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Volumn 141, Issue 6, 2010, Pages 1006-1017

A mammalian siderophore synthesized by an enzyme with a bacterial homolog involved in enterobactin production

Author keywords

Chembio; Proteins

Indexed keywords

2,3 DIHYDROXYBENZOIC ACID; 3 HYDROXYBUTYRATE DEHYDROGENASE; ENTEROCHELIN; GENTISIC ACID; HEME; IRON; NEUTROPHIL GELATINASE ASSOCIATED LIPOCALIN; REACTIVE OXYGEN METABOLITE; SIDEROPHORE; SMALL INTERFERING RNA;

EID: 77953690176     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cell.2010.04.040     Document Type: Article
Times cited : (248)

References (37)
  • 2
    • 47649126246 scopus 로고    scopus 로고
    • Forging a field: the golden age of iron biology
    • Andrews N.C. Forging a field: the golden age of iron biology. Blood 2008, 112:219-230.
    • (2008) Blood , vol.112 , pp. 219-230
    • Andrews, N.C.1
  • 3
    • 37849020181 scopus 로고    scopus 로고
    • A Novel iron-chelating derivative of the neuroprotective peptide NAPVSIPQ shows superior antioxidant and antineurodegenerative capabilities
    • Blat D., Weiner L., Youdim M.B., Fridkin M. A Novel iron-chelating derivative of the neuroprotective peptide NAPVSIPQ shows superior antioxidant and antineurodegenerative capabilities. J. Med. Chem. 2008, 51:126-134.
    • (2008) J. Med. Chem. , vol.51 , pp. 126-134
    • Blat, D.1    Weiner, L.2    Youdim, M.B.3    Fridkin, M.4
  • 6
    • 3042763187 scopus 로고    scopus 로고
    • Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity
    • Bulteau A.L., O'Neill H.A., Kennedy M.C., Ikeda-Saito M., Isaya G., Szweda L.I. Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity. Science 2004, 305:242-245.
    • (2004) Science , vol.305 , pp. 242-245
    • Bulteau, A.L.1    O'Neill, H.A.2    Kennedy, M.C.3    Ikeda-Saito, M.4    Isaya, G.5    Szweda, L.I.6
  • 7
    • 57649243073 scopus 로고    scopus 로고
    • Mitochondrial ferritin limits oxidative damage regulating mitochondrial iron availability: hypothesis for a protective role in Friedreich ataxia
    • Campanella A., Rovelli E., Santambrogio P., Cozzi A., Taroni F., Levi S. Mitochondrial ferritin limits oxidative damage regulating mitochondrial iron availability: hypothesis for a protective role in Friedreich ataxia. Hum. Mol. Genet. 2009, 18:1-11.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 1-11
    • Campanella, A.1    Rovelli, E.2    Santambrogio, P.3    Cozzi, A.4    Taroni, F.5    Levi, S.6
  • 9
    • 0035800508 scopus 로고    scopus 로고
    • Induction of apoptosis by a secreted lipocalin that is transcriptionally regulated by IL-3 deprivation
    • Devireddy L.R., Teodoro J.G., Richard F.A., Green M.R. Induction of apoptosis by a secreted lipocalin that is transcriptionally regulated by IL-3 deprivation. Science 2001, 293:829-834.
    • (2001) Science , vol.293 , pp. 829-834
    • Devireddy, L.R.1    Teodoro, J.G.2    Richard, F.A.3    Green, M.R.4
  • 10
    • 29244492306 scopus 로고    scopus 로고
    • A cell-surface receptor for lipocalin 24p3 selectively mediates apoptosis and iron uptake
    • Devireddy L.R., Gazin C., Zhu X., Green M.R. A cell-surface receptor for lipocalin 24p3 selectively mediates apoptosis and iron uptake. Cell 2005, 123:1293-1305.
    • (2005) Cell , vol.123 , pp. 1293-1305
    • Devireddy, L.R.1    Gazin, C.2    Zhu, X.3    Green, M.R.4
  • 11
    • 0034949363 scopus 로고    scopus 로고
    • Iron metabolism, free radicals, and oxidative injury
    • Emerit J., Beaumont C., Trivin F. Iron metabolism, free radicals, and oxidative injury. Biomed. Pharmacother. 2001, 55:333-339.
    • (2001) Biomed. Pharmacother. , vol.55 , pp. 333-339
    • Emerit, J.1    Beaumont, C.2    Trivin, F.3
  • 12
    • 0018232931 scopus 로고
    • Isolation and characterization of a siderophore-like growth factor from mutants of SV40-transformed cells adapted to picolinic acid
    • Fernandez-Pol J.A. Isolation and characterization of a siderophore-like growth factor from mutants of SV40-transformed cells adapted to picolinic acid. Cell 1978, 14:489-499.
    • (1978) Cell , vol.14 , pp. 489-499
    • Fernandez-Pol, J.A.1
  • 15
    • 0031567601 scopus 로고    scopus 로고
    • Deletion of the yeast homologue of the human gene associated with Friedreich's ataxia elicits iron accumulation in mitochondria
