메뉴 건너뛰기




Volumn 143, Issue 2, 2014, Pages 138-145

Transplantation and inflammation: Implications for the modification of chemokine function

Author keywords

Chemokines; Inflammation; Post translational modification; Stress

Indexed keywords

AUTACOID; BIOLOGICAL MARKER; CHEMOKINE;

EID: 84908159023     PISSN: 00192805     EISSN: 13652567     Source Type: Journal    
DOI: 10.1111/imm.12332     Document Type: Article
Times cited : (38)

References (63)
  • 1
    • 81255195550 scopus 로고    scopus 로고
    • Ischemia and reperfusion - from mechanism to translation
    • Eltzschig HK, Eckle T. Ischemia and reperfusion - from mechanism to translation. Nat Med 2011; 17:1391-401.
    • (2011) Nat Med , vol.17 , pp. 1391-1401
    • Eltzschig, H.K.1    Eckle, T.2
  • 2
    • 77958114712 scopus 로고    scopus 로고
    • Some current insights into oxidative stress
    • Ďuračková Z. Some current insights into oxidative stress. Physiol Res 2010; 59:459-69.
    • (2010) Physiol Res , vol.59 , pp. 459-469
    • Ďuračková, Z.1
  • 4
    • 8344282655 scopus 로고    scopus 로고
    • The role of oxidative damage and stress in aging
    • Bokov A, Chaudhuri A, Richardson A. The role of oxidative damage and stress in aging. Mech Ageing Dev 2004; 125 (10-11 SPEC. ISS.):811-26.
    • (2004) Mech Ageing Dev , vol.125 , Issue.10-11 SPEC. ISS. , pp. 811-826
    • Bokov, A.1    Chaudhuri, A.2    Richardson, A.3
  • 5
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • Dröge W. Free radicals in the physiological control of cell function. Physiol Rev 2002; 82:47-95.
    • (2002) Physiol Rev , vol.82 , pp. 47-95
    • Dröge, W.1
  • 6
    • 80051670219 scopus 로고    scopus 로고
    • Hepatic consequences of vascular adhesion protein-1 expression
    • Weston CJ, Adams DH. Hepatic consequences of vascular adhesion protein-1 expression. J Neural Transm 2011; 118:1055-64.
    • (2011) J Neural Transm , vol.118 , pp. 1055-1064
    • Weston, C.J.1    Adams, D.H.2
  • 7
    • 54549111991 scopus 로고    scopus 로고
    • Oxidative and nitrosative stress and fibrogenic response
    • Urtasun R, de la Rosa LC, Nieto N. Oxidative and nitrosative stress and fibrogenic response. Clin Liver Dis 2008; 12:769-90.
    • (2008) Clin Liver Dis , vol.12 , pp. 769-790
    • Urtasun, R.1    de la Rosa, L.C.2    Nieto, N.3
  • 8
    • 0031002421 scopus 로고    scopus 로고
    • Superoxide and peroxynitrite generation from inducible nitric oxide synthase in macrophages
    • Xia Y, Zweier JL. Superoxide and peroxynitrite generation from inducible nitric oxide synthase in macrophages. Proc Natl Acad Sci USA 1997; 94:6954-8.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 6954-6958
    • Xia, Y.1    Zweier, J.L.2
  • 9
    • 80052512520 scopus 로고    scopus 로고
    • Endogenously induced DNA double strand breaks arise in heterochromatic DNA regions and require ataxia telangiectasia mutated and Artemis for their repair
    • Woodbine L, Brunton H, Goodarzi AA, Shibata A, Jeggo PA. Endogenously induced DNA double strand breaks arise in heterochromatic DNA regions and require ataxia telangiectasia mutated and Artemis for their repair. Nucleic Acids Res 2011; 39:6986-97.
    • (2011) Nucleic Acids Res , vol.39 , pp. 6986-6997
    • Woodbine, L.1    Brunton, H.2    Goodarzi, A.A.3    Shibata, A.4    Jeggo, P.A.5
  • 10
    • 78549237781 scopus 로고    scopus 로고
    • Oxidation in the nucleotide pool, the DNA damage response and cellular senescence: defective bricks build a defective house
    • Rai P. Oxidation in the nucleotide pool, the DNA damage response and cellular senescence: defective bricks build a defective house. Mutat Res 2010; 703:71-81.
