메뉴 건너뛰기




Volumn 63, Issue 3, 2006, Pages 316-332

The role of the nuclear envelope in cellular organization

Author keywords

Chromatin; Nuclear envelope; Nuclear pore complex

Indexed keywords

LAMIN; MEMBRANE PROTEIN; NUCLEAR PROTEIN; NUCLEOPORIN; NUCLEOPORIN 84; RAN PROTEIN; UNCLASSIFIED DRUG;

EID: 32044433784     PISSN: 1420682X     EISSN: 15691632     Source Type: Journal    
DOI: 10.1007/s00018-005-5361-3     Document Type: Review
Times cited : (79)

References (253)
  • 1
    • 3242807744 scopus 로고
    • The nuclear envelope; its structure and relation to cytoplasmic membranes
    • Watson M. L. (1955). The nuclear envelope; its structure and relation to cytoplasmic membranes. J Biophys Biochem Cytol 1: 257-270
    • (1955) J Biophys Biochem Cytol , vol.1 , pp. 257-270
    • Watson, M.L.1
  • 2
    • 0019842267 scopus 로고
    • The nuclear envelope and the architecture of the nuclear periphery
    • Franke W. W., Scheer U., Krohne G. and Jarasch E. D. (1981) The nuclear envelope and the architecture of the nuclear periphery. J. Cell Biol. 91: 39s-50s
    • (1981) J. Cell Biol. , vol.91
    • Franke, W.W.1    Scheer, U.2    Krohne, G.3    Jarasch, E.D.4
  • 3
    • 0023085878 scopus 로고
    • The nucleus: Structure, function, and dynamics
    • Newport J. W. and Forbes D. J. (1987) The nucleus: structure, function, and dynamics. Annu. Rev. Biochem. 56: 535-565
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 535-565
    • Newport, J.W.1    Forbes, D.J.2
  • 4
    • 0024147084 scopus 로고
    • Functional organization of the nuclear envelope
    • Gerace L. and Burke B. (1988) Functional organization of the nuclear envelope. Annu. Rev. Cell. Biol. 4: 335-374
    • (1988) Annu. Rev. Cell. Biol. , vol.4 , pp. 335-374
    • Gerace, L.1    Burke, B.2
  • 5
    • 0346094458 scopus 로고    scopus 로고
    • The C. elegans hook protein, ZYG-12: Mediates the essential attachment between the centrosome and nucleus
    • Malone C. J., Misner L., Le Bot N., Tsai M. C., Campbell J. M., 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
    • (2003) Cell , vol.115 , pp. 825-836
    • Malone, C.J.1    Misner, L.2    Le Bot, N.3    Tsai, M.C.4    Campbell, J.M.5    Ahringer, J.6
  • 6
    • 0034644646 scopus 로고    scopus 로고
    • Syne-1: A dystrophin- and Klarsicht-related protein associated with synaptic nuclei at the neuromuscular junction
    • Apel E. D., Lewis R. M., Grady R. M. and Sanes J. R. (2000) Syne-1: a dystrophin- and Klarsicht-related protein associated with synaptic nuclei at the neuromuscular junction. J. Biol. Chem. 275: 31986-31995
    • (2000) J. Biol. Chem. , vol.275 , pp. 31986-31995
    • Apel, E.D.1    Lewis, R.M.2    Grady, R.M.3    Sanes, J.R.4
  • 7
    • 10844286384 scopus 로고    scopus 로고
    • Drosophila klarsicht has distinct subcellular localization domains for nuclear envelope and microtubule localization in the eye
    • Fischer J. A., Acosta S., Kenny A., Cater C., Robinson C. and Hook J. (2004) Drosophila klarsicht has distinct subcellular localization domains for nuclear envelope and microtubule localization in the eye. Genetics 168: 1385-1393
    • (2004) Genetics , vol.168 , pp. 1385-1393
    • Fischer, J.A.1    Acosta, S.2    Kenny, A.3    Cater, C.4    Robinson, C.5    Hook, J.6
  • 8
    • 0037064176 scopus 로고    scopus 로고
    • Role of ANC-1 in tethering nuclei to the actin cytoskeleton
