature , vol.402 , pp. 47-52
    • Page, C.C.1    Moser, C.C.2    Chen, X.3    Dutton, P.L.4
  • 25
    • 0034653650 scopus 로고    scopus 로고
    • The trap depth (in DNA) of 8-oxo-7,8-dihydro-2′deoxyguanosine as derived from electron-transfer equilibria in aqueous solution
    • S. Steenken, S.V. Jovanovic, M. Bietti, and K. Bernhard The trap depth (in DNA) of 8-oxo-7,8-dihydro-2′deoxyguanosine as derived from electron-transfer equilibria in aqueous solution J. Am. Chem. Soc. 122 2000 2373 2374
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 2373-2374
    • Steenken, S.1    Jovanovic, S.V.2    Bietti, M.3    Bernhard, K.4
  • 26
    • 0027251053 scopus 로고
    • The pecking order of free radicals and antioxidants: Lipid peroxidation, alpha-tocopherol, and ascorbate
    • G.R. Buettner The pecking order of free radicals and antioxidants: lipid peroxidation, alpha-tocopherol, and ascorbate Arch. Biochem. Biophys. 300 1993 535 543
    • (1993) Arch. Biochem. Biophys. , vol.300 , pp. 535-543
    • Buettner, G.R.1
  • 27
    • 0035105114 scopus 로고    scopus 로고
    • Nitrogen dioxide as an oxidizing agent of 8-oxo-7,8-dihydro-2′- deoxyguanosine but not of 2′-deoxyguanosine
    • V. Shafirovich, J. Cadet, D. Gasparutto, A. Dourandin, and N.E. Geacintov Nitrogen dioxide as an oxidizing agent of 8-oxo-7,8-dihydro-2′- deoxyguanosine but not of 2′-deoxyguanosine Chem. Res. Toxicol. 14 2001 233 241
    • (2001) Chem. Res. Toxicol. , vol.14 , pp. 233-241
    • Shafirovich, V.1    Cadet, J.2    Gasparutto, D.3    Dourandin, A.4    Geacintov, N.E.5
  • 28
    • 0032023777 scopus 로고    scopus 로고
    • Protein radicals in enzyme catalysis
    • J. Stubbe, and W.A. van der Donk Protein radicals in enzyme catalysis Chem. Rev. 98 1998 705 762
    • (1998) Chem. Rev. , vol.98 , pp. 705-762
    • Stubbe, J.1    Van Der Donk, W.A.2
  • 30
    • 0028960178 scopus 로고
    • Switching nucleotide specificity of Ha-Ras p21 by a single amino acid substitution at aspartate 119
    • J.M. Zhong, M.C. Chen-Hwang, and Y.W. Hwang Switching nucleotide specificity of Ha-Ras p21 by a single amino acid substitution at aspartate 119 J. Biol. Chem. 270 1995 10002 10007
    • (1995) J. Biol. Chem. , vol.270 , pp. 10002-10007
    • Zhong, J.M.1    Chen-Hwang, M.C.2    Hwang, Y.W.3
  • 32
    • 0023885845 scopus 로고
    • Relationship among guanine nucleotide exchange, GTP hydrolysis, and transforming potential of mutated ras proteins
    • L.A. Feig, and G.M. Cooper Relationship among guanine nucleotide exchange, GTP hydrolysis, and transforming potential of mutated ras proteins Mol. Cell. Biol. 8 1988 2472 2478
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 2472-2478
    • Feig, L.A.1    Cooper, G.M.2
  • 33
    • 3543140038 scopus 로고    scopus 로고
    • PH-dependent perturbation of Ras guanine-nucleotide interactions and Ras-guanine-nucleotide exchange
    • J. Heo, G. Gao, and S. Campbell pH-dependent perturbation of Ras guanine-nucleotide interactions and Ras-guanine-nucleotide exchange Biochemistry 43 2004 10102 10111
    • (2004) Biochemistry , vol.43 , pp. 10102-10111
    • Heo, J.1    Gao, G.2    Campbell, S.3
  • 35
    • 0026002058 scopus 로고
    • P21 with a phenylalanine 28 - Leucine mutation reacts normally with the GTPase activating protein GAP but nevertheless has transforming properties