    • (2010) Mutat Res , vol.703 , pp. 71-81
    • Rai, P.1
  • 11
    • 34547673497 scopus 로고    scopus 로고
    • Peroxynitrite: biochemistry, pathophysiology and development of therapeutics
    • Szabo C, Ischiropoulos H, Radi R. Peroxynitrite: biochemistry, pathophysiology and development of therapeutics. Nat Rev Drug Discovery 2007; 6:662-80.
    • (2007) Nat Rev Drug Discovery , vol.6 , pp. 662-680
    • Szabo, C.1    Ischiropoulos, H.2    Radi, R.3
  • 12
    • 80052278961 scopus 로고    scopus 로고
    • Vascular cell-adhesion molecule-1 plays a central role in the proangiogenic effects of oxidative stress
    • Dong A, Shen J, Zeng M, Campochiaro PA. Vascular cell-adhesion molecule-1 plays a central role in the proangiogenic effects of oxidative stress. Proc Natl Acad Sci U S A 2011; 108:14614-9.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 14614-14619
    • Dong, A.1    Shen, J.2    Zeng, M.3    Campochiaro, P.A.4
  • 13
    • 77953357715 scopus 로고    scopus 로고
    • Oxidative stress causes reversible changes in mitochondrial permeability and structure
    • Cole NB, Daniels MP, Levine RL, Kim G. Oxidative stress causes reversible changes in mitochondrial permeability and structure. Exp Gerontol 2010; 45:596-602.
    • (2010) Exp Gerontol , vol.45 , pp. 596-602
    • Cole, N.B.1    Daniels, M.P.2    Levine, R.L.3    Kim, G.4
  • 14
    • 44649120132 scopus 로고    scopus 로고
    • Chemokine signaling via the CXCR2 receptor reinforces senescence
    • Acosta JC, O'Loghlen A, Banito A et al. Chemokine signaling via the CXCR2 receptor reinforces senescence. Cell 2008; 133:1006-18.
    • (2008) Cell , vol.133 , pp. 1006-1018
    • Acosta, J.C.1    O'Loghlen, A.2    Banito, A.3
  • 15
    • 77955304095 scopus 로고    scopus 로고
    • Modulation of the microenvironment by senescent biliary epithelial cells may be involved in the pathogenesis of primary biliary cirrhosis
    • Sasaki M, Miyakoshi M, Sato Y, Nakanuma Y. Modulation of the microenvironment by senescent biliary epithelial cells may be involved in the pathogenesis of primary biliary cirrhosis. J Hepatol 2010; 53:318-25.
    • (2010) J Hepatol , vol.53 , pp. 318-325
    • Sasaki, M.1    Miyakoshi, M.2    Sato, Y.3    Nakanuma, Y.4
  • 16
    • 84879554094 scopus 로고    scopus 로고
    • Biliary epithelial senescence and plasticity in acute cellular rejection
    • Brain JG, Robertson H, Thompson E et al. Biliary epithelial senescence and plasticity in acute cellular rejection. Am J Transplant 2013; 13:1688-702.
    • (2013) Am J Transplant , vol.13 , pp. 1688-1702
    • Brain, J.G.1    Robertson, H.2    Thompson, E.3
  • 17
    • 0036773977 scopus 로고    scopus 로고
    • Chemokines: directing leukocyte infiltration into allografts
    • El-Sawy T, Fahmy NM, Fairchild RL. Chemokines: directing leukocyte infiltration into allografts. Curr Opin Immunol 2002; 14:562-8.
    • (2002) Curr Opin Immunol , vol.14 , pp. 562-568
    • El-Sawy, T.1    Fahmy, N.M.2    Fairchild, R.L.3
  • 18
    • 0034144269 scopus 로고    scopus 로고
    • Chemokines: a new classification system and their role in immunity
    • Zlotnik A, Yoshie O. Chemokines: a new classification system and their role in immunity. Immunity 2000; 12:121-7.
