메뉴 건너뛰기




Volumn 22, Issue 2, 2011, Pages 300-307

The value of Arabidopsis research in understanding human disease states

Author keywords

[No Author keywords available]

Indexed keywords

ALZHEIMER'S; ARABIDOPSIS; ARABIDOPSIS THALIANA; CELLULAR PROCESS; HUMAN DISEASE; HUMAN GENOMES; KEY MODELS; MOLECULAR MECHANISM; NEURODEGENERATIVE DISORDERS; NEUROLOGICAL DISORDERS; PARKINSON'S DISEASE; PLANT BIOLOGY; PROTEIN FUNCTIONS;

EID: 79954418589     PISSN: 09581669     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.copbio.2010.11.007     Document Type: Review
Times cited : (24)

References (62)
  • 3
    • 77957743879 scopus 로고    scopus 로고
    • ROS removal by DJ-1: ARABIDOPSIS as a new model to understand Parkinson disease
    • Xu X.M., Møller S.G. ROS removal by DJ-1: ARABIDOPSIS as a new model to understand Parkinson disease. Plant Signal Behav 2010, 5.
    • (2010) Plant Signal Behav , pp. 5
    • Xu, X.M.1    Møller, S.G.2
  • 4
    • 3943092621 scopus 로고    scopus 로고
    • Pathways towards and away from Alzheimer's disease
    • Mattson M.P. Pathways towards and away from Alzheimer's disease. Nature 2004, 430:631-639.
    • (2004) Nature , vol.430 , pp. 631-639
    • Mattson, M.P.1
  • 5
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: genes, proteins, and therapy
    • Selkoe D.J. Alzheimer's disease: genes, proteins, and therapy. Physiol Rev 2001, 81:741-766.
    • (2001) Physiol Rev , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 6
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics
    • Hardy J., Selkoe D.J. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 2002, 297:353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 7
    • 39149122810 scopus 로고    scopus 로고
    • Amyloid beta, mitochondrial dysfunction and synaptic damage: implications for cognitive decline in aging and Alzheimer's disease
    • Reddy P.H., Beal M.F. Amyloid beta, mitochondrial dysfunction and synaptic damage: implications for cognitive decline in aging and Alzheimer's disease. Trends Mol Med 2008, 14:45-53.
    • (2008) Trends Mol Med , vol.14 , pp. 45-53
    • Reddy, P.H.1    Beal, M.F.2
  • 8
    • 77953886784 scopus 로고    scopus 로고
    • Current status on Alzheimer disease molecular genetics: from past, to present, to future
    • Bettens K., Sleegers K., Van Broeckhoven C. Current status on Alzheimer disease molecular genetics: from past, to present, to future. Hum Mol Genet 2010, 19:R4-R11.
    • (2010) Hum Mol Genet , vol.19
    • Bettens, K.1    Sleegers, K.2    Van Broeckhoven, C.3
  • 9
    • 70449393908 scopus 로고    scopus 로고
    • Mitochondria and Alzheimer's disease: amyloid-beta peptide uptake and degradation by the presequence protease, hPreP
    • Alikhani N., Ankarcrona M., Glaser E. Mitochondria and Alzheimer's disease: amyloid-beta peptide uptake and degradation by the presequence protease, hPreP. J Bioenerg Biomembr 2009, 41:447-451.
    • (2009) J Bioenerg Biomembr , vol.41 , pp. 447-451
    • Alikhani, N.1    Ankarcrona, M.2    Glaser, E.3
  • 10
    • 77953772172 scopus 로고    scopus 로고
    • The organellar peptidasome, PreP: a journey from Arabidopsis to Alzheimer's disease
    • Glaser E., Alikhani N. The organellar peptidasome, PreP: a journey from Arabidopsis to Alzheimer's disease. Biochim Biophys Acta 2010, 1797:1076-1080.
    • (2010) Biochim Biophys Acta , vol.1797 , pp. 1076-1080
    • Glaser, E.1    Alikhani, N.2
  • 11
    • 0034254704 scopus 로고    scopus 로고
    • Rapid degradation of the presequence of the f1beta precursor of the ATP synthase inside mitochondria
    • Stahl A., Pavlov P.F., Szigyarto C., Glaser E. Rapid degradation of the presequence of the f1beta precursor of the ATP synthase inside mitochondria. Biochem J 2000, 349(Pt 3):703-707.
