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Volumn 14, Issue 4, 2009, Pages 194-199

Nuclear regulators with a second home in organelles

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS PROTEIN; DNA BINDING PROTEIN; MITOCHONDRIAL PROTEIN; NUCLEAR PROTEIN; VEGETABLE PROTEIN; WHIRLY1 PROTEIN, ARABIDOPSIS;

EID: 63549122411     PISSN: 13601385     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tplants.2009.01.005     Document Type: Article
Times cited : (68)

References (62)
  • 1
    • 0022470359 scopus 로고
    • The HTS1 gene encodes both the cytoplasmic and mitochondrial histidine tRNA synthetases of S. cerevisiae
    • Natsoulis G., et al. The HTS1 gene encodes both the cytoplasmic and mitochondrial histidine tRNA synthetases of S. cerevisiae. Cell 46 (1986) 235-243
    • (1986) Cell , vol.46 , pp. 235-243
    • Natsoulis, G.1
  • 2
    • 0029347014 scopus 로고
    • Simultaneous targeting of pea glutathione reductase and of a bacterial fusion protein to chloroplasts and mitochondria in transgenic tobacco
    • Creissen G., et al. Simultaneous targeting of pea glutathione reductase and of a bacterial fusion protein to chloroplasts and mitochondria in transgenic tobacco. Plant J. 8 (1995) 167-175
    • (1995) Plant J. , vol.8 , pp. 167-175
    • Creissen, G.1
  • 3
    • 20044387943 scopus 로고    scopus 로고
    • Single translation - dual destination: mechanisms of dual protein targeting in eukaryotes
    • Karniely S., and Pines O. Single translation - dual destination: mechanisms of dual protein targeting in eukaryotes. EMBO Rep. 6 (2005) 420-425
    • (2005) EMBO Rep. , vol.6 , pp. 420-425
    • Karniely, S.1    Pines, O.2
  • 4
    • 0032168849 scopus 로고    scopus 로고
    • Two birds with one stone: genes that encode products targeted to two or more compartments
    • Small I., et al. Two birds with one stone: genes that encode products targeted to two or more compartments. Plant Mol. Biol. 38 (1998) 265-277
    • (1998) Plant Mol. Biol. , vol.38 , pp. 265-277
    • Small, I.1
  • 5
    • 0344962439 scopus 로고    scopus 로고
    • One ticket for multiple destinations: dual targeting of proteins to distinct subcellular locations
    • Silva-Filho M.C. One ticket for multiple destinations: dual targeting of proteins to distinct subcellular locations. Curr. Opin. Plant Biol. 6 (2003) 589-595
    • (2003) Curr. Opin. Plant Biol. , vol.6 , pp. 589-595
    • Silva-Filho, M.C.1
  • 6
    • 0030294560 scopus 로고    scopus 로고
    • MFP1, a novel plant filament-like protein with affinity for matrix attachment region DNA
    • Meier I., et al. MFP1, a novel plant filament-like protein with affinity for matrix attachment region DNA. Plant Cell 8 (1996) 2105-2115
    • (1996) Plant Cell , vol.8 , pp. 2105-2115
    • Meier, I.1
  • 7
    • 0033150016 scopus 로고    scopus 로고
    • Matrix attachment region binding protein MFP1 is localized in discrete domains at the nuclear envelope
    • Gindullis F., and Meier I. Matrix attachment region binding protein MFP1 is localized in discrete domains at the nuclear envelope. Plant Cell 11 (1999) 1117-1128
    • (1999) Plant Cell , vol.11 , pp. 1117-1128
    • Gindullis, F.1    Meier, I.2
  • 8
    • 0345306340 scopus 로고    scopus 로고
    • MFP1 is a thylakoid-associated, nucleoid-binding protein with a coiled-coil structure
    • Jeong S.Y., et al. MFP1 is a thylakoid-associated, nucleoid-binding protein with a coiled-coil structure. Nucleic Acids Res. 31 (2003) 5175-5185
    • (2003) Nucleic Acids Res. , vol.31 , pp. 5175-5185
    • Jeong, S.Y.1
  • 9
    • 29344471771 scopus 로고    scopus 로고