    • (2000) Immunity , vol.12 , pp. 121-127
    • Zlotnik, A.1    Yoshie, O.2
  • 19
    • 84887512970 scopus 로고    scopus 로고
    • International Union of Pharmacology LXXXIX. Update on the extended family of chemokine receptors and introducing a new nomenclature for atypical chemokine receptors
    • Bachelerie F, Ben-Baruch A, Burkhardt AM et al. International Union of Pharmacology LXXXIX. Update on the extended family of chemokine receptors and introducing a new nomenclature for atypical chemokine receptors. Pharmacol Rev 2014; 66:1-79.
    • (2014) Pharmacol Rev , vol.66 , pp. 1-79
    • Bachelerie, F.1    Ben-Baruch, A.2    Burkhardt, A.M.3
  • 20
    • 26844504998 scopus 로고    scopus 로고
    • Characterization of a novel chemokine-containing storage granule in endothelial cells: evidence for preferential exocytosis mediated by protein kinase A and diacylglycerol
    • Øynebråten I, Barois N, Hagelsteen K, Johansen FE, Bakke O, Haraldsen G. Characterization of a novel chemokine-containing storage granule in endothelial cells: evidence for preferential exocytosis mediated by protein kinase A and diacylglycerol. J Immunol 2005; 175:5358-69.
    • (2005) J Immunol , vol.175 , pp. 5358-5369
    • Øynebråten, I.1    Barois, N.2    Hagelsteen, K.3    Johansen, F.E.4    Bakke, O.5    Haraldsen, G.6
  • 21
    • 80052992000 scopus 로고    scopus 로고
    • Chemokines in transplantation: what can atypical receptors teach us about anti-inflammatory therapy?
    • O'Boyle G, Ali S, Kirby JA. Chemokines in transplantation: what can atypical receptors teach us about anti-inflammatory therapy? Transplant Rev (Orlando) 2011; 25:136-44.
    • (2011) Transplant Rev (Orlando) , vol.25 , pp. 136-144
    • O'Boyle, G.1    Ali, S.2    Kirby, J.A.3
  • 22
    • 84872435502 scopus 로고    scopus 로고
    • Interstitial dendritic cell guidance by haptotactic chemokine gradients
    • Weber M, Hauschild R, Schwarz J et al. Interstitial dendritic cell guidance by haptotactic chemokine gradients. Science 2013; 339:328-32.
    • (2013) Science , vol.339 , pp. 328-332
    • Weber, M.1    Hauschild, R.2    Schwarz, J.3
  • 23
    • 16244368041 scopus 로고    scopus 로고
    • Renal transplantation: examination of the regulation of chemokine binding during acute rejection
    • Ali S, Malik G, Burns A, Robertson H, Kirby JA. Renal transplantation: examination of the regulation of chemokine binding during acute rejection. Transplantation 2005; 79:672-9.
    • (2005) Transplantation , vol.79 , pp. 672-679
    • Ali, S.1    Malik, G.2    Burns, A.3    Robertson, H.4    Kirby, J.A.5
  • 24
    • 48349144664 scopus 로고    scopus 로고
    • The puzzling role of CXCR3 and its ligands in organ allograft rejection
    • Halloran PF, Fairchild RL. The puzzling role of CXCR3 and its ligands in organ allograft rejection. Am J Transplant 2008; 8:1578-9.
    • (2008) Am J Transplant , vol.8 , pp. 1578-1579
    • Halloran, P.F.1    Fairchild, R.L.2
  • 25
    • 8144225160 scopus 로고    scopus 로고
    • Stromal cell-derived factor-1 and CXCR4 interaction is critical for development of transplant arteriosclerosis
    • Sakihama H, Masunaga T, Yamashita K, Hashimoto T, Inobe M, Todo S, Uede T. Stromal cell-derived factor-1 and CXCR4 interaction is critical for development of transplant arteriosclerosis. Circulation 2004; 110:2924-30.
    • (2004) Circulation , vol.110 , pp. 2924-2930
    • Sakihama, H.1    Masunaga, T.2    Yamashita, K.3    Hashimoto, T.4    Inobe, M.5    Todo, S.6    Uede, T.7
  • 26
    • 54049109715 scopus 로고    scopus 로고
    • Chemokines and transplant vasculopathy
    • Belperio JA, Ardehali A. Chemokines and transplant vasculopathy. Circ Res 2008; 103:454-66.
