메뉴 건너뛰기




Volumn 1820, Issue 6, 2012, Pages 701-711

S-nitrosylation in the regulation of gene transcription

Author keywords

Gene transcription; Nitric oxide; S nitrosylation; Transcription factors

Indexed keywords

COLECALCIFEROL RECEPTOR; CYCLIC GMP; EARLY GROWTH RESPONSE FACTOR 1; ESTROGEN RECEPTOR; GLUCOCORTICOID RECEPTOR; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; HEPATOCYTE NUCLEAR FACTOR 4; HETEROGENEOUS NUCLEAR RIBONUCLEOPROTEIN; HISTONE DEACETYLASE; HYPOXIA INDUCIBLE FACTOR 1; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; IMMUNOMODULATING AGENT; INDUCIBLE NITRIC OXIDE SYNTHASE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; NITRIC OXIDE; NITRIC OXIDE SYNTHASE; PREGNANCY SPECIFIC BETA1 GLYCOPROTEIN; PROTEIN P53; RAS PROTEIN; RETINOID X RECEPTOR; S NITROSOTHIOL; STRESS ACTIVATED PROTEIN KINASE; TRANSCRIPTION FACTOR; TRANSCRIPTION FACTOR AP 1; TRANSCRIPTION FACTOR NRF2; TRANSCRIPTION FACTOR YY1;

EID: 84860494348     PISSN: 03044165     EISSN: 18728006     Source Type: Journal    
DOI: 10.1016/j.bbagen.2011.05.008     Document Type: Review
Times cited : (85)

References (167)
  • 2
    • 18044393604 scopus 로고    scopus 로고
    • Analysis of differentially expressed genes in nitric oxide-exposed human monocytic cells
    • DOI 10.1016/j.freeradbiomed.2005.02.002
    • K. Turpaev, C. Bouton, A. Diet, A. Glatigny, and J.C. Drapier Analysis of differentially expressed genes in nitric oxide-exposed human monocytic cells Free Radic. Biol. Med. 38 2005 1392 1400 (Pubitemid 40602841)
    • (2005) Free Radical Biology and Medicine , vol.38 , Issue.10 , pp. 1392-1400
    • Turpaev, K.1    Bouton, C.2    Diet, A.3    Glatigny, A.4    Drapier, J.-C.5
  • 3
    • 1842834977 scopus 로고    scopus 로고
    • A DNA microarray study of nitric oxide-induced genes in mouse hepatocytes: Implications for hepatic heme oxygenase-1 expression in ischemia/reperfusion
    • DOI 10.1016/S1089-8603(02)00104-0, PII S1089860302001040
    • R. Zamora, Y. Vodovotz, K.S. Aulak, P.K. Kim, J.M. Kane III, L. Alarcon, D.J. Stuehr, and T.R. Billiar A DNA microarray study of nitric oxide-induced genes in mouse hepatocytes: implications for hepatic heme oxygenase-1 expression in ischemia/reperfusion Nitric Oxide 7 2002 165 186 (Pubitemid 35346222)
    • (2002) Nitric Oxide - Biology and Chemistry , vol.7 , Issue.3 , pp. 165-186
    • Zamora, R.1    Vodovotz, Y.2    Aulak, K.S.3    Kim, P.K.4    Kane III, J.M.5    Alarcon, L.6    Stuehr, D.J.7    Billiar, T.R.8
  • 4
    • 0031844664 scopus 로고    scopus 로고
    • A novel mechanism for upregulation of the Escherichia coil K-12 hmp (flavohaemoglobin) gene by the 'NO releaser', S-nitrosoglutathione: Nitrosation of homocysteine and modulation of MetR binding to the glyA-hmp intergenic region
    • DOI 10.1046/j.1365-2958.1998.01000.x
    • J. Membrillo-Hernandez, M.D. Coopamah, A. Channa, M.N. Hughes, and R.K. Poole A novel mechanism for upregulation of the Escherichia coli K-12 hmp (flavohaemoglobin) gene by the 'NO releaser', S-nitrosoglutathione: nitrosation of homocysteine and modulation of MetR binding to the glyA-hmp intergenic region Mol. Microbiol. 29 1998 1101 1112 (Pubitemid 28389449)
    • (1998) Molecular Microbiology , vol.29 , Issue.4 , pp. 1101-1112
    • Membrillo-Hernandez, J.1    Coopamah, M.D.2    Channa, A.3    Hughes, M.N.4    Poole, R.K.5
  • 5
    • 15444363634 scopus 로고    scopus 로고
    • Transcriptional responses of Escherichia coli to S-nitrosoglutathione under defined chemostat conditions reveal major changes in methionine biosynthesis
    • DOI 10.1074/jbc.M410393200
    • J. Flatley, J. Barrett, S.T. Pullan, M.N. Hughes, J. Green, and R.K. Poole Transcriptional responses of Escherichia coli to S-nitrosoglutathione under defined chemostat conditions reveal major changes in methionine biosynthesis J. Biol. Chem. 280 2005 10065 10072 (Pubitemid 40395858)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.11 , pp. 10065-10072
    • Flatley, J.1    Barrett, J.2    Pullan, S.T.3    Hughes, M.N.4    Green, J.5    Poolet, R.K.6
  • 7
    • 14644387541 scopus 로고    scopus 로고
    • Nitric oxide and nitrosative stress tolerance in bacteria
    • DOI 10.1042/BST0330176
    • R.K. Poole Nitric oxide and nitrosative stress tolerance in bacteria Biochem. Soc. Trans. 33 2005 176 180 (Pubitemid 40313794)
    • (2005) Biochemical Society Transactions , vol.33 , Issue.1 , pp. 176-180
    • Poole, R.K.1
  • 8
    • 0032529962 scopus 로고    scopus 로고
    • Activation of a consensus FNR-dependent promoter by DNR of Pseudomonas aeruginosa in response to nitrite
    • PII S0378109798003346
    • N. Hasegawa, H. Arai, and Y. Igarashi Activation of a consensus FNR-dependent promoter by DNR of Pseudomonas aeruginosa in response to nitrite FEMS Microbiol. Lett. 166 1998 213 217 (Pubitemid 128384162)
    • (1998) FEMS Microbiology Letters , vol.166 , Issue.2 , pp. 213-217
    • Hasegawa, N.1    Arai, H.2    Igarashi, Y.3
  • 9
    • 33846892483 scopus 로고    scopus 로고
    • Regulators of bacterial responses to nitric oxide
    • DOI 10.1111/j.1574-6976.2006.00061.x
    • S. Spiro Regulators of bacterial responses to nitric oxide FEMS Microbiol. Rev. 31 2007 193 211 (Pubitemid 46227144)
    • (2007) FEMS Microbiology Reviews , vol.31 , Issue.2 , pp. 193-211
    • Spiro, S.1
  • 10
    • 33947420458 scopus 로고    scopus 로고
    • Nitric oxide in chemostat-cultured Escherichia coli is sensed by Fnr and other global regulators: Unaltered methionine biosynthesis indicates lack of S nitrosation
    • DOI 10.1128/JB.01354-06
    • S.T. Pullan, M.D. Gidley, R.A. Jones, J. Barrett, T.M. Stevanin, R.C. Read, J. Green, and R.K. Poole Nitric oxide in chemostat-cultured Escherichia coli is sensed by Fnr and other global regulators: unaltered methionine biosynthesis indicates lack of S nitrosation J. Bacteriol. 189 2007 1845 1855 (Pubitemid 46446147)
    • (2007) Journal of Bacteriology , vol.189 , Issue.5 , pp. 1845-1855
    • Pullan, S.T.1    Gidley, M.D.2    Jones, R.A.3    Barrett, J.4    Stevanin, T.M.5    Read, R.C.6    Green, J.7    Poole, R.K.8
  • 12
    • 0034625165 scopus 로고    scopus 로고
    • Direct nitric oxide signal transduction via nitrosylation of iron-sulfur centers SoxR transcription activator
    • DOI 10.1073/pnas.97.10.5146
    • H. Ding, and B. Demple Direct nitric oxide signal transduction via nitrosylation of iron-sulfur centers in the SoxR transcription activator Proc. Natl Acad. Sci. U. S. A. 97 2000 5146 5150 (Pubitemid 30313686)
    • (2000) Proceedings of the National Academy of Sciences of the United States of America , vol.97 , Issue.10 , pp. 5146-5150
    • Ding, H.1    Demple, B.2
  • 13
    • 67649406254 scopus 로고    scopus 로고
    • SoxRS-mediated lipopolysaccharide modification enhances resistance against multiple drugs in Escherichia coli
    • J.H. Lee, K.L. Lee, W.S. Yeo, S.J. Park, and J.H. Roe SoxRS-mediated lipopolysaccharide modification enhances resistance against multiple drugs in Escherichia coli J. Bacteriol. 191 2009 4441 4450
    • (2009) J. Bacteriol. , vol.191 , pp. 4441-4450
    • Lee, J.H.1    Lee, K.L.2    Yeo, W.S.3    Park, S.J.4    Roe, J.H.5
  • 14
    • 69449087074 scopus 로고    scopus 로고
    • DNA-mediated redox signaling for transcriptional activation of SoxR
    • P.E. Lee, B. Demple, and J.K. Barton DNA-mediated redox signaling for transcriptional activation of SoxR Proc. Natl Acad. Sci. U. S. A. 106 2009 13164 13168
    • (2009) Proc. Natl Acad. Sci. U. S. A. , vol.106 , pp. 13164-13168
    • Lee, P.E.1    Demple, B.2    Barton, J.K.3
  • 15
    • 77956285812 scopus 로고    scopus 로고
    • Redox sensor SsrB Cys203 enhances Salmonella fitness against nitric oxide generated in the host immune response to oral infection
    • M. Husain, J. Jones-Carson, M. Song, B.D. McCollister, T.J. Bourret, and A. Vazquez-Torres Redox sensor SsrB Cys203 enhances Salmonella fitness against nitric oxide generated in the host immune response to oral infection Proc. Natl Acad. Sci. U. S. A. 107 2010 14396 14401
    • (2010) Proc. Natl Acad. Sci. U. S. A. , vol.107 , pp. 14396-14401
    • Husain, M.1    Jones-Carson, J.2    Song, M.3    McCollister, B.D.4    Bourret, T.J.5    Vazquez-Torres, A.6
  • 16
    • 0030572708 scopus 로고    scopus 로고
    • Nitrosative stress: Activation of the transcription factor OxyR
