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Volumn 290, Issue 2, 2015, Pages 1020-1038

Measuring glutathione redox potential of HIV-1-infected macrophages

Author keywords

[No Author keywords available]

Indexed keywords

CELL DEATH; PEPTIDES; PHYSIOLOGY; REDOX REACTIONS; VIRUSES;

EID: 84920911591     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.588913     Document Type: Article
Times cited : (53)

References (84)
  • 1
    • 0033752413 scopus 로고    scopus 로고
    • Genetic and metabolic control of the mitochondrial transmembrane potential and reactive oxygen intermediate production in HIV disease
    • Perl, A., and Banki, K. (2000) Genetic and metabolic control of the mitochondrial transmembrane potential and reactive oxygen intermediate production in HIV disease. Antioxid. Redox Signal. 2, 551-573
    • (2000) Antioxid. Redox Signal. , vol.2 , pp. 551-573
    • Perl, A.1    Banki, K.2
  • 2
    • 0025677250 scopus 로고
    • Intracellular thiols regulate activation of nuclear factor κB and transcription of human immunodeficiency virus
    • Staal, F. J., Roederer, M., and Herzenberg, L. A. (1990) Intracellular thiols regulate activation of nuclear factor κB and transcription of human immunodeficiency virus. Proc. Natl. Acad. Sci. U.S.A. 87, 9943-9947
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 9943-9947
    • Staal, F.J.1    Roederer, M.2    Herzenberg, L.A.3
  • 3
    • 52349112869 scopus 로고    scopus 로고
    • Reactive oxygen species activate HIV long terminal repeat via post-translational control of NF-κB
    • Pyo, C. W., Yang, Y. L., Yoo, N. K., and Choi, S. Y. (2008) Reactive oxygen species activate HIV long terminal repeat via post-translational control of NF-κB. Biochem. Biophys. Res. Commun. 376, 180-185
    • (2008) Biochem. Biophys. Res. Commun. , vol.376 , pp. 180-185
    • Pyo, C.W.1    Yang, Y.L.2    Yoo, N.K.3    Choi, S.Y.4
  • 4
    • 79957888573 scopus 로고    scopus 로고
    • Mechanisms of HIV-associated lymphocyte apoptosis: 2010
    • Cummins, N. W., and Badley, A. D. (2010) Mechanisms of HIV-associated lymphocyte apoptosis: 2010. Cell Death Dis. 1, e99
    • (2010) Cell Death Dis. , vol.1 , pp. e99
    • Cummins, N.W.1    Badley, A.D.2
  • 5
    • 36549005035 scopus 로고    scopus 로고
    • Endogenous TGF-β activation by reactive oxygen species is key to Foxp3 induction in TCR-stimulated and HIV-1-infected human CD4+CD25- T cells
    • Amarnath, S., Dong, L., Li, J., Wu, Y., and Chen, W. (2007) Endogenous TGF-β activation by reactive oxygen species is key to Foxp3 induction in TCR-stimulated and HIV-1-infected human CD4+CD25- T cells. Retrovirology 4, 57
    • (2007) Retrovirology , vol.4 , pp. 57
    • Amarnath, S.1    Dong, L.2    Li, J.3    Wu, Y.4    Chen, W.5
  • 6
    • 40449092356 scopus 로고    scopus 로고
    • Naive precursors of human regulatory T cells require FoxP3 for suppression and are susceptible to HIV infection
    • Antons, A. K., Wang, R., Oswald-Richter, K., Tseng, M., Arendt, C. W., Kalams, S. A., and Unutmaz, D. (2008) Naive precursors of human regulatory T cells require FoxP3 for suppression and are susceptible to HIV infection. J. Immunol. 180, 764-773
    • (2008) J. Immunol. , vol.180 , pp. 764-773
    • Antons, A.K.1    Wang, R.2    Oswald-Richter, K.3    Tseng, M.4    Arendt, C.W.5    Kalams, S.A.6    Unutmaz, D.7
  • 7
    • 0035371184 scopus 로고    scopus 로고
    • Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple
    • Schafer, F. Q., and Buettner, G. R. (2001) Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radic. Biol. Med. 30, 1191-1212
    • (2001) Free Radic. Biol. Med. , vol.30 , pp. 1191-1212
    • Schafer, F.Q.1    Buettner, G.R.2
  • 9
    • 0032539920 scopus 로고    scopus 로고
    • Glutathione levels in antigen-presenting cells modulate Th1 versus Th2 response patterns
    • Peterson, J. D., Herzenberg, L. A., Vasquez, K., and Waltenbaugh, C. (1998) Glutathione levels in antigen-presenting cells modulate Th1 versus Th2 response patterns. Proc. Natl. Acad. Sci. U.S.A. 95, 3071-3076
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 3071-3076
    • Peterson, J.D.1    Herzenberg, L.A.2    Vasquez, K.3    Waltenbaugh, C.4
  • 10
    • 0026491132 scopus 로고
    • Reactive oxygen intermediates and human immunodeficiency virus (HIV) infection
    • Müller, F. (1992) Reactive oxygen intermediates and human immunodeficiency virus (HIV) infection. Free Radic. Biol. Med. 13, 651-657
    • (1992) Free Radic. Biol. Med. , vol.13 , pp. 651-657
    • Müller, F.1
  • 11
    • 0031435786 scopus 로고    scopus 로고
    • Oxidative stress in human immunodeficiency virus infection
    • Israël, N., and Gougerot-Pocidalo, M. A. (1997) Oxidative stress in human immunodeficiency virus infection. Cell. Mol. Life Sci. 53, 864-870
    • (1997) Cell. Mol. Life Sci. , vol.53 , pp. 864-870
    • Israël, N.1    Gougerot-Pocidalo, M.A.2
  • 12
    • 0036240673 scopus 로고    scopus 로고
    • Role of nitric oxide in HIV-1 infection: Friend or foe?