    • Dual location of MAR-binding, filament-like protein 1 in Arabidopsis, tobacco, and tomato
    • Samaniego R., et al. Dual location of MAR-binding, filament-like protein 1 in Arabidopsis, tobacco, and tomato. Planta 223 (2006) 1201-1206
    • (2006) Planta , vol.223 , pp. 1201-1206
    • Samaniego, R.1
  • 10
    • 51749084868 scopus 로고    scopus 로고
    • Characterization, expression and subcellular distribution of a novel MFP1 (matrix attachment region-binding filament-like protein 1) in onion
    • Samaniego R., et al. Characterization, expression and subcellular distribution of a novel MFP1 (matrix attachment region-binding filament-like protein 1) in onion. Protoplasma 233 (2008) 31-38
    • (2008) Protoplasma , vol.233 , pp. 31-38
    • Samaniego, R.1
  • 11
    • 33745808015 scopus 로고    scopus 로고
    • An evolutionarily conserved translation initiation mechanism regulates nuclear or mitochondrial targeting of DNA ligase 1 in Arabidopsis thaliana
    • Sunderland P.A., et al. An evolutionarily conserved translation initiation mechanism regulates nuclear or mitochondrial targeting of DNA ligase 1 in Arabidopsis thaliana. Plant J. 47 (2006) 356-367
    • (2006) Plant J. , vol.47 , pp. 356-367
    • Sunderland, P.A.1
  • 12
    • 0034087609 scopus 로고    scopus 로고
    • Specific association of a small protein with the telomeric DNA-protein complex during the onset of leaf senescence in Arabidopsis thaliana
    • Zentgraf U., et al. Specific association of a small protein with the telomeric DNA-protein complex during the onset of leaf senescence in Arabidopsis thaliana. Plant Mol. Biol. 42 (2000) 429-438
    • (2000) Plant Mol. Biol. , vol.42 , pp. 429-438
    • Zentgraf, U.1
  • 13
    • 1842424853 scopus 로고    scopus 로고
    • Interaction of an Arabidopsis RNA-binding protein with plant single-stranded telomeric DNA modulates telomerase activity
    • Kwon C., and Chung I.K. Interaction of an Arabidopsis RNA-binding protein with plant single-stranded telomeric DNA modulates telomerase activity. J. Biol. Chem. 279 (2004) 12812-12818
    • (2004) J. Biol. Chem. , vol.279 , pp. 12812-12818
    • Kwon, C.1    Chung, I.K.2
  • 14
    • 0029240302 scopus 로고
    • Three types of nuclear genes encoding chloroplast RNA-binding proteins (cp29, cp31 and cp33) are present in Arabidopsis thaliana: presence of cp31 in chloroplasts and its homologue in nuclei/cytoplasms
    • Ohta M., et al. Three types of nuclear genes encoding chloroplast RNA-binding proteins (cp29, cp31 and cp33) are present in Arabidopsis thaliana: presence of cp31 in chloroplasts and its homologue in nuclei/cytoplasms. Plant Mol. Biol. 27 (1995) 529-539
    • (1995) Plant Mol. Biol. , vol.27 , pp. 529-539
    • Ohta, M.1
  • 15
    • 0035205970 scopus 로고    scopus 로고
    • Repression of the defense gene PR-10a by the single-stranded DNA binding protein SEBF
    • Boyle B., and Brisson N. Repression of the defense gene PR-10a by the single-stranded DNA binding protein SEBF. Plant Cell 13 (2001) 2525-2537
    • (2001) Plant Cell , vol.13 , pp. 2525-2537
    • Boyle, B.1    Brisson, N.2
  • 16
    • 21244500215 scopus 로고    scopus 로고
    • DNA-binding proteins of the Whirly family in Arabidopsis thaliana are targeted to the organelles
    • Krause K., et al. DNA-binding proteins of the Whirly family in Arabidopsis thaliana are targeted to the organelles. FEBS Lett. 579 (2005) 3707-3712
    • (2005) FEBS Lett. , vol.579 , pp. 3707-3712
    • Krause, K.1
  • 17
    • 33846412615 scopus 로고    scopus 로고
    • Single-stranded DNA binding factor AtWHY1 modulates telomere length homeostasis in Arabidopsis