    • (2000) Biochem J , vol.349 , Issue.PART 3 , pp. 703-707
    • Stahl, A.1    Pavlov, P.F.2    Szigyarto, C.3    Glaser, E.4
  • 12
    • 0036828801 scopus 로고    scopus 로고
    • Isolation and identification of a novel mitochondrial metalloprotease (PreP) that degrades targeting presequences in plants
    • Stahl A., Moberg P., Ytterberg J., Panfilov O., Brockenhuus Von Lowenhielm H., Nilsson F., Glaser E. Isolation and identification of a novel mitochondrial metalloprotease (PreP) that degrades targeting presequences in plants. J Biol Chem 2002, 277:41931-41939.
    • (2002) J Biol Chem , vol.277 , pp. 41931-41939
    • Stahl, A.1    Moberg, P.2    Ytterberg, J.3    Panfilov, O.4    Brockenhuus Von Lowenhielm, H.5    Nilsson, F.6    Glaser, E.7
  • 13
    • 9644276886 scopus 로고    scopus 로고
    • Shaping the mitochondrial proteome
    • Gabaldon T., Huynen M.A. Shaping the mitochondrial proteome. Biochim Biophys Acta 2004, 1659:212-220.
    • (2004) Biochim Biophys Acta , vol.1659 , pp. 212-220
    • Gabaldon, T.1    Huynen, M.A.2
  • 15
    • 0344668824 scopus 로고    scopus 로고
    • Characterization of a novel zinc metalloprotease involved in degrading targeting peptides in mitochondria and chloroplasts
    • Moberg P., Stahl A., Bhushan S., Wright S.J., Eriksson A., Bruce B.D., Glaser E. Characterization of a novel zinc metalloprotease involved in degrading targeting peptides in mitochondria and chloroplasts. Plant J 2003, 36:616-628.
    • (2003) Plant J , vol.36 , pp. 616-628
    • Moberg, P.1    Stahl, A.2    Bhushan, S.3    Wright, S.J.4    Eriksson, A.5    Bruce, B.D.6    Glaser, E.7
  • 17
    • 70350242932 scopus 로고    scopus 로고
    • Deletion of an organellar peptidasome PreP affects early development in Arabidopsis thaliana
    • Nilsson Cederholm S., Backman H.G., Pesaresi P., Leister D., Glaser E. Deletion of an organellar peptidasome PreP affects early development in Arabidopsis thaliana. Plant Mol Biol 2009, 71:497-508.
    • (2009) Plant Mol Biol , vol.71 , pp. 497-508
    • Nilsson Cederholm, S.1    Backman, H.G.2    Pesaresi, P.3    Leister, D.4    Glaser, E.5
  • 22
    • 53549129483 scopus 로고    scopus 로고
    • Cyclophilin D deficiency attenuates mitochondrial and neuronal perturbation and ameliorates learning and memory in Alzheimer's disease
    • Du H., Guo L., Fang F., Chen D., Sosunov A.A., McKhann G.M., Yan Y., Wang C., Zhang H., Molkentin J.D., et al. Cyclophilin D deficiency attenuates mitochondrial and neuronal perturbation and ameliorates learning and memory in Alzheimer's disease. Nat Med 2008, 14:1097-1105.
    • (2008) Nat Med , vol.14 , pp. 1097-1105
    • Du, H.1    Guo, L.2    Fang, F.3    Chen, D.4    Sosunov, A.A.5    McKhann, G.M.6    Yan, Y.7    Wang, C.8    Zhang, H.9    Molkentin, J.D.10
  • 23
    • 33745919520 scopus 로고    scopus 로고
    • Epidemiology of Parkinson's disease
    • de Lau L.M., Breteler M.M. Epidemiology of Parkinson's disease. Lancet Neurol 2006, 5:525-535.
    • (2006) Lancet Neurol , vol.5 , pp. 525-535
    • de Lau, L.M.1    Breteler, M.M.2
  • 25
    • 77952353245 scopus 로고    scopus 로고
    • The Arabidopsis DJ-1a protein confers stress protection through cytosolic SOD activation
    • Xu X.M., Lin H., Maple J., Bjorkblom B., Alves G., Larsen J.P., Møller S.G. The Arabidopsis DJ-1a protein confers stress protection through cytosolic SOD activation. J Cell Sci 2010, 123:1644-1651.
    • (2010) J Cell Sci , vol.123 , pp. 1644-1651
    • Xu, X.M.1    Lin, H.2    Maple, J.3    Bjorkblom, B.4    Alves, G.5    Larsen, J.P.6    Møller, S.G.7
  • 27
    • 33947633494 scopus 로고    scopus 로고
    • Experimental encephalomyelitis induces changes in DJ-1: implications for oxidative stress in multiple sclerosis
    • Lev N., Ickowicz D., Barhum Y., Blondheim N., Melamed E., Offen D. Experimental encephalomyelitis induces changes in DJ-1: implications for oxidative stress in multiple sclerosis. Antioxid Redox Signal 2006, 8:1987-1995.
