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Volumn 1800, Issue 8, 2010, Pages 806-814

Ferritins and iron storage in plants

Author keywords

Chloroplast; Iron homeostasis; Oxidative stress; Vacuole

Indexed keywords

FERRITIN; IRON; MUTANT PROTEIN;

EID: 77953811994     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2009.12.003     Document Type: Review
Times cited : (270)

References (69)
  • 2
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: molecular properties, iron storage function and cellular regulation
    • Harrison P.M., Arosio P. The ferritins: molecular properties, iron storage function and cellular regulation. Biochim. Biophys. Acta 1996, 1275:161-203.
    • (1996) Biochim. Biophys. Acta , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 3
    • 67349100157 scopus 로고    scopus 로고
    • Ferritins: a family of molecules for iron storage, antioxidation and more
    • Arosio P., Ingrassia R., Cavadini P. Ferritins: a family of molecules for iron storage, antioxidation and more. Biochim. Biophys. Acta 2009, 1790:589-599.
    • (2009) Biochim. Biophys. Acta , vol.1790 , pp. 589-599
    • Arosio, P.1    Ingrassia, R.2    Cavadini, P.3
  • 4
    • 0025186372 scopus 로고
    • Evidence for a conservation of ferritin sequences among plants and animals and for a transit peptide in soybean
    • Ragland M., Briat J.F., Gagnon J., Laulhère J.P., Massenet O., Theil E.C. Evidence for a conservation of ferritin sequences among plants and animals and for a transit peptide in soybean. J. Biol. Chem. 1990, 265:18339-18344.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18339-18344
    • Ragland, M.1    Briat, J.F.2    Gagnon, J.3    Laulhère, J.P.4    Massenet, O.5    Theil, E.C.6
  • 5
    • 0025970277 scopus 로고
    • Ferritin accumulation and degradation in different organs of pea (Pisum sativum) during development
    • Lobréaux S., Briat J.F. Ferritin accumulation and degradation in different organs of pea (Pisum sativum) during development. Biochem. J. 1991, 274:601-606.
    • (1991) Biochem. J. , vol.274 , pp. 601-606
    • Lobréaux, S.1    Briat, J.F.2
  • 6
    • 0028938594 scopus 로고
    • Conformational changes and in vitro core-formation modifications induced by site-directed mutagenesis of the specific N-terminus of pea seed ferritin
    • van Wuytswinkel O., Briat J.F. Conformational changes and in vitro core-formation modifications induced by site-directed mutagenesis of the specific N-terminus of pea seed ferritin. Biochem. J. 1995, 305:959-965.
    • (1995) Biochem. J. , vol.305 , pp. 959-965
    • van Wuytswinkel, O.1    Briat, J.F.2
  • 7
    • 0027056014 scopus 로고
    • Amino-acid sequence and predicted three-dimensional structure of pea seed (Pisum sativum) ferritin
    • Lobréaux S., Yewdall S., Briat J.F., Harrison P.M. Amino-acid sequence and predicted three-dimensional structure of pea seed (Pisum sativum) ferritin. Biochem. J. 1992, 288:931-939.
    • (1992) Biochem. J. , vol.288 , pp. 931-939
    • Lobréaux, S.1    Yewdall, S.2    Briat, J.F.3    Harrison, P.M.4
  • 9
    • 0024977973 scopus 로고
    • Mechanism of the transition from plant ferritin to phytosiderin
    • Laulhère J.P., Labouré A.M., Briat J.F. Mechanism of the transition from plant ferritin to phytosiderin. J. Biol. Chem. 1989, 264:3629-3635.
    • (1989) J. Biol. Chem. , vol.264 , pp. 3629-3635
    • Laulhère, J.P.1    Labouré, A.M.2    Briat, J.F.3
  • 10
    • 0034649566 scopus 로고    scopus 로고
    • Analysis of the genome sequence of the flowering plant Arabidopsis thaliana
    • AGI (Arabidopsis Genome Initiative)
    • Analysis of the genome sequence of the flowering plant Arabidopsis thaliana. Nature 2000, 408:796-815. AGI (Arabidopsis Genome Initiative).
