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Volumn 6, Issue 12, 2011, Pages

The pathogenic potential of campylobacter concisus strains associated with chronic intestinal diseases

Author keywords

[No Author keywords available]

Indexed keywords

GENTAMICIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 12; CYTOKINE; MUCIN; PROTEOME;

EID: 83355170686     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0029045     Document Type: Article
Times cited : (60)

References (58)
  • 1
    • 34047139587 scopus 로고    scopus 로고
    • Inflammatory bowel disease genetics: Nod2
    • Cho JH, Abraham C, (2007) Inflammatory bowel disease genetics: Nod2. Annu Rev Med 58: 401-416.
    • (2007) Annu Rev Med , vol.58 , pp. 401-416
    • Cho, J.H.1    Abraham, C.2
  • 2
    • 0028199222 scopus 로고
    • Observer variation and discriminatory value of biopsy features in inflammatory bowel disease
    • Theodossi A, Spiegelhalter DJ, Jass J, Firth J, Dixon M, et al. (1994) Observer variation and discriminatory value of biopsy features in inflammatory bowel disease. Gut 35: 961-968.
    • (1994) Gut , vol.35 , pp. 961-968
    • Theodossi, A.1    Spiegelhalter, D.J.2    Jass, J.3    Firth, J.4    Dixon, M.5
  • 3
    • 33745775434 scopus 로고    scopus 로고
    • Mechanisms of disease: pathogenesis of Crohn's disease and ulcerative colitis
    • Sartor RB, (2006) Mechanisms of disease: pathogenesis of Crohn's disease and ulcerative colitis. Nat Clin Pract Gastroenterol Hepatol 3: 390-407.
    • (2006) Nat Clin Pract Gastroenterol Hepatol , vol.3 , pp. 390-407
    • Sartor, R.B.1
  • 4
    • 0033986473 scopus 로고    scopus 로고
    • Prevalence of Campylobacter, Arcobacter, Helicobacter, and Sutterella spp. in human fecal samples as estimated by a reevaluation of isolation methods for Campylobacters
    • Engberg J, On SL, Harrington CS, Gerner-Smidt P, (2000) Prevalence of Campylobacter, Arcobacter, Helicobacter, and Sutterella spp. in human fecal samples as estimated by a reevaluation of isolation methods for Campylobacters. J Clin Microbiol 38: 286-291.
    • (2000) J Clin Microbiol , vol.38 , pp. 286-291
    • Engberg, J.1    On, S.L.2    Harrington, C.S.3    Gerner-Smidt, P.4
  • 5
    • 0030036542 scopus 로고    scopus 로고
    • Identification methods for campylobacters, helicobacters, and related organisms
    • On SL, (1996) Identification methods for campylobacters, helicobacters, and related organisms. Clin Microbiol Rev 9: 405-422.
    • (1996) Clin Microbiol Rev , vol.9 , pp. 405-422
    • On, S.L.1
  • 6
    • 60849125086 scopus 로고    scopus 로고
    • Detection and isolation of Campylobacter species other than C. jejuni from children with Crohn's disease
    • Zhang L, Man SM, Day AS, Leach ST, Lemberg DA, et al. (2009) Detection and isolation of Campylobacter species other than C. jejuni from children with Crohn's disease. J Clin Microbiol 47: 453-455.
    • (2009) J Clin Microbiol , vol.47 , pp. 453-455
    • Zhang, L.1    Man, S.M.2    Day, A.S.3    Leach, S.T.4    Lemberg, D.A.5
  • 7
    • 77952689163 scopus 로고    scopus 로고
    • Campylobacter concisus and other Campylobacter species in children with newly diagnosed Crohn's disease
    • Man SM, Zhang L, Day AS, Leach ST, Lemberg DA, et al. (2010) Campylobacter concisus and other Campylobacter species in children with newly diagnosed Crohn's disease. Inflamm Bowel Dis 16: 1008-1016.