    • Torre, D., Pugliese, A., and Speranza, F. (2002) Role of nitric oxide in HIV-1 infection: friend or foe? Lancet Infect. Dis. 2, 273-280
    • (2002) Lancet Infect. Dis. , vol.2 , pp. 273-280
    • Torre, D.1    Pugliese, A.2    Speranza, F.3
  • 13
    • 0035037447 scopus 로고    scopus 로고
    • Nitric oxide and chronic HCV and HIV infections
    • Lake-Bakaar, G., Sorbi, D., and Mazzoccoli, V. (2001) Nitric oxide and chronic HCV and HIV infections. Dig. Dis. Sci. 46, 1072-1076
    • (2001) Dig. Dis. Sci. , vol.46 , pp. 1072-1076
    • Lake-Bakaar, G.1    Sorbi, D.2    Mazzoccoli, V.3
  • 14
    • 0013656996 scopus 로고    scopus 로고
    • Measurement of reduced glutathione using high-pressure liquid chromatography
    • Hogarth, L. A., Rabello, C. M., and Hall, A. G. (1999) Measurement of reduced glutathione using high-pressure liquid chromatography. Methods Mol. Med. 28, 91-94
    • (1999) Methods Mol. Med. , vol.28 , pp. 91-94
    • Hogarth, L.A.1    Rabello, C.M.2    Hall, A.G.3
  • 15
    • 0036043924 scopus 로고    scopus 로고
    • Detection of reactive oxygen and nitrogen species in tissues using redox-sensitive fluorescent probes
    • Zuo, L., and Clanton, T. L. (2002) Detection of reactive oxygen and nitrogen species in tissues using redox-sensitive fluorescent probes. Methods Enzymol. 352, 307-325
    • (2002) Methods Enzymol. , vol.352 , pp. 307-325
    • Zuo, L.1    Clanton, T.L.2
  • 16
    • 0032830132 scopus 로고    scopus 로고
    • Evidence for free radical formation during the oxidation of 2'-7'-dichlorofluorescein to the fluorescent dye 2'-7'-dichlorofluorescein by horseradish peroxidase: Possible implications for oxidative stress measurements
    • Rota, C., Chignell, C. F., and Mason, R. P. (1999) Evidence for free radical formation during the oxidation of 2'-7'-dichlorofluorescein to the fluorescent dye 2'-7'-dichlorofluorescein by horseradish peroxidase: possible implications for oxidative stress measurements. Free Radic. Biol. Med. 27, 873-881
    • (1999) Free Radic. Biol. Med. , vol.27 , pp. 873-881
    • Rota, C.1    Chignell, C.F.2    Mason, R.P.3
  • 17
    • 1342289237 scopus 로고    scopus 로고
    • Methods for detection of reactive metabolites of oxygen and nitrogen: In vitro and in vivo considerations
    • Tarpey, M. M., Wink, D. A., and Grisham, M. B. (2004) Methods for detection of reactive metabolites of oxygen and nitrogen: in vitro and in vivo considerations. Am. J. Physiol. Regul. Integr. Comp. Physiol. 286, R431-R444
    • (2004) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.286 , pp. R431-R444
    • Tarpey, M.M.1    Wink, D.A.2    Grisham, M.B.3
  • 18
    • 80255126081 scopus 로고    scopus 로고
    • Measuring E(GSH) and H2O2 with roGFP2-based redox probes
    • Morgan, B., Sobotta, M. C., and Dick, T. P. (2011) Measuring E(GSH) and H2O2 with roGFP2-based redox probes. Free Radic. Biol. Med. 51, 1943-1951
    • (2011) Free Radic. Biol. Med. , vol.51 , pp. 1943-1951
    • Morgan, B.1    Sobotta, M.C.2    Dick, T.P.3
  • 20
    • 0030819379 scopus 로고    scopus 로고
    • Multiply attenuated lentiviral vector achieves efficient gene delivery in vivo
    • Zufferey, R., Nagy, D., Mandel, R. J., Naldini, L., and Trono, D. (1997) Multiply attenuated lentiviral vector achieves efficient gene delivery in vivo. Nat. Biotechnol. 15, 871-875
    • (1997) Nat. Biotechnol. , vol.15 , pp. 871-875
    • Zufferey, R.1    Nagy, D.2    Mandel, R.J.3    Naldini, L.4    Trono, D.5
  • 21
    • 82955227412 scopus 로고    scopus 로고
    • In vivo mapping of hydrogen peroxide and oxidized glutathione reveals chemical and regional specificity of redox homeostasis
    • Albrecht, S. C., Barata, A. G., Grosshans, J., Teleman, A. A., and Dick, T. P. (2011) In vivo mapping of hydrogen peroxide and oxidized glutathione reveals chemical and regional specificity of redox homeostasis. Cell Metab. 14, 819-829
    • (2011) Cell Metab. , vol.14 , pp. 819-829
    • Albrecht, S.C.1    Barata, A.G.2    Grosshans, J.3    Teleman, A.A.4    Dick, T.P.5