    • (2000) Nature , vol.408 , pp. 796-815
  • 11
    • 58849163578 scopus 로고    scopus 로고
    • Ferritins control interaction between iron homeostasis and oxidative stress in Arabidopsis
    • Ravet K., Touraine B., Boucherez J., Briat J.F., Gaymard F., Cellier F. Ferritins control interaction between iron homeostasis and oxidative stress in Arabidopsis. Plant J. 2009, 57:400-412.
    • (2009) Plant J. , vol.57 , pp. 400-412
    • Ravet, K.1    Touraine, B.2    Boucherez, J.3    Briat, J.F.4    Gaymard, F.5    Cellier, F.6
  • 12
    • 0035379652 scopus 로고    scopus 로고
    • A novel plant ferritin subunit from soybean that is related to a mechanism in iron release
    • Masuda T., Goto F., Yoshihara T. A novel plant ferritin subunit from soybean that is related to a mechanism in iron release. J. Biol. Chem. 2001, 276:19575-19579.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19575-19579
    • Masuda, T.1    Goto, F.2    Yoshihara, T.3
  • 13
    • 58849146095 scopus 로고    scopus 로고
    • Two different H-type subunits from pea seed (Pisum sativum) ferritin that are responsible for fast Fe(II) oxidation
    • Li C., Hu X., Zhao G. Two different H-type subunits from pea seed (Pisum sativum) ferritin that are responsible for fast Fe(II) oxidation. Biochimie 2009, 91:230-239.
    • (2009) Biochimie , vol.91 , pp. 230-239
    • Li, C.1    Hu, X.2    Zhao, G.3
  • 16
    • 0028854811 scopus 로고
    • Purification and characterization of recombinant pea-seed ferritins expressed in Escherichia coli: influence of N-terminus deletions on protein solubility and core formation in vitro
    • van Wuytswinkel O., Savino G., Briat J.F. Purification and characterization of recombinant pea-seed ferritins expressed in Escherichia coli: influence of N-terminus deletions on protein solubility and core formation in vitro. Biochem. J. 1995, 305:253-261.
    • (1995) Biochem. J. , vol.305 , pp. 253-261
    • van Wuytswinkel, O.1    Savino, G.2    Briat, J.F.3
  • 17
    • 0027523668 scopus 로고
    • Iron release and uptake by plant ferritin: effects of pH, reduction and chelation
    • Laulhère J.P., Briat J.F. Iron release and uptake by plant ferritin: effects of pH, reduction and chelation. Biochem. J. 1993, 290:693-699.
    • (1993) Biochem. J. , vol.290 , pp. 693-699
    • Laulhère, J.P.1    Briat, J.F.2
  • 18
    • 0025298553 scopus 로고
    • Photoreduction and incorporation of iron into ferritins
    • Laulhère J.P., Labouré A.M., Briat J.F. Photoreduction and incorporation of iron into ferritins. Biochem. J. 1990, 269:79-84.
    • (1990) Biochem. J. , vol.269 , pp. 79-84
    • Laulhère, J.P.1    Labouré, A.M.2    Briat, J.F.3
  • 19
    • 0023646092 scopus 로고
    • Reconstituted and native iron-cores of bacterioferritin and ferritin
    • Mann S., Williams J.M., Treffry A., Harrison P.M. Reconstituted and native iron-cores of bacterioferritin and ferritin. J. Mol. Biol. 1987, 198:405-416.
    • (1987) J. Mol. Biol. , vol.198 , pp. 405-416
    • Mann, S.1    Williams, J.M.2    Treffry, A.3    Harrison, P.M.4
  • 23
    • 84959964018 scopus 로고
    • Ferreting out the secret of plant ferritin-a review
    • Seckback J.J. Ferreting out the secret of plant ferritin-a review. J. Plant Nutr. 1982, 5:369-394.