    • Starr D. A. and Han M. (2002) Role of ANC-1 in tethering nuclei to the actin cytoskeleton. Science 298: 406-409
    • (2002) Science , vol.298 , pp. 406-409
    • Starr, D.A.1    Han, M.2
  • 9
    • 1842850780 scopus 로고    scopus 로고
    • Enaptin, a giant actin-binding protein, is an element of the nuclear membrane and the actin cytoskeleton
    • Padmakumar V. C., Abraham S., Braune S., Noegel A. A., Tunggal B., Karakesisoglou I. et al. (2004) Enaptin, a giant actin-binding protein, is an element of the nuclear membrane and the actin cytoskeleton. Exp. Cell Res. 295: 330-339
    • (2004) Exp. Cell Res. , vol.295 , pp. 330-339
    • Padmakumar, V.C.1    Abraham, S.2    Braune, S.3    Noegel, A.A.4    Tunggal, B.5    Karakesisoglou, I.6
  • 10
    • 0036674866 scopus 로고    scopus 로고
    • NUANCE, a giant protein connecting the nucleus and actin cytoskeleton
    • Zhen Y. Y., Libotte T., Munck M., Noegel A. A. and Korenbaum E. (2002) NUANCE, a giant protein connecting the nucleus and actin cytoskeleton. J. Cell. Sci. 115: 3207-3222
    • (2002) J. Cell. Sci. , vol.115 , pp. 3207-3222
    • Zhen, Y.Y.1    Libotte, T.2    Munck, M.3    Noegel, A.A.4    Korenbaum, E.5
  • 12
    • 0036347096 scopus 로고    scopus 로고
    • Life at the edge: The nuclear envelope and human disease
    • Burke B. and Stewart C. L. (2002) Life at the edge: the nuclear envelope and human disease. Nat. Rev. Mol. Cell Biol. 3: 575-585
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 575-585
    • Burke, B.1    Stewart, C.L.2
  • 13
    • 0035197416 scopus 로고    scopus 로고
    • Inner nuclear membrane proteins: Functions and targeting
    • Holmer L. and Worman H. J. (2001) Inner nuclear membrane proteins: functions and targeting. Cell. Mol. Life Sci. 58: 1741-1747
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 1741-1747
    • Holmer, L.1    Worman, H.J.2
  • 17
    • 0033279841 scopus 로고    scopus 로고
    • Transport between the cell nucleus and the cytoplasm
    • Gorlich D. and Kutay U. (1999) Transport between the cell nucleus and the cytoplasm. Annu. Rev. Cell Dev. Biol. 15: 607-660
    • (1999) Annu. Rev. Cell Dev. Biol. , vol.15 , pp. 607-660
    • Gorlich, D.1    Kutay, U.2
  • 18
    • 0031707505 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: The soluble phase
    • Mattaj I. W. and Englmeier L. (1998) Nucleocytoplasmic transport: the soluble phase. Annu. Rev. Biochem. 67: 265-306
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 265-306
    • Mattaj, I.W.1    Englmeier, L.2
  • 19
    • 0034717044 scopus 로고    scopus 로고
    • Gatekeepers of the nucleus
    • Wente S. R. (2000) Gatekeepers of the nucleus. Science 288: 1374-1377
    • (2000) Science , vol.288 , pp. 1374-1377
    • Wente, S.R.1
  • 20
    • 0036591883 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: Cargo trafficking across the border
    • Weis K. (2002) Nucleocytoplasmic transport: cargo trafficking across the border. Curr. Opin. Cell Biol. 14: 328-335
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 328-335
    • Weis, K.1
  • 21
    • 0035370938 scopus 로고    scopus 로고
    • Nuclear pores and nuclear assembly
    • Vasu S. K. and Forbes D. J. (2001) Nuclear pores and nuclear assembly. Curr. Opin. Cell Biol. 13: 363-375
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 363-375
    • Vasu, S.K.1    Forbes, D.J.2