    • DOI 10.1016/S0092-8674(00)80147-6
    • A. Hausladen, C.T. Privalle, T. Keng, J. DeAngelo, and J.S. Stamler Nitrosative stress: activation of the transcription factor OxyR Cell 86 1996 719 729 (Pubitemid 26303441)
    • (1996) Cell , vol.86 , Issue.5 , pp. 719-729
    • Hausladen, A.1    Privalle, C.T.2    Keng, T.3    DeAngelo, J.4    Stamler, J.S.5
  • 19
    • 34248214667 scopus 로고    scopus 로고
    • Microarray-based gene expression profiling to elucidate cellular responses to nitric oxide-A review from an analytical and biomedical point of view
    • DOI 10.1016/j.jchromb.2006.07.023, PII S1570023206005915, Analysis of the L-Arginine/NO Pathway
    • T. Thum, and J. Bauersachs Microarray-based gene expression profiling to elucidate cellular responses to nitric oxide - a review from an analytical and biomedical point of view J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 851 2007 3 11 (Pubitemid 46720131)
    • (2007) Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences , vol.851 , Issue.1-2 , pp. 3-11
    • Thum, T.1    Bauersachs, J.2
  • 20
    • 0345803942 scopus 로고    scopus 로고
    • Oxidized Phospholipids Induce Expression of Human Heme Oxygenase-1 Involving Activation of cAMP-responsive Element-binding Protein
    • DOI 10.1074/jbc.M304103200
    • G. Kronke, V.N. Bochkov, J. Huber, F. Gruber, S. Bluml, A. Furnkranz, A. Kadl, B.R. Binder, and N. Leitinger Oxidized phospholipids induce expression of human heme oxygenase-1 involving activation of cAMP-responsive element-binding protein J. Biol. Chem. 278 2003 51006 51014 (Pubitemid 38020334)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.51 , pp. 51006-51014
    • Kronke, G.1    Bochkov, V.N.2    Huber, J.3    Gruber, F.4    Bluml, S.5    Furnkranz, A.6    Kadl, A.7    Binder, B.R.8    Leitinger, N.9
  • 21
    • 31944431855 scopus 로고    scopus 로고
    • Nitric oxide-induced nuclear translocation of the metal responsive transcription factor, MTF-1 is mediated by zinc release from metallothionein
    • DOI 10.1016/j.vph.2005.10.004, PII S1537189105002107
    • M.S. Stitt, K.J. Wasserloos, X. Tang, X. Liu, B.R. Pitt, and C.M. St Croix Nitric oxide-induced nuclear translocation of the metal responsive transcription factor, MTF-1 is mediated by zinc release from metallothionein Vascul. Pharmacol. 44 2006 149 155 (Pubitemid 43185989)
    • (2006) Vascular Pharmacology , vol.44 , Issue.3 , pp. 149-155
    • Stitt, M.S.1    Wasserloos, K.J.2    Tang, X.3    Liu, X.4    Pitt, B.R.5    St. Croix, C.M.6
  • 22
    • 15944409156 scopus 로고    scopus 로고
    • Tyrosine nitration on p65: A novel mechanism to rapidly inactive nuclear factor-κB
    • DOI 10.1074/mcp.M400195-MCP200
    • S.W. Park, M.D. Huq, X. Hu, and L.N. Wei Tyrosine nitration on p65: a novel mechanism to rapidly inactivate nuclear factor-kappaB Mol. Cell. Proteomics 4 2005 300 309 (Pubitemid 40439773)
    • (2005) Molecular and Cellular Proteomics , vol.4 , Issue.3 , pp. 300-309
    • Park, S.W.1    Huq, M.D.M.2    Hu, X.3    Wei, L.-N.4
  • 24
    • 77953894189 scopus 로고    scopus 로고
    • Nitration of the tumor suppressor protein p53 at tyrosine 327 promotes p53 oligomerization and activation
    • V.A. Yakovlev, A.S. Bayden, P.R. Graves, G.E. Kellogg, and R.B. Mikkelsen Nitration of the tumor suppressor protein p53 at tyrosine 327 promotes p53 oligomerization and activation Biochemistry 49 2010 5331 5339
    • (2010) Biochemistry , vol.49 , pp. 5331-5339
    • Yakovlev, V.A.1    Bayden, A.S.2    Graves, P.R.3    Kellogg, G.E.4    Mikkelsen, R.B.5
  • 27
    • 0344011964 scopus 로고    scopus 로고
    • Regulation of Gene Expression by Cyclic GMP
    • DOI 10.1161/01.RES.0000103311.52853.48
    • R.B. Pilz, and D.E. Casteel Regulation of gene expression by cyclic GMP Circ. Res. 93 2003 1034 1046 (Pubitemid 37485034)
    • (2003) Circulation Research , vol.93 , Issue.11 , pp. 1034-1046
    • Pilz, R.B.1    Casteel, D.E.2
  • 28
    • 0033815334 scopus 로고    scopus 로고
    • Nitrosation and oxidation in the regulation of gene expression
    • H.E. Marshall, K. Merchant, and J.S. Stamler Nitrosation and oxidation in the regulation of gene expression FASEB J. 14 2000 1889 1900
    • (2000) FASEB J. , vol.14 , pp. 1889-1900
    • Marshall, H.E.1    Merchant, K.2    Stamler, J.S.3
  • 29
    • 0031439772 scopus 로고    scopus 로고
    • Nitric oxide synthases and cardiac muscle: Autocrine and paracrine influences
    • J.L. Balligand, and P.J. Cannon Nitric oxide synthases and cardiac muscle. Autocrine and paracrine influences Arterioscler. Thromb. Vasc. Biol. 17 1997 1846 1858 (Pubitemid 28057081)
    • (1997) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.17 , Issue.10 , pp. 1846-1858
    • Balligand, J.-L.1    Cannon, P.J.2
  • 30
    • 0034875525 scopus 로고    scopus 로고
    • Signal transduction in smooth muscle selected contribution: Insulin utilizes NO/cGMP pathway to activate myosin phosphatase via Rho inhibition in vascular smooth muscle
    • O.A. Sandu, M. Ito, and N. Begum Selected contribution: insulin utilizes NO/cGMP pathway to activate myosin phosphatase via Rho inhibition in vascular smooth muscle J. Appl. Physiol. 91 2001 1475 1482 (Pubitemid 32803948)
    • (2001) Journal of Applied Physiology , vol.91 , Issue.3 , pp. 1475-1482
    • Sandu, O.A.1    Ito, M.2    Begum, N.3
  • 31
    • 0038660670 scopus 로고    scopus 로고
    • RhoA expression is controlled by nitric oxide through cGMP-dependent protein kinase activation
    • DOI 10.1074/jbc.M212776200
    • V. Sauzeau, M. Rolli-Derkinderen, C. Marionneau, G. Loirand, and P. Pacaud RhoA expression is controlled by nitric oxide through cGMP-dependent protein kinase activation J. Biol. Chem. 278 2003 9472 9480 (Pubitemid 36800439)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.11 , pp. 9472-9480
    • Sauzeau, V.1    Rolli-Derkinderen, M.2    Marionneau, C.3    Loirand, G.4    Pacaud, P.5
  • 32
    • 0034712704 scopus 로고    scopus 로고
    • Nitric oxide modulates expression of cell cycle regulatory proteins: A cytostatic strategy for inhibition of human vascular smooth muscle cell proliferation
    • F.C. Tanner, P. Meier, H. Greutert, C. Champion, E.G. Nabel, and T.F. Luscher Nitric oxide modulates expression of cell cycle regulatory proteins: a cytostatic strategy for inhibition of human vascular smooth muscle cell proliferation Circulation 101 2000 1982 1989 (Pubitemid 30225281)
    • (2000) Circulation , vol.101 , Issue.16 , pp. 1982-1989
    • Tanner, F.C.1    Meier, P.2    Greutert, H.3    Champion, C.4    Nabel, E.G.5    Luscher, T.F.6
  • 33
    • 33646908329 scopus 로고    scopus 로고
    • Nitric oxide-dependent negative feedback of PARP-1 trans-activation of the inducible nitric-oxide synthase gene
    • DOI 10.1074/jbc.M511049200
    • Z. Yu, T. Kuncewicz, W.P. Dubinsky, and B.C. Kone Nitric oxide-dependent negative feedback of PARP-1 trans-activation of the inducible nitric-oxide synthase gene J. Biol. Chem. 281 2006 9101 9109 (Pubitemid 43864623)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.14 , pp. 9101-9109
    • Yu, Z.1    Kuncewicz, T.2    Dubinsky, W.P.3    Kone, B.C.4
  • 35
    • 0345306295 scopus 로고    scopus 로고
    • Superoxide Dismutase Targets NO from GSNO to Cysβ93 of Oxyhemoglobin in Concentrated but Not Dilute Solutions of the Protein
    • DOI 10.1021/ja0289752
    • A.A. Romeo, J.A. Capobianco, and A.M. English Superoxide dismutase targets NO from GSNO to Cysbeta93 of oxyhemoglobin in concentrated but not dilute solutions of the protein J. Am. Chem. Soc. 125 2003 14370 14378 (Pubitemid 37452375)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.47 , pp. 14370-14378
    • Romeo, A.A.1    Capobianco, J.A.2    English, A.M.3
  • 36
    • 1842535318 scopus 로고    scopus 로고
    • Involvement of Glycosylphosphatidylinositol-linked Ceruloplasmin in the Copper/Zinc-Nitric Oxide-dependent Degradation of Glypican-1 Heparan Sulfate in Rat C6 Glioma Cells
    • DOI 10.1074/jbc.M313678200
    • K. Mani, F. Cheng, B. Havsmark, S. David, and L.A. Fransson Involvement of glycosylphosphatidylinositol-linked ceruloplasmin in the copper/zinc-nitric oxide-dependent degradation of glypican-1 heparan sulfate in rat C6 glioma cells J. Biol. Chem. 279 2004 12918 12923 (Pubitemid 38450705)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.13 , pp. 12918-12923