    • (1982) J. Plant Nutr. , vol.5 , pp. 369-394
    • Seckback, J.J.1
  • 24
    • 0021104879 scopus 로고
    • Phytoferritin is synthesized in vitro as a high-molecular-weight precursor
    • Van der Mark F., Van der Briel W., Huisman H.G. Phytoferritin is synthesized in vitro as a high-molecular-weight precursor. Biochem. J. 1983, 214:943-950.
    • (1983) Biochem. J. , vol.214 , pp. 943-950
    • Van der Mark, F.1    Van der Briel, W.2    Huisman, H.G.3
  • 25
    • 0000242126 scopus 로고
    • Iron induction of ferritin synthesis in soyabean cell suspensions
    • Proudhon D., Briat J.F., Lescure A.M. Iron induction of ferritin synthesis in soyabean cell suspensions. Plant Physiol. 1989, 90:586-590.
    • (1989) Plant Physiol. , vol.90 , pp. 586-590
    • Proudhon, D.1    Briat, J.F.2    Lescure, A.M.3
  • 27
    • 0029944620 scopus 로고    scopus 로고
    • Ferritin gene organization: differences between plants and animals suggest possible kingdom-specific selective constraints
    • Proudhon D., Wei J., Briat J.F., Theil E.C. Ferritin gene organization: differences between plants and animals suggest possible kingdom-specific selective constraints. J. Mol. Evol. 1996, 42:325-336.
    • (1996) J. Mol. Evol. , vol.42 , pp. 325-336
    • Proudhon, D.1    Wei, J.2    Briat, J.F.3    Theil, E.C.4
  • 28
    • 0024542834 scopus 로고
    • Domain structure of mitochondrial and chloroplast targeting peptides
    • Von Heijne G.V., Steppuhn J., Herrmann R.G. Domain structure of mitochondrial and chloroplast targeting peptides. Eur. J. Biochem. 1989, 180:535-545.
    • (1989) Eur. J. Biochem. , vol.180 , pp. 535-545
    • Von Heijne, G.V.1    Steppuhn, J.2    Herrmann, R.G.3
  • 29
    • 0025200444 scopus 로고
    • Purification and characterization of an iron-induced ferritin from soybean (Glycine max) cell suspensions
    • Lescure A.M., Massenet O., Briat J.F. Purification and characterization of an iron-induced ferritin from soybean (Glycine max) cell suspensions. Biochem. J. 1990, 272:147-150.
    • (1990) Biochem. J. , vol.272 , pp. 147-150
    • Lescure, A.M.1    Massenet, O.2    Briat, J.F.3
  • 30
    • 0026887039 scopus 로고
    • Iron induces ferritin synthesis in maize plantlets
    • Lobréaux S., Massenet O., Briat J.F. Iron induces ferritin synthesis in maize plantlets. Plant Mol. Biol. 1992, 19:563-575.
    • (1992) Plant Mol. Biol. , vol.19 , pp. 563-575
    • Lobréaux, S.1    Massenet, O.2    Briat, J.F.3
  • 31
    • 0029788634 scopus 로고    scopus 로고
    • Characterization of a ferritin mRNA from Arabidopsis thaliana accumulated in response to iron through an oxidative pathway independant of abscisic acid
    • Gaymard F., Boucherez J., Briat J.F. Characterization of a ferritin mRNA from Arabidopsis thaliana accumulated in response to iron through an oxidative pathway independant of abscisic acid. Biochem. J. 1996, 15:67-73.
    • (1996) Biochem. J. , vol.15 , pp. 67-73
    • Gaymard, F.1    Boucherez, J.2    Briat, J.F.3
  • 32
    • 0026227806 scopus 로고
    • The structure of a Phaseolus vulgaris cDNA encoding the iron storage protein ferritin
    • Spence M.J., Henzl M.T., Lammers P.J. The structure of a Phaseolus vulgaris cDNA encoding the iron storage protein ferritin. Plant Mol. Biol. 1991, 17:499-504.