    • Yoo H.H., et al. Single-stranded DNA binding factor AtWHY1 modulates telomere length homeostasis in Arabidopsis. Plant J. 49 (2007) 442-451
    • (2007) Plant J. , vol.49 , pp. 442-451
    • Yoo, H.H.1
  • 18
    • 33748951905 scopus 로고    scopus 로고
    • Eukaryotic transcription factors in plastids - bioinformatic assessment and implications for the evolution of gene expression machineries in plants
    • Wagner R., and Pfannschmidt T. Eukaryotic transcription factors in plastids - bioinformatic assessment and implications for the evolution of gene expression machineries in plants. Gene 381 (2006) 62-70
    • (2006) Gene , vol.381 , pp. 62-70
    • Wagner, R.1    Pfannschmidt, T.2
  • 19
    • 34248676824 scopus 로고    scopus 로고
    • Comparative survey of plastid and mitochondrial targeting properties of transcription factors in Arabidopsis and rice
    • Schwacke R., et al. Comparative survey of plastid and mitochondrial targeting properties of transcription factors in Arabidopsis and rice. Mol. Genet. Genomics 277 (2007) 631-646
    • (2007) Mol. Genet. Genomics , vol.277 , pp. 631-646
    • Schwacke, R.1
  • 20
    • 62149097250 scopus 로고    scopus 로고
    • Approaches to defining dual-targeted proteins in Arabidopsis
    • Carrie C., et al. Approaches to defining dual-targeted proteins in Arabidopsis. Plant J. 57 (2008) 1128-1139
    • (2008) Plant J. , vol.57 , pp. 1128-1139
    • Carrie, C.1
  • 21
    • 13744250057 scopus 로고    scopus 로고
    • Whirly transcription factors: defense gene regulation and beyond
    • Desveaux D., et al. Whirly transcription factors: defense gene regulation and beyond. Trends Plant Sci. 10 (2005) 95-102
    • (2005) Trends Plant Sci. , vol.10 , pp. 95-102
    • Desveaux, D.1
  • 22
    • 0033827449 scopus 로고    scopus 로고
    • PBF-2 is a novel single-stranded DNA binding factor implicated in PR-10a gene activation in potato
    • Desveaux D., et al. PBF-2 is a novel single-stranded DNA binding factor implicated in PR-10a gene activation in potato. Plant Cell 12 (2000) 1477-1489
    • (2000) Plant Cell , vol.12 , pp. 1477-1489
    • Desveaux, D.1
  • 23
    • 53749103783 scopus 로고    scopus 로고
    • Single-stranded DNA-binding protein Whirly1 in barley leaves is located in plastids and the nucleus of the same cell
    • Grabowski E., et al. Single-stranded DNA-binding protein Whirly1 in barley leaves is located in plastids and the nucleus of the same cell. Plant Physiol. 147 (2008) 1800-1804
    • (2008) Plant Physiol. , vol.147 , pp. 1800-1804
    • Grabowski, E.1
  • 24
    • 52649136147 scopus 로고    scopus 로고
    • A member of the Whirly family is a multifunctional RNA- and DNA-binding protein that is essential for chloroplast biogenesis
    • Prikryl J., et al. A member of the Whirly family is a multifunctional RNA- and DNA-binding protein that is essential for chloroplast biogenesis. Nucleic Acids Res. 36 (2008) 5152-5165
    • (2008) Nucleic Acids Res. , vol.36 , pp. 5152-5165
    • Prikryl, J.1
  • 25
    • 33745840868 scopus 로고    scopus 로고
    • Two cell-cycle regulated SET-domain proteins interact with proliferating cell nuclear antigen (PCNA) in Arabidopsis
    • Raynaud C., et al. Two cell-cycle regulated SET-domain proteins interact with proliferating cell nuclear antigen (PCNA) in Arabidopsis. Plant J. 47 (2006) 395-407
    • (2006) Plant J. , vol.47 , pp. 395-407
    • Raynaud, C.1
  • 26
    • 0036591878 scopus 로고    scopus 로고
    • The many faces of histone lysine methylation