    • Mani, K.1    Cheng, F.2    Havsmark, B.3    David, S.4    Fransson, L.-A.5
  • 38
    • 0035932413 scopus 로고    scopus 로고
    • A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans
    • DOI 10.1038/35068596
    • 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 (Pubitemid 32240051)
    • (2001) Nature , vol.410 , Issue.6827 , pp. 490-494
    • Liu, L.1    Hausladen, A.2    Zeng, M.3    Que, L.4    Heitman, J.5    Stamler, J.S.6
  • 39
    • 0035955724 scopus 로고    scopus 로고
    • Accelerated s-nitrosothiol breakdown by amyotrophic lateral sclerosis mutant copper, zinc-superoxide dismutase
    • M.A. Johnson, T.L. Macdonald, J.B. Mannick, M.R. Conaway, and B. Gaston Accelerated s-nitrosothiol breakdown by amyotrophic lateral sclerosis mutant copper, zinc-superoxide dismutase J. Biol. Chem. 276 2001 39872 39878
    • (2001) J. Biol. Chem. , vol.276 , pp. 39872-39878
    • Johnson, M.A.1    MacDonald, T.L.2    Mannick, J.B.3    Conaway, M.R.4    Gaston, B.5
  • 40
    • 15744403464 scopus 로고    scopus 로고
    • Characterization of the S-denitrosation activity of protein disulfide isomerase
    • DOI 10.1074/jbc.M408080200
    • I. Sliskovic, A. Raturi, and B. Mutus Characterization of the S-denitrosation activity of protein disulfide isomerase J. Biol. Chem. 280 2005 8733 8741 (Pubitemid 40409560)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.10 , pp. 8733-8741
    • Sliskovic, I.1    Raturi, A.2    Mutus, B.3
  • 41
    • 0035852845 scopus 로고    scopus 로고
    • Inhibition of NF-kappa B by S-nitrosylation
    • H.E. Marshall, and J.S. Stamler Inhibition of NF-kappa B by S-nitrosylation Biochemistry 40 2001 1688 1693
    • (2001) Biochemistry , vol.40 , pp. 1688-1693
    • Marshall, H.E.1    Stamler, J.S.2
  • 43
    • 28844456563 scopus 로고    scopus 로고
    • Identification of novel mediators of NF-κB through genome-wide survey of monocyte adherence-induced genes
    • DOI 10.1189/jlb.0405211
    • L. Diatchenko, S. Romanov, I. Malinina, J. Clarke, I. Tchivilev, X. Li, and S.S. Makarov Identification of novel mediators of NF-kappaB through genome-wide survey of monocyte adherence-induced genes J. Leukoc. Biol. 78 2005 1366 1377 (Pubitemid 41779243)
    • (2005) Journal of Leukocyte Biology , vol.78 , Issue.6 , pp. 1366-1377
    • Diatchenko, L.1    Romanov, S.2    Malinina, I.3    Clarke, J.4    Tchivilev, I.5    Li, X.6    Makarov, S.S.7
  • 45
    • 0027939931 scopus 로고
    • Role of transcription factor NF-κB/Rel in induction of nitric oxide synthase
    • Q.W. Xie, Y. Kashiwabara, and C. Nathan Role of transcription factor NF-kappa B/Rel in induction of nitric oxide synthase J. Biol. Chem. 269 1994 4705 4708 (Pubitemid 24239438)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.7 , pp. 4705-4708
    • Xie, Q.-W.1    Kashiwabara, Y.2    Nathan, C.3
  • 47
    • 38849199203 scopus 로고    scopus 로고
    • Shared principles in NF-kappaB signaling
    • M.S. Hayden, and S. Ghosh Shared principles in NF-kappaB signaling Cell 132 2008 344 362
    • (2008) Cell , vol.132 , pp. 344-362
    • Hayden, M.S.1    Ghosh, S.2
  • 50
    • 38949178374 scopus 로고    scopus 로고
    • Regulation of MyD88-dependent signaling events by S nitrosylation retards toll-like receptor signal transduction and initiation of acute-phase immune responses
    • DOI 10.1128/MCB.01412-07
    • T. Into, M. Inomata, M. Nakashima, K. Shibata, H. Hacker, and K. Matsushita Regulation of MyD88-dependent signaling events by S nitrosylation retards toll-like receptor signal transduction and initiation of acute-phase immune responses Mol. Cell. Biol. 28 2008 1338 1347 (Pubitemid 351214135)
    • (2008) Molecular and Cellular Biology , vol.28 , Issue.4 , pp. 1338-1347
    • Into, T.1    Inomata, M.2    Nakashima, M.3    Shibata, K.-I.4    Hacker, H.5    Matsushita, K.6
  • 51
    • 35148828429 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1 (HIF-1) pathway
    • cm8
    • G.L. Semenza Hypoxia-inducible factor 1 (HIF-1) pathway Sci. STKE 2007 cm8
    • (2007) Sci. STKE
    • Semenza, G.L.1
  • 52
    • 18344416054 scopus 로고    scopus 로고
    • Nitrosative stress and transcription
    • K.D. Kroncke Nitrosative stress and transcription Biol. Chem. 384 2003 1365 1377
    • (2003) Biol. Chem. , vol.384 , pp. 1365-1377
    • Kroncke, K.D.1
  • 53
    • 0034638623 scopus 로고    scopus 로고
    • Induction of hypoxia-inducible-factor 1 by nitric oxide is mediated via the PI 3K pathway
    • K.B. Sandau, H.G. Faus, and B. Brune Induction of hypoxia-inducible- factor 1 by nitric oxide is mediated via the PI 3K pathway Biochem. Biophys. Res. Commun. 278 2000 263 267
    • (2000) Biochem. Biophys. Res. Commun. , vol.278 , pp. 263-267
    • Sandau, K.B.1    Faus, H.G.2    Brune, B.3
  • 54
    • 0035910429 scopus 로고    scopus 로고
    • Identification of hypoxia-inducible factor 1 ancillary sequence and its function in vascular endothelial growth factor gene induction by hypoxia and nitric oxide
    • H. Kimura, A. Weisz, T. Ogura, Y. Hitomi, Y. Kurashima, K. Hashimoto, F. D'Acquisto, M. Makuuchi, and H. Esumi Identification of hypoxia-inducible factor 1 ancillary sequence and its function in vascular endothelial growth factor gene induction by hypoxia and nitric oxide J. Biol. Chem. 276 2001 2292 2298 (Pubitemid 32109715)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.3 , pp. 2292-2298
    • Kimura, H.1    Weisz, A.2    Ogura, T.3    Hitomi, Y.4    Kurashima, Y.5    Hashimoto, K.6    D'Acquisto, F.7    Makuuchi, M.8    Esumi, H.9
  • 55
    • 0033673457 scopus 로고    scopus 로고
    • Normoxic stabilization of hypoxia-inducible factor-1 expression and activity: Redox-dependent effect of nitrogen oxides
    • L.A. Palmer, B. Gaston, and R.A. Johns Normoxic stabilization of hypoxia-inducible factor-1 expression and activity: redox-dependent effect of nitrogen oxides Mol. Pharmacol. 58 2000 1197 1203
    • (2000) Mol. Pharmacol. , vol.58 , pp. 1197-1203
    • Palmer, L.A.1    Gaston, B.2    Johns, R.A.3
  • 59
    • 0042469448 scopus 로고    scopus 로고
    • Nitric oxide impairs normoxic degradation of HIF-1α by inhibition of prolyl hydroxylases
    • DOI 10.1091/mbc.E02-12-0791
    • E. Metzen, J. Zhou, W. Jelkmann, J. Fandrey, and B. Brune Nitric oxide impairs normoxic degradation of HIF-1alpha by inhibition of prolyl hydroxylases Mol. Biol. Cell 14 2003 3470 3481 (Pubitemid 37013142)
    • (2003) Molecular Biology of the Cell , vol.14 , Issue.8 , pp. 3470-3481
    • Metzen, E.1    Zhou, J.2    Jelkmann, W.3    Fandrey, J.4    Brune, B.5
  • 60
    • 18844413584 scopus 로고    scopus 로고
    • Nitric oxide reverses desferrioxamine- and hypoxia-evoked HIF-1α accumulation - Implications for prolyl hydroxylase activity and iron
    • DOI 10.1016/j.yexcr.2005.02.018, PII S0014482705000844
    • M. Callapina, J. Zhou, S. Schnitzer, E. Metzen, C. Lohr, J.W. Deitmer, and B. Brune Nitric oxide reverses desferrioxamine- and hypoxia-evoked HIF-1alpha accumulation - implications for prolyl hydroxylase activity and iron Exp. Cell Res. 306 2005 274 284 (Pubitemid 40692790)
    • (2005) Experimental Cell Research , vol.306 , Issue.1 , pp. 274-284
    • Callapina, M.1    Zhou, J.2    Schnitzer, S.3    Metzen, E.4    Lohr, C.5    Deitmer, J.W.6    Brune, B.7
  • 61
    • 0042564792 scopus 로고    scopus 로고
    • S-nitrosation of Cys-800 of HIF-1α protein activates its interaction with p300 and stimulates its transcriptional activity
    • DOI 10.1016/S0014-5793(03)00807-X
    • I.M. Yasinska, and V.V. Sumbayev S-nitrosation of Cys-800 of HIF-1alpha protein activates its interaction with p300 and stimulates its transcriptional activity FEBS Lett. 549 2003 105 109 (Pubitemid 36959853)
    • (2003) FEBS Letters , vol.549 , Issue.1-3 , pp. 105-109
    • Yasinska, I.M.1    Sumbayev, V.V.2
  • 62
    • 34047124233 scopus 로고    scopus 로고
    • Modulation of p300 binding by posttranslational modifications of the C-terminal activation domain of hypoxia-inducible factor-1α
    • DOI 10.1016/j.febslet.2007.03.015, PII S0014579307002657
    • H. Cho, D.R. Ahn, H. Park, and E.G. Yang Modulation of p300 binding by posttranslational modifications of the C-terminal activation domain of hypoxia-inducible factor-1alpha FEBS Lett. 581 2007 1542 1548 (Pubitemid 46528919)
    • (2007) FEBS Letters , vol.581 , Issue.8 , pp. 1542-1548