    • J. Reinstein, I. Schlichting, M. Frech, R.S. Goody, and A. Wittinghofer p21 with a phenylalanine 28 - leucine mutation reacts normally with the GTPase activating protein GAP but nevertheless has transforming properties J. Biol. Chem. 266 1991 17700 17706
    • (1991) J. Biol. Chem. , vol.266 , pp. 17700-17706
    • Reinstein, J.1    Schlichting, I.2    Frech, M.3    Goody, R.S.4    Wittinghofer, A.5
  • 36
    • 1642483018 scopus 로고    scopus 로고
    • Identification of free radicals on hemoglobin from its self-peroxidation using mass spectrometry and immuno-spin trapping: Observation of a histidinyl radical
    • L.J. Deterding, D.C. Ramirez, J.R. Dubin, R.P. Mason, and K.B. Tomer Identification of free radicals on hemoglobin from its self-peroxidation using mass spectrometry and immuno-spin trapping: observation of a histidinyl radical J. Biol. Chem. 279 2004 11600 11607
    • (2004) J. Biol. Chem. , vol.279 , pp. 11600-11607
    • Deterding, L.J.1    Ramirez, D.C.2    Dubin, J.R.3    Mason, R.P.4    Tomer, K.B.5
  • 37
    • 0035976006 scopus 로고    scopus 로고
    • P700: The primary electron donor of photosystem I
    • A.N. Webber, and W. Lubitz P700: the primary electron donor of photosystem I Biochim. Biophys. Acta 1507 2001 61 79
    • (2001) Biochim. Biophys. Acta , vol.1507 , pp. 61-79
    • Webber, A.N.1    Lubitz, W.2
  • 38
    • 0017769705 scopus 로고
    • Anion radicals of bacteriochlorophyll a and bacteriopheophytin a. Electron spin resonance and electron nuclear double resonance studies
    • J. Fajer, A. Forman, M.S. Davis, L.D. Spaulding, D.C. Brune, and R.H. Felton Anion radicals of bacteriochlorophyll a and bacteriopheophytin a. Electron spin resonance and electron nuclear double resonance studies J. Am. Chem. Soc. 99 1977 4134 4140
    • (1977) J. Am. Chem. Soc. , vol.99 , pp. 4134-4140
    • Fajer, J.1    Forman, A.2    Davis, M.S.3    Spaulding, L.D.4    Brune, D.C.5    Felton, R.H.6
  • 41
    • 0021112837 scopus 로고
    • Heme-heme orientation and electron transfer kinetic behavior of multisite oxidation-reduction enzymes
    • M.W. Makinen, S.A. Schichman, S.C. Hill, and H.B. Gray Heme-heme orientation and electron transfer kinetic behavior of multisite oxidation-reduction enzymes Science 222 1983 929 931
    • (1983) Science , vol.222 , pp. 929-931
    • Makinen, M.W.1    Schichman, S.A.2    Hill, S.C.3    Gray, H.B.4
  • 42
    • 0031149127 scopus 로고    scopus 로고
    • Long-range oxidation of guanine by Ru(III) in duplex DNA
    • M.R. Arkin, E.D. Stemp, S.C. Pulver, and J.K. Barton Long-range oxidation of guanine by Ru(III) in duplex DNA Chem. Biol. 4 1997 389 400
    • (1997) Chem. Biol. , vol.4 , pp. 389-400
    • Arkin, M.R.1    Stemp, E.D.2    Pulver, S.C.3    Barton, J.K.4
  • 43
    • 0035852024 scopus 로고    scopus 로고
    • A novel nitroimidazole compound formed during the reaction of peroxynitrite with 2′,3′,5′-tri-O-acetyl-guanosine
    • J.C. Niles, J.S. Wishnok, and S.R. Tannenbaum A novel nitroimidazole compound formed during the reaction of peroxynitrite with 2′,3′, 5′-tri-O-acetyl-guanosine J. Am. Chem. Soc. 123 2001 12147 12151
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 12147-12151
    • Niles, J.C.1    Wishnok, J.S.2    Tannenbaum, S.R.3
  • 44
    • 0034803513 scopus 로고    scopus 로고
    • Direct observation of radical intermediates in protein-dependent DNA charge transport
    • H.A. Wagenknecht, S.R. Rajski, M. Pascaly, E.D. Stemp, and J.K. Barton Direct observation of radical intermediates in protein-dependent DNA charge transport J. Am. Chem. Soc. 123 2001 4400 4407