    • (2006) Antioxid Redox Signal , vol.8 , pp. 1987-1995
    • Lev, N.1    Ickowicz, D.2    Barhum, Y.3    Blondheim, N.4    Melamed, E.5    Offen, D.6
  • 28
    • 70350447105 scopus 로고    scopus 로고
    • LRRK2 in Parkinson's disease: genetic and clinical studies from patients
    • Kumari U., Tan E.K. LRRK2 in Parkinson's disease: genetic and clinical studies from patients. FEBS J 2009, 276:6455-6463.
    • (2009) FEBS J , vol.276 , pp. 6455-6463
    • Kumari, U.1    Tan, E.K.2
  • 29
    • 0030866902 scopus 로고    scopus 로고
    • A putative leucine-rich repeat receptor kinase involved in brassinosteroid signal transduction
    • Li J., Chory J. A putative leucine-rich repeat receptor kinase involved in brassinosteroid signal transduction. Cell 1997, 90:929-938.
    • (1997) Cell , vol.90 , pp. 929-938
    • Li, J.1    Chory, J.2
  • 30
    • 77952507231 scopus 로고    scopus 로고
    • Brassinosteroid signal transduction from receptor kinases to transcription factors
    • Kim T.W., Wang Z.Y. Brassinosteroid signal transduction from receptor kinases to transcription factors. Annu Rev Plant Biol 2010, 61:681-704.
    • (2010) Annu Rev Plant Biol , vol.61 , pp. 681-704
    • Kim, T.W.1    Wang, Z.Y.2
  • 31
    • 0036603021 scopus 로고    scopus 로고
    • Friedreich ataxia: a paradigm for mitochondrial diseases
    • Puccio H., Koenig M. Friedreich ataxia: a paradigm for mitochondrial diseases. Curr Opin Genet Dev 2002, 12:272-277.
    • (2002) Curr Opin Genet Dev , vol.12 , pp. 272-277
    • Puccio, H.1    Koenig, M.2
  • 32
    • 77953669993 scopus 로고    scopus 로고
    • Human iron-sulfur cluster assembly, cellular iron homeostasis, and disease
    • Ye H., Rouault T.A. Human iron-sulfur cluster assembly, cellular iron homeostasis, and disease. Biochemistry 2010, 49:4945-4956.
    • (2010) Biochemistry , vol.49 , pp. 4945-4956
    • Ye, H.1    Rouault, T.A.2
  • 33
    • 33845520813 scopus 로고    scopus 로고
    • Deficiency of Arabidopsis thaliana frataxin alters activity of mitochondrial Fe-S proteins and induces oxidative stress
    • Busi M.V., Maliandi M.V., Valdez H., Clemente M., Zabaleta E.J., Araya A., Gomez-Casati D.F. Deficiency of Arabidopsis thaliana frataxin alters activity of mitochondrial Fe-S proteins and induces oxidative stress. Plant J 2006, 48:873-882.
    • (2006) Plant J , vol.48 , pp. 873-882
    • Busi, M.V.1    Maliandi, M.V.2    Valdez, H.3    Clemente, M.4    Zabaleta, E.J.5    Araya, A.6    Gomez-Casati, D.F.7
  • 34
    • 58749093283 scopus 로고    scopus 로고
    • Nitric oxide accumulation is required to protect against iron-mediated oxidative stress in frataxin-deficient Arabidopsis plants
    • Martin M., Colman M.J., Gomez-Casati D.F., Lamattina L., Zabaleta E.J. Nitric oxide accumulation is required to protect against iron-mediated oxidative stress in frataxin-deficient Arabidopsis plants. FEBS Lett 2009, 583:542-548.
    • (2009) FEBS Lett , vol.583 , pp. 542-548
    • Martin, M.1    Colman, M.J.2    Gomez-Casati, D.F.3    Lamattina, L.4    Zabaleta, E.J.5
  • 35
    • 20744446399 scopus 로고    scopus 로고
    • Structure, function, and formation of biological iron-sulfur clusters
    • Johnson D.C., Dean D.R., Smith A.D., Johnson M.K. Structure, function, and formation of biological iron-sulfur clusters. Annu Rev Biochem 2005, 74:247-281.
    • (2005) Annu Rev Biochem , vol.74 , pp. 247-281
    • Johnson, D.C.1    Dean, D.R.2    Smith, A.D.3    Johnson, M.K.4
  • 36
    • 21444455377 scopus 로고    scopus 로고
    • Biogenesis of iron-sulfur proteins in plants
    • Balk J., Lobreaux S. Biogenesis of iron-sulfur proteins in plants. Trends Plant Sci 2005, 10:324-331.