    • Cho, H.1    Ahn, D.-R.2    Park, H.3    Yang, E.G.4
  • 63
    • 0036098552 scopus 로고    scopus 로고
    • AP-1 as a regulator of cell life and death
    • E. Shaulian, and M. Karin AP-1 as a regulator of cell life and death Nat. Cell Biol. 4 2002 E131 E136
    • (2002) Nat. Cell Biol. , vol.4
    • Shaulian, E.1    Karin, M.2
  • 64
    • 0029005508 scopus 로고
    • Nitric oxide and cGMP analogs activate transcription from AP-1-responsive promoters in mammalian cells
    • R.B. Pilz, M. Suhasini, S. Idriss, J.L. Meinkoth, and G.R. Boss Nitric oxide and cGMP analogs activate transcription from AP-1-responsive promoters in mammalian cells FASEB J. 9 1995 552 558
    • (1995) FASEB J. , vol.9 , pp. 552-558
    • Pilz, R.B.1    Suhasini, M.2    Idriss, S.3    Meinkoth, J.L.4    Boss, G.R.5
  • 66
    • 0025077481 scopus 로고
    • Redox regulation of fos and jun DNA-binding activity in vitro
    • C. Abate, L. Patel, F.J. Rauscher III, and T. Curran Redox regulation of fos and jun DNA-binding activity in vitro Science 249 1990 1157 1161
    • (1990) Science , vol.249 , pp. 1157-1161
    • Abate, C.1    Patel, L.2    Rauscher Iii, F.J.3    Curran, T.4
  • 67
    • 0000128590 scopus 로고    scopus 로고
    • Inhibition of AP-1 DNA binding by nitric oxide involving conserved cysteine residues in Jun and Fos
    • DOI 10.1006/bbrc.1997.7930
    • D. Nikitovic, A. Holmgren, and G. Spyrou Inhibition of AP-1 DNA binding by nitric oxide involving conserved cysteine residues in Jun and Fos Biochem. Biophys. Res. Commun. 242 1998 109 112 (Pubitemid 28412386)
    • (1998) Biochemical and Biophysical Research Communications , vol.242 , Issue.1 , pp. 109-112
    • Nikitovic, D.1    Holmgren, A.2    Spyrou, G.3
  • 68
    • 0032983979 scopus 로고    scopus 로고
    • Nitric oxide inhibits c-Jun DNA binding by specifically targeted S-glutathionylation
    • P. Klatt, E.P. Molina, and S. Lamas Nitric oxide inhibits c-Jun DNA binding by specifically targeted S-glutathionylation J. Biol. Chem. 274 1999 15857 15864
    • (1999) J. Biol. Chem. , vol.274 , pp. 15857-15864
    • Klatt, P.1    Molina, E.P.2    Lamas, S.3
  • 70
    • 71449099635 scopus 로고    scopus 로고
    • Antioxidant-induced modification of INrf2 cysteine 151 and PKC-delta-mediated phosphorylation of Nrf2 serine 40 are both required for stabilization and nuclear translocation of Nrf2 and increased drug resistance
    • S.K. Niture, A.K. Jain, and A.K. Jaiswal Antioxidant-induced modification of INrf2 cysteine 151 and PKC-delta-mediated phosphorylation of Nrf2 serine 40 are both required for stabilization and nuclear translocation of Nrf2 and increased drug resistance J. Cell Sci. 122 2009 4452 4464
    • (2009) J. Cell Sci. , vol.122 , pp. 4452-4464
    • Niture, S.K.1    Jain, A.K.2    Jaiswal, A.K.3
  • 71
    • 2442535969 scopus 로고    scopus 로고
    • Nitric Oxide-induced Transcriptional Up-regulation of Protective Genes by Nrf2 via the Antioxidant Response Element Counteracts Apoptosis of Neuroblastoma Cells
    • DOI 10.1074/jbc.M312492200
    • S. Dhakshinamoorthy, and A.G. Porter Nitric oxide-induced transcriptional up-regulation of protective genes by Nrf2 via the antioxidant response element counteracts apoptosis of neuroblastoma cells J. Biol. Chem. 279 2004 20096 20107 (Pubitemid 38623454)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.19 , pp. 20096-20107
    • Dhakshinamoorthy, S.1    Porter, A.G.2
  • 72
    • 38649104828 scopus 로고    scopus 로고
    • Keap1 modification and nuclear accumulation in response to S-nitrosocysteine
    • B.J. Buckley, S. Li, and A.R. Whorton Keap1 modification and nuclear accumulation in response to S-nitrosocysteine Free Radic. Biol. Med. 44 2008 692 698
    • (2008) Free Radic. Biol. Med. , vol.44 , pp. 692-698
    • Buckley, B.J.1    Li, S.2    Whorton, A.R.3
  • 73
    • 38949110010 scopus 로고    scopus 로고
    • Negative feedback regulation of lipopolysaccharide-induced inducible nitric oxide synthase gene expression by heme oxygenase-1 induction in macrophages
    • DOI 10.1016/j.molimm.2007.10.011, PII S016158900700805X
    • T. Ashino, R. Yamanaka, M. Yamamoto, H. Shimokawa, K. Sekikawa, Y. Iwakura, S. Shioda, S. Numazawa, and T. Yoshida Negative feedback regulation of lipopolysaccharide-induced inducible nitric oxide synthase gene expression by heme oxygenase-1 induction in macrophages Mol. Immunol. 45 2008 2106 2115 (Pubitemid 351226260)
    • (2008) Molecular Immunology , vol.45 , Issue.7 , pp. 2106-2115
    • Ashino, T.1    Yamanaka, R.2    Yamamoto, M.3    Shimokawa, H.4    Sekikawa, K.5    Iwakura, Y.6    Shioda, S.7    Numazawa, S.8    Yoshida, T.9
  • 76
    • 0034859507 scopus 로고    scopus 로고
    • Zinc binding and redox control of p53 structure and function
    • P. Hainaut, and K. Mann Zinc binding and redox control of p53 structure and function Antioxid. Redox Signal. 3 2001 611 623 (Pubitemid 32785984)
    • (2001) Antioxidants and Redox Signaling , vol.3 , Issue.4 , pp. 611-623
    • Hainaut, P.1    Mann, K.2
  • 78
    • 0037137226 scopus 로고    scopus 로고
    • Nitric oxide-mediated inhibition of Hdm2-p53 binding
    • DOI 10.1021/bi026262q
    • C.M. Schonhoff, M.C. Daou, S.N. Jones, C.A. Schiffer, and A.H. Ross Nitric oxide-mediated inhibition of Hdm2-p53 binding Biochemistry 41 2002 13570 13574 (Pubitemid 35332692)
    • (2002) Biochemistry , vol.41 , Issue.46 , pp. 13570-13574
    • Schonhoff, C.M.1    Daou, M.-C.2    Jones, S.N.3    Schiffer, C.A.4    Ross, A.H.5
  • 79
    • 0034649496 scopus 로고    scopus 로고
    • Specific pattern of p53 phosphorylation during nitric oxide-induced cell cycle arrest
    • DOI 10.1038/sj.onc.1204100
    • N. Nakaya, S.W. Lowe, Y. Taya, A. Chenchik, and G. Enikolopov Specific pattern of p53 phosphorylation during nitric oxide-induced cell cycle arrest Oncogene 19 2000 6369 6375 (Pubitemid 32641851)
    • (2000) Oncogene , vol.19 , Issue.54 , pp. 6369-6375
    • Nakaya, N.1    Lowe, S.W.2    Taya, Y.3    Chenchik, A.4    Enikolopov, G.5
  • 80
    • 0029942290 scopus 로고    scopus 로고
    • Induction of p53 and p21/WAF1/CIP1 expression by nitric oxide and their association with apoptosis in human cancer cells
    • Y.S. Ho, Y.J. Wang, and J.K. Lin Induction of p53 and p21/WAF1/CIP1 expression by nitric oxide and their association with apoptosis in human cancer cells Mol. Carcinog. 16 1996 20 31
    • (1996) Mol. Carcinog. , vol.16 , pp. 20-31
    • Ho, Y.S.1    Wang, Y.J.2    Lin, J.K.3
  • 81
    • 22244454400 scopus 로고    scopus 로고
    • Nitric oxide-induced apoptosis in lymphoblastoid and fibroblast cells dependent on the phosphorylation and activation of p53
    • DOI 10.1158/0008-5472.CAN-04-4254
    • L.M. McLaughlin, and B. Demple Nitric oxide-induced apoptosis in lymphoblastoid and fibroblast cells dependent on the phosphorylation and activation of p53 Cancer Res. 65 2005 6097 6104 (Pubitemid 40994394)
    • (2005) Cancer Research , vol.65 , Issue.14 , pp. 6097-6104
    • McLaughlin, L.M.1    Demple, B.2
  • 83
    • 65249150214 scopus 로고    scopus 로고
    • SDF-1alpha stimulates JNK3 activity via eNOS-dependent nitrosylation of MKP7 to enhance endothelial migration
    • X. Pi, Y. Wu, J.E. Ferguson III, A.L. Portbury, and C. Patterson SDF-1alpha stimulates JNK3 activity via eNOS-dependent nitrosylation of MKP7 to enhance endothelial migration Proc. Natl Acad. Sci. U. S. A. 106 2009 5675 5680
    • (2009) Proc. Natl Acad. Sci. U. S. A. , vol.106 , pp. 5675-5680
    • Pi, X.1    Wu, Y.2    Ferguson Iii, J.E.3    Portbury, A.L.4    Patterson, C.5
  • 85
    • 0033137330 scopus 로고    scopus 로고
    • Mammalian Kruppel-like transcription factors: More than just a pretty finger
    • J. Turner, and M. Crossley Mammalian Kruppel-like transcription factors: more than just a pretty finger Trends Biochem. Sci. 24 1999 236 240
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 236-240
    • Turner, J.1    Crossley, M.2
  • 86
    • 0034859653 scopus 로고    scopus 로고
    • Zinc finger proteins as molecular targets for nitric oxide-mediated gene regulation
    • K.D. Kroncke Zinc finger proteins as molecular targets for nitric oxide-mediated gene regulation Antioxid. Redox Signal. 3 2001 565 575
    • (2001) Antioxid. Redox Signal. , vol.3 , pp. 565-575
    • Kroncke, K.D.1
  • 87
    • 0033276622 scopus 로고    scopus 로고
