메뉴 건너뛰기




Volumn 585, Issue 4, 2011, Pages 613-617

The ribonuclease/angiogenin inhibitor is also present in mitochondria and nuclei

Author keywords

Mitochondria; Nucleus; Reactive oxygen species; Reactive oxygen species scavenger; Ribonuclease angiogenin inhibitor

Indexed keywords

RIBONUCLEASE INHIBITOR;

EID: 79951580697     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2011.01.034     Document Type: Article
Times cited : (27)

References (23)
  • 1
    • 0027718173 scopus 로고
    • Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats
    • DOI 10.1038/366751a0
    • B. Kobe, and J. Deisenhofer Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats Nature 366 1993 751 756 (Pubitemid 24038517)
    • (1993) Nature , vol.366 , Issue.6457 , pp. 751-756
    • Kobe, B.1    Deisenhofer, J.2
  • 2
    • 0028911034 scopus 로고
    • A structural basis of the interactions between leucine-rich repeats and protein ligands
    • B. Kobe, and J. Deisenhofer A structural basis of the interactions between leucine-rich repeats and protein ligands Nature 374 1995 183 186
    • (1995) Nature , vol.374 , pp. 183-186
    • Kobe, B.1    Deisenhofer, J.2
  • 5
    • 0037324378 scopus 로고    scopus 로고
    • Ribonuclease inhibitor as an intracellular sentry
    • DOI 10.1093/nar/gkg163
    • M.C. Haigis, E.L. Kurten, and R.T. Raines Ribonuclease inhibitor as an intracellular sentry Nucleic Acids Res. 31 2003 1024 1032 (Pubitemid 36240441)
    • (2003) Nucleic Acids Research , vol.31 , Issue.3 , pp. 1024-1032
    • Haigis, M.C.1    Kurten, E.L.2    Raines, R.T.3
  • 7
    • 55549133584 scopus 로고    scopus 로고
    • Interaction of onconase with the human ribonuclease inhibitor protein
    • R.F. Turcotte, and R.T. Raines Interaction of onconase with the human ribonuclease inhibitor protein Biochem. Biophys. Res. Commun. 377 2008 512 514
    • (2008) Biochem. Biophys. Res. Commun. , vol.377 , pp. 512-514
    • Turcotte, R.F.1    Raines, R.T.2
  • 10
    • 4544330800 scopus 로고    scopus 로고
    • Cytosolic RNase inhibitor only affects RNases with intrinsic cytotoxicity
    • DOI 10.1074/jbc.C400311200
    • D.M. Monti, and G. D'Alessio Cytosolic RNase inhibitor only affects RNases with intrinsic cytotoxicity J. Biol. Chem. 279 2004 39195 39198 (Pubitemid 39258179)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.38 , pp. 39195-39198
    • Monti, D.M.1    D'Alessio, G.2
  • 12
    • 18144387601 scopus 로고    scopus 로고
    • Interactions of the cytotoxic RNase A dimers with the cytosolic ribonuclease inhibitor
    • DOI 10.1016/j.febslet.2005.03.087
    • M. Naddeo, L. Vitagliano, A. Russo, G. Gotte, G. D'Alessio, and S. Sorrentino Interactions of the cytotoxic RNase A dimers with the cytosolic ribonuclease inhibitor FEBS Lett. 579 2005 2663 2668 (Pubitemid 40615674)
    • (2005) FEBS Letters , vol.579 , Issue.12 , pp. 2663-2668
    • Naddeo, M.1    Vitagliano, L.2    Russo, A.3    Gotte, G.4    D'Alessio, G.5    Sorrentino, S.6
  • 13
    • 0029768918 scopus 로고    scopus 로고
    • Oxidation of sulfhydryl groups of ribonuclease inhibitor in epithelial cells is sufficient for its intracellular degradation
    • DOI 10.1074/jbc.271.31.18638
    • M. Blazquez, J.M. Fominaya, and J. Hofsteenge Oxidation of sulfhydryl groups of ribonuclease inhibitor in epithelial cells is sufficient for its intracellular degradation J. Biol. Chem. 271 1996 18638 18642 (Pubitemid 26322728)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.31 , pp. 18638-18642
    • Blazquez, M.1    Fominaya, J.M.2    Hofsteenge, J.3
  • 14
    • 0142094028 scopus 로고    scopus 로고
    • The antioxidant effects of ribonuclease inhibitor
    • DOI 10.1080/10715760310001600408