    • (2005) Trends Plant Sci , vol.10 , pp. 324-331
    • Balk, J.1    Lobreaux, S.2
  • 38
    • 79954425480 scopus 로고    scopus 로고
    • Iron-sulfur clusters: biogenesis, molecular mechanisms and their functional significance
    • in press.
    • Xu XM, Møller SG: Iron-sulfur clusters: biogenesis, molecular mechanisms and their functional significance. Antioxid Redox Signal 2010, 12, in press.
    • (2010) Antioxid Redox Signal , vol.12
    • Xu, X.M.1    Møller, S.G.2
  • 39
    • 70449585173 scopus 로고    scopus 로고
    • Dual localized AtHscB involved in iron sulfur protein biogenesis in Arabidopsis
    • Xu X.M., Lin H., Latijnhouwers M., Møller S.G. Dual localized AtHscB involved in iron sulfur protein biogenesis in Arabidopsis. PLoS ONE 2009, 4:e7662.
    • (2009) PLoS ONE , vol.4
    • Xu, X.M.1    Lin, H.2    Latijnhouwers, M.3    Møller, S.G.4
  • 40
    • 33751177803 scopus 로고    scopus 로고
    • Iron-sulfur protein biogenesis in eukaryotes: components and mechanisms
    • Lill R., Muhlenhoff U. Iron-sulfur protein biogenesis in eukaryotes: components and mechanisms. Annu Rev Cell Dev Biol 2006, 22:457-486.
    • (2006) Annu Rev Cell Dev Biol , vol.22 , pp. 457-486
    • Lill, R.1    Muhlenhoff, U.2
  • 41
    • 51649098663 scopus 로고    scopus 로고
    • The evolving functions of DNA methylation
    • Zilberman D. The evolving functions of DNA methylation. Curr Opin Plant Biol 2008, 11:554-559.
    • (2008) Curr Opin Plant Biol , vol.11 , pp. 554-559
    • Zilberman, D.1
  • 42
    • 77950518292 scopus 로고    scopus 로고
    • SiRNAs and DNA methylation: seedy epigenetics
    • Mosher R.A., Melnyk C.W. siRNAs and DNA methylation: seedy epigenetics. Trends Plant Sci 2010, 15:204-210.
    • (2010) Trends Plant Sci , vol.15 , pp. 204-210
    • Mosher, R.A.1    Melnyk, C.W.2
  • 43
    • 77952500831 scopus 로고    scopus 로고
    • Histone methylation in higher plants
    • Liu C., Lu F., Cui X., Cao X. Histone methylation in higher plants. Annu Rev Plant Biol 2010, 61:395-420.
    • (2010) Annu Rev Plant Biol , vol.61 , pp. 395-420
    • Liu, C.1    Lu, F.2    Cui, X.3    Cao, X.4
  • 44
    • 70349623177 scopus 로고    scopus 로고
    • Gamete-specific epigenetic mechanisms shape genomic imprinting
    • Jullien P.E., Berger F. Gamete-specific epigenetic mechanisms shape genomic imprinting. Curr Opin Plant Biol 2009, 12:637-642.
    • (2009) Curr Opin Plant Biol , vol.12 , pp. 637-642
    • Jullien, P.E.1    Berger, F.2
  • 45
    • 73349104113 scopus 로고    scopus 로고
    • Active DNA demethylation mediated by DNA glycosylases
    • Zhu J.K. Active DNA demethylation mediated by DNA glycosylases. Annu Rev Genet 2009, 43:143-166.
    • (2009) Annu Rev Genet , vol.43 , pp. 143-166
    • Zhu, J.K.1
  • 46
    • 78049249340 scopus 로고    scopus 로고
    • Similarities in the circadian clock and photoperiodism in plants
    • Song Y.H., Ito S., Imaizumi T. Similarities in the circadian clock and photoperiodism in plants. Curr Opin Plant Biol 2010, 13:594-603.
    • (2010) Curr Opin Plant Biol , vol.13 , pp. 594-603
    • Song, Y.H.1    Ito, S.2    Imaizumi, T.3
  • 47
    • 74549157153 scopus 로고    scopus 로고
    • Arabidopsis circadian clock and photoperiodism: time to think about location
    • Imaizumi T. Arabidopsis circadian clock and photoperiodism: time to think about location. Curr Opin Plant Biol 2010, 13:83-89.