    • (2010) Inflamm Bowel Dis , vol.16 , pp. 1008-1016
    • Man, S.M.1    Zhang, L.2    Day, A.S.3    Leach, S.T.4    Lemberg, D.A.5
  • 8
    • 78650386765 scopus 로고    scopus 로고
    • Host attachment, invasion, and stimulation of proinflammatory cytokines by Campylobacter concisus and other non-Campylobacter jejuni Campylobacter species
    • Man SM, Kaakoush NO, Leach ST, Nahidi L, Lu HK, et al. (2010) Host attachment, invasion, and stimulation of proinflammatory cytokines by Campylobacter concisus and other non-Campylobacter jejuni Campylobacter species. J Infect Dis 202: 1855-1865.
    • (2010) J Infect Dis , vol.202 , pp. 1855-1865
    • Man, S.M.1    Kaakoush, N.O.2    Leach, S.T.3    Nahidi, L.4    Lu, H.K.5
  • 10
    • 0035985335 scopus 로고    scopus 로고
    • Prevalence of Campylobacter concisus in diarrhoea of immunocompromised patients
    • Aabenhus R, Permin H, On SL, Andersen LP, (2002) Prevalence of Campylobacter concisus in diarrhoea of immunocompromised patients. Scand J Infect Dis 34: 248-252.
    • (2002) Scand J Infect Dis , vol.34 , pp. 248-252
    • Aabenhus, R.1    Permin, H.2    On, S.L.3    Andersen, L.P.4
  • 11
    • 56349166516 scopus 로고    scopus 로고
    • Liquid culture medium for the rapid cultivation of Helicobacter pylori from biopsy specimens
    • Sainsus N, Cattori V, Lepadatu C, Hofmann-Lehmann R, (2008) Liquid culture medium for the rapid cultivation of Helicobacter pylori from biopsy specimens. Eur J Clin Microbiol Infect Dis 27: 1209-1217.
    • (2008) Eur J Clin Microbiol Infect Dis , vol.27 , pp. 1209-1217
    • Sainsus, N.1    Cattori, V.2    Lepadatu, C.3    Hofmann-Lehmann, R.4
  • 12
    • 0033914773 scopus 로고    scopus 로고
    • Efficient isolation of campylobacteria from stools
    • Lastovica AJ, le Roux E, (2000) Efficient isolation of campylobacteria from stools. J Clin Microbiol 38: 2798-2799.
    • (2000) J Clin Microbiol , vol.38 , pp. 2798-2799
    • Lastovica, A.J.1    le Roux, E.2
  • 13
    • 78349275669 scopus 로고    scopus 로고
    • Detection of Helicobacteraceae in intestinal biopsies of children with Crohn's disease
    • Kaakoush NO, Holmes J, Octavia S, Man SM, Zhang L, et al. (2010) Detection of Helicobacteraceae in intestinal biopsies of children with Crohn's disease. Helicobacter 15: 549-557.
    • (2010) Helicobacter , vol.15 , pp. 549-557
    • Kaakoush, N.O.1    Holmes, J.2    Octavia, S.3    Man, S.M.4    Zhang, L.5
  • 14
    • 0037335681 scopus 로고    scopus 로고
    • Comparison of broth microdilution, E Test, and agar dilution methods for antibiotic susceptibility testing of Campylobacter jejuni and Campylobacter coli
    • Luber P, Bartelt E, Genschow E, Wagner J, Hahn H, (2003) Comparison of broth microdilution, E Test, and agar dilution methods for antibiotic susceptibility testing of Campylobacter jejuni and Campylobacter coli. J Clin Microbiol 41: 1062-1068.
    • (2003) J Clin Microbiol , vol.41 , pp. 1062-1068
    • Luber, P.1    Bartelt, E.2    Genschow, E.3    Wagner, J.4    Hahn, H.5
  • 15
    • 33645834311 scopus 로고    scopus 로고
    • Antimicrobial susceptibility of clinical isolates of non-jejuni/coli campylobacters and arcobacters from Belgium
    • Vandenberg O, Houf K, Douat N, Vlaes L, Retore P, et al. (2006) Antimicrobial susceptibility of clinical isolates of non-jejuni/coli campylobacters and arcobacters from Belgium. J Antimicrob Chemother 57: 908-913.