    • (2008) Circ Res , vol.103 , pp. 454-466
    • Belperio, J.A.1    Ardehali, A.2
  • 27
    • 79251527204 scopus 로고    scopus 로고
    • Serum chemokine CXC ligand 10 (CXCL10) predicts fibrosis progression after liver transplantation for hepatitis C infection
    • Berres ML, Trautwein C, Schmeding M et al. Serum chemokine CXC ligand 10 (CXCL10) predicts fibrosis progression after liver transplantation for hepatitis C infection. Hepatology 2011; 53:596-603.
    • (2011) Hepatology , vol.53 , pp. 596-603
    • Berres, M.L.1    Trautwein, C.2    Schmeding, M.3
  • 28
    • 53749083136 scopus 로고    scopus 로고
    • Regulation of chemokine activity by posttranslational modification
    • Mortier A, Van Damme J, Proost P. Regulation of chemokine activity by posttranslational modification. Pharmacol Ther 2008; 120:197-217.
    • (2008) Pharmacol Ther , vol.120 , pp. 197-217
    • Mortier, A.1    Van Damme, J.2    Proost, P.3
  • 29
    • 0036305443 scopus 로고    scopus 로고
    • Regulation of matrix metalloproteinases and effect of MMP-inhibition in heart transplant related reperfusion injury
    • Falk V, Soccal PM, Grünenfelder J, Hoyt G, Walther T, Robbins RC. Regulation of matrix metalloproteinases and effect of MMP-inhibition in heart transplant related reperfusion injury. Eur J Cardiothorac Surg 2002; 22:53-8.
    • (2002) Eur J Cardiothorac Surg , vol.22 , pp. 53-58
    • Falk, V.1    Soccal, P.M.2    Grünenfelder, J.3    Hoyt, G.4    Walther, T.5    Robbins, R.C.6
  • 30
    • 12144290341 scopus 로고    scopus 로고
    • Plasma MMP-2 and MMP-9 and their inhibitors TIMP-1 and TIMP-2 during human orthotopic liver transplantation. The effect of aprotinin and the relation to ischemia/reperfusion injury
    • Kuyvenhoven JP, Molenaar IQ, Verspaget HW et al. Plasma MMP-2 and MMP-9 and their inhibitors TIMP-1 and TIMP-2 during human orthotopic liver transplantation. The effect of aprotinin and the relation to ischemia/reperfusion injury. Thromb Haemost 2004; 91:506-13.
    • (2004) Thromb Haemost , vol.91 , pp. 506-513
    • Kuyvenhoven, J.P.1    Molenaar, I.Q.2    Verspaget, H.W.3
  • 31
    • 54049106148 scopus 로고    scopus 로고
    • + CXC chemokines and generates CCL2, -7, -8, and -13 antagonists: potential role of the macrophage in terminating polymorphonuclear leukocyte influx
    • + CXC chemokines and generates CCL2, -7, -8, and -13 antagonists: potential role of the macrophage in terminating polymorphonuclear leukocyte influx. Blood 2008; 112:3455-64.
    • (2008) Blood , vol.112 , pp. 3455-3464
    • Dean, R.A.1    Cox, J.H.2    Bellac, C.L.3    Doucet, A.4    Starr, A.E.5    Overall, C.M.6
  • 32
    • 62949143804 scopus 로고    scopus 로고
    • Reactive nitrogen species switch on early extracellular matrix remodeling via induction of MMP1 and TNFa
    • 1410-22e4
    • Urtasun R, Cubero FJ, Vera M, Nieto N. Reactive nitrogen species switch on early extracellular matrix remodeling via induction of MMP1 and TNFa. Gastroenterology 2009; 136:1410-22.e4.
    • (2009) Gastroenterology , vol.136
    • Urtasun, R.1    Cubero, F.J.2    Vera, M.3    Nieto, N.4
  • 34
    • 0034667542 scopus 로고    scopus 로고
    • Neutrophil gelatinase B potentiates interleukin-8 tenfold by aminoterminal processing, whereas it degrades CTAP-III, PF-4, and GRO-α and leaves RANTES and MCP-2 intact
    • Van Den Steen PE, Proost P, Wuyts A, Van Damme J, Opdenakker G. Neutrophil gelatinase B potentiates interleukin-8 tenfold by aminoterminal processing, whereas it degrades CTAP-III, PF-4, and GRO-α and leaves RANTES and MCP-2 intact. Blood 2000; 96:2673-81.