    • X.Y. Cui, P.F. Fu, D.N. Pan, Y. Zhao, J. Zhao, and B.C. Zhao The antioxidant effects of ribonuclease inhibitor Free Radic. Res. 37 2003 1079 1085 (Pubitemid 37265330)
    • (2003) Free Radical Research , vol.37 , Issue.10 , pp. 1079-1085
    • Cui, X.Y.1    Fu, P.F.2    Pan, D.N.3    Zhao, Y.4    Zhao, J.5    Zhao, B.C.6
  • 15
    • 33744521821 scopus 로고    scopus 로고
    • Radical scavenging activity of ribonuclease inhibitor from cow placenta
    • DOI 10.1134/S0006297906050087
    • S. Wang, and H. Li Radical scavenging activity of ribonuclease inhibitor from cow placenta Biochemistry (Moscow) 71 2006 520 524 (Pubitemid 43814013)
    • (2006) Biochemistry (Moscow) , vol.71 , Issue.5 , pp. 520-524
    • Wang, S.1    Li, H.2
  • 16
    • 33847179441 scopus 로고    scopus 로고
    • The cytosolic ribonuclease inhibitor contributes to intracellular redox homeostasis
    • D.M. Monti, N. Montesano Gesualdi, J. Matousek, F. Esposito, and G. D'Alessio The cytosolic ribonuclease inhibitor contributes to intracellular redox homeostasis FEBS Lett. 581 2007 930 934
    • (2007) FEBS Lett. , vol.581 , pp. 930-934
    • Monti, D.M.1    Montesano Gesualdi, N.2    Matousek, J.3    Esposito, F.4    D'Alessio, G.5
  • 18
    • 65249129859 scopus 로고    scopus 로고
    • Angiogenin cleaves tRNA and promotes stress-induced translational repression
    • S. Yamasaki, P. Ivanov, G.F. Hu, and P. Anderson Angiogenin cleaves tRNA and promotes stress-induced translational repression J. Cell Biol. 185 2009 35 42
    • (2009) J. Cell Biol. , vol.185 , pp. 35-42
    • Yamasaki, S.1    Ivanov, P.2    Hu, G.F.3    Anderson, P.4
  • 20
    • 0024556511 scopus 로고
    • Expression of human placental ribonuclease inhibitor in Escherichia coli
    • DOI 10.1016/0006-291X(89)91628-8
    • F.S. Lee, and B.L. Vallee Expression of human placental ribonuclease inhibitor in Escherichia coli Biochem. Biophys. Res. Commun. 160 1989 115 120 (Pubitemid 19116469)
    • (1989) Biochemical and Biophysical Research Communications , vol.160 , Issue.1 , pp. 115-120
    • Lee, F.S.1    Vallee, B.L.2
  • 21
    • 36048939725 scopus 로고    scopus 로고
    • Hydrogen peroxide induces apoptosis in HeLa cells through mitochondrial pathway
    • DOI 10.1016/j.mito.2007.07.003, PII S1567724907001183
    • M. Singh, H. Sharma, and N. Singh Hydrogen peroxide induces apoptosis in HeLa cells through mitochondrial pathway Mitochondrion 7 2007 367 373 (Pubitemid 350082358)
    • (2007) Mitochondrion , vol.7 , Issue.6 , pp. 367-373
    • Singh, M.1    Sharma, H.2    Singh, N.3
  • 22
    • 0041810128 scopus 로고    scopus 로고
    • The adenine nucleotide translocase: A central component of the mitochondrial permeability transition pore and key player in cell death
    • A.P. Halestrap, and C. Brenner The adenine nucleotide translocase: a central component of the mitochondrial permeability transition pore and key player in cell death Curr. Med. Chem. 10 2003 1507 1525 (Pubitemid 36896553)
    • (2003) Current Medicinal Chemistry , vol.10 , Issue.16 , pp. 1507-1525
    • Halestrap, A.P.1    Brenner, C.2
  • 23
    • 13944277097 scopus 로고    scopus 로고
    • Angiogenin is translocated to the nucleus of HeLa cells and is involved in ribosomal RNA transcription and cell proliferation
    • DOI 10.1158/0008-5472.CAN-04-2058
    • T. Tsuji, Y. Sun, K. Kishimoto, K.A. Olson, S. Liu, S. Hirukawa, and G.F. Hu Angiogenin is translocated to the nucleus of HeLa cells and is involved in ribosomal RNA transcription and cell proliferation Cancer Res. 65 2005 1352 1360 (Pubitemid 40270162)
    • (2005) Cancer Research , vol.65 , Issue.4 , pp. 1352-1360
    • Tsuji, T.1    Sun, Y.2    Kishimoto, K.3    Olson, K.A.4    Liu, S.5    Hirukawa, S.6    Hu, G.-F.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.