    • (2006) J Antimicrob Chemother , vol.57 , pp. 908-913
    • Vandenberg, O.1    Houf, K.2    Douat, N.3    Vlaes, L.4    Retore, P.5
  • 16
  • 18
    • 0027287348 scopus 로고
    • Early colonic damage and invasion of Campylobacter jejuni in experimentally challenged infant Macaca mulatta
    • Russell RG, O'Donnoghue M, Blake DC Jr, Zulty J, DeTolla LJ, (1993) Early colonic damage and invasion of Campylobacter jejuni in experimentally challenged infant Macaca mulatta. J Infect Dis 168: 210-215.
    • (1993) J Infect Dis , vol.168 , pp. 210-215
    • Russell, R.G.1    O'Donnoghue, M.2    Blake Jr., D.C.3    Zulty, J.4    DeTolla, L.J.5
  • 19
    • 0036042549 scopus 로고    scopus 로고
    • Molecular microbiology and pathogenesis of Helicobacter and Campylobacter updated: a meeting report of the 11th conference on Campylobacter, Helicobacter and related organisms
    • Bereswill S, Kist M, (2002) Molecular microbiology and pathogenesis of Helicobacter and Campylobacter updated: a meeting report of the 11th conference on Campylobacter, Helicobacter and related organisms. Mol Microbiol 45: 255-262.
    • (2002) Mol Microbiol , vol.45 , pp. 255-262
    • Bereswill, S.1    Kist, M.2
  • 20
    • 0030635485 scopus 로고    scopus 로고
    • Pathogenesis of enteric infection by Campylobacter
    • Ketley JM, (1997) Pathogenesis of enteric infection by Campylobacter. Microbiology 143: 5-21.
    • (1997) Microbiology , vol.143 , pp. 5-21
    • Ketley, J.M.1
  • 21
    • 0017064628 scopus 로고
    • Human colonic adenocarcinoma cells. I. Establishment and description of a new line
    • Tom BH, Rutzky LP, Jakstys MM, Oyasu R, Kaye CI, et al. (1976) Human colonic adenocarcinoma cells. I. Establishment and description of a new line. In Vitro 12: 180-191.
    • (1976) In Vitro , vol.12 , pp. 180-191
    • Tom, B.H.1    Rutzky, L.P.2    Jakstys, M.M.3    Oyasu, R.4    Kaye, C.I.5
  • 22
    • 23744505064 scopus 로고    scopus 로고
    • Identification of a fibronectin-binding domain within the Campylobacter jejuni CadF protein
    • Konkel ME, Christensen JE, Keech AM, Monteville MR, Klena JD, et al. (2005) Identification of a fibronectin-binding domain within the Campylobacter jejuni CadF protein. Mol Microbiol 57: 1022-1035.
    • (2005) Mol Microbiol , vol.57 , pp. 1022-1035
    • Konkel, M.E.1    Christensen, J.E.2    Keech, A.M.3    Monteville, M.R.4    Klena, J.D.5
  • 23
    • 0030798150 scopus 로고    scopus 로고
    • Identification and molecular cloning of a gene encoding a fibronectin-binding protein (CadF) from Campylobacter jejuni
    • Konkel ME, Garvis SG, Tipton SL, Anderson DE Jr, Cieplak W Jr, (1997) Identification and molecular cloning of a gene encoding a fibronectin-binding protein (CadF) from Campylobacter jejuni. Mol Microbiol 24: 953-963.
    • (1997) Mol Microbiol , vol.24 , pp. 953-963
    • Konkel, M.E.1    Garvis, S.G.2    Tipton, S.L.3    Anderson Jr., D.E.4    Cieplak Jr., W.5
  • 24
    • 34548443431 scopus 로고    scopus 로고
    • Role of the small Rho GTPases Rac1 and Cdc42 in host cell invasion of Campylobacter jejuni
    • Krause-Gruszczynska M, Rohde M, Hartig R, Genth H, Schmidt G, et al. (2007) Role of the small Rho GTPases Rac1 and Cdc42 in host cell invasion of Campylobacter jejuni. Cell Microbiol 9: 2431-2444.