    • (1991) Plant Mol. Biol. , vol.17 , pp. 499-504
    • Spence, M.J.1    Henzl, M.T.2    Lammers, P.J.3
  • 34
    • 35348996059 scopus 로고    scopus 로고
    • Iron dynamics in plants
    • Briat J.F. Iron dynamics in plants. Adv. Bot. Res. 2008, 46:138-180.
    • (2008) Adv. Bot. Res. , vol.46 , pp. 138-180
    • Briat, J.F.1
  • 35
    • 0000578020 scopus 로고
    • Transport of iron into leaves following iron resupply to iron-stressed sugar beet plants
    • Young T.F., Terry N. Transport of iron into leaves following iron resupply to iron-stressed sugar beet plants. J. Plant Nutr. 1982, 5:1273-1283.
    • (1982) J. Plant Nutr. , vol.5 , pp. 1273-1283
    • Young, T.F.1    Terry, N.2
  • 36
    • 0027472177 scopus 로고
    • Abscisic acid is involved in the iron-induced synthesis of maize ferritin
    • Lobréaux S., Hardy T., Briat J.F. Abscisic acid is involved in the iron-induced synthesis of maize ferritin. EMBO J. 1993, 12:651-657.
    • (1993) EMBO J. , vol.12 , pp. 651-657
    • Lobréaux, S.1    Hardy, T.2    Briat, J.F.3
  • 37
    • 0035937161 scopus 로고    scopus 로고
    • Characterization of an iron dependent regulatory sequence (IDRS) involved in the transcriptional control of AtFer1 and ZmFer1 plant ferritin genes by iron
    • Petit J.M., Van Wuytswinkel O., Briat J.F., Lobréaux S. Characterization of an iron dependent regulatory sequence (IDRS) involved in the transcriptional control of AtFer1 and ZmFer1 plant ferritin genes by iron. J. Biol. Chem. 2001, 276:5584-5590.
    • (2001) J. Biol. Chem. , vol.276 , pp. 5584-5590
    • Petit, J.M.1    Van Wuytswinkel, O.2    Briat, J.F.3    Lobréaux, S.4
  • 38
    • 0034625385 scopus 로고    scopus 로고
    • Identification and characterization of the iron regulatory element in the ferritin gene of a plant (soybean)
    • Wei J., Theil E.C. Identification and characterization of the iron regulatory element in the ferritin gene of a plant (soybean). J. Biol. Chem. 2000, 275:17488-17493.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17488-17493
    • Wei, J.1    Theil, E.C.2
  • 39
    • 0024516594 scopus 로고
    • Oxidation-reduction and the molecular mechanism of a regulatory RNA-protein interaction
    • Hentze M.W., Rouault T.A., Harford J.B., Klausner R.D. Oxidation-reduction and the molecular mechanism of a regulatory RNA-protein interaction. Science 1989, 244:357-359.
    • (1989) Science , vol.244 , pp. 357-359
    • Hentze, M.W.1    Rouault, T.A.2    Harford, J.B.3    Klausner, R.D.4
  • 42
    • 77951995410 scopus 로고    scopus 로고
    • New insights into ferritin synthesis and function highlight a link between iron homeostasis and oxidative stress in plants
    • doi: mcp128 [pii]10.1093/aob/mcp128.
    • Briat J.F., Ravet K., Arnaud N., Duc C., Boucherez J., Touraine B., Cellier F., Gaymard F. New insights into ferritin synthesis and function highlight a link between iron homeostasis and oxidative stress in plants. Ann. Bot. 2009, doi: mcp128 [pii]10.1093/aob/mcp128.
    • (2009) Ann. Bot.
    • Briat, J.F.1    Ravet, K.2    Arnaud, N.3    Duc, C.4    Boucherez, J.5    Touraine, B.6    Cellier, F.7    Gaymard, F.8
  • 43
    • 33747667570 scopus 로고    scopus 로고
    • An iron-induced nitric oxide burst precedes ubiquitin-dependent protein degradation for Arabidopsis AtFer1 ferritin gene expression
    • Arnaud N., Murgia I., Boucherez J., Briat J.F., Cellier F., Gaymard F. An iron-induced nitric oxide burst precedes ubiquitin-dependent protein degradation for Arabidopsis AtFer1 ferritin gene expression. J. Biol. Chem. 2006, 18:23579-23588.