    • Lachner M., and Jenuwein T. The many faces of histone lysine methylation. Curr. Opin. Cell Biol. 14 (2002) 286-298
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 286-298
    • Lachner, M.1    Jenuwein, T.2
  • 27
    • 0036532202 scopus 로고    scopus 로고
    • Histone methylation in transcriptional control
    • Kouzarides T. Histone methylation in transcriptional control. Curr. Opin. Genet. Dev. 12 (2002) 198-209
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 198-209
    • Kouzarides, T.1
  • 28
    • 48949120166 scopus 로고    scopus 로고
    • Farnesylation directs AtIPT3 subcellular localization and modulates cytokinin biosynthesis in Arabidopsis
    • Galichet A., et al. Farnesylation directs AtIPT3 subcellular localization and modulates cytokinin biosynthesis in Arabidopsis. Plant Physiol. 146 (2008) 1155-1164
    • (2008) Plant Physiol. , vol.146 , pp. 1155-1164
    • Galichet, A.1
  • 29
    • 33747507688 scopus 로고    scopus 로고
    • Tobacco Tsip1, a DnaJ-type Zn finger protein, is recruited to and potentiates Tsi1-mediated transcriptional activation
    • Ham B.K., et al. Tobacco Tsip1, a DnaJ-type Zn finger protein, is recruited to and potentiates Tsi1-mediated transcriptional activation. Plant Cell 18 (2006) 2005-2020
    • (2006) Plant Cell , vol.18 , pp. 2005-2020
    • Ham, B.K.1
  • 30
    • 33845955743 scopus 로고    scopus 로고
    • Evolution of a basic helix-loop-helix protein from a transcriptional repressor to a plastid-resident regulatory factor: involvement in hypersensitive cell death in tobacco plants
    • Kodama Y., and Sano H. Evolution of a basic helix-loop-helix protein from a transcriptional repressor to a plastid-resident regulatory factor: involvement in hypersensitive cell death in tobacco plants. J. Biol. Chem. 281 (2006) 35369-35380
    • (2006) J. Biol. Chem. , vol.281 , pp. 35369-35380
    • Kodama, Y.1    Sano, H.2
  • 31
    • 53149117026 scopus 로고    scopus 로고
    • Membrane-bound transcription factors in plants
    • Seo P.J., et al. Membrane-bound transcription factors in plants. Trends Plant Sci. 13 (2008) 550-556
    • (2008) Trends Plant Sci. , vol.13 , pp. 550-556
    • Seo, P.J.1
  • 32
    • 17044404640 scopus 로고    scopus 로고
    • An Arabidopsis transcription factor, AtbZIP60, regulates the endoplasmic reticulum stress response in a manner unique to plants
    • Iwata Y., and Koizumi N. An Arabidopsis transcription factor, AtbZIP60, regulates the endoplasmic reticulum stress response in a manner unique to plants. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 5280-5285
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 5280-5285
    • Iwata, Y.1    Koizumi, N.2
  • 33
    • 0037405692 scopus 로고    scopus 로고
    • Transcription factor IIB (TFIIB)-related protein (pBrp), a plant-specific member of the TFIIB-related protein family
    • Lagrange T., et al. Transcription factor IIB (TFIIB)-related protein (pBrp), a plant-specific member of the TFIIB-related protein family. Mol. Cell. Biol. 23 (2003) 3274-3286
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 3274-3286
    • Lagrange, T.1
  • 34
    • 51049084399 scopus 로고    scopus 로고
    • The plant-specific TFIIB-related protein, pBrp, is a general transcription factor for RNA polymerase I
    • Imamura S., et al. The plant-specific TFIIB-related protein, pBrp, is a general transcription factor for RNA polymerase I. EMBO J. 27 (2008) 2317-2327
    • (2008) EMBO J. , vol.27 , pp. 2317-2327
    • Imamura, S.1
  • 35
    • 0033818171 scopus 로고    scopus 로고
    • Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretome
    • Tjalsma H., et al. Signal peptide-dependent protein transport in Bacillus subtilis: a genome-based survey of the secretome. Microbiol. Mol. Biol. Rev. 64 (2000) 515-547
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 515-547
    • Tjalsma, H.1
  • 36
    • 49649095178 scopus 로고    scopus 로고
    • Secreted transcription factor controls Mycobacterium tuberculosis virulence
    • Raghavan S., et al. Secreted transcription factor controls Mycobacterium tuberculosis virulence. Nature 454 (2008) 717-721
    • (2008) Nature , vol.454 , pp. 717-721
    • Raghavan, S.1
  • 37
    • 33745208665 scopus 로고    scopus 로고
    • Mitochondrial import of human and yeast fumarase in live mammalian cells: retrograde translocation of the yeast enzyme is mainly caused by its poor targeting sequence
    • Singh B., and Gupta R.S. Mitochondrial import of human and yeast fumarase in live mammalian cells: retrograde translocation of the yeast enzyme is mainly caused by its poor targeting sequence. Biochem. Biophys. Res. Commun. 346 (2006) 911-918
    • (2006) Biochem. Biophys. Res. Commun. , vol.346 , pp. 911-918
    • Singh, B.1    Gupta, R.S.2
  • 38
    • 0035943626 scopus 로고    scopus 로고
    • Cloning and characterization of MDDX28, a putative dead-box helicase with mitochondrial and nuclear localization
    • Valgardsdottir R., et al. Cloning and characterization of MDDX28, a putative dead-box helicase with mitochondrial and nuclear localization. J. Biol. Chem. 276 (2001) 32056-32063
    • (2001) J. Biol. Chem. , vol.276 , pp. 32056-32063
    • Valgardsdottir, R.1
  • 39
    • 0038079978 scopus 로고    scopus 로고
    • Transport signals and transcription-dependent nuclear localization of the putative DEAD-box helicase MDDX28
    • Valgardsdottir R., and Prydz H. Transport signals and transcription-dependent nuclear localization of the putative DEAD-box helicase MDDX28. J. Biol. Chem. 278 (2003) 21146-21154
    • (2003) J. Biol. Chem. , vol.278 , pp. 21146-21154
    • Valgardsdottir, R.1    Prydz, H.2
  • 40
    • 0035839555 scopus 로고    scopus 로고
    • The Arabidopsis thaliana ABC protein superfamily, a complete inventory
    • Sanchez-Fernandez R., et al. The Arabidopsis thaliana ABC protein superfamily, a complete inventory. J. Biol. Chem. 276 (2001) 30231-30244
    • (2001) J. Biol. Chem. , vol.276 , pp. 30231-30244
    • Sanchez-Fernandez, R.1
  • 41
    • 0031663159 scopus 로고    scopus 로고
    • Gram-negative bacteria produce membrane vesicles which are capable of killing other bacteria
    • Li Z., et al. Gram-negative bacteria produce membrane vesicles which are capable of killing other bacteria. J. Bacteriol. 180 (1998) 5478-5483
    • (1998) J. Bacteriol. , vol.180 , pp. 5478-5483
    • Li, Z.1
  • 42
    • 0030023858 scopus 로고    scopus 로고
    • Immunoelectron microscopic localization of the 60-kDa heat shock chaperonin protein (Hsp60) in mammalian cells
    • Soltys B.J., and Gupta R.S. Immunoelectron microscopic localization of the 60-kDa heat shock chaperonin protein (Hsp60) in mammalian cells. Exp. Cell Res. 222 (1996) 16-27
    • (1996) Exp. Cell Res. , vol.222 , pp. 16-27
    • Soltys, B.J.1    Gupta, R.S.2
  • 43
    • 0031213629 scopus 로고    scopus 로고
    • Cloning and some novel characteristics of mitochondrial Hsp70 from Chinese hamster cells
    • Singh B., et al. Cloning and some novel characteristics of mitochondrial Hsp70 from Chinese hamster cells. Exp. Cell Res. 234 (1997) 205-216
    • (1997) Exp. Cell Res. , vol.234 , pp. 205-216
    • Singh, B.1
  • 44
    • 33746368041 scopus 로고    scopus 로고
    • Evidence for an ER to Golgi to chloroplast protein transport pathway
