메뉴 건너뛰기




Volumn 4, Issue NOV, 2013, Pages

Corrigendum: The GIP Gamma- Tubulin Complex-Associated Proteins are Involved in Nuclear Architecture in Arabidopsis Thaliana (Frontiers in Plant Science, (2013), 4, (480), 10.3389/fpls.2013.00480);The GIP gamma-tubulin complex-associated proteins are involved in nuclear architecture in Arabidopsis thaliana

Author keywords

Arabidopsis thaliana; AtGIP1 MOZART1; AtTSA1; Gamma tubulin complex; Nuclear envelope; nuclear envelope; gamma tubulin complex

Indexed keywords


EID: 84899865900     PISSN: None     EISSN: 1664462X     Source Type: Journal    
DOI: 10.3389/fpls.2020.589954     Document Type: Erratum
Times cited : (49)

References (67)
  • 1
    • 0000256866 scopus 로고
    • Formation of spindle fibers, kinetochore orientation, and behavior of the nuclear envelope during mitosis in endosperm
    • doi: 10.1007/BF00325682
    • Bajer, A., and Mole-Bajer, J. (1969). Formation of spindle fibers, kinetochore orientation, and behavior of the nuclear envelope during mitosis in endosperm. Chromosoma 27, 448-484. doi: 10.1007/BF00325682
    • (1969) Chromosoma , vol.27 , pp. 448-484
    • Bajer, A.1    Mole-Bajer, J.2
  • 2
    • 0036303235 scopus 로고    scopus 로고
    • Remodelling the walls of the nucleus
    • doi: 10.1038/nrm860
    • Burke, B., and Ellenberg, J. (2002). Remodelling the walls of the nucleus. Nat. Rev. Mol. Cell. Biol. 3, 487-497. doi: 10.1038/nrm860
    • (2002) Nat. Rev. Mol. Cell. Biol. , vol.3 , pp. 487-497
    • Burke, B.1    Ellenberg, J.2
  • 3
    • 0034214418 scopus 로고    scopus 로고
    • Higher plant cells: Gamma-tubulin and microtubule nucleation in the absence of centrosomes
    • doi: 10.1002/(SICI)1097-0029(20000601)49:5<487::AID-JEMT11>3.0.CO;2-I
    • Canaday, J., Stoppin-Mellet, V., Mutterer, J., Lambert, A., and Schmit, A. (2000). Higher plant cells: gamma-tubulin and microtubule nucleation in the absence of centrosomes. Microsc. Res. Tech. 49, 487-495. doi: 10.1002/(SICI)1097-0029(20000601)49:5<487::AID-JEMT11>3.0.CO;2-I
    • (2000) Microsc. Res. Tech. , vol.49 , pp. 487-495
    • Canaday, J.1    Stoppin-Mellet, V.2    Mutterer, J.3    Lambert, A.4    Schmit, A.5
  • 4
    • 84889608926 scopus 로고    scopus 로고
    • NMCP/LINC proteins: Putative lamin analogs in plants?
    • Available online at: doi: 10.4161/psb.26669
    • Ciska, M., and Moreno Diaz de la Espina, S. (2013). NMCP/LINC proteins: putative lamin analogs in plants? Plant signal. Behav. 8. Available online at: http://www.ncbi.nlm.nih.gov/pubmed/24128696. doi: 10.4161/psb.26669
    • (2013) Plant signal. Behav. , pp. 8
    • Ciska, M.1    de la Espina Moreno Diaz, S.2
  • 5
    • 0032447801 scopus 로고    scopus 로고
    • Floral dip: A simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana
    • doi: 10.1046/j.1365-313x.1998.00343.x
    • Clough, S., and Bent, A. (1998). Floral dip: a simplified method for Agrobacterium-mediated transformation of Arabidopsis thaliana. Plant J. 16, 735-743. doi: 10.1046/j.1365-313x.1998.00343.x
    • (1998) Plant J. , vol.16 , pp. 735-743
    • Clough, S.1    Bent, A.2
  • 6
    • 29944445023 scopus 로고    scopus 로고
    • Coupling of the nucleus and cytoplasm: Role of the LINC complex
    • doi: 10.1083/jcb.200509124
    • Crisp, M., Liu, Q., Roux, K., Rattner, J., Shanahan, C., Burke, B., et al. (2006). Coupling of the nucleus and cytoplasm: role of the LINC complex. J. Cell Biol. 172, 41-53. doi: 10.1083/jcb.200509124
    • (2006) J. Cell Biol. , vol.172 , pp. 41-53
    • Crisp, M.1    Liu, Q.2    Roux, K.3    Rattner, J.4    Shanahan, C.5    Burke, B.6
  • 7
    • 84887080714 scopus 로고    scopus 로고
    • Mzt1/Tam4, a fission yeast MOZART1 homologue, is an essential component of the γ-tubulin complex and directly interacts with GCP3Alp6
    • doi: 10.1091/mbc.E13-05-0253
    • Dhani, D., Goult, B., George, G., Rogerson, D., Bitton, D., Miller, C., et al. (2013). Mzt1/Tam4, a fission yeast MOZART1 homologue, is an essential component of the γ-tubulin complex and directly interacts with GCP3Alp6. Mol. Biol. Cell 24, 3337-3349. doi: 10.1091/mbc.E13-05-0253
    • (2013) Mol. Biol. Cell , vol.24 , pp. 3337-3349
    • Dhani, D.1    Goult, B.2    George, G.3    Rogerson, D.4    Bitton, D.5    Miller, C.6
  • 8
    • 35748984432 scopus 로고    scopus 로고