  • 22
    • 0032933745 scopus 로고    scopus 로고
    • Receptor-mediated substrate translocation through the nuclear pore complex without nucleotide triphosphate hydrolysis
    • Englmeier L., Olivo J. C. and Mattaj I. W. (1999) Receptor-mediated substrate translocation through the nuclear pore complex without nucleotide triphosphate hydrolysis. Curr. Biol. 9: 30-41
    • (1999) Curr. Biol. , vol.9 , pp. 30-41
    • Englmeier, L.1    Olivo, J.C.2    Mattaj, I.W.3
  • 23
    • 0025247954 scopus 로고
    • Correlation between structure and mass distribution of the nuclear pore complex and of distinct pore complex components
    • Reichelt R., Holzenburg A., Buhle E. L. Jr., Jarnik M., Engel A. and Aebi U. (1990) Correlation between structure and mass distribution of the nuclear pore complex and of distinct pore complex components. J. Cell Biol. 110: 883-894
    • (1990) J. Cell Biol. , vol.110 , pp. 883-894
    • Reichelt, R.1    Holzenburg, A.2    Buhle Jr., E.L.3    Jarnik, M.4    Engel, A.5    Aebi, U.6
  • 24
    • 0027366167 scopus 로고
    • Isolation of the yeast nuclear pore complex
    • Rout M. P. and Blobel G. (1993) Isolation of the yeast nuclear pore complex. J. Cell Biol. 123: 771-783
    • (1993) J. Cell Biol. , vol.123 , pp. 771-783
    • Rout, M.P.1    Blobel, G.2
  • 25
    • 0031604505 scopus 로고    scopus 로고
    • Three-dimensional architecture of the isolated yeast nuclear pore complex: Functional and evolutionary implications
    • Yang Q., Rout M. P. and Akey C. W. (1998) Three-dimensional architecture of the isolated yeast nuclear pore complex: functional and evolutionary implications. Mol. Cell 1: 223-234
    • (1998) Mol. Cell , vol.1 , pp. 223-234
    • Yang, Q.1    Rout, M.P.2    Akey, C.W.3
  • 26
    • 8644262258 scopus 로고    scopus 로고
    • Importin beta: Conducting a much larger cellular symphony
    • Harel A. and Forbes D. J. (2004) Importin beta: conducting a much larger cellular symphony. Mol. Cell 16: 319-330
    • (2004) Mol. Cell , vol.16 , pp. 319-330
    • Harel, A.1    Forbes, D.J.2
  • 27
    • 0035907248 scopus 로고    scopus 로고
    • The nuclear pore complex as a transport machine
    • Rout M. P. and Aitchison J. D. (2001) The nuclear pore complex as a transport machine. J. Biol. Chem. 276: 16593-16596
    • (2001) J. Biol. Chem. , vol.276 , pp. 16593-16596
    • Rout, M.P.1    Aitchison, J.D.2
  • 28
    • 0037459085 scopus 로고    scopus 로고
    • Regulating access to the genome: Nucleocytoplasmic transport throughout the cell cycle
    • Weis K. (2003) Regulating access to the genome: nucleocytoplasmic transport throughout the cell cycle. Cell 112: 441-451
    • (2003) Cell , vol.112 , pp. 441-451
    • Weis, K.1
  • 29
    • 0037162398 scopus 로고    scopus 로고
    • The Ran GTPase: Theme and variations
    • Dasso M. (2002) The Ran GTPase: theme and variations. Curr. Biol. 12: R502-R508
    • (2002) Curr. Biol. , vol.12
    • Dasso, M.1
  • 30
    • 1042278767 scopus 로고    scopus 로고
    • Nuclear transport and cancer: From mechanism to intervention
    • Kau T. R., Way J. C. and Silver P. A. (2004) Nuclear transport and cancer: from mechanism to intervention. Nat. Rev. Cancer 4: 106-117
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 106-117
    • Kau, T.R.1    Way, J.C.2    Silver, P.A.3
  • 31
    • 0015160648 scopus 로고