    • Zinc finger transcription factors as molecular targets for nitric oxide-mediated immunosuppression: Inhibition of IL-2 gene expression in murine lymphocytes
    • D. Berendji, V. Kolb-Bachofen, P.F. Zipfel, C. Skerka, C. Carlberg, and K.D. Kroncke Zinc finger transcription factors as molecular targets for nitric oxide-mediated immunosuppression: inhibition of IL-2 gene expression in murine lymphocytes Mol. Med. 5 1999 721 730 (Pubitemid 32937032)
    • (1999) Molecular Medicine , vol.5 , Issue.11 , pp. 721-730
    • Berendji, D.1    Kolb-Bachofen, V.2    Zipfel, P.F.3    Skerka, C.4    Carlberg, C.5    Kroncke, K.-D.6
  • 89
    • 48349092316 scopus 로고    scopus 로고
    • Glutathione and copper, zinc superoxide dismutase are modulated by overexpression of neuronal nitric oxide synthase
    • S. Baldelli, K. Aquilano, G. Rotilio, and M.R. Ciriolo Glutathione and copper, zinc superoxide dismutase are modulated by overexpression of neuronal nitric oxide synthase Int. J. Biochem. Cell Biol. 40 2008 2660 2670
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 2660-2670
    • Baldelli, S.1    Aquilano, K.2    Rotilio, G.3    Ciriolo, M.R.4
  • 90
    • 78650233501 scopus 로고    scopus 로고
    • Neuronal nitric oxide synthase interacts with Sp1 through the PDZ domain inhibiting Sp1-mediated copper-zinc superoxide dismutase expression
    • S. Baldelli, K. Aquilano, G. Rotilio, and M.R. Ciriolo Neuronal nitric oxide synthase interacts with Sp1 through the PDZ domain inhibiting Sp1-mediated copper-zinc superoxide dismutase expression Int. J. Biochem. Cell Biol. 43 2011 163 169
    • (2011) Int. J. Biochem. Cell Biol. , vol.43 , pp. 163-169
    • Baldelli, S.1    Aquilano, K.2    Rotilio, G.3    Ciriolo, M.R.4
  • 91
    • 34548313708 scopus 로고    scopus 로고
    • Inhibition of nitric oxide synthase and farnesyltransferase change the activities of several transcription factors
    • E. Zhuravliova, T. Barbakadze, N. Narmania, J. Ramsden, and D. Mikeladze Inhibition of nitric oxide synthase and farnesyltransferase change the activities of several transcription factors J. Mol. Neurosci. 31 2007 281 287 (Pubitemid 47338420)
    • (2007) Journal of Molecular Neuroscience , vol.31 , Issue.3 , pp. 281-287
    • Zhuravliova, E.1    Barbakadze, T.2    Narmania, N.3    Ramsden, J.4    Mikeladze, D.5
  • 92
    • 0042707606 scopus 로고    scopus 로고
    • Adjacent sequence controls the response polarity of nitric oxide-sensitive Sp factor binding sites
    • DOI 10.1074/jbc.M213043200
    • J. Zhang, S. Wang, R.A. Wesley, and R.L. Danner Adjacent sequence controls the response polarity of nitric oxide-sensitive Sp factor binding sites J. Biol. Chem. 278 2003 29192 29200 (Pubitemid 36935835)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.31 , pp. 29192-29200
    • Zhang, J.1    Wang, S.2    Wesley, R.A.3    Danner, R.L.4
  • 93
    • 0033584997 scopus 로고    scopus 로고
    • A Sp1 binding site of the tumor necrosis factor α promoter functions as a nitric oxide response element
    • S. Wang, W. Wang, R.A. Wesley, and R.L. Danner A Sp1 binding site of the tumor necrosis factor alpha promoter functions as a nitric oxide response element J. Biol. Chem. 274 1999 33190 33193 (Pubitemid 129511612)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.47 , pp. 33190-33193
    • Wang, S.1    Wang, W.2    Wesley, R.A.3    Danner, R.L.4
  • 94
    • 78650698054 scopus 로고    scopus 로고
    • Interplay between heme oxygenase-1 and the multifunctional transcription factor yin yang 1 in the inhibition of intimal hyperplasia
    • K. Beck, B.J. Wu, J. Ni, F.S. Santiago, K.P. Malabanan, C. Li, Y. Wang, L.M. Khachigian, and R. Stocker Interplay between heme oxygenase-1 and the multifunctional transcription factor yin yang 1 in the inhibition of intimal hyperplasia Circ. Res. 107 2010 1490 1497
    • (2010) Circ. Res. , vol.107 , pp. 1490-1497
    • Beck, K.1    Wu, B.J.2    Ni, J.3    Santiago, F.S.4    Malabanan, K.P.5    Li, C.6    Wang, Y.7    Khachigian, L.M.8    Stocker, R.9
  • 95
    • 0035399797 scopus 로고    scopus 로고
    • Nitric oxide inhibits the transcription repressor yin-yang 1 binding activity at the silencer region of the Fas promoter: A pivotal role for nitric oxide in the up-regulation of Fas gene expression in human tumor cells
    • H.J. Garban, and B. Bonavida Nitric oxide inhibits the transcription repressor Yin-Yang 1 binding activity at the silencer region of the Fas promoter: a pivotal role for nitric oxide in the up-regulation of Fas gene expression in human tumor cells J. Immunol. 167 2001 75 81 (Pubitemid 32567763)
    • (2001) Journal of Immunology , vol.167 , Issue.1 , pp. 75-81
    • Garban, H.J.1    Bonavida, B.2
  • 97
    • 55549127510 scopus 로고    scopus 로고
    • Nitric oxide sensitizes tumor cells to TRAIL-induced apoptosis via inhibition of the DR5 transcription repressor Yin Yang 1
    • S. Huerta-Yepez, M. Vega, S.E. Escoto-Chavez, B. Murdock, T. Sakai, S. Baritaki, and B. Bonavida Nitric oxide sensitizes tumor cells to TRAIL-induced apoptosis via inhibition of the DR5 transcription repressor Yin Yang 1 Nitric Oxide 20 2009 39 52
    • (2009) Nitric Oxide , vol.20 , pp. 39-52
    • Huerta-Yepez, S.1    Vega, M.2    Escoto-Chavez, S.E.3    Murdock, B.4    Sakai, T.5    Baritaki, S.6    Bonavida, B.7
  • 98
    • 0034957480 scopus 로고    scopus 로고
    • Nuclear hormone receptors and gene expression
    • A. Aranda, and A. Pascual Nuclear hormone receptors and gene expression Physiol. Rev. 81 2001 1269 1304 (Pubitemid 32606670)
    • (2001) Physiological Reviews , vol.81 , Issue.3 , pp. 1269-1304
    • Aranda, A.1    Pascual, A.2
  • 99
    • 0033053615 scopus 로고    scopus 로고
    • Inhibition of glucocorticoid receptor binding by nitric oxide
    • M.D. Galigniana, G. Piwien-Pilipuk, and J. Assreuy Inhibition of glucocorticoid receptor binding by nitric oxide Mol. Pharmacol. 55 1999 317 323 (Pubitemid 29076029)
    • (1999) Molecular Pharmacology , vol.55 , Issue.2 , pp. 317-323
    • Galigniana, M.D.1    Piwien-Pilipuk, G.2    Assreuy, J.3
  • 101
    • 77954945965 scopus 로고    scopus 로고
    • Estradiol-17beta stimulates specific receptor and endogenous nitric oxide-dependent dynamic endothelial protein S-nitrosylation: Analysis of endothelial nitrosyl-proteome
    • H.H. Zhang, L. Feng, I. Livnat, J.K. Hoh, J.Y. Shim, W.X. Liao, and D.B. Chen Estradiol-17beta stimulates specific receptor and endogenous nitric oxide-dependent dynamic endothelial protein S-nitrosylation: analysis of endothelial nitrosyl-proteome Endocrinology 151 2010 3874 3887
    • (2010) Endocrinology , vol.151 , pp. 3874-3887
    • Zhang, H.H.1    Feng, L.2    Livnat, I.3    Hoh, J.K.4    Shim, J.Y.5    Liao, W.X.6    Chen, D.B.7
  • 102
    • 67651108601 scopus 로고    scopus 로고
    • Estrogen receptor-beta activation results in S-nitrosylation of proteins involved in cardioprotection
    • J. Lin, C. Steenbergen, E. Murphy, and J. Sun Estrogen receptor-beta activation results in S-nitrosylation of proteins involved in cardioprotection Circulation 120 2009 245 254
    • (2009) Circulation , vol.120 , pp. 245-254
    • Lin, J.1    Steenbergen, C.2    Murphy, E.3    Sun, J.4
  • 103
    • 0028395604 scopus 로고
    • Orphan receptor HNF-4 and liver-specific gene expression
    • F.M. Sladek Orphan receptor HNF-4 and liver-specific gene expression Receptor 4 1994 64
    • (1994) Receptor , vol.4 , pp. 64
    • Sladek, F.M.1
  • 104
    • 0035124052 scopus 로고    scopus 로고
    • Cytochrome P450 regulation by hepatocyte nuclear factor 4 in human hepatocytes: A study using adenovirus-mediated antisense targeting
    • DOI 10.1053/jhep.2001.22176
    • R. Jover, R. Bort, M.J. Gomez-Lechon, and J.V. Castell Cytochrome P450 regulation by hepatocyte nuclear factor 4 in human hepatocytes: a study using adenovirus-mediated antisense targeting Hepatology 33 2001 668 675 (Pubitemid 32185230)
    • (2001) Hepatology , vol.33 , Issue.3 , pp. 668-675
    • Jover, R.1    Bort, R.2    Gomez-Lechon, M.J.3    Castell, J.V.4
  • 105
    • 0036142546 scopus 로고    scopus 로고
    • Contribution of hepatocyte nuclear factor-4 to down-regulation of CYP2D6 gene expression by nitric oxide
    • DOI 10.1124/mol.61.1.194
    • H. Hara, and T. Adachi Contribution of hepatocyte nuclear factor-4 to down-regulation of CYP2D6 gene expression by nitric oxide Mol. Pharmacol. 61 2002 194 200 (Pubitemid 34049527)