    • LITTLE NUCLEI genes affecting nuclear morphology in Arabidopsis thaliana
    • doi: 10.1105/tpc.107.053231
    • Dittmer, T., Stacey, N., Sugimoto-Shirasu, K., and Richards, E. (2007). LITTLE NUCLEI genes affecting nuclear morphology in Arabidopsis thaliana. Plant Cell 19, 2793-2803. doi: 10.1105/tpc.107.053231
    • (2007) Plant Cell , vol.19 , pp. 2793-2803
    • Dittmer, T.1    Stacey, N.2    Sugimoto-Shirasu, K.3    Richards, E.4
  • 9
    • 0036181909 scopus 로고    scopus 로고
    • Spatio-temporal relationship between nuclear-envelope breakdown and preprophase band disappearance in cultured tobacco cells
    • doi: 10.1007/s007090200012
    • Dixit, R., and Cyr, R. (2002). Spatio-temporal relationship between nuclear-envelope breakdown and preprophase band disappearance in cultured tobacco cells. Protoplasma 219, 116-121. doi: 10.1007/s007090200012
    • (2002) Protoplasma , vol.219 , pp. 116-121
    • Dixit, R.1    Cyr, R.2
  • 10
    • 0035834037 scopus 로고    scopus 로고
    • Nuclear envelope proteomics: Novel integral membrane proteins of the inner nuclear membrane
    • doi: 10.1073/pnas.211201898
    • Dreger, M., Bengtsson, L., Schöneberg, T., Otto, H., and Hucho, F. (2001). Nuclear envelope proteomics: novel integral membrane proteins of the inner nuclear membrane. Proc. Natl. Acad. Sci. U.S.A. 98, 11943-11948. doi: 10.1073/pnas.211201898
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 11943-11948
    • Dreger, M.1    Bengtsson, L.2    Schöneberg, T.3    Otto, H.4    Hucho, F.5
  • 11
    • 33847257329 scopus 로고    scopus 로고
    • Nuclear envelope
    • doi: 10.1016/j.cub.2006.12.035
    • Dultz, E., and Ellenberg, J. (2007). Nuclear envelope. Curr. Biol. 17, R154-R156. doi: 10.1016/j.cub.2006.12.035
    • (2007) Curr. Biol. , vol.17
    • Dultz, E.1    Ellenberg, J.2
  • 12
    • 0036591957 scopus 로고    scopus 로고
    • The plant Spc98p homologue colocalizes with gamma-tubulin at microtubule nucleation sites and is required for microtubule nucleation
    • Erhardt, M., Stoppin-Mellet, V., Campagne, S., Canaday, J., Mutterer, J., Fabian, T., et al. (2002). The plant Spc98p homologue colocalizes with gamma-tubulin at microtubule nucleation sites and is required for microtubule nucleation. J. Cell Sci. 115, 2423-2431.
    • (2002) J. Cell Sci. , vol.115 , pp. 2423-2431
    • Erhardt, M.1    Stoppin-Mellet, V.2    Campagne, S.3    Canaday, J.4    Mutterer, J.5    Fabian, T.6
  • 13
    • 67649703990 scopus 로고    scopus 로고
    • Nuclear envelope and nuclear pore complex structure and organization in tobacco BY-2 cells
    • doi: 10.1111/j.1365-313X.2009.03865.x
    • Fiserova, J., Kiseleva, E., and Goldberg, M. (2009). Nuclear envelope and nuclear pore complex structure and organization in tobacco BY-2 cells. Plant J. 59, 243-255. doi: 10.1111/j.1365-313X.2009.03865.x
    • (2009) Plant J. , vol.59 , pp. 243-255
    • Fiserova, J.1    Kiseleva, E.2    Goldberg, M.3
  • 14
    • 0037195153 scopus 로고    scopus 로고
    • Interphase chromosomes in Arabidopsis are organized as well defined chromocenters from which euchromatin loops emanate
    • doi: 10.1073/pnas.212325299
    • Fransz, P., De Jong, J., Lysak, M., Castiglione, M., and Schubert, I. (2002). Interphase chromosomes in Arabidopsis are organized as well defined chromocenters from which euchromatin loops emanate. Proc. Natl. Acad. Sci. U.S.A. 99, 14584-14589. doi: 10.1073/pnas.212325299
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 14584-14589
    • Fransz, P.1    De Jong, J.2    Lysak, M.3    Castiglione, M.4    Schubert, I.5
  • 15
    • 84873527779 scopus 로고    scopus 로고
    • SUNrises on the international plant nucleus consortium: SEB Salzburg 2012
    • doi: 10.4161/nucl.23385
    • Graumann, K., Bass, H. W., and Parry, G. (2013). SUNrises on the international plant nucleus consortium: SEB Salzburg 2012. Nucleus 4, 3-7. doi: 10.4161/nucl.23385
    • (2013) Nucleus , vol.4 , pp. 3-7
    • Graumann, K.1    Bass, H.W.2    Parry, G.3
  • 16
    • 72749086154 scopus 로고    scopus 로고
    • Characterization of SUN-domain proteins at the higher plant nuclear envelope
    • doi: 10.1111/j.1365-313X.2009.04038.x
    • Graumann, K., Runions, J., and Evans, D. (2010). Characterization of SUN-domain proteins at the higher plant nuclear envelope. Plant J. 61, 134-144. doi: 10.1111/j.1365-313X.2009.04038.x