    • (2000) Blood , vol.96 , pp. 2673-2681
    • Van Den Steen, P.E.1    Proost, P.2    Wuyts, A.3    Van Damme, J.4    Opdenakker, G.5
  • 35
    • 0141782259 scopus 로고    scopus 로고
    • Gelatinase B/MMP-9 and neutrophil collagenase/MMP-8 process the chemokines human GCP-2/CXCL6, ENA-78/CXCL5 and mouse GCP-2/LIX and modulate their physiological activities
    • Van Den Steen PE, Wuyts A, Husson SJ, Proost P, Van Damme J, Opdenakker G. Gelatinase B/MMP-9 and neutrophil collagenase/MMP-8 process the chemokines human GCP-2/CXCL6, ENA-78/CXCL5 and mouse GCP-2/LIX and modulate their physiological activities. Eur J Biochem 2003; 270:3739-49.
    • (2003) Eur J Biochem , vol.270 , pp. 3739-3749
    • Van Den Steen, P.E.1    Wuyts, A.2    Husson, S.J.3    Proost, P.4    Van Damme, J.5    Opdenakker, G.6
  • 37
    • 44549085494 scopus 로고    scopus 로고
    • Revisiting an old acquaintance: CD26 and its molecular mechanisms in T cell function
    • Ohnuma K, Dang NH, Morimoto C. Revisiting an old acquaintance: CD26 and its molecular mechanisms in T cell function. Trends Immunol 2008; 29:295-301.
    • (2008) Trends Immunol , vol.29 , pp. 295-301
    • Ohnuma, K.1    Dang, N.H.2    Morimoto, C.3
  • 38
    • 0036659179 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV (CD26) on T cells cleaves the CXC chemokine CXCL11 (I-TAC) and abolishes the stimulating but not the desensitizing potential of the chemokine
    • Ludwig A, Schiemann F, Mentlein R, Lindner B, Brandt E. Dipeptidyl peptidase IV (CD26) on T cells cleaves the CXC chemokine CXCL11 (I-TAC) and abolishes the stimulating but not the desensitizing potential of the chemokine. J Leukoc Biol 2002; 72:183-91.
    • (2002) J Leukoc Biol , vol.72 , pp. 183-191
    • Ludwig, A.1    Schiemann, F.2    Mentlein, R.3    Lindner, B.4    Brandt, E.5
  • 39
    • 0030819309 scopus 로고    scopus 로고
    • Regulation of the receptor specificity and function of the chemokine RANTES (regulated on activation, normal T cell expressed and secreted) by dipeptidyl peptidase IV (CD26)-mediated cleavage
    • Oravecz T, Pall M, Roderiquez G et al. Regulation of the receptor specificity and function of the chemokine RANTES (regulated on activation, normal T cell expressed and secreted) by dipeptidyl peptidase IV (CD26)-mediated cleavage. J Exp Med 1997; 186:1865-72.
    • (1997) J Exp Med , vol.186 , pp. 1865-1872
    • Oravecz, T.1    Pall, M.2    Roderiquez, G.3
  • 40
    • 0031981959 scopus 로고    scopus 로고
    • Natural truncation of RANTES abolishes signaling through the CC chemokine receptors CCR1 and CCR3, impairs its chemotactic potency and generates a CC chemokine inhibitor
    • Struyf S, De Meester I, Scharpé S, Lenaerts JP, Menten P, Wang JM, Proost P, Van Damme J. Natural truncation of RANTES abolishes signaling through the CC chemokine receptors CCR1 and CCR3, impairs its chemotactic potency and generates a CC chemokine inhibitor. Eur J Immunol 1998; 28:1262-71.