    • Radhamony R.N., and Theg S.M. Evidence for an ER to Golgi to chloroplast protein transport pathway. Trends Cell Biol. 16 (2006) 385-387
    • (2006) Trends Cell Biol. , vol.16 , pp. 385-387
    • Radhamony, R.N.1    Theg, S.M.2
  • 45
    • 28544447361 scopus 로고    scopus 로고
    • Evidence for a protein transported through the secretory pathway en route to the higher plant chloroplast
    • Villarejo A., et al. Evidence for a protein transported through the secretory pathway en route to the higher plant chloroplast. Nat. Cell Biol. 7 (2005) 1224-1231
    • (2005) Nat. Cell Biol. , vol.7 , pp. 1224-1231
    • Villarejo, A.1
  • 46
    • 18644382130 scopus 로고    scopus 로고
    • Plastid stromules: video microscopy of their outgrowth, retraction, tensioning, anchoring, branching, bridging, and tip-shedding
    • Gunning B.E. Plastid stromules: video microscopy of their outgrowth, retraction, tensioning, anchoring, branching, bridging, and tip-shedding. Protoplasma 225 (2005) 33-42
    • (2005) Protoplasma , vol.225 , pp. 33-42
    • Gunning, B.E.1
  • 48
    • 0141976351 scopus 로고    scopus 로고
    • Exclusion of ribulose-1,5-bisphosphate carboxylase/oxygenase from chloroplasts by specific bodies in naturally senescing leaves of wheat
    • Chiba A., et al. Exclusion of ribulose-1,5-bisphosphate carboxylase/oxygenase from chloroplasts by specific bodies in naturally senescing leaves of wheat. Plant Cell Physiol. 44 (2003) 914-921
    • (2003) Plant Cell Physiol. , vol.44 , pp. 914-921
    • Chiba, A.1
  • 49
    • 44649165814 scopus 로고    scopus 로고
    • Cysteine proteinases regulate chloroplast protein content and composition in tobacco leaves: a model for dynamic interactions with ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) vesicular bodies
    • Prins A., et al. Cysteine proteinases regulate chloroplast protein content and composition in tobacco leaves: a model for dynamic interactions with ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) vesicular bodies. J. Exp. Bot. 59 (2008) 1935-1950
    • (2008) J. Exp. Bot. , vol.59 , pp. 1935-1950
    • Prins, A.1
  • 50
    • 1542544600 scopus 로고    scopus 로고
    • GFP-labelled Rubisco and aspartate aminotransferase are present in plastid stromules and traffic between plastids
    • Kwok E.Y., and Hanson M.R. GFP-labelled Rubisco and aspartate aminotransferase are present in plastid stromules and traffic between plastids. J. Exp. Bot. 55 (2004) 595-604
    • (2004) J. Exp. Bot. , vol.55 , pp. 595-604
    • Kwok, E.Y.1    Hanson, M.R.2
  • 51
    • 6344233800 scopus 로고    scopus 로고
    • Plastids and stromules interact with the nucleus and cell membrane in vascular plants
    • Kwok E.Y., and Hanson M.R. Plastids and stromules interact with the nucleus and cell membrane in vascular plants. Plant Cell Rep. 23 (2004) 188-195
    • (2004) Plant Cell Rep. , vol.23 , pp. 188-195
    • Kwok, E.Y.1    Hanson, M.R.2
  • 52
    • 57749098549 scopus 로고    scopus 로고
    • The mitochondrial cycle of Arabidopsis shoot apical meristem and leaf primordium meristematic cells is defined by a perinuclear tentaculate/cage-like mitochondrion
    • Segui-Simarro J.M., et al. The mitochondrial cycle of Arabidopsis shoot apical meristem and leaf primordium meristematic cells is defined by a perinuclear tentaculate/cage-like mitochondrion. Plant Physiol. 148 (2008) 1380-1393
    • (2008) Plant Physiol. , vol.148 , pp. 1380-1393
    • Segui-Simarro, J.M.1
  • 53
    • 0033133729 scopus 로고    scopus 로고
    • Mitochondrial-matrix proteins at unexpected locations: are they exported?