    • (2002) Molecular Pharmacology , vol.61 , Issue.1 , pp. 194-200
    • Hara, H.1    Adachi, T.2
  • 107
    • 18944390248 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase and the therapeutic effects of its inhibitors
    • DOI 10.1038/nrd1718
    • P. Jagtap, and C. Szabo Poly(ADP-ribose) polymerase and the therapeutic effects of its inhibitors Nat. Rev. Drug Discov. 4 2005 421 440 (Pubitemid 40704125)
    • (2005) Nature Reviews Drug Discovery , vol.4 , Issue.5 , pp. 421-440
    • Jagtap, P.1    Szabo, C.2
  • 108
    • 0035861675 scopus 로고    scopus 로고
    • The sequence-specific DNA binding of NF-kappa B is reversibly regulated by the automodification reaction of poly (ADP-ribose) polymerase 1
    • W.J. Chang, and R. Alvarez-Gonzalez The sequence-specific DNA binding of NF-kappa B is reversibly regulated by the automodification reaction of poly (ADP-ribose) polymerase 1 J. Biol. Chem. 276 2001 47664 47670
    • (2001) J. Biol. Chem. , vol.276 , pp. 47664-47670
    • Chang, W.J.1    Alvarez-Gonzalez, R.2
  • 109
    • 5644302206 scopus 로고    scopus 로고
    • Critical role of the automodification of poly(ADP-ribose) polymerase-1 in nuclear factor-κB-dependent gene expression in primary cultured mouse glial cells
    • DOI 10.1074/jbc.M407923200
    • H. Nakajima, H. Nagaso, N. Kakui, M. Ishikawa, T. Hiranuma, and S. Hoshiko Critical role of the automodification of poly(ADP-ribose) polymerase-1 in nuclear factor-kappaB-dependent gene expression in primary cultured mouse glial cells J. Biol. Chem. 279 2004 42774 42786 (Pubitemid 39372165)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.41 , pp. 42774-42786
    • Nakajima, H.1    Nagaso, H.2    Kakui, N.3    Ishikawa, M.4    Hiranuma, T.5    Hoshiko, S.6
  • 110
    • 0037166259 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein A1 interferes with the binding of the human T cell leukemia virus type 1 Rex regulatory protein to its response element
    • DOI 10.1074/jbc.M109087200
    • M.D. Dodon, S. Hamaia, J. Martin, and L. Gazzolo Heterogeneous nuclear ribonucleoprotein A1 interferes with the binding of the human T cell leukemia virus type 1 rex regulatory protein to its response element J. Biol. Chem. 277 2002 18744 18752 (Pubitemid 34952432)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.21 , pp. 18744-18752
    • Dodon, M.D.1    Hamaia, S.2    Martin, J.3    Gazzolo, L.4
  • 111
    • 68849124716 scopus 로고    scopus 로고
    • Lung cancer and inflammation: Interaction of chemokines and hnRNPs
    • J. Tauler, and J.L. Mulshine Lung cancer and inflammation: interaction of chemokines and hnRNPs Curr. Opin. Pharmacol. 9 2009 384 388
    • (2009) Curr. Opin. Pharmacol. , vol.9 , pp. 384-388
    • Tauler, J.1    Mulshine, J.L.2
  • 112
    • 0036070957 scopus 로고    scopus 로고
    • Inflammation modulates the interaction of heterogeneous nuclear ribonucleoprotein (hnRNP) I/polypyrimidine tract binding protein and hnRNP L with the 3′untranslated region of the murine inducible nitric-oxide synthase mRNA
    • DOI 10.1124/mol.62.2.423
    • M. Soderberg, F. Raffalli-Mathieu, and M.A. Lang Inflammation modulates the interaction of heterogeneous nuclear ribonucleoprotein (hnRNP) I/polypyrimidine tract binding protein and hnRNP L with the 3′untranslated region of the murine inducible nitric-oxide synthase mRNA Mol. Pharmacol. 62 2002 423 431 (Pubitemid 34804123)
    • (2002) Molecular Pharmacology , vol.62 , Issue.2 , pp. 423-431
    • Soderberg, M.1    Raffalli-Mathieu, F.2    Lang, M.A.3
  • 113
    • 34247253736 scopus 로고    scopus 로고
    • Regulation of the murine inducible nitric oxide synthase gene by dexamethasone involves a heterogeneous nuclear ribonucleoprotein I (hnRNPI) dependent pathway
    • DOI 10.1016/j.molimm.2007.01.029, PII S0161589007000491
    • M. Soderberg, F. Raffalli-Mathieu, and M.A. Lang Regulation of the murine inducible nitric oxide synthase gene by dexamethasone involves a heterogeneous nuclear ribonucleoprotein I (hnRNPI) dependent pathway Mol. Immunol. 44 2007 3204 3210 (Pubitemid 46610501)
    • (2007) Molecular Immunology , vol.44 , Issue.12 , pp. 3204-3210
    • Soderberg, M.1    Raffalli-Mathieu, F.2    Lang, M.A.3
  • 114
    • 3843068715 scopus 로고    scopus 로고
    • A transcriptional repressor of osteopontin expression in the 4T1 murine breast cancer cell line
    • DOI 10.1016/j.bbrc.2004.07.063, PII S0006291X0401561X
    • C. Gao, Z. Mi, H. Guo, J. Wei, P.Y. Wai, and P.C. Kuo A transcriptional repressor of osteopontin expression in the 4T1 murine breast cancer cell line Biochem. Biophys. Res. Commun. 321 2004 1010 1016 (Pubitemid 39044410)
    • (2004) Biochemical and Biophysical Research Communications , vol.321 , Issue.4 , pp. 1010-1016
    • Gao, C.1    Mi, Z.2    Guo, H.3    Wei, J.4    Wai, P.Y.5    Kuo, P.C.6
  • 115
    • 1642483507 scopus 로고    scopus 로고
    • S-Nitrosylation of Heterogeneous Nuclear Ribonucleoprotein A/B Regulates Osteopontin Transcription in Endotoxin-stimulated Murine Macrophages
    • DOI 10.1074/jbc.M313385200
    • C. Gao, H. Guo, J. Wei, Z. Mi, P. Wai, and P.C. Kuo S-nitrosylation of heterogeneous nuclear ribonucleoprotein A/B regulates osteopontin transcription in endotoxin-stimulated murine macrophages J. Biol. Chem. 279 2004 11236 11243 (Pubitemid 38401619)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.12 , pp. 11236-11243
    • Gao, C.1    Guo, H.2    Wei, J.3    Mi, Z.4    Wai, P.5    Kuo, P.C.6
  • 116
    • 21244472980 scopus 로고    scopus 로고
    • Transcriptional regulatory functions of heterogeneous nuclear ribonucleoprotein-U and -A/B in endotoxin-mediated macrophage expression of osteopontin
    • C. Gao, H. Guo, Z. Mi, P.Y. Wai, and P.C. Kuo Transcriptional regulatory functions of heterogeneous nuclear ribonucleoprotein-U and -A/B in endotoxin-mediated macrophage expression of osteopontin J. Immunol. 175 2005 523 530 (Pubitemid 40884358)
    • (2005) Journal of Immunology , vol.175 , Issue.1 , pp. 523-530
    • Gao, C.1    Guo, H.2    Mi, Z.3    Wai, P.Y.4    Kuo, P.C.5
  • 117
    • 67749117934 scopus 로고    scopus 로고
    • Signal integration by JNK and p38 MAPK pathways in cancer development
    • E.F. Wagner, and A.R. Nebreda Signal integration by JNK and p38 MAPK pathways in cancer development Nat. Rev. Cancer 9 2009 537 549
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 537-549
    • Wagner, E.F.1    Nebreda, A.R.2
  • 118
    • 54249119561 scopus 로고    scopus 로고
    • JNK signaling in apoptosis
    • D.N. Dhanasekaran, and E.P. Reddy JNK signaling in apoptosis Oncogene 27 2008 6245 6251
    • (2008) Oncogene , vol.27 , pp. 6245-6251
    • Dhanasekaran, D.N.1    Reddy, E.P.2
  • 119
    • 48749124859 scopus 로고    scopus 로고
    • Exogenous nitric oxide negatively regulates c-Jun N-terminal kinase activation via inhibiting endogenous NO-induced S-nitrosylation during cerebral ischemia and reperfusion in rat hippocampus
    • D.S. Pei, Y.J. Song, H.M. Yu, W.W. Hu, Y. Du, and G.Y. Zhang Exogenous nitric oxide negatively regulates c-Jun N-terminal kinase activation via inhibiting endogenous NO-induced S-nitrosylation during cerebral ischemia and reperfusion in rat hippocampus J. Neurochem. 106 2008 1952 1963
    • (2008) J. Neurochem. , vol.106 , pp. 1952-1963
    • Pei, D.S.1    Song, Y.J.2    Yu, H.M.3    Hu, W.W.4    Du, Y.5    Zhang, G.Y.6
  • 120
    • 33745149283 scopus 로고    scopus 로고
    • Neuronal nitric oxide synthase (nNOS) modulates the JNK1 activity through redox mechanism: A cGMP independent pathway
    • DOI 10.1016/j.bbrc.2006.05.122, PII S0006291X06011454
    • H.S. Park, S.H. Huh, M.S. Kim, D.Y. Kim, B.J. Gwag, S.G. Cho, and E.J. Choi Neuronal nitric oxide synthase (nNOS) modulates the JNK1 activity through redox mechanism: a cGMP independent pathway Biochem. Biophys. Res. Commun. 346 2006 408 414 (Pubitemid 43902702)
    • (2006) Biochemical and Biophysical Research Communications , vol.346 , Issue.2 , pp. 408-414
    • Park, H.-S.1    Huh, S.-H.2    Kim, M.-S.3    Kim, D.Y.4    Gwag, B.J.5    Cho, S.-G.6    Choi, E.-J.7
  • 121
    • 33750348549 scopus 로고    scopus 로고
    • Nitric oxide inhibits an interaction between JNK1 and c-Jun through nitrosylation
    • H.S. Park, J.S. Mo, and E.J. Choi Nitric oxide inhibits an interaction between JNK1 and c-Jun through nitrosylation Biochem. Biophys. Res. Commun. 351 2006 281 286