    • (1998) Eur J Immunol , vol.28 , pp. 1262-1271
    • Struyf, S.1    De Meester, I.2    Scharpé, S.3    Lenaerts, J.P.4    Menten, P.5    Wang, J.M.6    Proost, P.7    Van Damme, J.8
  • 41
    • 0037199997 scopus 로고    scopus 로고
    • Natural truncation of the chemokine MIP-b/CCL4 affects receptor specificity but not anti-HIV-1 activity
    • Guan E, Wang J, Roderiquez G, Norcross MA. Natural truncation of the chemokine MIP-b/CCL4 affects receptor specificity but not anti-HIV-1 activity. J Biol Chem 2002; 277:32348-52.
    • (2002) J Biol Chem , vol.277 , pp. 32348-32352
    • Guan, E.1    Wang, J.2    Roderiquez, G.3    Norcross, M.A.4
  • 42
    • 6344284808 scopus 로고    scopus 로고
    • Heparan sulfate/heparin oligosaccharides protect stromal cell-derived factor-1 (SDF-1)/CXCL12 against proteolysis induced by CD26/dipeptidyl peptidase IV
    • Sadir R, Imberty A, Baleux F, Lortat-Jacob H. Heparan sulfate/heparin oligosaccharides protect stromal cell-derived factor-1 (SDF-1)/CXCL12 against proteolysis induced by CD26/dipeptidyl peptidase IV. J Biol Chem 2004; 279:43854-60.
    • (2004) J Biol Chem , vol.279 , pp. 43854-43860
    • Sadir, R.1    Imberty, A.2    Baleux, F.3    Lortat-Jacob, H.4
  • 43
    • 34447508446 scopus 로고    scopus 로고
    • Eotaxin selectively binds heparin: an interaction that protects eotaxin from proteolysis and potentiates chemotactic activity in vivo
    • Ellyard JI, Simson L, Bezos A, Johnston K, Freeman C, Parish CR. Eotaxin selectively binds heparin: an interaction that protects eotaxin from proteolysis and potentiates chemotactic activity in vivo. J Biol Chem 2007; 282:15238-47.
    • (2007) J Biol Chem , vol.282 , pp. 15238-15247
    • Ellyard, J.I.1    Simson, L.2    Bezos, A.3    Johnston, K.4    Freeman, C.5    Parish, C.R.6
  • 44
    • 23944488853 scopus 로고    scopus 로고
    • Specific C-terminal cleavage and inactivation of interleukin-8 by invasive disease isolates of Streptococcus pyogenes
    • Edwards RJ, Taylor GW, Ferguson M et al. Specific C-terminal cleavage and inactivation of interleukin-8 by invasive disease isolates of Streptococcus pyogenes. J Infect Dis 2005; 192:783-90.
    • (2005) J Infect Dis , vol.192 , pp. 783-790
    • Edwards, R.J.1    Taylor, G.W.2    Ferguson, M.3
  • 45
    • 77953496864 scopus 로고    scopus 로고
    • Chemokine-cleaving Streptococcus pyogenes protease SpyCEP is necessary and sufficient for bacterial dissemination within soft tissues and the respiratory tract
    • Kurupati P, Turner CE, Tziona I et al. Chemokine-cleaving Streptococcus pyogenes protease SpyCEP is necessary and sufficient for bacterial dissemination within soft tissues and the respiratory tract. Mol Microbiol 2010; 76:1387-97.
    • (2010) Mol Microbiol , vol.76 , pp. 1387-1397
    • Kurupati, P.1    Turner, C.E.2    Tziona, I.3
  • 46
    • 0032407820 scopus 로고    scopus 로고
    • Modulation of interleukin-8 activity by gingipains from Porphyromonas gingivalis: implications for pathogenicity of periodontal disease
    • Mikolajczyk-Pawlinska J, Travis J, Potempa J. Modulation of interleukin-8 activity by gingipains from Porphyromonas gingivalis: implications for pathogenicity of periodontal disease. FEBS Lett 1998; 440:282-6.
    • (1998) FEBS Lett , vol.440 , pp. 282-286
    • Mikolajczyk-Pawlinska, J.1    Travis, J.2    Potempa, J.3
  • 47
    • 84900427578 scopus 로고    scopus 로고
    • Citrullination and proteolytic processing of chemokines by Porphyromonas gingivalis
    • Moelants EA, Loozen G, Mortier A et al. Citrullination and proteolytic processing of chemokines by Porphyromonas gingivalis. Infect Immun 2014; 82:2511-9.