    • (2010) Plant J. , vol.61 , pp. 134-144
    • Graumann, K.1    Runions, J.2    Evans, D.3
  • 17
    • 33745628312 scopus 로고    scopus 로고
    • MGOUN3: Evidence for chromatin-mediated regulation of FLC expression
    • doi: 10.1093/jxb/erj169
    • Guyomarc'h, S., Benhamed, M., Lemonnier, G., Renou, J.-P., Zhou, D.-X., and Delarue, M. (2006). MGOUN3: evidence for chromatin-mediated regulation of FLC expression. J. Exp. Bot. 57, 2111-2119. doi: 10.1093/jxb/erj169
    • (2006) J. Exp. Bot. , vol.57 , pp. 2111-2119
    • Guyomarc'h, S.1    Benhamed, M.2    Lemonnier, G.3    Renou, J.-P.4    Zhou, D.-X.5    Delarue, M.6
  • 18
    • 48249151759 scopus 로고    scopus 로고
    • The concept of translocational regulation
    • doi: 10.1083/jcb.200804157
    • Hegde, R., and Kang, S.-W. (2008). The concept of translocational regulation. J. Cell Biol. 182, 225-232. doi: 10.1083/jcb.200804157
    • (2008) J. Cell Biol. , vol.182 , pp. 225-232
    • Hegde, R.1    Kang, S.-W.2
  • 19
    • 28444472419 scopus 로고    scopus 로고
    • Pushing the envelope: Structure, function, and dynamics of the nuclear periphery
    • doi: 10.1146/annurev.cellbio.21.090704.151152
    • Hetzer, M., Walther, T., and Mattaj, I. (2005). Pushing the envelope: structure, function, and dynamics of the nuclear periphery. Annu. Rev. Cell Dev. Biol. 21, 347-380. doi: 10.1146/annurev.cellbio.21.090704.151152
    • (2005) Annu. Rev. Cell Dev. Biol. , vol.21 , pp. 347-380
    • Hetzer, M.1    Walther, T.2    Mattaj, I.3
  • 20
    • 77951819088 scopus 로고    scopus 로고
    • Systematic analysis of human protein complexes identifies chromosome segregation proteins
    • doi: 10.1126/science.1181348
    • Hutchins, J., Toyoda, Y., Hegemann, B., Poser, I., Hériché, J.-K., Sykora, M., et al. (2010). Systematic analysis of human protein complexes identifies chromosome segregation proteins. Science 328, 593-599. doi: 10.1126/science.1181348
    • (2010) Science , vol.328 , pp. 593-599
    • Hutchins, J.1    Toyoda, Y.2    Hegemann, B.3    Poser, I.4    Hériché, J.-K.5    Sykora, M.6
  • 21
    • 44149107367 scopus 로고    scopus 로고
    • Identification of a novel small Arabidopsis protein interacting with gamma-tubulin complex protein 3
    • doi: 10.1016/j.cellbi.2007.11.006
    • Janski, N., Herzog, E., and Schmit, A.-C. (2008). Identification of a novel small Arabidopsis protein interacting with gamma-tubulin complex protein 3. Cell Biol. Int. 32, 546-548. doi: 10.1016/j.cellbi.2007.11.006
    • (2008) Cell Biol. Int. , vol.32 , pp. 546-548
    • Janski, N.1    Herzog, E.2    Schmit, A.-C.3
  • 22
    • 84860124908 scopus 로고    scopus 로고
    • The GCP3-interacting proteins GIP1 and GIP2 are required for γ-tubulin complex protein localization, spindle integrity, and chromosomal stability
    • doi: 10.1105/tpc.111.094904
    • Janski, N., Masoud, K., Batzenschlager, M., Herzog, E., Evrard, J.-L., Houlné, G., et al. (2012). The GCP3-interacting proteins GIP1 and GIP2 are required for γ-tubulin complex protein localization, spindle integrity, and chromosomal stability. Plant Cell 24, 1171-1187. doi: 10.1105/tpc.111.094904
    • (2012) Plant Cell , vol.24 , pp. 1171-1187
    • Janski, N.1    Masoud, K.2    Batzenschlager, M.3    Herzog, E.4    Evrard, J.-L.5    Houlné, G.6
  • 23
    • 0036581417 scopus 로고    scopus 로고
    • GATEWAY vectors for Agrobacterium-mediated plant transformation
    • doi: 10.1016/S1360-1385(02)02251-3
    • Karimi, M., Inzé, D., and Depicker, A. (2002). GATEWAY vectors for Agrobacterium-mediated plant transformation. Trends Plant Sci. 7, 193-195. doi: 10.1016/S1360-1385(02)02251-3
    • (2002) Trends Plant Sci. , vol.7 , pp. 193-195
    • Karimi, M.1    Inzé, D.2    Depicker, A.3
  • 24
    • 23444456924 scopus 로고    scopus 로고
    • How to study proteins by circular dichroism
    • doi: 10.1016/j.bbapap.2005.06.005
    • Kelly, S., Jess, T., and Price, N. (2005). How to study proteins by circular dichroism. Biochim. Biophys. Acta 1751, 119-139. doi: 10.1016/j.bbapap.2005.06.005
    • (2005) Biochim. Biophys. Acta , vol.1751 , pp. 119-139
    • Kelly, S.1    Jess, T.2    Price, N.3
  • 25
    • 33750970858 scopus 로고    scopus 로고
    • Loading of Arabidopsis centromeric histone CENH3 occurs mainly during G2 and requires the presence of the histone fold domain