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 4400-4407
    • Wagenknecht, H.A.1    Rajski, S.R.2    Pascaly, M.3    Stemp, E.D.4    Barton, J.K.5
  • 45
    • 0037062625 scopus 로고    scopus 로고
    • Peroxynitrite-induced reactions of synthetic oligo 2′- deoxynucleotides and DNA containing guanine: Formation and stability of a 5-guanidino-4-nitroimidazole lesion
    • F. Gu, W.G. Stillwell, J.S. Wishnok, A.J. Shallop, R.A. Jones, and S.R. Tannenbaum Peroxynitrite-induced reactions of synthetic oligo 2′-deoxynucleotides and DNA containing guanine: formation and stability of a 5-guanidino-4-nitroimidazole lesion Biochemistry 41 2002 7508 7518
    • (2002) Biochemistry , vol.41 , pp. 7508-7518
    • Gu, F.1    Stillwell, W.G.2    Wishnok, J.S.3    Shallop, A.J.4    Jones, R.A.5    Tannenbaum, S.R.6
  • 46
    • 0041360606 scopus 로고    scopus 로고
    • Oxidative generation of guanine radicals by carbonate radicals and their reactions with nitrogen dioxide to form site specific 5-guanidino-4- nitroimidazole lesions in oligodeoxynucleotides
    • A. Joffe, S. Mock, B.H. Yun, A. Kolbanovskiy, N.E. Geacintov, and V. Shafirovich Oxidative generation of guanine radicals by carbonate radicals and their reactions with nitrogen dioxide to form site specific 5-guanidino-4- nitroimidazole lesions in oligodeoxynucleotides Chem. Res. Toxicol. 16 2003 966 973
    • (2003) Chem. Res. Toxicol. , vol.16 , pp. 966-973
    • Joffe, A.1    Mock, S.2    Yun, B.H.3    Kolbanovskiy, A.4    Geacintov, N.E.5    Shafirovich, V.6
  • 47
    • 0041931062 scopus 로고    scopus 로고
    • Direct observation of guanine radical cation deprotonation in duplex DNA using pulse radiolysis
    • K. Kobayashi, and S. Tagawa Direct observation of guanine radical cation deprotonation in duplex DNA using pulse radiolysis J. Am. Chem. Soc. 125 2003 10213 10218
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 10213-10218
    • Kobayashi, K.1    Tagawa, S.2
  • 48
    • 0030839865 scopus 로고    scopus 로고
    • Oxidative decay of DNA
    • K.B. Beckman, and B.N. Ames Oxidative decay of DNA J. Biol. Chem. 272 1997 19633 19636
    • (1997) J. Biol. Chem. , vol.272 , pp. 19633-19636
    • Beckman, K.B.1    Ames, B.N.2
  • 49
    • 0033565994 scopus 로고    scopus 로고
    • Oxygen and nitrogen are pro-carcinogens. Damage to DNA by reactive oxygen, chlorine and nitrogen species: Measurement, mechanism and the effects of nutrition
    • B. Halliwell Oxygen and nitrogen are pro-carcinogens. Damage to DNA by reactive oxygen, chlorine and nitrogen species: measurement, mechanism and the effects of nutrition Mutat. Res. 443 1999 37 52
    • (1999) Mutat. Res. , vol.443 , pp. 37-52
    • Halliwell, B.1
  • 50
    • 0028785105 scopus 로고
    • Formation of 8-nitroguanine in DNA treated with peroxynitrite in vitro and its rapid removal from DNA by depurination
    • V. Yermilov, J. Rubio, and H. Ohshima Formation of 8-nitroguanine in DNA treated with peroxynitrite in vitro and its rapid removal from DNA by depurination FEBS Letters 376 1995 207 210
    • (1995) FEBS Letters , vol.376 , pp. 207-210
    • Yermilov, V.1    Rubio, J.2    Ohshima, H.3
  • 52
    • 3543068747 scopus 로고    scopus 로고
    • Backbone dynamics of an oncogenic mutant of Cdc42Hs shows increased flexibility at the nucleotide-binding site