    • (2014) Infect Immun , vol.82 , pp. 2511-2519
    • Moelants, E.A.1    Loozen, G.2    Mortier, A.3
  • 49
    • 0029862502 scopus 로고    scopus 로고
    • Nitration and inactivation of manganese superoxide dismutase in chronic rejection of human renal allografts
    • Macmillan-Crow LA, Crow JP, Kerby JD, Beckman JS, Thompson JA. Nitration and inactivation of manganese superoxide dismutase in chronic rejection of human renal allografts. Proc Natl Acad Sci USA 1996; 93:11853-8.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 11853-11858
    • Macmillan-Crow, L.A.1    Crow, J.P.2    Kerby, J.D.3    Beckman, J.S.4    Thompson, J.A.5
  • 50
    • 80054694464 scopus 로고    scopus 로고
    • Chemokine nitration prevents intratumoral infiltration of antigen-specific T cells
    • Molon B, Ugel S, Del Pozzo F et al. Chemokine nitration prevents intratumoral infiltration of antigen-specific T cells. J Exp Med 2011; 208:1949-62.
    • (2011) J Exp Med , vol.208 , pp. 1949-1962
    • Molon, B.1    Ugel, S.2    Del Pozzo, F.3
  • 51
    • 0032888715 scopus 로고    scopus 로고
    • Effects of reactive oxygen and nitrogen metabolites on MCP-1-induced monocyte chemotactic activity in vitro
    • Sato E, Simpson KL, Grisham MB, Koyama S, Robbins RA. Effects of reactive oxygen and nitrogen metabolites on MCP-1-induced monocyte chemotactic activity in vitro. Am J Physiol Lung Cell Mol Physiol 1999; 277:L543-9.
    • (1999) Am J Physiol Lung Cell Mol Physiol , vol.277 , pp. L543-L549
    • Sato, E.1    Simpson, K.L.2    Grisham, M.B.3    Koyama, S.4    Robbins, R.A.5
  • 52
    • 0032778825 scopus 로고    scopus 로고
    • Effects of reactive oxygen and nitrogen metabolites on RANTES- and IL- 5-induced eosinophil chemotactic activity in vitro
    • Sato E, Simpson KL, Grisham MB, Koyama S, Robbins RA. Effects of reactive oxygen and nitrogen metabolites on RANTES- and IL- 5-induced eosinophil chemotactic activity in vitro. Am J Pathol 1999; 155:591-8.
    • (1999) Am J Pathol , vol.155 , pp. 591-598
    • Sato, E.1    Simpson, K.L.2    Grisham, M.B.3    Koyama, S.4    Robbins, R.A.5
  • 53
    • 81455158817 scopus 로고    scopus 로고
    • A copper-hydrogen peroxide redox system induces dityrosine cross-links and chemokine oligomerisation
    • MacGregor HJ, Kato Y, Marshall LJ, Nevell TG, Shute JK. A copper-hydrogen peroxide redox system induces dityrosine cross-links and chemokine oligomerisation. Cytokine 2011; 56:669-75.
    • (2011) Cytokine , vol.56 , pp. 669-675
    • MacGregor, H.J.1    Kato, Y.2    Marshall, L.J.3    Nevell, T.G.4    Shute, J.K.5
  • 54
    • 84873090537 scopus 로고    scopus 로고
    • Peptidylarginine deiminases: physiological function, interaction with chemokines and role in pathology
    • Moelants EAV, Mortier A, Van Damme J, Proost P, Loos T. Peptidylarginine deiminases: physiological function, interaction with chemokines and role in pathology. Drug Discov Today Technol 2012; 9:e261-80.
    • (2012) Drug Discov Today Technol , vol.9 , pp. e261-e280
    • Moelants, E.A.V.1    Mortier, A.2    Van Damme, J.3    Proost, P.4    Loos, T.5
  • 55
    • 84860390022 scopus 로고    scopus 로고
    • Peptidylarginine deiminase 2, 3 and 4 have distinct specificities against cellular substrates: novel insights into autoantigen selection in rheumatoid arthritis
    • Darrah E, Rosen A, Giles JT, Andrade F. Peptidylarginine deiminase 2, 3 and 4 have distinct specificities against cellular substrates: novel insights into autoantigen selection in rheumatoid arthritis. Ann Rheum Dis 2012; 71:92-8.