  • 22
    • 33748705388 scopus 로고    scopus 로고
    • Transactivation and signaling functions of Tat are not correlated: Biological and immunological characterization of HIV-1 subtype-C Tat protein
    • Siddappa, N. B., Venkatramanan, M., Venkatesh, P., Janki, M. V., Jayasuryan, N., Desai, A., Ravi, V., and Ranga, U. (2006) Transactivation and signaling functions of Tat are not correlated: biological and immunological characterization of HIV-1 subtype-C Tat protein. Retrovirology 3, 53
    • (2006) Retrovirology , vol.3 , pp. 53
    • Siddappa, N.B.1    Venkatramanan, M.2    Venkatesh, P.3    Janki, M.V.4    Jayasuryan, N.5    Desai, A.6    Ravi, V.7    Ranga, U.8
  • 23
    • 33947715044 scopus 로고    scopus 로고
    • Atwo-pronged mechanism for HIV-1 Nef-mediated endocytosis of immune costimulatory molecules CD80 and CD86
    • Chaudhry, A., Das, S. R., Jameel, S., George, A., Bal, V., Mayor, S., and Rath, S. (2007)Atwo-pronged mechanism for HIV-1 Nef-mediated endocytosis of immune costimulatory molecules CD80 and CD86. Cell Host Microbe 1, 37-49
    • (2007) Cell Host Microbe , vol.1 , pp. 37-49
    • Chaudhry, A.1    Das, S.R.2    Jameel, S.3    George, A.4    Bal, V.5    Mayor, S.6    Rath, S.7
  • 24
    • 70149116303 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis WhiB3 maintains redox homeostasis by regulating virulence lipid anabolism to modulate macrophage response
    • Singh, A., Crossman, D. K., Mai, D., Guidry, L., Voskuil, M. I., Renfrow, M. B., and Steyn, A. J. (2009) Mycobacterium tuberculosis WhiB3 maintains redox homeostasis by regulating virulence lipid anabolism to modulate macrophage response. PLoS Pathog. 5, e1000545
    • (2009) PLoS Pathog. , vol.5 , pp. e1000545
    • Singh, A.1    Crossman, D.K.2    Mai, D.3    Guidry, L.4    Voskuil, M.I.5    Renfrow, M.B.6    Steyn, A.J.7
  • 25
    • 84879380362 scopus 로고    scopus 로고
    • Quantitative real time PCR expression analysis of peripheral blood mononuclear cells in pancreatic cancer patients
    • Baine, M. J., Mallya, K., and Batra, S. K. (2013) Quantitative real time PCR expression analysis of peripheral blood mononuclear cells in pancreatic cancer patients. Methods Mol. Biol. 980, 157-173
    • (2013) Methods Mol. Biol. , vol.980 , pp. 157-173
    • Baine, M.J.1    Mallya, K.2    Batra, S.K.3
  • 26
    • 0023508507 scopus 로고
    • Cytokine-induced expression of HIV-1 in a chronically infected promonocyte cell line
    • Folks, T. M., Justement, J., Kinter, A., Dinarello, C. A., and Fauci, A. S. (1987) Cytokine-induced expression of HIV-1 in a chronically infected promonocyte cell line. Science 238, 800-802
    • (1987) Science , vol.238 , pp. 800-802
    • Folks, T.M.1    Justement, J.2    Kinter, A.3    Dinarello, C.A.4    Fauci, A.S.5
  • 27
    • 0025012838 scopus 로고
    • Tumor necrosis factor α functions in an autocrine manner in the induction of human immunodeficiency virus expression
    • Poli, G., Kinter, A., Justement, J. S., Kehrl, J. H., Bressler, P., Stanley, S., and Fauci, A. S. (1990) Tumor necrosis factor α functions in an autocrine manner in the induction of human immunodeficiency virus expression. Proc. Natl. Acad. Sci. U.S.A. 87, 782-785
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 782-785
    • Poli, G.1    Kinter, A.2    Justement, J.S.3    Kehrl, J.H.4    Bressler, P.5    Stanley, S.6    Fauci, A.S.7
  • 28
    • 36349007756 scopus 로고    scopus 로고
    • Redox-sensitive GFP in Arabidopsis thaliana is a quantitative biosensor for the redox potential of the cellular glutathione redox buffer
    • Meyer, A. J., Brach, T., Marty, L., Kreye, S., Rouhier, N., Jacquot, J. P., and Hell, R. (2007) Redox-sensitive GFP in Arabidopsis thaliana is a quantitative biosensor for the redox potential of the cellular glutathione redox buffer. Plant J. 52, 973-986
    • (2007) Plant J. , vol.52 , pp. 973-986
    • Meyer, A.J.1    Brach, T.2    Marty, L.3    Kreye, S.4    Rouhier, N.5    Jacquot, J.P.6    Hell, R.7
