메뉴 건너뛰기




Volumn 346, Issue 1, 2005, Pages 69-76

Assessment of S-nitrosothiols on diaminofluorescein gels

Author keywords

Gel; Mitochondria; N Nitrosation; Nitric oxide; Peptides; Proteins; S Nitrosylation

Indexed keywords

AMINO ACIDS; CELL PROLIFERATION; CELL SIGNALING; MAMMALS; MITOCHONDRIA; NITRIC OXIDE; PEPTIDES; PROTEINS;

EID: 26844480191     PISSN: 00032697     EISSN: 10960309     Source Type: Journal    
DOI: 10.1016/j.ab.2005.07.025     Document Type: Article
Times cited : (19)

References (23)
  • 1
    • 0035929149 scopus 로고    scopus 로고
    • Nitrosylation: The prototypic redox-based signaling mechanism
    • J.S. Stamler, S. Lamas, and F.C. Fang Nitrosylation: the prototypic redox-based signaling mechanism Cell 106 2001 675 683
    • (2001) Cell , vol.106 , pp. 675-683
    • Stamler, J.S.1    Lamas, S.2    Fang, F.C.3
  • 2
    • 0028132836 scopus 로고
    • Redox signaling: Nitrosylation and related target interactions of nitric oxide
    • J.S. Stamler Redox signaling: nitrosylation and related target interactions of nitric oxide Cell 78 1994 931 936
    • (1994) Cell , vol.78 , pp. 931-936
    • Stamler, J.S.1
  • 3
    • 0000741366 scopus 로고    scopus 로고
    • Preparation and detection of S-nitrosothiols
    • M. Feelisch J.S. Stamler John Wiley New York
    • J.S. Stamler, and M. Feelisch Preparation and detection of S-nitrosothiols M. Feelisch J.S. Stamler Methods in Nitric Oxide Research 1996 John Wiley New York 521 539
    • (1996) Methods in Nitric Oxide Research , pp. 521-539
    • Stamler, J.S.1    Feelisch, M.2
  • 4
    • 0036846736 scopus 로고    scopus 로고
    • Concomitant S-, N-, and heme-nitros(yl)ation in biological tissues and fluids: Implications for the fate of NO in vivo
    • M. Feelisch, T. Rassaf, S. Mnaimneh, N. Singh, N.S. Bryan, D. Jourd'Heuil, and M. Kelm Concomitant S-, N-, and heme-nitros(yl)ation in biological tissues and fluids: implications for the fate of NO in vivo FASEB J. 16 2002 1775 1785
    • (2002) FASEB J. , vol.16 , pp. 1775-1785
    • Feelisch, M.1    Rassaf, T.2    Mnaimneh, S.3    Singh, N.4    Bryan, N.S.5    Jourd'Heuil, D.6    Kelm, M.7
  • 6
    • 0000741366 scopus 로고    scopus 로고
    • Preparation and detection of S-nitrosothiols
    • M. Feelisch J.S. Stamler John Wiley New York
    • J.S. Stamler, and M. Feelisch Preparation and detection of S-nitrosothiols M. Feelisch J.S. Stamler Methods in Nitric Oxide Research 1996 John Wiley New York 527
    • (1996) Methods in Nitric Oxide Research , pp. 527
    • Stamler, J.S.1    Feelisch, M.2
  • 7
    • 0038381423 scopus 로고    scopus 로고
    • Nitrosylation of cytochrome c during apoptosis
    • C.M. Schonhoff, B. Gaston, and J.B. Mannick Nitrosylation of cytochrome c during apoptosis J. Biol. Chem. 278 2003 18265 18270
    • (2003) J. Biol. Chem. , vol.278 , pp. 18265-18270
    • Schonhoff, C.M.1    Gaston, B.2    Mannick, J.B.3
  • 8
    • 0028340452 scopus 로고
    • Nitric oxide binding to ferrous native horse heart cytochrome c and to its carboxymethylated derivative: A spectroscopic and thermodynamic study
    • P. Ascenzi, M. Coletta, R. Santucci, F. Polizio, and A. Desideri Nitric oxide binding to ferrous native horse heart cytochrome c and to its carboxymethylated derivative: a spectroscopic and thermodynamic study J. Inorg. Biochem. 53 1994 273 280
    • (1994) J. Inorg. Biochem. , vol.53 , pp. 273-280
    • Ascenzi, P.1    Coletta, M.2    Santucci, R.3    Polizio, F.4    Desideri, A.5
  • 10
    • 0034672204 scopus 로고    scopus 로고
    • Determination and bioimaging method for nitric oxide in biological specimens by diaminofluorescein fluorometry
    • Y. Itoh, F.H. Ma, H. Hoshi, M. Oka, K. Noda, Y. Ukai, H. Kojima, T. Nagano, and N. Toda Determination and bioimaging method for nitric oxide in biological specimens by diaminofluorescein fluorometry Anal. Biochem. 287 2000 203 209
    • (2000) Anal. Biochem. , vol.287 , pp. 203-209
    • Itoh, Y.1    Ma, F.H.2    Hoshi, H.3    Oka, M.4    Noda, K.5    Ukai, Y.6    Kojima, H.7    Nagano, T.8    Toda, N.9