    • doi: 10.1105/tpc.106.043174
    • Lermontova, I., Schubert, V., Fuchs, J., Klatte, S., Macas, J., and Schubert, I. (2006). Loading of Arabidopsis centromeric histone CENH3 occurs mainly during G2 and requires the presence of the histone fold domain. Plant Cell 18, 2443-2451. doi: 10.1105/tpc.106.043174
    • (2006) Plant Cell , vol.18 , pp. 2443-2451
    • Lermontova, I.1    Schubert, V.2    Fuchs, J.3    Klatte, S.4    Macas, J.5    Schubert, I.6
  • 26
    • 82455210870 scopus 로고    scopus 로고
    • TSA1 interacts with CSN1/CSN and may be functionally involved in Arabidopsis seedling development in darkness
    • doi: 10.1016/j.jgg.2011.08.007
    • Li, W., Zang, B., Liu, C., Lu, L., Wei, N., Cao, K., et al. (2011). TSA1 interacts with CSN1/CSN and may be functionally involved in Arabidopsis seedling development in darkness. J. Genet. Genomics 38, 539-546. doi: 10.1016/j.jgg.2011.08.007
    • (2011) J. Genet. Genomics , vol.38 , pp. 539-546
    • Li, W.1    Zang, B.2    Liu, C.3    Lu, L.4    Wei, N.5    Cao, K.6
  • 27
    • 0030932134 scopus 로고    scopus 로고
    • A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2
    • doi: 10.1016/S0092-8674(00)81862-0
    • Mahajan, R., Delphin, C., Guan, T., Gerace, L., and Melchior, F. (1997). A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2. Cell 88, 97-107. doi: 10.1016/S0092-8674(00)81862-0
    • (1997) Cell , vol.88 , pp. 97-107
    • Mahajan, R.1    Delphin, C.2    Guan, T.3    Gerace, L.4    Melchior, F.5
  • 28
    • 0346094458 scopus 로고    scopus 로고
    • The C. elegans hook protein, ZYG-12, mediates the essential attachment between the centrosome and nucleus
    • doi: 10.1016/S0092-8674(03)00985-1
    • Malone, C., Misner, L., Le Bot, N., Tsai, M.-C., Campbell, J., Ahringer, J., et al. (2003). The C. elegans hook protein, ZYG-12, mediates the essential attachment between the centrosome and nucleus. Cell 115, 825-836. doi: 10.1016/S0092-8674(03)00985-1
    • (2003) Cell , vol.115 , pp. 825-836
    • Malone, C.1    Misner, L.2    Le Bot, N.3    Tsai, M.-C.4    Campbell, J.5    Ahringer, J.6
  • 29
    • 0032189258 scopus 로고    scopus 로고
    • Signal sequences: More than just greasy peptides
    • doi: 10.1016/S0962-8924(98)01360-9
    • Martoglio, B., and Dobberstein, B. (1998). Signal sequences: more than just greasy peptides. Trends Cell Biol. 8, 410-415. doi: 10.1016/S0962-8924(98)01360-9
    • (1998) Trends Cell Biol. , vol.8 , pp. 410-415
    • Martoglio, B.1    Dobberstein, B.2
  • 30
    • 84884485078 scopus 로고    scopus 로고
    • Fission yeast MOZART1/Mzt1 is an essential γ-tubulin complex component required for complex recruitment to the MTOC, but not its assembly
    • doi: 10.1091/mbc.E13-05-0235
    • Masuda, H., Mori, R., Yukawa, M., and Toda, T. (2013). Fission yeast MOZART1/Mzt1 is an essential γ-tubulin complex component required for complex recruitment to the MTOC, but not its assembly. Mol. Biol. Cell 24, 2894-2906. doi: 10.1091/mbc.E13-05-0235
    • (2013) Mol. Biol. Cell , vol.24 , pp. 2894-2906
    • Masuda, H.1    Mori, R.2    Yukawa, M.3    Toda, T.4
  • 31
    • 32144456009 scopus 로고    scopus 로고
    • Paircoil2: Improved prediction of coiled coils from sequence
    • doi: 10.1093/bioinformatics/bti797
    • McDonnell, A., Jiang, T., Keating, A., and Berger, B. (2006). Paircoil2: improved prediction of coiled coils from sequence. Bioinformatics 22, 356-358. doi: 10.1093/bioinformatics/bti797
    • (2006) Bioinformatics , vol.22 , pp. 356-358
    • McDonnell, A.1    Jiang, T.2    Keating, A.3    Berger, B.4
  • 32
    • 77957678443 scopus 로고    scopus 로고
    • LINC complexes in health and disease
    • doi: 10.4161/nucl.1.1.10530
    • Méjat, A., and Misteli, T. (2010). LINC complexes in health and disease. Nucleus 1, 40-52. doi: 10.4161/nucl.1.1.10530
    • (2010) Nucleus , vol.1 , pp. 40-52
    • Méjat, A.1    Misteli, T.2
  • 33
    • 77951616674 scopus 로고    scopus 로고
    • The nuclear envelope in genome organization, expression and stability
    • doi: 10.1038/nrm2894
    • Mekhail, K., and Moazed, D. (2010). The nuclear envelope in genome organization, expression and stability. Nat. Rev. Mol. Cell Biol. 11, 317-328. doi: 10.1038/nrm2894
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 317-328
    • Mekhail, K.1    Moazed, D.2