    • Foury F., Cazzalini O. Deletion of the yeast homologue of the human gene associated with Friedreich's ataxia elicits iron accumulation in mitochondria. FEBS Lett. 1997, 411:373-377.
    • (1997) FEBS Lett. , vol.411 , pp. 373-377
    • Foury, F.1    Cazzalini, O.2
  • 16
    • 0028075773 scopus 로고
    • Aconitase is a sensitive and critical target of oxygen poisoning in cultured mammalian cells and in rat lungs
    • Gardner P.R., Nguyen D.D., White C.W. Aconitase is a sensitive and critical target of oxygen poisoning in cultured mammalian cells and in rat lungs. Proc. Natl. Acad. Sci. USA 1994, 91:12248-12252.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 12248-12252
    • Gardner, P.R.1    Nguyen, D.D.2    White, C.W.3
  • 17
    • 0036865552 scopus 로고    scopus 로고
    • The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition
    • Goetz D.H., Holmes M.A., Borregaard N., Bluhm M.E., Raymond K.N., Strong R.K. The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition. Mol. Cell 2002, 10:1033-1043.
    • (2002) Mol. Cell , vol.10 , pp. 1033-1043
    • Goetz, D.H.1    Holmes, M.A.2    Borregaard, N.3    Bluhm, M.E.4    Raymond, K.N.5    Strong, R.K.6
  • 18
    • 33744541159 scopus 로고    scopus 로고
    • Characterization of human DHRS6, an orphan short chain dehydrogenase/reductase enzyme: a novel, cytosolic type 2 R-beta-hydroxybutyrate dehydrogenase
    • Guo K., Lukacik P., Papagrigoriou E., Meier M., Lee W.H., Adamski J., Oppermann U. Characterization of human DHRS6, an orphan short chain dehydrogenase/reductase enzyme: a novel, cytosolic type 2 R-beta-hydroxybutyrate dehydrogenase. J. Biol. Chem. 2006, 281:10291-10297.
    • (2006) J. Biol. Chem. , vol.281 , pp. 10291-10297
    • Guo, K.1    Lukacik, P.2    Papagrigoriou, E.3    Meier, M.4    Lee, W.H.5    Adamski, J.6    Oppermann, U.7
  • 19
    • 37249014601 scopus 로고    scopus 로고
    • Initiation of zebrafish haematopoiesis by the TATA-box-binding protein-related factor Trf3
    • Hart D.O., Raha T., Lawson N.D., Green M.R. Initiation of zebrafish haematopoiesis by the TATA-box-binding protein-related factor Trf3. Nature 2007, 450:1082-1085.
    • (2007) Nature , vol.450 , pp. 1082-1085
    • Hart, D.O.1    Raha, T.2    Lawson, N.D.3    Green, M.R.4
  • 20
    • 0020774067 scopus 로고
    • Erythropoiesis in the developing rainbow trout, Salmo gairdneri irideus: histochemical and immunochemical detection of erythropoietic organs
    • Iuchi I., Yamamoto M. Erythropoiesis in the developing rainbow trout, Salmo gairdneri irideus: histochemical and immunochemical detection of erythropoietic organs. J. Exp. Zool. 1983, 226:409-417.
    • (1983) J. Exp. Zool. , vol.226 , pp. 409-417
    • Iuchi, I.1    Yamamoto, M.2
  • 21
    • 0028788316 scopus 로고
    • Requirements for iron-regulated degradation of the RNA binding protein, iron regulatory protein 2
    • Iwai K., Klausner R.D., Rouault T.A. Requirements for iron-regulated degradation of the RNA binding protein, iron regulatory protein 2. EMBO J. 1995, 14:5350-5357.
    • (1995) EMBO J. , vol.14 , pp. 5350-5357
    • Iwai, K.1    Klausner, R.D.2    Rouault, T.A.3
  • 22
    • 0018889904 scopus 로고
    • Low molecular weight iron-binding factor from mammalian tissue that potentiates bacterial growth
    • Jones R.L., Peterson C.M., Grady R.W., Cerami A. Low molecular weight iron-binding factor from mammalian tissue that potentiates bacterial growth. J. Exp. Med. 1980, 151:418-428.
    • (1980) J. Exp. Med. , vol.151 , pp. 418-428
    • Jones, R.L.1    Peterson, C.M.2    Grady, R.W.3    Cerami, A.4
  • 23
    • 0037108199 scopus 로고    scopus 로고
    • The labile iron pool: characterization, measurement, and participation in cellular processes(1)
    • Kakhlon O., Cabantchik Z.I. The labile iron pool: characterization, measurement, and participation in cellular processes(1). Free Radic. Biol. Med. 2002, 33:1037-1046.
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 1037-1046
    • Kakhlon, O.1    Cabantchik, Z.I.2
  • 24
    • 0024616004 scopus 로고
    • Nucleotide sequence of a cluster of Escherichia coli enterobactin biosynthesis genes: identification of entA and purification of its product 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase
    • Liu J., Duncan K., Walsh C.T. Nucleotide sequence of a cluster of Escherichia coli enterobactin biosynthesis genes: identification of entA and purification of its product 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase. J. Bacteriol. 1989, 171:791-798.
    • (1989) J. Bacteriol. , vol.171 , pp. 791-798
    • Liu, J.1    Duncan, K.2    Walsh, C.T.3
  • 26
    • 14944387002 scopus 로고    scopus 로고
    • Iron trafficking in the mitochondrion: novel pathways revealed by disease
    • Napier I., Ponka P., Richardson D.R. Iron trafficking in the mitochondrion: novel pathways revealed by disease. Blood 2005, 105:1867-1874.
    • (2005) Blood , vol.105 , pp. 1867-1874
    • Napier, I.1    Ponka, P.2    Richardson, D.R.3
  • 27
    • 59449083869 scopus 로고    scopus 로고
    • Regulation of mitochondrial iron import through differential turnover of mitoferrin 1 and mitoferrin 2
    • Paradkar P.N., Zumbrennen K.B., Paw B.H., Ward D.M., Kaplan J. Regulation of mitochondrial iron import through differential turnover of mitoferrin 1 and mitoferrin 2. Mol. Cell. Biol. 2009, 29:1007-1016.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 1007-1016
    • Paradkar, P.N.1    Zumbrennen, K.B.2    Paw, B.H.3    Ward, D.M.4    Kaplan, J.5
  • 28
    • 0037974679 scopus 로고    scopus 로고
    • Mitochondrial complex I, aconitase, and succinate dehydrogenase during hypoxia-reoxygenation: modulation of enzyme activities by MnSOD
    • Powell C.S., Jackson R.M. Mitochondrial complex I, aconitase, and succinate dehydrogenase during hypoxia-reoxygenation: modulation of enzyme activities by MnSOD. Am. J. Physiol. Lung Cell. Mol. Physiol. 2003, 285:L189-L198.
    • (2003) Am. J. Physiol. Lung Cell. Mol. Physiol. , vol.285
    • Powell, C.S.1    Jackson, R.M.2
  • 29
    • 34547602992 scopus 로고    scopus 로고
    • Assessment of chelatable mitochondrial iron by using mitochondrion-selective fluorescent iron indicators with different iron-binding affinities
    • Rauen U., Springer A., Weisheit D., Petrat F., Korth H.G., de Groot H., Sustmann R. Assessment of chelatable mitochondrial iron by using mitochondrion-selective fluorescent iron indicators with different iron-binding affinities. ChemBioChem 2007, 8:341-352.
    • (2007) ChemBioChem , vol.8 , pp. 341-352
    • Rauen, U.1    Springer, A.2    Weisheit, D.3    Petrat, F.4    Korth, H.G.5    de Groot, H.6    Sustmann, R.7
  • 30
    • 0037389797 scopus 로고    scopus 로고
    • Enterobactin: an archetype for microbial iron transport
    • Raymond K.N., Dertz E.A., Kim S.S. Enterobactin: an archetype for microbial iron transport. Proc. Natl. Acad. Sci. USA 2003, 100:3584-3588.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 3584-3588
    • Raymond, K.N.1    Dertz, E.A.2    Kim, S.S.3
  • 31
    • 17144378216 scopus 로고    scopus 로고
    • Iron-sulphur cluster biogenesis and mitochondrial iron homeostasis
    • Rouault T.A., Tong W.H. Iron-sulphur cluster biogenesis and mitochondrial iron homeostasis. Nat. Rev. Mol. Cell Biol. 2005, 6:345-351.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 345-351
    • Rouault, T.A.1    Tong, W.H.2
  • 32
    • 0026062191 scopus 로고
    • Structural relationship between an iron-regulated RNA-binding protein (IRE-BP) and aconitase: functional implications
    • Rouault T.A., Stout C.D., Kaptain S., Harford J.B., Klausner R.D. Structural relationship between an iron-regulated RNA-binding protein (IRE-BP) and aconitase: functional implications. Cell 1991, 64:881-883.
    • (1991) Cell , vol.64 , pp. 881-883
    • Rouault, T.A.1    Stout, C.D.2    Kaptain, S.3    Harford, J.B.4    Klausner, R.D.5
  • 34
    • 45849123222 scopus 로고    scopus 로고
    • A cytosolic iron chaperone that delivers iron to ferritin
    • Shi H., Bencze K.Z., Stemmler T.L., Philpott C.C. A cytosolic iron chaperone that delivers iron to ferritin. Science 2008, 320:1207-1210.
    • (2008) Science , vol.320 , pp. 1207-1210
    • Shi, H.1    Bencze, K.Z.2    Stemmler, T.L.3    Philpott, C.C.4
  • 35
    • 0034468736 scopus 로고    scopus 로고
    • Role of reactive oxygen species (ROS) in apoptosis induction
    • Simon H.U., Haj-Yehia A., Levi-Schaffer F. Role of reactive oxygen species (ROS) in apoptosis induction. Apoptosis 2000, 5:415-418.
    • (2000) Apoptosis , vol.5 , pp. 415-418
    • Simon, H.U.1    Haj-Yehia, A.2    Levi-Schaffer, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.