    • (2007) Cell Microbiol , vol.9 , pp. 2431-2444
    • Krause-Gruszczynska, M.1    Rohde, M.2    Hartig, R.3    Genth, H.4    Schmidt, G.5
  • 25
    • 56349130548 scopus 로고    scopus 로고
    • The biofilm forming potential of bacterial species in the genus Campylobacter
    • Gunther NWt, Chen CY, (2009) The biofilm forming potential of bacterial species in the genus Campylobacter. Food Microbiol 26: 44-51.
    • (2009) Food Microbiol , vol.26 , pp. 44-51
    • Gunther, N.W.1    Chen, C.Y.2
  • 26
    • 79960911372 scopus 로고    scopus 로고
    • Sequencing and validation of the genome of a Campylobacter concisus reveals extensive intra-species diversity
    • Deshpande N, Kaakoush NO, Mitchell H, Janitz K, Raftery MJ, et al. (2011) Sequencing and validation of the genome of a Campylobacter concisus reveals extensive intra-species diversity. PLoS One 6: e22170.
    • (2011) PLoS One , vol.6
    • Deshpande, N.1    Kaakoush, N.O.2    Mitchell, H.3    Janitz, K.4    Raftery, M.J.5
  • 27
    • 0031725252 scopus 로고    scopus 로고
    • A family of stability determinants in pathogenic bacteria
    • Hayes F, (1998) A family of stability determinants in pathogenic bacteria. J Bacteriol 180: 6415-6418.
    • (1998) J Bacteriol , vol.180 , pp. 6415-6418
    • Hayes, F.1
  • 28
    • 0033777863 scopus 로고    scopus 로고
    • Cyclin' on the viral path to destruction
    • Hardwick JM, (2000) Cyclin' on the viral path to destruction. Nat Cell Biol 2: E203-204.
    • (2000) Nat Cell Biol , vol.2
    • Hardwick, J.M.1
  • 29
    • 0028805908 scopus 로고
    • Role of the Plasmodium falciparum mature-parasite-infected erythrocyte surface antigen (MESA/PfEMP-2) in malarial infection of erythrocytes
    • Magowan C, Coppel RL, Lau AO, Moronne MM, Tchernia G, et al. (1995) Role of the Plasmodium falciparum mature-parasite-infected erythrocyte surface antigen (MESA/PfEMP-2) in malarial infection of erythrocytes. Blood 86: 3196-3204.
    • (1995) Blood , vol.86 , pp. 3196-3204
    • Magowan, C.1    Coppel, R.L.2    Lau, A.O.3    Moronne, M.M.4    Tchernia, G.5
  • 30
    • 0041940227 scopus 로고    scopus 로고
    • Mature parasite-infected erythrocyte surface antigen (MESA) of Plasmodium falciparum binds to the 30-kDa domain of protein 4.1 in malaria-infected red blood cells
    • Waller KL, Nunomura W, An X, Cooke BM, Mohandas N, et al. (2003) Mature parasite-infected erythrocyte surface antigen (MESA) of Plasmodium falciparum binds to the 30-kDa domain of protein 4.1 in malaria-infected red blood cells. Blood 102: 1911-1914.