    • (2006) Biochem. Biophys. Res. Commun. , vol.351 , pp. 281-286
    • Park, H.S.1    Mo, J.S.2    Choi, E.J.3
  • 122
    • 0038511319 scopus 로고    scopus 로고
    • S-nitrosylation of thioredoxin mediates activation of apoptosis signal-regulating kinase 1
    • DOI 10.1016/S0003-9861(03)00199-1
    • V.V. Sumbayev S-nitrosylation of thioredoxin mediates activation of apoptosis signal-regulating kinase 1 Arch. Biochem. Biophys. 415 2003 133 136 (Pubitemid 36687926)
    • (2003) Archives of Biochemistry and Biophysics , vol.415 , Issue.1 , pp. 133-136
    • Sumbayev, V.V.1
  • 123
    • 1542320091 scopus 로고    scopus 로고
    • Inhibition of Apoptosis Signal-regulating Kinase 1 by Nitric Oxide through a Thiol Redox Mechanism
    • DOI 10.1074/jbc.M304183200
    • H.S. Park, J.W. Yu, J.H. Cho, M.S. Kim, S.H. Huh, K. Ryoo, and E.J. Choi Inhibition of apoptosis signal-regulating kinase 1 by nitric oxide through a thiol redox mechanism J. Biol. Chem. 279 2004 7584 7590 (Pubitemid 38294637)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.9 , pp. 7584-7590
    • Park, H.-S.1    Yu, J.-W.2    Cho, J.-H.3    Kim, M.-S.4    Huh, S.-H.5    Ryoo, K.6    Choi, E.-J.7
  • 126
    • 2442717744 scopus 로고    scopus 로고
    • NO stimulation of ATP-sensitive potassium channels: Involvement of Ras/mitogen-activated protein kinase pathway and contribution to neuroprotection
    • DOI 10.1073/pnas.0402496101
    • Y.F. Lin, K. Raab-Graham, Y.N. Jan, and L.Y. Jan NO stimulation of ATP-sensitive potassium channels: involvement of Ras/mitogen-activated protein kinase pathway and contribution to neuroprotection Proc. Natl Acad. Sci. U. S. A. 101 2004 7799 7804 (Pubitemid 38658108)
    • (2004) Proceedings of the National Academy of Sciences of the United States of America , vol.101 , Issue.20 , pp. 7799-7804
    • Lin, Y.-F.1    Raab-Graham, K.2    Jan, Y.N.3    Jan, L.Y.4
  • 127
    • 33845920075 scopus 로고    scopus 로고
    • Activation of Ras up-regulates pro-apoptotic BNIP3 in nitric oxide-induced cell death
    • DOI 10.1074/jbc.M605819200
    • H.J. An, O. Maeng, K.H. Kang, J.O. Lee, Y.S. Kim, S.G. Paik, and H. Lee Activation of Ras up-regulates pro-apoptotic BNIP3 in nitric oxide-induced cell death J. Biol. Chem. 281 2006 33939 33948 (Pubitemid 46036606)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.45 , pp. 33939-33948
    • An, H.-J.1    Maeng, O.2    Kang, K.-H.3    Lee, J.-O.4    Kim, Y.-S.5    Paik, S.-G.6    Lee, H.7
  • 128
    • 41649108639 scopus 로고    scopus 로고
    • Tumour maintenance is mediated by eNOS
    • DOI 10.1038/nature06778, PII NATURE06778
    • K.H. Lim, B.B. Ancrile, D.F. Kashatus, and C.M. Counter Tumour maintenance is mediated by eNOS Nature 452 2008 646 649 (Pubitemid 351483359)
    • (2008) Nature , vol.452 , Issue.7187 , pp. 646-649
    • Lim, K.-H.1    Ancrile, B.B.2    Kashatus, D.F.3    Counter, C.M.4
  • 130
    • 14844300857 scopus 로고    scopus 로고
    • S-nitrosylation-dependent inactivation of Akt/protein kinase B in insulin resistance
    • DOI 10.1074/jbc.M411871200
    • T. Yasukawa, E. Tokunaga, H. Ota, H. Sugita, J.A. Martyn, and M. Kaneki S-nitrosylation-dependent inactivation of Akt/protein kinase B in insulin resistance J. Biol. Chem. 280 2005 7511 7518 (Pubitemid 40349643)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.9 , pp. 7511-7518
    • Yasukawa, T.1    Tokunaga, E.2    Ota, H.3    Sugita, H.4    Martyn, J.A.J.5    Kaneki, M.6
  • 132
  • 133
    • 58649088011 scopus 로고    scopus 로고
    • S-Nitrosylation of the epidermal growth factor receptor: A regulatory mechanism of receptor tyrosine kinase activity
    • M. Murillo-Carretero, A. Torroglosa, C. Castro, A. Villalobo, and C. Estrada S-Nitrosylation of the epidermal growth factor receptor: a regulatory mechanism of receptor tyrosine kinase activity Free Radic. Biol. Med. 46 2009 471 479
    • (2009) Free Radic. Biol. Med. , vol.46 , pp. 471-479
    • Murillo-Carretero, M.1    Torroglosa, A.2    Castro, C.3    Villalobo, A.4    Estrada, C.5
  • 134
    • 0037443130 scopus 로고    scopus 로고
    • Regulation of protein tyrosine phosphatase 1B in intact cells by S-nitrosothiols
    • DOI 10.1016/S0003-9861(02)00696-3
    • S. Li, and A.R. Whorton Regulation of protein tyrosine phosphatase 1B in intact cells by S-nitrosothiols Arch. Biochem. Biophys. 410 2003 269 279 (Pubitemid 36259827)
    • (2003) Archives of Biochemistry and Biophysics , vol.410 , Issue.2 , pp. 269-279
    • Li, S.1    Richard Whorton, A.2
  • 136
    • 58049200135 scopus 로고    scopus 로고
    • Cysteine S-nitrosylation protects protein-tyrosine phosphatase 1B against oxidation-induced permanent inactivation
    • Y.Y. Chen, H.M. Chu, K.T. Pan, C.H. Teng, D.L. Wang, A.H. Wang, K.H. Khoo, and T.C. Meng Cysteine S-nitrosylation protects protein-tyrosine phosphatase 1B against oxidation-induced permanent inactivation J. Biol. Chem. 283 2008 35265 35272
    • (2008) J. Biol. Chem. , vol.283 , pp. 35265-35272
    • Chen, Y.Y.1    Chu, H.M.2    Pan, K.T.3    Teng, C.H.4    Wang, D.L.5    Wang, A.H.6    Khoo, K.H.7    Meng, T.C.8
  • 137
    • 33947250704 scopus 로고    scopus 로고
    • Phosphorylation of the survival kinase Akt by superoxide is dependent on an ascorbate-reversible oxidation of PTEN
    • DOI 10.1016/j.freeradbiomed.2007.01.013, PII S0891584907000408
    • S. Lim, and M.V. Clement Phosphorylation of the survival kinase Akt by superoxide is dependent on an ascorbate-reversible oxidation of PTEN Free Radic. Biol. Med. 42 2007 1178 1192 (Pubitemid 46428511)
    • (2007) Free Radical Biology and Medicine , vol.42 , Issue.8 , pp. 1178-1192
    • Lim, S.1    Clement, M.-V.2
  • 138
    • 67349138163 scopus 로고    scopus 로고
    • S-nitrosylation of PTEN Invovled in ischemic brain injury in rat hippocampal CA1 region
    • D.S. Pei, Y.F. Sun, and Y.J. Song S-nitrosylation of PTEN Invovled in ischemic brain injury in rat hippocampal CA1 region Neurochem. Res. 34 2009 1507 1512
    • (2009) Neurochem. Res. , vol.34 , pp. 1507-1512
    • Pei, D.S.1    Sun, Y.F.2    Song, Y.J.3
  • 140
    • 0026453106 scopus 로고
    • Nitric oxide-induced S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase inhibits enzymatic activity and increases endogenous ADP-ribosylation
    • L. Molina y Vedia, B. McDonald, B. Reep, B. Brune, M. Di Silvio, T.R. Billiar, and E.G. Lapetina Nitric oxide-induced S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase inhibits enzymatic activity and increases endogenous ADP-ribosylation J. Biol. Chem. 267 1992 24929 24932
    • (1992) J. Biol. Chem. , vol.267 , pp. 24929-24932
    • Molina Vedia, Y.L.1    McDonald, B.2    Reep, B.3    Brune, B.4    Di Silvio, M.5    Billiar, T.R.6    Lapetina, E.G.7
  • 144
    • 3142705856 scopus 로고    scopus 로고
    • Targeting of endothelial nitric-oxide synthase to the cytoplasmic face of the Golgi complex or plasma membrane regulates Akt- versus calcium-dependent mechanisms for nitric oxide release
    • DOI 10.1074/jbc.M402155200
    • D. Fulton, R. Babbitt, S. Zoellner, J. Fontana, L. Acevedo, T.J. McCabe, Y. Iwakiri, and W.C. Sessa Targeting of endothelial nitric-oxide synthase to the cytoplasmic face of the Golgi complex or plasma membrane regulates Akt- versus calcium-dependent mechanisms for nitric oxide release J. Biol. Chem. 279 2004 30349 30357 (Pubitemid 38937962)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.29 , pp. 30349-30357
    • Fulton, D.1    Babbitt, R.2    Zoellner, S.3    Fontana, J.4    Acevedo, L.5    McCabe, T.J.6    Iwakiri, Y.7    Sessa, W.C.8
  • 146
    • 0037070634 scopus 로고    scopus 로고
    • Evidence for a functional nitric oxide synthase system in brown adipocyte nucleus
    • DOI 10.1016/S0014-5793(02)02245-7, PII S0014579302022457
    • A. Giordano, C. Tonello, A. Bulbarelli, V. Cozzi, S. Cinti, M.O. Carruba, and E. Nisoli Evidence for a functional nitric oxide synthase system in brown adipocyte nucleus FEBS Lett. 514 2002 135 140 (Pubitemid 34273927)
    • (2002) FEBS Letters , vol.514 , Issue.2-3 , pp. 135-140
    • Giordano, A.1    Tonello, C.2    Bulbarelli, A.3    Cozzi, V.4    Cinti, S.5    Carruba, M.O.6    Nisoli, E.7
  • 147
  • 148
    • 79952564943 scopus 로고    scopus 로고
    • CAT-1-mediated arginine uptake and regulation of nitric oxide synthases for the survival of human breast cancer cell lines