    • P.D. Adams, A.P. Loh, and R.E. Oswald Backbone dynamics of an oncogenic mutant of Cdc42Hs shows increased flexibility at the nucleotide-binding site Biochemistry 43 2004 9968 9977
    • (2004) Biochemistry , vol.43 , pp. 9968-9977
    • Adams, P.D.1    Loh, A.P.2    Oswald, R.E.3
  • 53
    • 0031000742 scopus 로고    scopus 로고
    • Structural and functional analysis of a mutant Ras protein that is insensitive to nitric oxide activation
    • H.R. Mott, J.W. Carpenter, and S.L. Campbell Structural and functional analysis of a mutant Ras protein that is insensitive to nitric oxide activation Biochemistry 36 1997 3640 3644
    • (1997) Biochemistry , vol.36 , pp. 3640-3644
    • Mott, H.R.1    Carpenter, J.W.2    Campbell, S.L.3
  • 54
    • 37049105665 scopus 로고
    • Thiyl free radicals: Direct observations of electron transfer reactions with phenothiazines and ascorbate
    • L. Forni, J. Monig, V. Mora-Arellano, and R. Willson Thiyl free radicals: direct observations of electron transfer reactions with phenothiazines and ascorbate J. Chem. Soc. [Perkin] 1983 961 965
    • (1983) J. Chem. Soc. [Perkin] , pp. 961-965
    • Forni, L.1    Monig, J.2    Mora-Arellano, V.3    Willson, R.4
  • 55
    • 0036223375 scopus 로고    scopus 로고
    • Photochemically catalyzed generation of site-specific 8-nitroguanine adducts in DNA by the reaction of long-lived neutral guanine radicals with nitrogen dioxide
    • V. Shafirovich, S. Mock, A. Kolbanovskiy, and N.E. Geacintov Photochemically catalyzed generation of site-specific 8-nitroguanine adducts in DNA by the reaction of long-lived neutral guanine radicals with nitrogen dioxide Chem. Res. Toxicol. 15 2002 591 597
    • (2002) Chem. Res. Toxicol. , vol.15 , pp. 591-597
    • Shafirovich, V.1    Mock, S.2    Kolbanovskiy, A.3    Geacintov, N.E.4
  • 56
    • 3142663363 scopus 로고    scopus 로고
    • S-glutathiolation of Ras mediates redox-sensitive signaling by angiotensin II in vascular smooth muscle cells
    • T. Adachi, D.R. Pimentel, T. Heibeck, X. Hou, Y.J. Lee, and B. Jiang S-glutathiolation of Ras mediates redox-sensitive signaling by angiotensin II in vascular smooth muscle cells J. Biol. Chem. 279 2004 29857 29862
    • (2004) J. Biol. Chem. , vol.279 , pp. 29857-29862
    • Adachi, T.1    Pimentel, D.R.2    Heibeck, T.3    Hou, X.4    Lee, Y.J.5    Jiang, B.6
  • 57
    • 0034698029 scopus 로고    scopus 로고
    • S-Nitrosocysteine increases palmitate turnover on Ha-Ras in NIH 3T3 cells
    • T. Baker, M. Booden, and J. Buss S-Nitrosocysteine increases palmitate turnover on Ha-Ras in NIH 3T3 cells J. Biol. Chem. 275 2000 22037 22047
    • (2000) J. Biol. Chem. , vol.275 , pp. 22037-22047
    • Baker, T.1    Booden, M.2    Buss, J.3
  • 59
  • 61
    • 0345258474 scopus 로고    scopus 로고
    • P21ras activation following hypoxia-ischemia in the newborn rat brain is dependent on nitric oxide synthase activity but p21ras does not contribute to neurologic injury
    • M.S. Wainwright, L.A. Brennan, M.L. Dizon, and S.M. Black p21ras activation following hypoxia-ischemia in the newborn rat brain is dependent on nitric oxide synthase activity but p21ras does not contribute to neurologic injury Brain Res. Dev. Brain Res. 146 2003 79 85
    • (2003) Brain Res. Dev. Brain Res. , vol.146 , pp. 79-85
    • Wainwright, M.S.1    Brennan, L.A.2    Dizon, M.L.3    Black, S.M.4
  • 62
    • 0038573978 scopus 로고    scopus 로고