    • (2003) Blood , vol.102 , pp. 1911-1914
    • Waller, K.L.1    Nunomura, W.2    An, X.3    Cooke, B.M.4    Mohandas, N.5
  • 31
    • 73949130326 scopus 로고    scopus 로고
    • Erythrocyte scaffolding protein p55/MPP1 functions as an essential regulator of neutrophil polarity
    • Quinn BJ, Welch EJ, Kim AC, Lokuta MA, Huttenlocher A, et al. (2009) Erythrocyte scaffolding protein p55/MPP1 functions as an essential regulator of neutrophil polarity. Proc Natl Acad Sci U S A 106: 19842-19847.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 19842-19847
    • Quinn, B.J.1    Welch, E.J.2    Kim, A.C.3    Lokuta, M.A.4    Huttenlocher, A.5
  • 32
    • 0026585611 scopus 로고
    • Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: the 'phosphocreatine circuit' for cellular energy homeostasis
    • Wallimann T, Wyss M, Brdiczka D, Nicolay K, Eppenberger HM, (1992) Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: the 'phosphocreatine circuit' for cellular energy homeostasis. Biochem J 281 (Pt 1): 21-40.
    • (1992) Biochem J , vol.281 , Issue.Pt 1 , pp. 21-40
    • Wallimann, T.1    Wyss, M.2    Brdiczka, D.3    Nicolay, K.4    Eppenberger, H.M.5
  • 33
    • 61449163214 scopus 로고    scopus 로고
    • Corruption of innate immunity by bacterial proteases
    • Potempa J, Pike RN, (2009) Corruption of innate immunity by bacterial proteases. J Innate Immun 1: 70-87.
    • (2009) J Innate Immun , vol.1 , pp. 70-87
    • Potempa, J.1    Pike, R.N.2
  • 34
    • 0031734967 scopus 로고    scopus 로고
    • Heat shock protein 27 kDa expression and phosphorylation regulates endothelial cell migration
    • Piotrowicz RS, Hickey E, Levin EG, (1998) Heat shock protein 27 kDa expression and phosphorylation regulates endothelial cell migration. FASEB J 12: 1481-1490.
    • (1998) FASEB J , vol.12 , pp. 1481-1490
    • Piotrowicz, R.S.1    Hickey, E.2    Levin, E.G.3
  • 35
    • 0030797467 scopus 로고    scopus 로고
    • Cofilin promotes rapid actin filament turnover in vivo
    • Lappalainen P, Drubin DG, (1997) Cofilin promotes rapid actin filament turnover in vivo. Nature 388: 78-82.
    • (1997) Nature , vol.388 , pp. 78-82
    • Lappalainen, P.1    Drubin, D.G.2
  • 36
    • 0030783012 scopus 로고    scopus 로고
    • Stathmin: a tubulin-sequestering protein which forms a ternary T2S complex with two tubulin molecules
    • Jourdain L, Curmi P, Sobel A, Pantaloni D, Carlier MF, (1997) Stathmin: a tubulin-sequestering protein which forms a ternary T2S complex with two tubulin molecules. Biochemistry 36: 10817-10821.
    • (1997) Biochemistry , vol.36 , pp. 10817-10821
    • Jourdain, L.1    Curmi, P.2    Sobel, A.3    Pantaloni, D.4    Carlier, M.F.5
  • 37
    • 0029847068 scopus 로고    scopus 로고
    • Breaking the connection: displacement of the desmosomal plaque protein desmoplakin from cell-cell interfaces disrupts anchorage of intermediate filament bundles and alters intercellular junction assembly
    • Bornslaeger EA, Corcoran CM, Stappenbeck TS, Green KJ, (1996) Breaking the connection: displacement of the desmosomal plaque protein desmoplakin from cell-cell interfaces disrupts anchorage of intermediate filament bundles and alters intercellular junction assembly. J Cell Biol 134: 985-1001.
    • (1996) J Cell Biol , vol.134 , pp. 985-1001
    • Bornslaeger, E.A.1    Corcoran, C.M.2    Stappenbeck, T.S.3    Green, K.J.4
  • 38
    • 0033674358 scopus 로고    scopus 로고
    • IL-18 and IL-12 induce intestinal inflammation and fatty liver in mice in an IFN-γ dependent manner
    • Chikano S, Sawada K, Shimoyama T, Kashiwamura SI, Sugihara A, et al. (2000) IL-18 and IL-12 induce intestinal inflammation and fatty liver in mice in an IFN-γ dependent manner. Gut 47: 779-786.