  • 29
    • 2542455473 scopus 로고    scopus 로고
    • Imaging dynamic redox changes in mammalian cells with green fluorescent protein indicators
    • Dooley, C. T., Dore, T. M., Hanson, G. T., Jackson, W. C., Remington, S. J., and Tsien, R. Y. (2004) Imaging dynamic redox changes in mammalian cells with green fluorescent protein indicators. J. Biol. Chem. 279, 22284-22293
    • (2004) J. Biol. Chem. , vol.279 , pp. 22284-22293
    • Dooley, C.T.1    Dore, T.M.2    Hanson, G.T.3    Jackson, W.C.4    Remington, S.J.5    Tsien, R.Y.6
  • 30
    • 0026006998 scopus 로고
    • An HIV-1-infectedTcell clone defective in IL-2 production and Ca2 mobilization after CD3 stimulation
    • Perez, V. L., Rowe, T., Justement, J. S., Butera, S. T., June, C. H., and Folks, T. M. (1991) An HIV-1-infectedTcell clone defective in IL-2 production and Ca2 mobilization after CD3 stimulation. J. Immunol. 147, 3145-3148
    • (1991) J. Immunol. , vol.147 , pp. 3145-3148
    • Perez, V.L.1    Rowe, T.2    Justement, J.S.3    Butera, S.T.4    June, C.H.5    Folks, T.M.6
  • 32
  • 34
    • 0033590630 scopus 로고    scopus 로고
    • Hydrogen peroxide-induced apoptosis is CD95-independent, requires the release of mitochondria-derived reactive oxygen species and the activation of NF-κB
    • Dumont, A., Hehner, S. P., Hofmann, T. G., Ueffing, M., Dröge, W., and Schmitz, M. L. (1999) Hydrogen peroxide-induced apoptosis is CD95-independent, requires the release of mitochondria-derived reactive oxygen species and the activation of NF-κB. Oncogene 18, 747-757
    • (1999) Oncogene , vol.18 , pp. 747-757
    • Dumont, A.1    Hehner, S.P.2    Hofmann, T.G.3    Ueffing, M.4    Dröge, W.5    Schmitz, M.L.6
  • 35
    • 84855998391 scopus 로고    scopus 로고
    • Investigation of the levels of oxidative stress parameters in HIV and HIV-TB co-infected patients
    • Awodele, O., Olayemi, S. O., Nwite, J. A., and Adeyemo, T. A. (2012) Investigation of the levels of oxidative stress parameters in HIV and HIV-TB co-infected patients. J. Infect. Dev. Ctries. 6, 79-85
    • (2012) J. Infect. Dev. Ctries. , vol.6 , pp. 79-85
    • Awodele, O.1    Olayemi, S.O.2    Nwite, J.A.3    Adeyemo, T.A.4
  • 36
    • 0029813309 scopus 로고    scopus 로고
    • Role of protein kinase C-β isozyme in activation of latent human immunodeficiency virus type 1 in promonocytic U1 cells by phorbol-12-myristate acetate
    • Kim, C. H., Gollapudi, S., Kim, A., Lee, T., and Gupta, S. (1996) Role of protein kinase C-β isozyme in activation of latent human immunodeficiency virus type 1 in promonocytic U1 cells by phorbol-12-myristate acetate. AIDS Res. Hum. Retroviruses 12, 1361-1366
    • (1996) AIDS Res. Hum. Retroviruses , vol.12 , pp. 1361-1366
    • Kim, C.H.1    Gollapudi, S.2    Kim, A.3    Lee, T.4    Gupta, S.5
  • 37
    • 0025322133 scopus 로고
    • Localization of urokinase-type plasminogen activator receptor on U937 cells: Phorbol ester PMA induces heterogeneity
    • Hansen, S. H., Behrendt, N., Danø, K., and Kristensen, P. (1990) Localization of urokinase-type plasminogen activator receptor on U937 cells: phorbol ester PMA induces heterogeneity. Exp. Cell Res. 187, 255-262
    • (1990) Exp. Cell Res. , vol.187 , pp. 255-262
    • Hansen, S.H.1    Behrendt, N.2    Danø, K.3    Kristensen, P.4
  • 40
    • 84896268678 scopus 로고    scopus 로고
    • Association between HIV/AIDS and multi-drug resistance tuberculosis: A systematic review and meta-analysis
    • Mesfin, Y. M., Hailemariam, D., Biadgilign, S., Biadglign, S., and Kibret, K. T. (2014) Association between HIV/AIDS and multi-drug resistance tuberculosis: a systematic review and meta-analysis. PLoS One 9, e82235
    • (2014) PLoS One , vol.9 , pp. e82235
    • Mesfin, Y.M.1    Hailemariam, D.2    Biadgilign, S.3    Biadglign, S.4    Kibret, K.T.5
  • 42
    • 80054732645 scopus 로고    scopus 로고
    • Evidence for oxidative stress and defective antioxidant response in guinea pigs with tuberculosis