    • (2012) Ann Rheum Dis , vol.71 , pp. 92-98
    • Darrah, E.1    Rosen, A.2    Giles, J.T.3    Andrade, F.4
  • 56
    • 72249096427 scopus 로고    scopus 로고
    • Regulation of protein citrullination through p53/PADI4Network in DNA damage response
    • Tanikawa C, Ueda K, Nakagawa H, Yoshida N, Nakamura Y, Matsuda K. Regulation of protein citrullination through p53/PADI4Network in DNA damage response. Cancer Res 2009; 69:8761-9.
    • (2009) Cancer Res , vol.69 , pp. 8761-8769
    • Tanikawa, C.1    Ueda, K.2    Nakagawa, H.3    Yoshida, N.4    Nakamura, Y.5    Matsuda, K.6
  • 57
    • 77952307740 scopus 로고    scopus 로고
    • Deimination is regulated at multiple levels including auto-deimination of peptidylarginine deiminases
    • Méchin MC, Coudane F, Adoue V et al. Deimination is regulated at multiple levels including auto-deimination of peptidylarginine deiminases. Cell Mol Life Sci 2010; 67:1491-503.
    • (2010) Cell Mol Life Sci , vol.67 , pp. 1491-1503
    • Méchin, M.C.1    Coudane, F.2    Adoue, V.3
  • 58
    • 83455233902 scopus 로고    scopus 로고
    • Peptidyl-arginine deiminase: an additional marker of rheumatoid arthritis
    • Basu PS, Majhi R, Ghosal S, Batabyal SK. Peptidyl-arginine deiminase: an additional marker of rheumatoid arthritis. Clin Lab 2011; 57:1021-5.
    • (2011) Clin Lab , vol.57 , pp. 1021-1025
    • Basu, P.S.1    Majhi, R.2    Ghosal, S.3    Batabyal, S.K.4
  • 59
    • 53449087927 scopus 로고    scopus 로고
    • Citrullination of CXCL10 and CXCL11 by peptidylarginine deiminase: a naturally occurring posttranslational modification of chemokines and new dimension of immunoregulation
    • Loos T, Mortier A, Gouwy M, Ronsse I, Put W, Lenaerts JP, Van Damme J, Proost P. Citrullination of CXCL10 and CXCL11 by peptidylarginine deiminase: a naturally occurring posttranslational modification of chemokines and new dimension of immunoregulation. Blood 2008; 112:2648-56.
    • (2008) Blood , vol.112 , pp. 2648-2656
    • Loos, T.1    Mortier, A.2    Gouwy, M.3    Ronsse, I.4    Put, W.5    Lenaerts, J.P.6    Van Damme, J.7    Proost, P.8
  • 60
    • 59849091593 scopus 로고    scopus 로고
    • Citrullination of CXCL12 differentially reduces CXCR4 and CXCR7 binding with loss of inflammatory and anti-HIV-1 activity via CXCR4
    • Struyf S, Noppen S, Loos T et al. Citrullination of CXCL12 differentially reduces CXCR4 and CXCR7 binding with loss of inflammatory and anti-HIV-1 activity via CXCR4. J Immunol 2009; 182:666-74.
    • (2009) J Immunol , vol.182 , pp. 666-674
    • Struyf, S.1    Noppen, S.2    Loos, T.3
  • 61
    • 51049113366 scopus 로고    scopus 로고
    • Citrullination of CXCL8 by peptidylarginine deiminase alters receptor usage, prevents proteolysis, and dampens tissue inflammation
    • Proost P, Loos T, Mortier A et al. Citrullination of CXCL8 by peptidylarginine deiminase alters receptor usage, prevents proteolysis, and dampens tissue inflammation. J Exp Med 2008; 205:2085-97.
    • (2008) J Exp Med , vol.205 , pp. 2085-2097
    • Proost, P.1    Loos, T.2    Mortier, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.