    • (2000) Gut , vol.47 , pp. 779-786
    • Chikano, S.1    Sawada, K.2    Shimoyama, T.3    Kashiwamura, S.I.4    Sugihara, A.5
  • 39
    • 0028234770 scopus 로고
    • Distinct 19 S and 20 S subcomplexes of the 26 S proteasome and their distribution in the nucleus and the cytoplasm
    • Peters JM, Franke WW, Kleinschmidt JA, (1994) Distinct 19 S and 20 S subcomplexes of the 26 S proteasome and their distribution in the nucleus and the cytoplasm. J Biol Chem 269: 7709-7718.
    • (1994) J Biol Chem , vol.269 , pp. 7709-7718
    • Peters, J.M.1    Franke, W.W.2    Kleinschmidt, J.A.3
  • 40
    • 77955602593 scopus 로고    scopus 로고
    • The Immunoproteasome Cleans up after Inflammation
    • van Deventer S, Neefjes J, (2010) The Immunoproteasome Cleans up after Inflammation. Cell 142: 517-518.
    • (2010) Cell , vol.142 , pp. 517-518
    • van Deventer, S.1    Neefjes, J.2
  • 41
    • 0034084163 scopus 로고    scopus 로고
    • Phosphorylation meets ubiquitination: the control of NF-κB activity
    • Karin M, Ben-Neriah Y, (2000) Phosphorylation meets ubiquitination: the control of NF-κB activity. Annu Rev Immunol 18: 621-663.
    • (2000) Annu Rev Immunol , vol.18 , pp. 621-663
    • Karin, M.1    Ben-Neriah, Y.2
  • 42
    • 0035379555 scopus 로고    scopus 로고
    • Akt stimulates the transactivation potential of the RelA/p65 Subunit of NF-κB through utilization of the IκB kinase and activation of the mitogen-activated protein kinase p38
    • Madrid LV, Mayo MW, Reuther JY, Baldwin AS Jr, (2001) Akt stimulates the transactivation potential of the RelA/p65 Subunit of NF-κB through utilization of the IκB kinase and activation of the mitogen-activated protein kinase p38. J Biol Chem 276: 18934-18940.
    • (2001) J Biol Chem , vol.276 , pp. 18934-18940
    • Madrid, L.V.1    Mayo, M.W.2    Reuther, J.Y.3    Baldwin Jr., A.S.4
  • 43
    • 0037039665 scopus 로고    scopus 로고
    • Distinct roles of the IκB kinase alpha and beta subunits in liberating nuclear factor kappa B (NF-κB) from IκB and in phosphorylating the p65 subunit of NF-κB
    • Sizemore N, Lerner N, Dombrowski N, Sakurai H, Stark GR, (2002) Distinct roles of the IκB kinase alpha and beta subunits in liberating nuclear factor kappa B (NF-κB) from IκB and in phosphorylating the p65 subunit of NF-κB. J Biol Chem 277: 3863-3869.
    • (2002) J Biol Chem , vol.277 , pp. 3863-3869
    • Sizemore, N.1    Lerner, N.2    Dombrowski, N.3    Sakurai, H.4    Stark, G.R.5
  • 44
    • 44849117768 scopus 로고    scopus 로고
    • Akt-dependent regulation of NF-κB is controlled by mTOR and Raptor in association with IKK
    • Dan HC, Cooper MJ, Cogswell PC, Duncan JA, Ting JP, et al. (2008) Akt-dependent regulation of NF-κB is controlled by mTOR and Raptor in association with IKK. Genes Dev 22: 1490-1500.
    • (2008) Genes Dev , vol.22 , pp. 1490-1500
    • Dan, H.C.1    Cooper, M.J.2    Cogswell, P.C.3    Duncan, J.A.4    Ting, J.P.5
  • 45
    • 77950235551 scopus 로고    scopus 로고
    • Annexin 1 induced by anti-inflammatory drugs binds to NF-κB and inhibits its activation: anticancer effects in vitro and in vivo
    • Zhang Z, Huang L, Zhao W, Rigas B, (2010) Annexin 1 induced by anti-inflammatory drugs binds to NF-κB and inhibits its activation: anticancer effects in vitro and in vivo. Cancer Res 70: 2379-2388.