    • Palanisamy, G. S., Kirk, N. M., Ackart, D. F., Shanley, C. A., Orme, I. M., and Basaraba, R. J. (2011) Evidence for oxidative stress and defective antioxidant response in guinea pigs with tuberculosis. PLoS One 6, e26254
    • (2011) PLoS One , vol.6 , pp. e26254
    • Palanisamy, G.S.1    Kirk, N.M.2    Ackart, D.F.3    Shanley, C.A.4    Orme, I.M.5    Basaraba, R.J.6
  • 43
    • 84893730144 scopus 로고    scopus 로고
    • Reengineering redox-sensitive GFP to measure mycothiol redox potential of Mycobacterium tuberculosis during infection
    • Bhaskar, A., Chawla, M., Mehta, M., Parikh, P., Chandra, P., Bhave, D., Kumar, D., Carroll, K. S., and Singh, A. (2014) Reengineering redox-sensitive GFP to measure mycothiol redox potential of Mycobacterium tuberculosis during infection. PLoS Pathog. 10, e1003902
    • (2014) PLoS Pathog. , vol.10 , pp. e1003902
    • Bhaskar, A.1    Chawla, M.2    Mehta, M.3    Parikh, P.4    Chandra, P.5    Bhave, D.6    Kumar, D.7    Carroll, K.S.8    Singh, A.9
  • 44
    • 84879860826 scopus 로고    scopus 로고
    • Peroxiredoxin-6 and NADPH oxidase activity
    • Ambruso, D. R. (2013) Peroxiredoxin-6 and NADPH oxidase activity. Methods Enzymol. 527, 145-167
    • (2013) Methods Enzymol. , vol.527 , pp. 145-167
    • Ambruso, D.R.1
  • 45
    • 80051783174 scopus 로고    scopus 로고
    • Uncoupling proteins and the control of mitochondrial reactive oxygen species production
    • Mailloux, R. J., and Harper, M. E. (2011) Uncoupling proteins and the control of mitochondrial reactive oxygen species production. Free Radic. Biol. Med. 51, 1106-1115
    • (2011) Free Radic. Biol. Med. , vol.51 , pp. 1106-1115
    • Mailloux, R.J.1    Harper, M.E.2
  • 46
    • 50949128741 scopus 로고    scopus 로고
    • Cytosolic phospholipase A(2), lipoxygenase metabolites, and reactive oxygen species
    • Kim, C., Kim, J. Y., and Kim, J. H. (2008) Cytosolic phospholipase A(2), lipoxygenase metabolites, and reactive oxygen species. BMB Rep. 41, 555-559
    • (2008) BMB Rep. , vol.41 , pp. 555-559
    • Kim, C.1    Kim, J.Y.2    Kim, J.H.3
  • 47
    • 84859385695 scopus 로고    scopus 로고
    • Aldehyde oxidase functions as a superoxide generating NADH oxidase:An important redox regulated pathway of cellular oxygen radical formation
    • Kundu, T. K., Velayutham, M., and Zweier, J. L. (2012) Aldehyde oxidase functions as a superoxide generating NADH oxidase: an important redox regulated pathway of cellular oxygen radical formation. Biochemistry 51, 2930-2939
    • (2012) Biochemistry , vol.51 , pp. 2930-2939
    • Kundu, T.K.1    Velayutham, M.2    Zweier, J.L.3
  • 48
    • 84895919381 scopus 로고    scopus 로고
    • Hydrogen peroxide generated by DUOX1 regulates the expression levels of specific differentiation markers in normal human keratinocytes
    • Choi, H., Park, J. Y., Kim, H. J., Noh, M., Ueyama, T., Bae, Y., Lee, T. R., and Shin, D. W. (2014) Hydrogen peroxide generated by DUOX1 regulates the expression levels of specific differentiation markers in normal human keratinocytes. J. Dermatol. Sci. 74, 56-63
    • (2014) J. Dermatol. Sci. , vol.74 , pp. 56-63
    • Choi, H.1    Park, J.Y.2    Kim, H.J.3    Noh, M.4    Ueyama, T.5    Bae, Y.6    Lee, T.R.7    Shin, D.W.8
  • 49
    • 84858324200 scopus 로고    scopus 로고
    • Lipocalin-type prostaglandinDsynthase protects against oxidative stress-induced neuronal cell death
    • Fukuhara, A., Yamada, M., Fujimori, K., Miyamoto, Y., Kusumoto, T., Nakajima, H., and Inui, T. (2012) Lipocalin-type prostaglandinDsynthase protects against oxidative stress-induced neuronal cell death. Biochem. J. 443, 75-84
    • (2012) Biochem. J. , vol.443 , pp. 75-84
    • Fukuhara, A.1    Yamada, M.2    Fujimori, K.3    Miyamoto, Y.4    Kusumoto, T.5    Nakajima, H.6    Inui, T.7
  • 50
    • 84872687926 scopus 로고    scopus 로고
    • Multiple glutathione disulfide removal pathways mediate cytosolic redox homeostasis