    • (2006) J. Biol. Chem. , vol.18 , pp. 23579-23588
    • Arnaud, N.1    Murgia, I.2    Boucherez, J.3    Briat, J.F.4    Cellier, F.5    Gaymard, F.6
  • 44
    • 0037125975 scopus 로고    scopus 로고
    • Nitrogen monoxide-mediated control of ferritin synthesis: implications for macrophage iron homeostasis
    • Kim S., Ponka P. Nitrogen monoxide-mediated control of ferritin synthesis: implications for macrophage iron homeostasis. Proc. Natl. Acad. Sci. U.S.A. 2002, 17:12214-12219.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.17 , pp. 12214-12219
    • Kim, S.1    Ponka, P.2
  • 45
    • 0037354312 scopus 로고    scopus 로고
    • Role of nitric oxide in cellular iron metabolism
    • Kim S., Ponka P. Role of nitric oxide in cellular iron metabolism. Biometals 2003, 16:125-135.
    • (2003) Biometals , vol.16 , pp. 125-135
    • Kim, S.1    Ponka, P.2
  • 46
    • 0347624596 scopus 로고    scopus 로고
    • S-nitrosylation of IRP2 regulates its stability via the ubiquitin-proteasome pathway
    • Kim S., Wing S.S., Ponka P. S-nitrosylation of IRP2 regulates its stability via the ubiquitin-proteasome pathway. Mol. Cell Biol. 2004, 24:330-337.
    • (2004) Mol. Cell Biol. , vol.24 , pp. 330-337
    • Kim, S.1    Wing, S.S.2    Ponka, P.3
  • 48
    • 73649085487 scopus 로고    scopus 로고
    • Regulation of iron homeostasis in Arabidopsis thaliana by the clock regulator time for coffee
    • Duc C., Cellier F., Lobréaux S., Briat J.F., Gaymard F. Regulation of iron homeostasis in Arabidopsis thaliana by the clock regulator time for coffee. J. Biol. Chem. 2009, 284:36271-36281.
    • (2009) J. Biol. Chem. , vol.284 , pp. 36271-36281
    • Duc, C.1    Cellier, F.2    Lobréaux, S.3    Briat, J.F.4    Gaymard, F.5
  • 49
    • 34347393267 scopus 로고    scopus 로고
    • TIME FOR COFFEE encodes a nuclear regulator in the Arabidopsis thaliana circadian clock
    • Ding Z., Millar A.J., Davis A.M., Davis S.J. TIME FOR COFFEE encodes a nuclear regulator in the Arabidopsis thaliana circadian clock. Plant Cell 2007, 19:1522-1536.
    • (2007) Plant Cell , vol.19 , pp. 1522-1536
    • Ding, Z.1    Millar, A.J.2    Davis, A.M.3    Davis, S.J.4
  • 51
    • 0141676561 scopus 로고    scopus 로고
    • Differential involvement of the IDRS cis-element in the developmental and environmental regulation of the AtFer1 ferritin gene from Arabidopsis
    • Tarantino D., Petit J.M., Lobréaux S., Briat J.F., Soave C., Murgia I. Differential involvement of the IDRS cis-element in the developmental and environmental regulation of the AtFer1 ferritin gene from Arabidopsis. Planta 2003, 217:709-716.
    • (2003) Planta , vol.217 , pp. 709-716
    • Tarantino, D.1    Petit, J.M.2    Lobréaux, S.3    Briat, J.F.4    Soave, C.5    Murgia, I.6
  • 53
    • 34548190012 scopus 로고    scopus 로고
    • A central integrator of transcription networks in plant stress and energy signalling
    • Baena-Gonzalez E., Rolland F., Thevelein J.M., Sheen J. A central integrator of transcription networks in plant stress and energy signalling. Nature 2007, 448:938-942.