  • 35
    • 27944487517 scopus 로고    scopus 로고
    • Functional isolation of novel nuclear proteins showing a variety of subnuclear localizations
    • doi: 10.1105/tpc.104.028456
    • Moriguchi, K., Suzuki, T., Ito, Y., Yamazaki, Y., Niwa, Y., and Kurata, N. (2005). Functional isolation of novel nuclear proteins showing a variety of subnuclear localizations. Plant Cell 17, 389-403. doi: 10.1105/tpc.104.028456
    • (2005) Plant Cell , vol.17 , pp. 389-403
    • Moriguchi, K.1    Suzuki, T.2    Ito, Y.3    Yamazaki, Y.4    Niwa, Y.5    Kurata, N.6
  • 36
    • 78649779114 scopus 로고    scopus 로고
    • Structure and expression of the maize (Zea mays L.) SUN-domain protein gene family: Evidence for the existence of two divergent classes of SUN proteins in plants
    • doi: 10.1186/1471-2229-10-269
    • Murphy, S., Simmons, C., and Bass, H. (2010). Structure and expression of the maize (Zea mays L.) SUN-domain protein gene family: evidence for the existence of two divergent classes of SUN proteins in plants. BMC Plant Biol. 10:269. doi: 10.1186/1471-2229-10-269
    • (2010) BMC Plant Biol. , vol.10 , pp. 269
    • Murphy, S.1    Simmons, C.2    Bass, H.3
  • 37
    • 84864418608 scopus 로고    scopus 로고
    • Arabidopsis GCP3-interacting protein 1/MOZART 1 is an integral component of the γ-tubulin-containing microtubule nucleating complex
    • doi: 10.1111/j.1365-313X.2012.04988.x
    • Nakamura, M., Yagi, N., Kato, T., Fujita, S., Kawashima, N., Ehrhardt, D., et al. (2012). Arabidopsis GCP3-interacting protein 1/MOZART 1 is an integral component of the γ-tubulin-containing microtubule nucleating complex. Plant J. 71, 216-225. doi: 10.1111/j.1365-313X.2012.04988.x
    • (2012) Plant J. , vol.71 , pp. 216-225
    • Nakamura, M.1    Yagi, N.2    Kato, T.3    Fujita, S.4    Kawashima, N.5    Ehrhardt, D.6
  • 38
    • 79954565013 scopus 로고    scopus 로고
    • Dynamics of Arabidopsis SUN proteins during mitosis and their involvement in nuclear shaping
    • doi: 10.1111/j.1365-313X.2011.04523.x
    • Oda, Y., and Fukuda, H. (2011). Dynamics of Arabidopsis SUN proteins during mitosis and their involvement in nuclear shaping. Plant J. 66, 629-641. doi: 10.1111/j.1365-313X.2011.04523.x
    • (2011) Plant J. , vol.66 , pp. 629-641
    • Oda, Y.1    Fukuda, H.2
  • 39
    • 80052671543 scopus 로고    scopus 로고
    • Ectopic gene expression and organogenesis in Arabidopsis mutants missing BRU1 required for genome maintenance
    • doi: 10.1534/genetics.111.130062
    • Ohno, Y., Narangajavana, J., Yamamoto, A., Hattori, T., Kagaya, Y., Paszkowski, J., et al. (2011). Ectopic gene expression and organogenesis in Arabidopsis mutants missing BRU1 required for genome maintenance. Genetics 189, 83-95. doi: 10.1534/genetics.111.130062
    • (2011) Genetics , vol.189 , pp. 83-95
    • Ohno, Y.1    Narangajavana, J.2    Yamamoto, A.3    Hattori, T.4    Kagaya, Y.5    Paszkowski, J.6
  • 40
    • 70849084351 scopus 로고    scopus 로고
    • Dynamics and molecular interactions of linker of nucleoskeleton and cytoskeleton (LINC) complex proteins
    • doi: 10.1242/jcs.057075
    • Ostlund, C., Folker, E., Choi, J., Gomes, E., Gundersen, G., and Worman, H. (2009). Dynamics and molecular interactions of linker of nucleoskeleton and cytoskeleton (LINC) complex proteins. J. Cell Sci. 122, 4099-4108. doi: 10.1242/jcs.057075
    • (2009) J. Cell Sci. , vol.122 , pp. 4099-4108
    • Ostlund, C.1    Folker, E.2    Choi, J.3    Gomes, E.4    Gundersen, G.5    Worman, H.6
  • 41
    • 84874677693 scopus 로고    scopus 로고
    • Assessing the function of the plant nuclear pore complex and the search for specificity
    • doi: 10.1093/jxb/ers289
    • Parry, G. (2013). Assessing the function of the plant nuclear pore complex and the search for specificity. J. Exp. Bot. 64, 833-845. doi: 10.1093/jxb/ers289
    • (2013) J. Exp. Bot. , vol.64 , pp. 833-845
    • Parry, G.1
  • 42
    • 0742285088 scopus 로고    scopus 로고
    • The plant nuclear envelope
    • doi: 10.1007/s00425-003-1132-2
    • Rose, A., Patel, S., and Meier, I. (2004). The plant nuclear envelope. Planta 218, 327-336. doi: 10.1007/s00425-003-1132-2
    • (2004) Planta , vol.218 , pp. 327-336
    • Rose, A.1    Patel, S.2    Meier, I.3
  • 43
    • 34548818532 scopus 로고    scopus 로고