  • 14
    • 0035860704 scopus 로고    scopus 로고
    • Nitric oxide inhibits ornithine decarboxylase via S-nitrosylation of cysteine 360 in the active site of the enzyme
    • P.M. Bauer, G.M. Buga, J.M. Fukuto, A.E. Pegg, and L.J. Ignarro Nitric oxide inhibits ornithine decarboxylase via S-nitrosylation of cysteine 360 in the active site of the enzyme J. Biol. Chem. 276 2001 34458 34464
    • (2001) J. Biol. Chem. , vol.276 , pp. 34458-34464
    • Bauer, P.M.1    Buga, G.M.2    Fukuto, J.M.3    Pegg, A.E.4    Ignarro, L.J.5
  • 16
    • 0035932413 scopus 로고    scopus 로고
    • A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans
    • L. Liu, A. Hausladen, M. Zeng, L. Que, J. Heitman, and J.S. Stamler A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans Nature 410 2001 490 494
    • (2001) Nature , vol.410 , pp. 490-494
    • Liu, L.1    Hausladen, A.2    Zeng, M.3    Que, L.4    Heitman, J.5    Stamler, J.S.6
  • 17
    • 0035849714 scopus 로고    scopus 로고
    • S-Nitrosylation is emerging as a specific and fundamental posttranslational protein modification: Head-to-head comparison with O-phosphorylation
    • P. Lane, G. Hao, S.S. Gross, S-Nitrosylation is emerging as a specific and fundamental posttranslational protein modification: head-to-head comparison with O-phosphorylation, Sci. STKE 2001 (2001) RE1.
    • (2001) Sci. STKE , vol.2001
    • Lane, P.1    Hao, G.2    Gross, S.S.3
  • 19
    • 0036710557 scopus 로고    scopus 로고
    • Increased nitric oxide-dependent nitrosylation of 4,5-diaminofluorescein by oxidants: Implications for the measurement of intracellular nitric oxide
    • D. Jourd'heuil Increased nitric oxide-dependent nitrosylation of 4,5-diaminofluorescein by oxidants: implications for the measurement of intracellular nitric oxide Free Radic. Biol. Med. 33 2002 676 684
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 676-684
    • Jourd'Heuil, D.1
  • 20
    • 0032929619 scopus 로고    scopus 로고
    • Inhibitory effects of catecholamines and anti-oxidants on the fluorescence reaction of 4,5-diaminofluorescein: DAF-2, a novel indicator of nitric oxide
    • N. Nagata, K. Momose, and Y. Ishida Inhibitory effects of catecholamines and anti-oxidants on the fluorescence reaction of 4,5-diaminofluorescein: DAF-2, a novel indicator of nitric oxide J. Biochem. (Tokyo) 125 1999 658 661
    • (1999) J. Biochem. (Tokyo) , vol.125 , pp. 658-661
    • Nagata, N.1    Momose, K.2    Ishida, Y.3
  • 21
    • 0037073738 scopus 로고    scopus 로고
    • Interfering with nitric oxide measurements: 4,5-Diaminofluorescein reacts with dehydroascorbic acid and ascorbic acid
    • X. Zhang, W.S. Kim, N. Hatcher, K. Potgieter, L.L. Moroz, R. Gillette, and J.V. Sweedler Interfering with nitric oxide measurements: 4,5-Diaminofluorescein reacts with dehydroascorbic acid and ascorbic acid J. Biol. Chem. 277 2002 48472 48478
    • (2002) J. Biol. Chem. , vol.277 , pp. 48472-48478
    • Zhang, X.1    Kim, W.S.2    Hatcher, N.3    Potgieter, K.4    Moroz, L.L.5    Gillette, R.6    Sweedler, J.V.7
  • 22
    • 11844295419 scopus 로고    scopus 로고
    • S-Nitrosoprotein formation and localization in endothelial cells
    • Y. Yang, and J. Loscalzo S-Nitrosoprotein formation and localization in endothelial cells Proc. Natl. Acad. Sci. USA 102 2005 117 122
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 117-122
    • Yang, Y.1    Loscalzo, J.2
  • 23
    • 0026523717 scopus 로고
    • The ionic strength of the intermembrane space of intact mitochondria is not affected by the pH or volume of the intermembrane space
    • J.D. Cortese, A.L. Voglino, and C.R. Hackenbrock The ionic strength of the intermembrane space of intact mitochondria is not affected by the pH or volume of the intermembrane space Biochim. Biophys. Acta 1100 1992 189 197
    • (1992) Biochim. Biophys. Acta , vol.1100 , pp. 189-197
    • Cortese, J.D.1    Voglino, A.L.2    Hackenbrock, C.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.