    • (2010) Cancer Res , vol.70 , pp. 2379-2388
    • Zhang, Z.1    Huang, L.2    Zhao, W.3    Rigas, B.4
  • 46
    • 70350120453 scopus 로고    scopus 로고
    • Prohibitin inhibits tumor necrosis factor alpha-induced nuclear factor-kappa B nuclear translocation via the novel mechanism of decreasing importin alpha3 expression
    • Theiss AL, Jenkins AK, Okoro NI, Klapproth JM, Merlin D, et al. (2009) Prohibitin inhibits tumor necrosis factor alpha-induced nuclear factor-kappa B nuclear translocation via the novel mechanism of decreasing importin alpha3 expression. Mol Biol Cell 20: 4412-4423.
    • (2009) Mol Biol Cell , vol.20 , pp. 4412-4423
    • Theiss, A.L.1    Jenkins, A.K.2    Okoro, N.I.3    Klapproth, J.M.4    Merlin, D.5
  • 47
    • 0037103765 scopus 로고    scopus 로고
    • Polyamine-modulated factor 1 binds to the human homologue of the 7a subunit of the Arabidopsis COP9 signalosome: implications in gene expression
    • Wang Y, Devereux W, Stewart TM, Casero RA Jr, (2002) Polyamine-modulated factor 1 binds to the human homologue of the 7a subunit of the Arabidopsis COP9 signalosome: implications in gene expression. Biochem J 366: 79-86.
    • (2002) Biochem J , vol.366 , pp. 79-86
    • Wang, Y.1    Devereux, W.2    Stewart, T.M.3    Casero Jr., R.A.4
  • 48
    • 59149098593 scopus 로고    scopus 로고
    • Sulforaphane protects against cytokine- and streptozotocin-induced beta-cell damage by suppressing the NF-κB pathway
    • Song MY, Kim EK, Moon WS, Park JW, Kim HJ, et al. (2009) Sulforaphane protects against cytokine- and streptozotocin-induced beta-cell damage by suppressing the NF-κB pathway. Toxicol Appl Pharmacol 235: 57-67.
    • (2009) Toxicol Appl Pharmacol , vol.235 , pp. 57-67
    • Song, M.Y.1    Kim, E.K.2    Moon, W.S.3    Park, J.W.4    Kim, H.J.5
  • 49
    • 79952271561 scopus 로고    scopus 로고
    • Nrf2 and NF-κB and Their Concerted Modulation in Cancer Pathogenesis and Progression
    • Bellezza I, Mierla AL, Minelli A, (2010) Nrf2 and NF-κB and Their Concerted Modulation in Cancer Pathogenesis and Progression. Cancers 2: 483-497.
    • (2010) Cancers , vol.2 , pp. 483-497
    • Bellezza, I.1    Mierla, A.L.2    Minelli, A.3
  • 50
    • 0033638507 scopus 로고    scopus 로고
    • Novel p19 protein engages IL-12p40 to form a cytokine, IL-23, with biological activities similar as well as distinct from IL-12
    • Oppmann B, Lesley R, Blom B, Timans JC, Xu Y, et al. (2000) Novel p19 protein engages IL-12p40 to form a cytokine, IL-23, with biological activities similar as well as distinct from IL-12. Immunity 13: 715-725.
    • (2000) Immunity , vol.13 , pp. 715-725
    • Oppmann, B.1    Lesley, R.2    Blom, B.3    Timans, J.C.4    Xu, Y.5
  • 51
    • 0031253635 scopus 로고    scopus 로고
    • IL-12 induces IFN-gamma expression and secretion in mouse peritoneal macrophages
    • Puddu P, Fantuzzi L, Borghi P, Varano B, Rainaldi G, et al. (1997) IL-12 induces IFN-gamma expression and secretion in mouse peritoneal macrophages. J Immunol 159: 3490-3497.