    • A novel role for the nuclear membrane protein emerin in association of the centrosome to the outer nuclear membrane
    • doi: 10.1083/jcb.200702026
    • Salpingidou, G., Smertenko, A., Hausmanowa-Petrucewicz, I., Hussey, P., and Hutchison, C. (2007). A novel role for the nuclear membrane protein emerin in association of the centrosome to the outer nuclear membrane. J. Cell Biol. 178, 897-904. doi: 10.1083/jcb.200702026
    • (2007) J. Cell Biol. , vol.178 , pp. 897-904
    • Salpingidou, G.1    Smertenko, A.2    Hausmanowa-Petrucewicz, I.3    Hussey, P.4    Hutchison, C.5
  • 44
    • 35148873565 scopus 로고    scopus 로고
    • Arabidopsis GCP2 and GCP3 are part of a soluble gamma-tubulin complex and have nuclear envelope targeting domains
    • doi: 10.1111/j.1365-313X.2007.03240.x
    • Seltzer, V., Janski, N., Canaday, J., Herzog, E., Erhardt, M., Evrard, J.-L., et al. (2007). Arabidopsis GCP2 and GCP3 are part of a soluble gamma-tubulin complex and have nuclear envelope targeting domains. Plant J. 52, 322-331. doi: 10.1111/j.1365-313X.2007.03240.x
    • (2007) Plant J. , vol.52 , pp. 322-331
    • Seltzer, V.1    Janski, N.2    Canaday, J.3    Herzog, E.4    Erhardt, M.5    Evrard, J.-L.6
  • 45
    • 0037011060 scopus 로고    scopus 로고
    • DNA methylation controls histone H3 lysine 9 methylation and heterochromatin assembly in Arabidopsis
    • doi: 10.1093/emboj/cdf657
    • Soppe, W. J., Jasencakova, Z., Houben, A., Kakutani, T., Meister, A., Huang, M., et al. (2002). DNA methylation controls histone H3 lysine 9 methylation and heterochromatin assembly in Arabidopsis. EMBO J. 21, 6549-6559. doi: 10.1093/emboj/cdf657
    • (2002) EMBO J. , vol.21 , pp. 6549-6559
    • Soppe, W.J.1    Jasencakova, Z.2    Houben, A.3    Kakutani, T.4    Meister, A.5    Huang, M.6
  • 46
    • 0034672325 scopus 로고    scopus 로고
    • Estimation of protein secondary structure from circular dichroism spectra: Comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set
    • doi: 10.1006/abio.2000.4880
    • Sreerama, N., and Woody, R. (2000). Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set. Anal. Biochem. 287, 252-260. doi: 10.1006/abio.2000.4880
    • (2000) Anal. Biochem. , vol.287 , pp. 252-260
    • Sreerama, N.1    Woody, R.2
  • 47
    • 84866177329 scopus 로고    scopus 로고
    • Laminopathies: Too much SUN is a bad thing
    • doi: 10.1016/j.cub.2012.06.070
    • Starr, D. (2012). Laminopathies: too much SUN is a bad thing. Curr. Biol. 22, R678-R680. doi: 10.1016/j.cub.2012.06.070
    • (2012) Curr. Biol. , vol.22
    • Starr, D.1
  • 48
    • 0028118071 scopus 로고
    • Isolated Plant nuclei nucleate microtubule assembly: The nuclear surface in higher plants has centrosome-like activity
    • Stoppin, V., Vantard, M., Schmit, A., and Lambert, A. (1994). Isolated Plant nuclei nucleate microtubule assembly: the nuclear surface in higher plants has centrosome-like activity. Plant Cell 6, 1099-1106.
    • (1994) Plant Cell , vol.6 , pp. 1099-1106
    • Stoppin, V.1    Vantard, M.2    Schmit, A.3    Lambert, A.4
  • 49
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • doi: 10.1016/j.pep.2005.01.016
    • Studier, F. (2005). Protein production by auto-induction in high density shaking cultures. Protein Expr. Purif. 41, 207-234. doi: 10.1016/j.pep.2005.01.016
    • (2005) Protein Expr. Purif. , vol.41 , pp. 207-234
    • Studier, F.1
  • 50
    • 0031686054 scopus 로고    scopus 로고
    • Nuclear lamins: Their structure, assembly, and interactions
    • doi: 10.1006/jsbi.1998.3987
    • Stuurman, N., Heins, S., and Aebi, U. (1998). Nuclear lamins: their structure, assembly, and interactions. J. Struct. Biol. 122, 42-66. doi: 10.1006/jsbi.1998.3987
    • (1998) J. Struct. Biol. , vol.122 , pp. 42-66
    • Stuurman, N.1    Heins, S.2    Aebi, U.3
  • 51
    • 1842794155 scopus 로고    scopus 로고
    • A novel Arabidopsis gene TONSOKU is required for proper cell arrangement in root and shoot apical meristems
    • doi: 10.1111/j.1365-313X.2004.02074.x
    • Suzuki, T., Inagaki, S., Nakajima, S., Akashi, T., Ohto, M.-A., Kobayashi, M., et al. (2004). A novel Arabidopsis gene TONSOKU is required for proper cell arrangement in root and shoot apical meristems. Plant J. 38, 673-684. doi: 10.1111/j.1365-313X.2004.02074.x
    • (2004) Plant J. , vol.38 , pp. 673-684