    • (2010) Curr Opin Plant Biol , vol.13 , pp. 83-89
    • Imaizumi, T.1
  • 48
    • 66449087281 scopus 로고    scopus 로고
    • The circadian system in higher plants
    • Harmer S.L. The circadian system in higher plants. Annu Rev Plant Biol 2009, 60:357-377.
    • (2009) Annu Rev Plant Biol , vol.60 , pp. 357-377
    • Harmer, S.L.1
  • 49
    • 70349546322 scopus 로고    scopus 로고
    • Time for circadian rhythms: plants get synchronized
    • Mas P., Yanovsky M.J. Time for circadian rhythms: plants get synchronized. Curr Opin Plant Biol 2009, 12:574-579.
    • (2009) Curr Opin Plant Biol , vol.12 , pp. 574-579
    • Mas, P.1    Yanovsky, M.J.2
  • 50
    • 77950865637 scopus 로고    scopus 로고
    • Sumoylation and other ubiquitin-like post-translational modifications in plants
    • Miura K., Hasegawa P.M. Sumoylation and other ubiquitin-like post-translational modifications in plants. Trends Cell Biol 2010, 20:223-232.
    • (2010) Trends Cell Biol , vol.20 , pp. 223-232
    • Miura, K.1    Hasegawa, P.M.2
  • 52
    • 77950401024 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system regulates plant hormone signaling
    • Santner A., Estelle M. The ubiquitin-proteasome system regulates plant hormone signaling. Plant J 2010, 61:1029-1040.
    • (2010) Plant J , vol.61 , pp. 1029-1040
    • Santner, A.1    Estelle, M.2
  • 53
    • 58149295514 scopus 로고    scopus 로고
    • Regulated proteolysis in light-related signaling pathways
    • Henriques R., Jang I.C., Chua N.H. Regulated proteolysis in light-related signaling pathways. Curr Opin Plant Biol 2009, 12:49-56.
    • (2009) Curr Opin Plant Biol , vol.12 , pp. 49-56
    • Henriques, R.1    Jang, I.C.2    Chua, N.H.3
  • 54
    • 56449094567 scopus 로고    scopus 로고
    • The COP9 signalosome: more than a protease
    • Wei N., Serino G., Deng X.W. The COP9 signalosome: more than a protease. Trends Biochem Sci 2008, 33:592-600.
    • (2008) Trends Biochem Sci , vol.33 , pp. 592-600
    • Wei, N.1    Serino, G.2    Deng, X.W.3
  • 55
    • 77950444157 scopus 로고    scopus 로고
    • Small RNAs-secrets and surprises of the genome
    • Chen X. Small RNAs-secrets and surprises of the genome. Plant J 2010, 61:941-958.
    • (2010) Plant J , vol.61 , pp. 941-958
    • Chen, X.1
  • 56
    • 77950452042 scopus 로고    scopus 로고
    • Linking genotype to phenotype using the Arabidopsis unimutant collection
    • O'Malley R.C., Ecker J.R. Linking genotype to phenotype using the Arabidopsis unimutant collection. Plant J 2010, 61:928-940.
    • (2010) Plant J , vol.61 , pp. 928-940
    • O'Malley, R.C.1    Ecker, J.R.2
  • 58
    • 77953414585 scopus 로고    scopus 로고
    • Genome-wide survey of Arabidopsis natural variation in downy mildew resistance using combined association and linkage mapping
    • Nemri A., Atwell S., Tarone A.M., Huang Y.S., Zhao K., Studholme D.J., Nordborg M., Jones J.D. Genome-wide survey of Arabidopsis natural variation in downy mildew resistance using combined association and linkage mapping. Proc Natl Acad Sci USA 2010, 107:10302-10307.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 10302-10307
    • Nemri, A.1    Atwell, S.2    Tarone, A.M.3    Huang, Y.S.4    Zhao, K.5    Studholme, D.J.6    Nordborg, M.7    Jones, J.D.8
  • 61
    • 77950428777 scopus 로고    scopus 로고
    • Arabidopsis and the plant immune system
    • Nishimura M.T., Dangl J.L. Arabidopsis and the plant immune system. Plant J 2010, 61:1053-1066.
    • (2010) Plant J , vol.61 , pp. 1053-1066
    • Nishimura, M.T.1    Dangl, J.L.2
  • 62
    • 77950398595 scopus 로고    scopus 로고
    • The development of Arabidopsis as a model plant
    • Koornneef M., Meinke D. The development of Arabidopsis as a model plant. Plant J 2010, 61:909-921.
    • (2010) Plant J , vol.61 , pp. 909-921
    • Koornneef, M.1    Meinke, D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.