    • Morgan, B., Ezeria, D., Amoako, T. N., Riemer, J., Seedorf, M., and Dick, T. P. (2013) Multiple glutathione disulfide removal pathways mediate cytosolic redox homeostasis. Nat. Chem. Biol. 9, 119-125
    • (2013) Nat. Chem. Biol. , vol.9 , pp. 119-125
    • Morgan, B.1    Ezeria, D.2    Amoako, T.N.3    Riemer, J.4    Seedorf, M.5    Dick, T.P.6
  • 52
    • 41749112013 scopus 로고    scopus 로고
    • Apoptosis resistance in HIV-1 persistently-infected cells is independent of active viral replication and involves modulation of the apoptotic mitochondrial pathway
    • Fernández Larrosa, P. N., Croci, D. O., Riva, D. A., Bibini, M., Luzzi, R., Saracco, M., Mersich, S. E., Rabinovich, G. A., and Martínez Peralta, L. (2008) Apoptosis resistance in HIV-1 persistently-infected cells is independent of active viral replication and involves modulation of the apoptotic mitochondrial pathway. Retrovirology 5, 19
    • (2008) Retrovirology , vol.5 , pp. 19
    • Fernández Larrosa, P.N.1    Croci, D.O.2    Riva, D.A.3    Bibini, M.4    Luzzi, R.5    Saracco, M.6    Mersich, S.E.7    Rabinovich, G.A.8    Martínez Peralta, L.9
  • 53
    • 80053278411 scopus 로고    scopus 로고
    • Brain cell reservoirs of latent virus in presymptomatic HIV-infected individuals
    • Thompson, K. A., Cherry, C. L., Bell, J. E., and McLean, C. A. (2011) Brain cell reservoirs of latent virus in presymptomatic HIV-infected individuals. Am. J. Pathol. 179, 1623-1629
    • (2011) Am. J. Pathol. , vol.179 , pp. 1623-1629
    • Thompson, K.A.1    Cherry, C.L.2    Bell, J.E.3    McLean, C.A.4
  • 54
    • 84871977941 scopus 로고    scopus 로고
    • Cyclin T1 and CDK9 T-loop phosphorylation are downregulated during establishment of HIV-1 latency in primary resting memory CD4 T cells
    • Budhiraja, S., Famiglietti, M., Bosque, A., Planelles, V., and Rice, A. P. (2013) Cyclin T1 and CDK9 T-loop phosphorylation are downregulated during establishment of HIV-1 latency in primary resting memory CD4 T cells. J. Virol. 87, 1211-1220
    • (2013) J. Virol. , vol.87 , pp. 1211-1220
    • Budhiraja, S.1    Famiglietti, M.2    Bosque, A.3    Planelles, V.4    Rice, A.P.5
  • 55
    • 0035145779 scopus 로고    scopus 로고
    • The multidrug resistance protein MRP1 mediates the release of glutathione disulfide from rat astrocytes during oxidative stress
    • Hirrlinger, J., König, J., Keppler, D., Lindenau, J., Schulz, J. B., and Dringen, R. (2001) The multidrug resistance protein MRP1 mediates the release of glutathione disulfide from rat astrocytes during oxidative stress. J. Neurochem. 76, 627-636
    • (2001) J. Neurochem. , vol.76 , pp. 627-636
    • Hirrlinger, J.1    König, J.2    Keppler, D.3    Lindenau, J.4    Schulz, J.B.5    Dringen, R.6
  • 56
    • 33750544319 scopus 로고    scopus 로고
    • Glutathione peroxidase 1 and a high cellular glutathione concentration are essential for effective organic hydroperoxide detoxification in astrocytes
    • Liddell, J. R., Dringen, R., Crack, P. J., and Robinson, S. R. (2006) Glutathione peroxidase 1 and a high cellular glutathione concentration are essential for effective organic hydroperoxide detoxification in astrocytes. Glia 54, 873-879
    • (2006) Glia , vol.54 , pp. 873-879
    • Liddell, J.R.1    Dringen, R.2    Crack, P.J.3    Robinson, S.R.4
  • 57
    • 65349093464 scopus 로고    scopus 로고
    • Naturally occurring regulatory T cells show reduced sensitivity toward oxidative stress-induced cell death
    • Mougiakakos, D., Johansson, C. C., and Kiessling, R. (2009) Naturally occurring regulatory T cells show reduced sensitivity toward oxidative stress-induced cell death. Blood 113, 3542-3545
    • (2009) Blood , vol.113 , pp. 3542-3545
    • Mougiakakos, D.1    Johansson, C.C.2    Kiessling, R.3
  • 59
    • 84864243685 scopus 로고    scopus 로고
    • HIV: Shock and kill
    • Deeks, S. G. (2012) HIV: Shock and kill. Nature 487, 439-440
    • (2012) Nature , vol.487 , pp. 439-440
    • Deeks, S.G.1
  • 61
    • 67649259174 scopus 로고    scopus 로고