    • (2007) Nature , vol.448 , pp. 938-942
    • Baena-Gonzalez, E.1    Rolland, F.2    Thevelein, J.M.3    Sheen, J.4
  • 55
    • 67649173091 scopus 로고    scopus 로고
    • Arabidopsis mutants reveal multiple singlet oxygen signaling pathways involved in stress response and development
    • Baruah A., Simkova K., Apel K., Laloi C. Arabidopsis mutants reveal multiple singlet oxygen signaling pathways involved in stress response and development. Plant Mol. Biol. 2009, 70:547-563.
    • (2009) Plant Mol. Biol. , vol.70 , pp. 547-563
    • Baruah, A.1    Simkova, K.2    Apel, K.3    Laloi, C.4
  • 56
    • 70349479573 scopus 로고    scopus 로고
    • 2-mediated retrograde signaling by the PLEIOTROPIC RESPONSE LOCUS 1 (PRL1) protein, a central integrator of stress and energy signaling
    • 2-mediated retrograde signaling by the PLEIOTROPIC RESPONSE LOCUS 1 (PRL1) protein, a central integrator of stress and energy signaling. Plant J. 2009, 60:20-32.
    • (2009) Plant J. , vol.60 , pp. 20-32
    • Baruah, A.1    Simkova, K.2    Hincha, D.K.3    Apel, K.4    Laloi, C.5
  • 57
    • 0343145729 scopus 로고    scopus 로고
    • Iron transport and storage in plants
    • Briat J.F., Lobréaux S. Iron transport and storage in plants. Trends Plant. Sci. 1997, 2:187-193.
    • (1997) Trends Plant. Sci. , vol.2 , pp. 187-193
    • Briat, J.F.1    Lobréaux, S.2
  • 58
    • 0009740235 scopus 로고
    • Plant and microbial ferritins
    • Academic Press, San Diego, L.L. Barton, B.C. Hemming (Eds.)
    • Theil E.C., Hase T. Plant and microbial ferritins. Iron Chelation in Plants and Soil Microorganisms 1993, 133-156. Academic Press, San Diego. L.L. Barton, B.C. Hemming (Eds.).
    • (1993) Iron Chelation in Plants and Soil Microorganisms , pp. 133-156
    • Theil, E.C.1    Hase, T.2
  • 59
    • 0035504261 scopus 로고    scopus 로고
    • Structure and differential expression of the four members of the Arabidopsis thaliana ferritin gene family
    • Petit J.M., Briat J.F., Lobréaux S. Structure and differential expression of the four members of the Arabidopsis thaliana ferritin gene family. Biochem. J. 2001, 359:575-582.
    • (2001) Biochem. J. , vol.359 , pp. 575-582
    • Petit, J.M.1    Briat, J.F.2    Lobréaux, S.3
  • 62
    • 70349598131 scopus 로고    scopus 로고
    • Post-translational regulation of AtFER2 ferritin in response to intracellular iron trafficking during fruit development in Arabidopsis
    • Ravet K., Touraine B., Kim S.A., Cellier F., Thomine S., Guerinot M.L., Briat J.F., Gaymard F. Post-translational regulation of AtFER2 ferritin in response to intracellular iron trafficking during fruit development in Arabidopsis. Mol. Plant 2009, 2:1095-1106.
    • (2009) Mol. Plant , vol.2 , pp. 1095-1106
    • Ravet, K.1    Touraine, B.2    Kim, S.A.3    Cellier, F.4    Thomine, S.5    Guerinot, M.L.6    Briat, J.F.7    Gaymard, F.8
  • 63
    • 0002252779 scopus 로고    scopus 로고
    • Addressing micronutrient malnutrition through enhancing the nutritional quality of staple foods: principles, perspectives and knowledge gaps
    • Graham R.D. Addressing micronutrient malnutrition through enhancing the nutritional quality of staple foods: principles, perspectives and knowledge gaps. Adv. Agron. 2001, 70:77-142.