    • (1997) J Immunol , vol.159 , pp. 3490-3497
    • Puddu, P.1    Fantuzzi, L.2    Borghi, P.3    Varano, B.4    Rainaldi, G.5
  • 52
    • 0035147230 scopus 로고    scopus 로고
    • Interferon gamma regulates accumulation of the proteasome activator PA28 and immunoproteasomes at nuclear PML bodies
    • Fabunmi RP, Wigley WC, Thomas PJ, DeMartino GN, (2001) Interferon gamma regulates accumulation of the proteasome activator PA28 and immunoproteasomes at nuclear PML bodies. J Cell Sci 114: 29-36.
    • (2001) J Cell Sci , vol.114 , pp. 29-36
    • Fabunmi, R.P.1    Wigley, W.C.2    Thomas, P.J.3    DeMartino, G.N.4
  • 53
    • 0037105392 scopus 로고    scopus 로고
    • Regulation of immunoproteasome subunit expression in vivo following pathogenic fungal infection
    • Barton LF, Cruz M, Rangwala R, Deepe GS Jr, Monaco JJ, (2002) Regulation of immunoproteasome subunit expression in vivo following pathogenic fungal infection. J Immunol 169: 3046-3052.
    • (2002) J Immunol , vol.169 , pp. 3046-3052
    • Barton, L.F.1    Cruz, M.2    Rangwala, R.3    Deepe Jr., G.S.4    Monaco, J.J.5
  • 54
    • 33750133513 scopus 로고    scopus 로고
    • Interleukin-12 and Th1 immune response in Crohn's disease: pathogenetic relevance and therapeutic implication
    • Peluso I, Pallone F, Monteleone G, (2006) Interleukin-12 and Th1 immune response in Crohn's disease: pathogenetic relevance and therapeutic implication. World J Gastroenterol 12: 5606-5610.
    • (2006) World J Gastroenterol , vol.12 , pp. 5606-5610
    • Peluso, I.1    Pallone, F.2    Monteleone, G.3
  • 56
    • 0030885492 scopus 로고    scopus 로고
    • Proteasome inhibition attenuates nitric oxide synthase expression, VCAM-1 transcription and the development of chronic colitis
    • Conner EM, Brand S, Davis JM, Laroux FS, Palombella VJ, et al. (1997) Proteasome inhibition attenuates nitric oxide synthase expression, VCAM-1 transcription and the development of chronic colitis. J Pharmacol Exp Ther 282: 1615-1622.
    • (1997) J Pharmacol Exp Ther , vol.282 , pp. 1615-1622
    • Conner, E.M.1    Brand, S.2    Davis, J.M.3    Laroux, F.S.4    Palombella, V.J.5
  • 57
    • 33845306274 scopus 로고    scopus 로고
    • Proteasome-mediated degradation of IκBα and processing of p105 in Crohn disease and ulcerative colitis
    • Visekruna A, Joeris T, Seidel D, Kroesen A, Loddenkemper C, et al. (2006) Proteasome-mediated degradation of IκBα and processing of p105 in Crohn disease and ulcerative colitis. J Clin Invest 116: 3195-3203.
    • (2006) J Clin Invest , vol.116 , pp. 3195-3203
    • Visekruna, A.1    Joeris, T.2    Seidel, D.3    Kroesen, A.4    Loddenkemper, C.5
  • 58
    • 33845968031 scopus 로고    scopus 로고
    • Prohibitin protects against oxidative stress in intestinal epithelial cells
    • Theiss AL, Idell RD, Srinivasan S, Klapproth JM, Jones DP, et al. (2007) Prohibitin protects against oxidative stress in intestinal epithelial cells. FASEB J 21: 197-206.
    • (2007) FASEB J , vol.21 , pp. 197-206
    • Theiss, A.L.1    Idell, R.D.2    Srinivasan, S.3    Klapproth, J.M.4    Jones, D.P.5


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