    • Suzuki, T.1    Inagaki, S.2    Nakajima, S.3    Akashi, T.4    Ohto, M.-A.5    Kobayashi, M.6
  • 52
    • 26444461164 scopus 로고    scopus 로고
    • An Arabidopsis protein with a novel calcium-binding repeat sequence interacts with TONSOKU/MGOUN3 /BRUSHY1 involved in meristem maintenance
    • doi: 10.1093/pcp/pci155
    • Suzuki, T., Nakajima, S., Morikami, A., and Nakamura, K. (2005). An Arabidopsis protein with a novel calcium-binding repeat sequence interacts with TONSOKU/MGOUN3 /BRUSHY1 involved in meristem maintenance. Plant Cell Physiol. 46, 1452-1461. doi: 10.1093/pcp/pci155
    • (2005) Plant Cell Physiol. , vol.46 , pp. 1452-1461
    • Suzuki, T.1    Nakajima, S.2    Morikami, A.3    Nakamura, K.4
  • 53
    • 11144358325 scopus 로고    scopus 로고
    • BRU1, a novel link between responses to DNA damage and epigenetic gene silencing in Arabidopsis
    • doi: 10.1101/gad.295404
    • Takeda, S., Tadele, Z., Hofmann, I., Probst, A., Angelis, K., Kaya, H., et al. (2004). BRU1, a novel link between responses to DNA damage and epigenetic gene silencing in Arabidopsis. Genes Dev. 18, 782-793. doi: 10.1101/gad.295404
    • (2004) Genes Dev. , vol.18 , pp. 782-793
    • Takeda, S.1    Tadele, Z.2    Hofmann, I.3    Probst, A.4    Angelis, K.5    Kaya, H.6
  • 54
    • 79551629546 scopus 로고    scopus 로고
    • Identification and characterization of nuclear pore complex components in Arabidopsis thaliana
    • doi: 10.1105/tpc.110.079947
    • Tamura, K., Fukao, Y., Iwamoto, M., Haraguchi, T., and Hara-Nishimura, I. (2010). Identification and characterization of nuclear pore complex components in Arabidopsis thaliana. Plant Cell 22, 4084-4097. doi: 10.1105/tpc.110.079947
    • (2010) Plant Cell , vol.22 , pp. 4084-4097
    • Tamura, K.1    Fukao, Y.2    Iwamoto, M.3    Haraguchi, T.4    Hara-Nishimura, I.5
  • 55
    • 84884595294 scopus 로고    scopus 로고
    • Myosin XI-i links the nuclear membrane to the cytoskeleton to control nuclear movement and shape in Arabidopsis
    • doi: 10.1016/j.cub.2013.07.035
    • Tamura, K., Iwabuchi, K., Fukao, Y., Kondo, M., Okamoto, K., Ueda, H., et al. (2013). Myosin XI-i links the nuclear membrane to the cytoskeleton to control nuclear movement and shape in Arabidopsis. Curr. Biol. 23, 1776-1781. doi: 10.1016/j.cub.2013.07.035
    • (2013) Curr. Biol. , vol.23 , pp. 1776-1781
    • Tamura, K.1    Iwabuchi, K.2    Fukao, Y.3    Kondo, M.4    Okamoto, K.5    Ueda, H.6
  • 56
    • 84861415993 scopus 로고    scopus 로고
    • Shedding light on large-scale chromatin reorganization in Arabidopsis thaliana
    • doi: 10.1093/mp/sss030
    • van Zanten, M., Tessadori, F., Peeters, A., and Fransz, P. (2012). Shedding light on large-scale chromatin reorganization in Arabidopsis thaliana. Mol. Plant 5, 583-590. doi: 10.1093/mp/sss030
    • (2012) Mol. Plant , vol.5 , pp. 583-590
    • van Zanten, M.1    Tessadori, F.2    Peeters, A.3    Fransz, P.4
  • 57
    • 84867055836 scopus 로고    scopus 로고
    • Structural insights into SUN-KASH complexes across the nuclear envelope
    • doi: 10.1038/cr.2012.126
    • Wang, W., Shi, Z., Jiao, S., Chen, C., Wang, H., Liu, G., et al. (2012). Structural insights into SUN-KASH complexes across the nuclear envelope. Cell Res. 22, 1440-1452. doi: 10.1038/cr.2012.126
    • (2012) Cell Res. , vol.22 , pp. 1440-1452
    • Wang, W.1    Shi, Z.2    Jiao, S.3    Chen, C.4    Wang, H.5    Liu, G.6
  • 58
    • 66149188986 scopus 로고    scopus 로고
    • Regulation of COP1 nuclear localization by the COP9 signalosome via direct interaction with CSN1
    • doi: 10.1111/j.1365-313X.2009.03805.x
    • Wang, X., Li, W., Piqueras, R., Cao, K., Deng, X., and Wei, N. (2009). Regulation of COP1 nuclear localization by the COP9 signalosome via direct interaction with CSN1. Plant J. 58, 655-667. doi: 10.1111/j.1365-313X.2009.03805.x
    • (2009) Plant J. , vol.58 , pp. 655-667
    • Wang, X.1    Li, W.2    Piqueras, R.3    Cao, K.4    Deng, X.5    Wei, N.6
  • 59
    • 78651324803 scopus 로고    scopus 로고
    • PCDDB: The protein circular dichroism data bank, a repository for circular dichroism spectral and metadata
    • doi: 10.1093/nar/gkq1026
    • Whitmore, L., Woollett, B., Miles, A., Klose, D., Janes, R., and Wallace, B. (2011). PCDDB: the protein circular dichroism data bank, a repository for circular dichroism spectral and metadata. Nucleic Acids Res. 39, D480-D486. doi: 10.1093/nar/gkq1026