    • Soltys B.J., and Gupta R.S. Mitochondrial-matrix proteins at unexpected locations: are they exported?. Trends Biochem. Sci. 24 (1999) 174-177
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 174-177
    • Soltys, B.J.1    Gupta, R.S.2
  • 54
    • 0031871330 scopus 로고    scopus 로고
    • A splice-isoform of vesicle-associated membrane protein-1 (VAMP-1) contains a mitochondrial targeting signal
    • Isenmann S., et al. A splice-isoform of vesicle-associated membrane protein-1 (VAMP-1) contains a mitochondrial targeting signal. Mol. Biol. Cell 9 (1998) 1649-1660
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1649-1660
    • Isenmann, S.1
  • 55
    • 33847760354 scopus 로고    scopus 로고
    • Optical manipulation reveals strong attracting forces at membrane contact sites between endoplasmic reticulum and chloroplasts
    • Andersson M.X., et al. Optical manipulation reveals strong attracting forces at membrane contact sites between endoplasmic reticulum and chloroplasts. J. Biol. Chem. 282 (2007) 1170-1174
    • (2007) J. Biol. Chem. , vol.282 , pp. 1170-1174
    • Andersson, M.X.1
  • 56
    • 0031105834 scopus 로고    scopus 로고
    • Multiple transcription start sites of the carrot dihydrofolate reductase-thymidylate synthase gene, and sub-cellular localization of the bifunctional protein
    • Luo M., et al. Multiple transcription start sites of the carrot dihydrofolate reductase-thymidylate synthase gene, and sub-cellular localization of the bifunctional protein. Plant Mol. Biol. 33 (1997) 709-722
    • (1997) Plant Mol. Biol. , vol.33 , pp. 709-722
    • Luo, M.1
  • 57
    • 0029869004 scopus 로고    scopus 로고
    • Mitochondria are a major site for folate and thymidylate synthesis in plants
    • Neuburger M., et al. Mitochondria are a major site for folate and thymidylate synthesis in plants. J. Biol. Chem. 271 (1996) 9466-9472
    • (1996) J. Biol. Chem. , vol.271 , pp. 9466-9472
    • Neuburger, M.1
  • 58
    • 20444394399 scopus 로고    scopus 로고
    • Cell and plastid division are coordinated through the prereplication factor AtCDT1
    • Raynaud C., et al. Cell and plastid division are coordinated through the prereplication factor AtCDT1. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 8216-8221
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 8216-8221
    • Raynaud, C.1
  • 59
    • 0345874789 scopus 로고    scopus 로고
    • A mutation in the nuclear-encoded plastid ribosomal protein S9 leads to early embryo lethality in maize
    • Ma Z., and Dooner H.K. A mutation in the nuclear-encoded plastid ribosomal protein S9 leads to early embryo lethality in maize. Plant J. 37 (2004) 92-103
    • (2004) Plant J. , vol.37 , pp. 92-103
    • Ma, Z.1    Dooner, H.K.2
  • 60
    • 0035137178 scopus 로고    scopus 로고
    • Pir1p mediates translocation of the yeast Apn1p endonuclease into the mitochondria to maintain genomic stability
    • Vongsamphanh R., et al. Pir1p mediates translocation of the yeast Apn1p endonuclease into the mitochondria to maintain genomic stability. Mol. Cell. Biol. 21 (2001) 1647-1655
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 1647-1655
    • Vongsamphanh, R.1
  • 61
    • 0032403084 scopus 로고    scopus 로고
    • A mitochondrial ketogenic enzyme regulates its gene expression by association with the nuclear hormone receptor PPARα
    • Meertens L.M., et al. A mitochondrial ketogenic enzyme regulates its gene expression by association with the nuclear hormone receptor PPARα. EMBO J. 17 (1998) 6972-6978
    • (1998) EMBO J. , vol.17 , pp. 6972-6978
    • Meertens, L.M.1
  • 62
    • 1942451885 scopus 로고    scopus 로고
    • Mechanisms for multiple intracellular localization of human mitochondrial proteins
    • Mueller J.C., et al. Mechanisms for multiple intracellular localization of human mitochondrial proteins. Mitochondrion 3 (2004) 315-325
    • (2004) Mitochondrion , vol.3 , pp. 315-325
    • Mueller, J.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.