    • S.A. Abdelmagid, J.A. Rickard, W.J. McDonald, L.N. Thomas, and C.K. Too CAT-1-mediated arginine uptake and regulation of nitric oxide synthases for the survival of human breast cancer cell lines J. Cell. Biochem. 112 2011 1084 1092
    • (2011) J. Cell. Biochem. , vol.112 , pp. 1084-1092
    • Abdelmagid, S.A.1    Rickard, J.A.2    McDonald, W.J.3    Thomas, L.N.4    Too, C.K.5
  • 150
    • 15444369648 scopus 로고    scopus 로고
    • Resistance to endotoxic shock in endothelial nitric-oxide synthase (eNOS) knock-out mice: A pro-inflammatory role for eNOS-derived no in vivo
    • DOI 10.1074/jbc.M411991200
    • L. Connelly, M. Madhani, and A.J. Hobbs Resistance to endotoxic shock in endothelial nitric-oxide synthase (eNOS) knock-out mice: a pro-inflammatory role for eNOS-derived no in vivo J. Biol. Chem. 280 2005 10040 10046 (Pubitemid 40395855)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.11 , pp. 10040-10046
    • Connelly, L.1    Madhani, M.2    Hobbs, A.J.3
  • 152
    • 0036067845 scopus 로고    scopus 로고
    • Histone deacetylases augment cytokine induction of the iNOS gene
    • DOI 10.1097/01.ASN.0000024253.59665.F1
    • Z. Yu, W. Zhang, and B.C. Kone Histone deacetylases augment cytokine induction of the iNOS gene J. Am. Soc. Nephrol. 13 2002 2009 2017 (Pubitemid 34790776)
    • (2002) Journal of the American Society of Nephrology , vol.13 , Issue.8 , pp. 2009-2017
    • Yu, Z.1    Zhang, W.2    Kone, B.C.3
  • 153
    • 0036842460 scopus 로고    scopus 로고
    • Inhibitors of histone deacetylation downregulate the expression of endothelial nitric oxide synthase and compromise endothelial cell function in vasorelaxation and angiogenesis
    • DOI 10.1161/01.RES.0000037983.07158.B1
    • L. Rossig, H. Li, B. Fisslthaler, C. Urbich, I. Fleming, U. Forstermann, A.M. Zeiher, and S. Dimmeler Inhibitors of histone deacetylation downregulate the expression of endothelial nitric oxide synthase and compromise endothelial cell function in vasorelaxation and angiogenesis Circ. Res. 91 2002 837 844 (Pubitemid 35285082)
    • (2002) Circulation Research , vol.91 , Issue.9 , pp. 837-844
    • Rossig, L.1    Li, H.2    Fisslthaler, B.3    Urbich, C.4    Fleming, I.5    Forstermann, U.6    Zeiher, A.M.7    Dimmeler, S.8
  • 154
    • 34248205235 scopus 로고    scopus 로고
    • Regulation of neuronal nitric oxide synthase exon 1f gene expression by nuclear factor-κB acetylation in human neuroblastoma cells
    • DOI 10.1111/j.1471-4159.2006.04407.x
    • Y. Li, Y. Zhao, G. Li, J. Wang, T. Li, W. Li, and J. Lu Regulation of neuronal nitric oxide synthase exon 1f gene expression by nuclear factor-kappaB acetylation in human neuroblastoma cells J. Neurochem. 101 2007 1194 1204 (Pubitemid 46718805)
    • (2007) Journal of Neurochemistry , vol.101 , Issue.5 , pp. 1194-1204
    • Li, Y.1    Zhao, Y.2    Li, G.3    Wang, J.4    Li, T.5    Li, W.6    Lu, J.7
  • 155
    • 28844493947 scopus 로고    scopus 로고
    • Acetylation of poly(ADP-ribose) polymerase-1 by p300/CREB-binding protein regulates coactivation of NF-κB-dependent transcription
    • DOI 10.1074/jbc.M507553200
    • P.O. Hassa, S.S. Haenni, C. Buerki, N.I. Meier, W.S. Lane, H. Owen, M. Gersbach, R. Imhof, and M.O. Hottiger Acetylation of poly(ADP-ribose) polymerase-1 by p300/CREB-binding protein regulates coactivation of NF-kappaB-dependent transcription J. Biol. Chem. 280 2005 40450 40464 (Pubitemid 41780532)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.49 , pp. 40450-40464
    • Hassa, P.O.1    Haenni, S.S.2    Buerki, C.3    Meier, N.I.4    Lane, W.S.5    Owen, H.6    Gersbach, M.7    Imhof, R.8    Hottiger, M.O.9
  • 156
    • 52149108919 scopus 로고    scopus 로고
    • S-Nitrosylation of histone deacetylase 2 induces chromatin remodelling in neurons
    • A. Nott, P.M. Watson, J.D. Robinson, L. Crepaldi, and A. Riccio S-Nitrosylation of histone deacetylase 2 induces chromatin remodelling in neurons Nature 455 2008 411 415
    • (2008) Nature , vol.455 , pp. 411-415
    • Nott, A.1    Watson, P.M.2    Robinson, J.D.3    Crepaldi, L.4    Riccio, A.5
  • 157
    • 60949095770 scopus 로고    scopus 로고
    • Nitric oxide and histone deacetylases: A new relationship between old molecules
    • P.M. Watson, and A. Riccio Nitric oxide and histone deacetylases: a new relationship between old molecules Commun. Integr. Biol. 2 2009 11 13
    • (2009) Commun. Integr. Biol. , vol.2 , pp. 11-13
    • Watson, P.M.1    Riccio, A.2
  • 159
    • 77954900569 scopus 로고    scopus 로고
    • Regulation of NF-kappaB circuitry by a component of the nucleosome remodeling and deacetylase complex controls inflammatory response homeostasis
    • S.B. Pakala, T.M. Bui-Nguyen, S.D. Reddy, D.Q. Li, S. Peng, S.K. Rayala, R.R. Behringer, and R. Kumar Regulation of NF-kappaB circuitry by a component of the nucleosome remodeling and deacetylase complex controls inflammatory response homeostasis J. Biol. Chem. 285 2010 23590 23597
    • (2010) J. Biol. Chem. , vol.285 , pp. 23590-23597
    • Pakala, S.B.1    Bui-Nguyen, T.M.2    Reddy, S.D.3    Li, D.Q.4    Peng, S.5    Rayala, S.K.6    Behringer, R.R.7    Kumar, R.8
  • 162
    • 9644290748 scopus 로고    scopus 로고
    • In situ detection and visualization of S-nitrosylated proteins following chemical derivatization: Identification of Ran GTPase as a target for S-nitrosylation
    • DOI 10.1016/j.niox.2004.06.002, PII S1089860304001272
    • K. Ckless, N.L. Reynaert, D.J. Taatjes, K.M. Lounsbury, A. van der Vliet, and Y. Janssen-Heininger In situ detection and visualization of S-nitrosylated proteins following chemical derivatization: identification of Ran GTPase as a target for S-nitrosylation Nitric Oxide 11 2004 216 227 (Pubitemid 39573524)
    • (2004) Nitric Oxide - Biology and Chemistry , vol.11 , Issue.3 , pp. 216-227
    • Ckless, K.1    Reynaert, N.L.2    Taatjes, D.J.3    Lounsbury, K.M.4    Van Der Vliet, A.5    Janssen-Heininger, Y.6
  • 163
    • 77949400181 scopus 로고    scopus 로고
    • Comprehensive identification and modified-site mapping of S-nitrosylated targets in prostate epithelial cells
    • Y.W. Lam, Y. Yuan, J. Isaac, C.V. Babu, J. Meller, and S.M. Ho Comprehensive identification and modified-site mapping of S-nitrosylated targets in prostate epithelial cells PLoS One 5 2010 e9075
    • (2010) PLoS One , vol.5 , pp. 9075
    • Lam, Y.W.1    Yuan, Y.2    Isaac, J.3    Babu, C.V.4    Meller, J.5    Ho, S.M.6
  • 164
    • 36048960679 scopus 로고    scopus 로고
    • Nuclear redox-signaling is essential for apoptosis inhibition in endothelial cells-important role for nuclear thioredoxin-1
    • DOI 10.1161/ATVBAHA.107.149419, PII 0004360520071100000009
    • P. Schroeder, R. Popp, B. Wiegand, J. Altschmied, and J. Haendeler Nuclear redox-signaling is essential for apoptosis inhibition in endothelial cells - important role for nuclear thioredoxin-1 Arterioscler. Thromb. Vasc. Biol. 27 2007 2325 2331 (Pubitemid 350203946)
    • (2007) Arteriosclerosis, Thrombosis, and Vascular Biology , vol.27 , Issue.11 , pp. 2325-2331
    • Schroeder, P.1    Popp, R.2    Wiegand, B.3    Altschmied, J.4    Haendeler, J.5
  • 165
    • 34250357205 scopus 로고    scopus 로고
    • Nitric oxide controls nuclear export of APE1/Ref-1 through S-nitrosation of Cysteines 93 and 310
    • DOI 10.1093/nar/gkl1163
    • J. Qu, G.H. Liu, B. Huang, and C. Chen Nitric oxide controls nuclear export of APE1/Ref-1 through S-nitrosation of cysteines 93 and 310 Nucleic Acids Res. 35 2007 2522 2532 (Pubitemid 47078742)
    • (2007) Nucleic Acids Research , vol.35 , Issue.8 , pp. 2522-2532
    • Qu, J.1    Liu, G.-H.2    Huang, B.3    Chen, C.4
  • 166
    • 48349107170 scopus 로고    scopus 로고
    • A new APE1/Ref-1-dependent pathway leading to reduction of NF-kappaB and AP-1, and activation of their DNA-binding activity
    • K. Ando, S. Hirao, Y. Kabe, Y. Ogura, I. Sato, Y. Yamaguchi, T. Wada, and H. Handa A new APE1/Ref-1-dependent pathway leading to reduction of NF-kappaB and AP-1, and activation of their DNA-binding activity Nucleic Acids Res. 36 2008 4327 4336
    • (2008) Nucleic Acids Res. , vol.36 , pp. 4327-4336
    • Ando, K.1    Hirao, S.2    Kabe, Y.3    Ogura, Y.4    Sato, I.5    Yamaguchi, Y.6    Wada, T.7    Handa, H.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.