    • (2011) Nucleic Acids Res. , vol.39
    • Whitmore, L.1    Woollett, B.2    Miles, A.3    Klose, D.4    Janes, R.5    Wallace, B.6
  • 60
    • 77957263769 scopus 로고    scopus 로고
    • Diseases of the nuclear envelope. Cold Spring Harb
    • doi: 10.1101/cshperspect.a000760
    • Worman, H., Ostlund, C., and Wang, Y. (2010). Diseases of the nuclear envelope. Cold Spring Harb. Perspect. Biol. 2:a000760. doi: 10.1101/cshperspect.a000760
    • (2010) Perspect. Biol. , vol.2
    • Worman, H.1    Ostlund, C.2    Wang, Y.3
  • 61
    • 34250851687 scopus 로고    scopus 로고
    • LOMETS: A local meta-threading-server for protein structure prediction
    • doi: 10.1093/nar/gkm251
    • Wu, S., and Zhang, Y. (2007). LOMETS: a local meta-threading-server for protein structure prediction. Nucleic Acids. Res. 35, 3375-3382. doi: 10.1093/nar/gkm251
    • (2007) Nucleic Acids. Res. , vol.35 , pp. 3375-3382
    • Wu, S.1    Zhang, Y.2
  • 62
    • 0029842243 scopus 로고    scopus 로고
    • Plant cells contain a novel member of the retinoblastoma family of growth regulatory proteins
    • Xie, Q., Sanz-Burgos, A., Hannon, G., and Gutiérrez, C. (1996). Plant cells contain a novel member of the retinoblastoma family of growth regulatory proteins. EMBO J. 15, 4900-4908.
    • (1996) EMBO J. , vol.15 , pp. 4900-4908
    • Xie, Q.1    Sanz-Burgos, A.2    Hannon, G.3    Gutiérrez, C.4
  • 63
    • 34250857058 scopus 로고    scopus 로고
    • Anchorage of plant RanGAP to the nuclear envelope involves novel nuclear-pore-associated proteins
    • doi: 10.1016/j.cub.2007.05.076
    • Xu, X., Meulia, T., and Meier, I. (2007). Anchorage of plant RanGAP to the nuclear envelope involves novel nuclear-pore-associated proteins. Curr. Biol. 17, 1157-1163. doi: 10.1016/j.cub.2007.05.076
    • (2007) Curr. Biol. , vol.17 , pp. 1157-1163
    • Xu, X.1    Meulia, T.2    Meier, I.3
  • 64
    • 57749091765 scopus 로고    scopus 로고
    • NAI2 is an endoplasmic reticulum body component that enables ER body formation in Arabidopsis thaliana
    • doi: 10.1105/tpc.108.059345
    • Yamada, K., Nagano, A., Nishina, M., Hara-Nishimura, I., and Nishimura, M. (2008). NAI2 is an endoplasmic reticulum body component that enables ER body formation in Arabidopsis thaliana. Plant Cell 20, 2529-2540. doi: 10.1105/tpc.108.059345
    • (2008) Plant Cell , vol.20 , pp. 2529-2540
    • Yamada, K.1    Nagano, A.2    Nishina, M.3    Hara-Nishimura, I.4    Nishimura, M.5
  • 65
    • 53149083819 scopus 로고    scopus 로고
    • Two distinct interacting classes of nuclear envelope-associated coiled-coil proteins are required for the tissue-specific nuclear envelope targeting of Arabidopsis RanGAP
    • doi: 10.1105/tpc.108.059220
    • Zhao, Q., Brkljacic, J., and Meier, I. (2008). Two distinct interacting classes of nuclear envelope-associated coiled-coil proteins are required for the tissue-specific nuclear envelope targeting of Arabidopsis RanGAP. Plant Cell 20, 1639-1651. doi: 10.1105/tpc.108.059220
    • (2008) Plant Cell , vol.20 , pp. 1639-1651
    • Zhao, Q.1    Brkljacic, J.2    Meier, I.3
  • 66
    • 67749135404 scopus 로고    scopus 로고
    • A ZYG-12-dynein interaction at the nuclear envelope defines cytoskeletal architecture in the C. elegans gonad
    • doi: 10.1083/jcb.200902101
    • Zhou, K., Rolls, M., Hall, D., Malone, C., and Hanna-Rose, W. (2009). A ZYG-12-dynein interaction at the nuclear envelope defines cytoskeletal architecture in the C. elegans gonad. J. Cell Biol 186, 229-241. doi: 10.1083/jcb.200902101
    • (2009) J. Cell Biol , vol.186 , pp. 229-241
    • Zhou, K.1    Rolls, M.2    Hall, D.3    Malone, C.4    Hanna-Rose, W.5
  • 67
    • 84863027078 scopus 로고    scopus 로고
    • Novel plant SUN-KASH bridges are involved in RanGAP anchoring and nuclear shape determination
    • doi: 10.1083/jcb.201108098
    • Zhou, X., Graumann, K., Evans, D., and Meier, I. (2012). Novel plant SUN-KASH bridges are involved in RanGAP anchoring and nuclear shape determination. J. Cell Biol. 196, 203-211. doi: 10.1083/jcb.201108098
    • (2012) J. Cell Biol. , vol.196 , pp. 203-211
    • Zhou, X.1    Graumann, K.2    Evans, D.3    Meier, I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.