    • Nitric oxide activates p21ras and leads to the inhibition of endothelial NO synthase by protein nitration
    • L.A. Brennan, S. Wedgwood, J.M. Bekker, and S.M. Black Nitric oxide activates p21ras and leads to the inhibition of endothelial NO synthase by protein nitration DNA Cell. Biol. 22 2003 317 328
    • (2003) DNA Cell. Biol. , vol.22 , pp. 317-328
    • Brennan, L.A.1    Wedgwood, S.2    Bekker, J.M.3    Black, S.M.4
  • 63
    • 0142106964 scopus 로고    scopus 로고
    • Nitric oxide and cGMP activate the Ras-MAP kinase pathway-stimulating protein tyrosine phosphorylation in rabbit aortic endothelial cells
    • C.J. Oliveira, F. Schindler, A.M. Ventura, M.S. Morais, R.J. Arai, and V. Debbas Nitric oxide and cGMP activate the Ras-MAP kinase pathway-stimulating protein tyrosine phosphorylation in rabbit aortic endothelial cells Free Radic. Biol. Med. 35 2003 381 396
    • (2003) Free Radic. Biol. Med. , vol.35 , pp. 381-396
    • Oliveira, C.J.1    Schindler, F.2    Ventura, A.M.3    Morais, M.S.4    Arai, R.J.5    Debbas, V.6
  • 64
    • 1642453685 scopus 로고    scopus 로고
    • Nitric oxide induces hypoxia-inducible factor 1 activation that is dependent on MAPK and phosphatidylinositol 3-kinase signaling
    • K. Kasuno, S. Takabuchi, K. Fukuda, S. Kizaka-Kondoh, J. Yodoi, and T. Adachi Nitric oxide induces hypoxia-inducible factor 1 activation that is dependent on MAPK and phosphatidylinositol 3-kinase signaling J. Biol. Chem. 279 2004 2550 2558
    • (2004) J. Biol. Chem. , vol.279 , pp. 2550-2558
    • Kasuno, K.1    Takabuchi, S.2    Fukuda, K.3    Kizaka-Kondoh, S.4    Yodoi, J.5    Adachi, T.6
  • 65
    • 85047695603 scopus 로고    scopus 로고
    • Cell density mediated pericellular hypoxia leads to induction of HIF-1alpha via nitric oxide and Ras/MAP kinase mediated signaling pathways
    • E.A. Sheta, H. Trout, J.J. Gildea, M.A. Harding, and D. Theodorescu Cell density mediated pericellular hypoxia leads to induction of HIF-1alpha via nitric oxide and Ras/MAP kinase mediated signaling pathways Oncogene 20 2001 7624 7634
    • (2001) Oncogene , vol.20 , pp. 7624-7634
    • Sheta, E.A.1    Trout, H.2    Gildea, J.J.3    Harding, M.A.4    Theodorescu, D.5
  • 66
    • 0037975678 scopus 로고    scopus 로고
    • Structural and biochemical studies of p21Ras S-nitrosylation and nitric oxide-mediated guanine nucleotide exchange
    • J.G. Williams, K. Pappu, and S.L. Campbell Structural and biochemical studies of p21Ras S-nitrosylation and nitric oxide-mediated guanine nucleotide exchange Proc. Natl Acad. Sci. USA 100 2003 6376 6381
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 6376-6381
    • Williams, J.G.1    Pappu, K.2    Campbell, S.L.3
  • 67
    • 0031656984 scopus 로고    scopus 로고
    • Use of 2-nitroimidazoles as bioreductive markers for tumour hypoxia
    • R.J. Hodgkiss Use of 2-nitroimidazoles as bioreductive markers for tumour hypoxia Anticancer Drug Des. 13 1998 687 702
    • (1998) Anticancer Drug Des. , vol.13 , pp. 687-702
    • Hodgkiss, R.J.1
  • 68
    • 0034285733 scopus 로고    scopus 로고
    • The role of hypoxia-activated prodrugs in cancer therapy
    • W.A. Denny The role of hypoxia-activated prodrugs in cancer therapy Lancet Oncol. 1 2000 25 29
    • (2000) Lancet Oncol. , vol.1 , pp. 25-29
    • Denny, W.A.1
  • 69
    • 0038293080 scopus 로고    scopus 로고
    • Prognostic significance of tumor oxygenation in humans