    • (2001) Adv. Agron. , vol.70 , pp. 77-142
    • Graham, R.D.1
  • 64
    • 0038605301 scopus 로고    scopus 로고
    • Micronutrient fortification of plants through plant breeding: can it improve nutrition in man at low cost
    • Bouis H.E. Micronutrient fortification of plants through plant breeding: can it improve nutrition in man at low cost. Proc. Nutr. Soc. 2003, 62:403-411.
    • (2003) Proc. Nutr. Soc. , vol.62 , pp. 403-411
    • Bouis, H.E.1
  • 65
    • 52049104256 scopus 로고    scopus 로고
    • FER1 and FER2 encoding two ferritin complexes in Chlamydomonas reinhardtii chloroplasts are regulated by iron
    • Long J.C., Sommer F., Allen M.D., Lu S.F., Merchant S.S. FER1 and FER2 encoding two ferritin complexes in Chlamydomonas reinhardtii chloroplasts are regulated by iron. Genetics 2008, 179:137-147.
    • (2008) Genetics , vol.179 , pp. 137-147
    • Long, J.C.1    Sommer, F.2    Allen, M.D.3    Lu, S.F.4    Merchant, S.S.5
  • 66
    • 55249089750 scopus 로고    scopus 로고
    • Ferritin is required for rapid remodeling of the photosynthetic apparatus and minimizes photo-oxidative stress in response to iron availability in Chlamydomonas reinhardtii
    • Busch A., Rimbauld B., Naumann B., Rensch S., Hippler M. Ferritin is required for rapid remodeling of the photosynthetic apparatus and minimizes photo-oxidative stress in response to iron availability in Chlamydomonas reinhardtii. Plant J. 2008, 55:201-211.
    • (2008) Plant J. , vol.55 , pp. 201-211
    • Busch, A.1    Rimbauld, B.2    Naumann, B.3    Rensch, S.4    Hippler, M.5
  • 67
    • 55649116603 scopus 로고    scopus 로고
    • Photo-oxidative stress impacts the expression of genes encoding iron metabolism components in Chlamydomonas
    • Long J.C., Merchant S.S. Photo-oxidative stress impacts the expression of genes encoding iron metabolism components in Chlamydomonas. Photochem. Photobiol. 2008, 84:1395-1403.
    • (2008) Photochem. Photobiol. , vol.84 , pp. 1395-1403
    • Long, J.C.1    Merchant, S.S.2
  • 68
    • 22544481462 scopus 로고    scopus 로고
    • Siderophore-mediated upregulation of Arabidopsis ferritin expression in response to Erwinia chrysanthemi infection
    • Dellagi A., Rigault M., Segond D., Roux C., Kraepiel Y., Cellier F., Briat J.F., Gaymard F., Expert D. Siderophore-mediated upregulation of Arabidopsis ferritin expression in response to Erwinia chrysanthemi infection. Plant J. 2005, 43:262-272.
    • (2005) Plant J. , vol.43 , pp. 262-272
    • Dellagi, A.1    Rigault, M.2    Segond, D.3    Roux, C.4    Kraepiel, Y.5    Cellier, F.6    Briat, J.F.7    Gaymard, F.8    Expert, D.9
  • 69
    • 72649083340 scopus 로고    scopus 로고
    • A new family of ferritin genes from Lupinus luteus-comparative analysis of plant ferritins, their gene structure, and evolution
    • doi: msp196 [pii]10.1093/molbev/msp196.
    • Strozycki P.M., Szymanski M., Szczurek A., Barciszewski J., Figlerowicz M. A new family of ferritin genes from Lupinus luteus-comparative analysis of plant ferritins, their gene structure, and evolution. Mol. Biol. Evol. 2009, doi: msp196 [pii]10.1093/molbev/msp196.
    • (2009) Mol. Biol. Evol.
    • Strozycki, P.M.1    Szymanski, M.2    Szczurek, A.3    Barciszewski, J.4    Figlerowicz, M.5


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