    • "Shock and kill" effects of class I-selective histone deacetylase inhibitors in combination with the glutathione synthesis inhibitor buthionine sulfoximine in cell line models for HIV-1 quiescence
    • Savarino, A., Mai, A., Norelli, S., El Daker, S., Valente, S., Rotili, D., Altucci, L., Palamara, A. T., and Garaci, E. (2009) "Shock and kill" effects of class I-selective histone deacetylase inhibitors in combination with the glutathione synthesis inhibitor buthionine sulfoximine in cell line models for HIV-1 quiescence. Retrovirology 6, 52
    • (2009) Retrovirology , vol.6 , pp. 52
    • Savarino, A.1    Mai, A.2    Norelli, S.3    El Daker, S.4    Valente, S.5    Rotili, D.6    Altucci, L.7    Palamara, A.T.8    Garaci, E.9
  • 62
    • 4143070452 scopus 로고    scopus 로고
    • Redox modulation of chromatin remodeling: Impact on histone acetylation and deacetylation, NF-κB and pro-inflammatory gene expression
    • Rahman, I., Marwick, J., and Kirkham, P. (2004) Redox modulation of chromatin remodeling: impact on histone acetylation and deacetylation, NF-κB and pro-inflammatory gene expression. Biochem. Pharmacol. 68, 1255-1267
    • (2004) Biochem. Pharmacol. , vol.68 , pp. 1255-1267
    • Rahman, I.1    Marwick, J.2    Kirkham, P.3
  • 65
    • 0035680476 scopus 로고    scopus 로고
    • Erythrocytic glutathione and plasma cysteine status of human immunodeficient patients
    • Lang, C. A., Huang, A., Ramirez, J. A., and Liu, M. C. (2001) Erythrocytic glutathione and plasma cysteine status of human immunodeficient patients. Exp. Biol. Med. 226, 866-869
    • (2001) Exp. Biol. Med. , vol.226 , pp. 866-869
    • Lang, C.A.1    Huang, A.2    Ramirez, J.A.3    Liu, M.C.4
  • 67
    • 0029049922 scopus 로고
    • Increased levels of oxidized glutathione in CD4 lymphocytes associated with disturbed intracellular redox balance in human immunodeficiency virus type 1 infection
    • Aukrust, P., Svardal, A. M., Müller, F., Lunden, B., Berge, R. K., Ueland, P. M., and Frøland, S. S. (1995) Increased levels of oxidized glutathione in CD4 lymphocytes associated with disturbed intracellular redox balance in human immunodeficiency virus type 1 infection. Blood 86, 258-267
    • (1995) Blood , vol.86 , pp. 258-267
    • Aukrust, P.1    Svardal, A.M.2    Müller, F.3    Lunden, B.4    Berge, R.K.5    Ueland, P.M.6    Frøland, S.S.7
  • 68
    • 0028988568 scopus 로고
    • Supplementation of N-acetylcysteine fails to increase glutathione in lymphocytes and plasma of patients with AIDS
    • Witschi, A., Junker, E., Schranz, C., Speck, R. F., and Lauterburg, B. H. (1995) Supplementation of N-acetylcysteine fails to increase glutathione in lymphocytes and plasma of patients with AIDS. AIDS Res. Hum. Retroviruses 11, 141-143
    • (1995) AIDS Res. Hum. Retroviruses , vol.11 , pp. 141-143
    • Witschi, A.1    Junker, E.2    Schranz, C.3    Speck, R.F.4    Lauterburg, B.H.5
  • 69
    • 84868124896 scopus 로고    scopus 로고
    • Increased oxidative stress condition found in different stages of HIV disease in patients undergoing antiretroviral therapy in Umuahia (Nigeria)
    • Ibeh, B. O., and Emeka-Nwabunnia, I. K. (2012) Increased oxidative stress condition found in different stages of HIV disease in patients undergoing antiretroviral therapy in Umuahia (Nigeria). Immunopharmacol. Immunotoxicol. 34, 1060-1066
    • (2012) Immunopharmacol. Immunotoxicol. , vol.34 , pp. 1060-1066
    • Ibeh, B.O.1    Emeka-Nwabunnia, I.K.2
  • 72
    • 67651240219 scopus 로고    scopus 로고
    • HIV-1 replication is differentially regulated by distinct clinical strains of Mycobacterium tuberculosis
    • Ranjbar, S., Boshoff, H. I., Mulder, A., Siddiqi, N., Rubin, E. J., and Goldfeld, A. E. (2009) HIV-1 replication is differentially regulated by distinct clinical strains of Mycobacterium tuberculosis. PLoS One 4, e6116
    • (2009) PLoS One , vol.4 , pp. e6116
    • Ranjbar, S.1    Boshoff, H.I.2    Mulder, A.3    Siddiqi, N.4    Rubin, E.J.5    Goldfeld, A.E.6