    • S.M. Evans, and C.J. Koch Prognostic significance of tumor oxygenation in humans Cancer Letters 195 2003 1 16
    • (2003) Cancer Letters , vol.195 , pp. 1-16
    • Evans, S.M.1    Koch, C.J.2
  • 70
    • 0038523737 scopus 로고    scopus 로고
    • Tumor hypoxia at the micro-regional level: Clinical relevance and predictive value of exogenous and endogenous hypoxic cell markers
    • J. Bussink, J.H. Kaanders, and A.J. van der Kogel Tumor hypoxia at the micro-regional level: clinical relevance and predictive value of exogenous and endogenous hypoxic cell markers Radiother. Oncol. 67 2003 3 15
    • (2003) Radiother. Oncol. , vol.67 , pp. 3-15
    • Bussink, J.1    Kaanders, J.H.2    Van Der Kogel, A.J.3
  • 71
    • 1542405875 scopus 로고    scopus 로고
    • Acute hypoxia enhances spontaneous lymph node metastasis in an orthotopic murine model of human cervical carcinoma
    • R.A. Cairns, and R.P. Hill Acute hypoxia enhances spontaneous lymph node metastasis in an orthotopic murine model of human cervical carcinoma Cancer Res. 64 2004 2054 2061
    • (2004) Cancer Res. , vol.64 , pp. 2054-2061
    • Cairns, R.A.1    Hill, R.P.2
  • 72
    • 0029107760 scopus 로고
    • The 2.2 a crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue
    • N. Nassar, G. Horn, C. Herrmann, A. Scherer, F. McCormick, and A. Wittinghofer The 2.2 A crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue Nature 375 1995 554 560
    • (1995) Nature , vol.375 , pp. 554-560
    • Nassar, N.1    Horn, G.2    Herrmann, C.3    Scherer, A.4    McCormick, F.5    Wittinghofer, A.6
  • 73
    • 0033561376 scopus 로고    scopus 로고
    • Structural basis of activation and GTP hydrolysis in Rab proteins
    • J.J. Dumas, Z. Zhu, J.L. Connolly, and D.G. Lambright Structural basis of activation and GTP hydrolysis in Rab proteins Structure 7 1999 413 423
    • (1999) Structure , vol.7 , pp. 413-423
    • Dumas, J.J.1    Zhu, Z.2    Connolly, J.L.3    Lambright, D.G.4
  • 74
    • 37049066149 scopus 로고
    • A scheme for the colorimetric determination of microgram amounts of thiols
    • B. Saville A scheme for the colorimetric determination of microgram amounts of thiols Analyst 83 1958 670 672
    • (1958) Analyst , vol.83 , pp. 670-672
    • Saville, B.1
  • 76
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • M.M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding Anal. Biochem. 72 1976 248 254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 78
    • 0029112918 scopus 로고
    • Analysis of intrinsic and CDC25-stimulated guanine nucleotide exchange of p21ras-nucleotide complexes by fluorescence measurements
    • C. Lenzen, R.H. Cool, and A. Wittinghofer Analysis of intrinsic and CDC25-stimulated guanine nucleotide exchange of p21ras-nucleotide complexes by fluorescence measurements Methods Enzymol. 255 1995 95 109
    • (1995) Methods Enzymol. , vol.255 , pp. 95-109
    • Lenzen, C.1    Cool, R.H.2    Wittinghofer, A.3
  • 79
    • 0033105390 scopus 로고    scopus 로고
    • Regulation of 2-carboxy-d-arabinitol 1-phosphate phosphatase: Activation by glutathione and interaction with thiol reagents
    • J. Heo, and G. Holbrook Regulation of 2-carboxy-d-arabinitol 1-phosphate phosphatase: activation by glutathione and interaction with thiol reagents Biochem. J. 338 1999 409 416
    • (1999) Biochem. J. , vol.338 , pp. 409-416
    • Heo, J.1    Holbrook, G.2


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