  • 74
    • 0027198219 scopus 로고
    • Tat protein of human immunodeficiency virus type 1 represses expression of manganese superoxide dismutase in HeLa cells
    • Flores, S. C., Marecki, J. C., Harper, K. P., Bose, S. K., Nelson, S. K., and McCord, J. M. (1993) Tat protein of human immunodeficiency virus type 1 represses expression of manganese superoxide dismutase in HeLa cells. Proc. Natl. Acad. Sci. U.S.A. 90, 7632-7636
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 7632-7636
    • Flores, S.C.1    Marecki, J.C.2    Harper, K.P.3    Bose, S.K.4    Nelson, S.K.5    McCord, J.M.6
  • 76
    • 0031931047 scopus 로고    scopus 로고
    • Mutations in the tat gene are responsible for human immunodeficiency virus type 1 postintegration latency in the U1 cell line
    • Emiliani, S., Fischle, W., Ott, M., Van Lint, C., Amella, C. A., and Verdin, E. (1998) Mutations in the tat gene are responsible for human immunodeficiency virus type 1 postintegration latency in the U1 cell line. J. Virol. 72, 1666-1670
    • (1998) J. Virol. , vol.72 , pp. 1666-1670
    • Emiliani, S.1    Fischle, W.2    Ott, M.3    Van Lint, C.4    Amella, C.A.5    Verdin, E.6
  • 77
    • 0037449797 scopus 로고    scopus 로고
    • HIV-1 antiviral activity of recombinant natural killer cell enhancing factors, NKEF-A and NKEF-B, members of the peroxiredoxin family
    • Geiben-Lynn, R., Kursar, M., Brown, N. V., Addo, M. M., Shau, H., Lieberman, J., Luster, A. D., and Walker, B. D. (2003) HIV-1 antiviral activity of recombinant natural killer cell enhancing factors, NKEF-A and NKEF-B, members of the peroxiredoxin family. J. Biol. Chem. 278, 1569-1574
    • (2003) J. Biol. Chem. , vol.278 , pp. 1569-1574
    • Geiben-Lynn, R.1    Kursar, M.2    Brown, N.V.3    Addo, M.M.4    Shau, H.5    Lieberman, J.6    Luster, A.D.7    Walker, B.D.8
  • 78
    • 84866179947 scopus 로고    scopus 로고
    • Heme and HO-1 inhibition of HCV, HBV, and HIV
    • Schmidt, W. N., Mathahs, M. M., and Zhu, Z. (2012) Heme and HO-1 inhibition of HCV, HBV, and HIV. Front. Pharmacol. 3, 129
    • (2012) Front. Pharmacol. , vol.3 , pp. 129
    • Schmidt, W.N.1    Mathahs, M.M.2    Zhu, Z.3
  • 79
    • 84870903592 scopus 로고    scopus 로고
    • Glyceraldehyde-3-phosphate dehydrogenase negatively regulates human immunodeficiency virus type 1 infection
    • Kishimoto, N., Onitsuka, A., Kido, K., Takamune, N., Shoji, S., and Misumi, S. (2012) Glyceraldehyde-3-phosphate dehydrogenase negatively regulates human immunodeficiency virus type 1 infection. Retrovirology 9, 107
    • (2012) Retrovirology , vol.9 , pp. 107
    • Kishimoto, N.1    Onitsuka, A.2    Kido, K.3    Takamune, N.4    Shoji, S.5    Misumi, S.6
  • 81
    • 57749099233 scopus 로고    scopus 로고
    • Thioredoxin reductase-1 negatively regulates HIV-1 transactivating protein Tat-dependent transcription in human macrophages
    • Kalantari, P., Narayan, V., Natarajan, S. K., Muralidhar, K., Gandhi, U. H., Vunta, H., Henderson, A. J., and Prabhu, K. S. (2008) Thioredoxin reductase-1 negatively regulates HIV-1 transactivating protein Tat-dependent transcription in human macrophages. J. Biol. Chem. 283, 33183-33190
    • (2008) J. Biol. Chem. , vol.283 , pp. 33183-33190
    • Kalantari, P.1    Narayan, V.2    Natarajan, S.K.3    Muralidhar, K.4    Gandhi, U.H.5    Vunta, H.6    Henderson, A.J.7    Prabhu, K.S.8
  • 82
    • 4143065816 scopus 로고    scopus 로고
    • Host cell gene expression during human immunodeficiency virus type 1 latency and reactivation and effects of targeting genes that are differentially expressed in viral latency
    • Krishnan, V., and Zeichner, S. L. (2004) Host cell gene expression during human immunodeficiency virus type 1 latency and reactivation and effects of targeting genes that are differentially expressed in viral latency. J. Virol. 78, 9458-9473
    • (2004) J. Virol. , vol.78 , pp. 9458-9473
    • Krishnan, V.1    Zeichner, S.L.2


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