    • On the octagonality of the nuclear pore complex
    • Maul G. G. (1971) On the octagonality of the nuclear pore complex. J. Cell Biol. 51: 558-563
    • (1971) J. Cell Biol. , vol.51 , pp. 558-563
    • Maul, G.G.1
  • 32
    • 0034695924 scopus 로고    scopus 로고
    • The yeast nuclear pore complex: Composition, architecture and transport mechanism
    • Rout M. P., Aitchison J. D., Suprapto A., Hjertaas K., Zhao Y. and Chait B. T. (2000) The yeast nuclear pore complex: composition, architecture and transport mechanism. J. Cell Biol. 148: 635-651
    • (2000) J. Cell Biol. , vol.148 , pp. 635-651
    • Rout, M.P.1    Aitchison, J.D.2    Suprapto, A.3    Hjertaas, K.4    Zhao, Y.5    Chait, B.T.6
  • 35
    • 0036469369 scopus 로고    scopus 로고
    • Modular self-assembly of a Y-shaped multiprotein complex from seven nucleoporins
    • Lutzmann M., Kunze R., Buerer A., Aebi U. and Hurt E. (2002) Modular self-assembly of a Y-shaped multiprotein complex from seven nucleoporins. EMBO J. 21: 387-397
    • (2002) EMBO J. , vol.21 , pp. 387-397
    • Lutzmann, M.1    Kunze, R.2    Buerer, A.3    Aebi, U.4    Hurt, E.5
  • 36
    • 0031056904 scopus 로고    scopus 로고
    • Dimples, pores, star-rings and thin rings on growing nuclear envelopes: Evidence for structural intermediates in nuclear pore complex assembly
    • Goldberg M. W., Wiese C., Allen T. D. and Wilson K. L. (1997) Dimples, pores, star-rings and thin rings on growing nuclear envelopes: evidence for structural intermediates in nuclear pore complex assembly. J. Cell. Sci. 110 (Pt 4): 409-420
    • (1997) J. Cell. Sci. , vol.110 , Issue.4 PART , pp. 409-420
    • Goldberg, M.W.1    Wiese, C.2    Allen, T.D.3    Wilson, K.L.4
  • 37
    • 0031005268 scopus 로고    scopus 로고
    • From nucleoporins to nuclear pore complexes
    • Doye V. and Hurt E. (1997) From nucleoporins to nuclear pore complexes. Curr. Opin. Cell Biol. 9: 401-411
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 401-411
    • Doye, V.1    Hurt, E.2
  • 38
    • 0030031968 scopus 로고    scopus 로고
    • A novel complex of nucleoporins, which includes Sec 13p and a Sec13p homolog, is essential for normal nuclear pores
    • Siniossoglou S., Wimmer C., Rieger M., Doye V., Tekotte H., Weise C. et al. (1996) A novel complex of nucleoporins, which includes Sec 13p and a Sec13p homolog, is essential for normal nuclear pores. Cell 84: 265-275
    • (1996) Cell , vol.84 , pp. 265-275
    • Siniossoglou, S.1    Wimmer, C.2    Rieger, M.3    Doye, V.4    Tekotte, H.5    Weise, C.6
  • 39
    • 3042712133 scopus 로고    scopus 로고
    • The fission yeast Nup107-120 complex functionally interacts with the small GTPase Ran/Spi1 and is required for mRNA export, nuclear pore distribution and proper cell division
    • Bai S. W., Rouquette J., Umeda M., Faigle W., Loew D., Sazer S. et al. (2004) The fission yeast Nup107-120 complex functionally interacts with the small GTPase Ran/Spi1 and is required for mRNA export, nuclear pore distribution and proper cell division. Mol. Cell. Biol. 24: 6379-6392
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 6379-6392
    • Bai, S.W.1    Rouquette, J.2    Umeda, M.3    Faigle, W.4    Loew, D.5    Sazer, S.6
  • 40
    • 0033594084 scopus 로고    scopus 로고
    • A conserved biogenesis pathway for nucleoporins: Proteolytic processing of a 186-kilodalton precursor generates Nup98 and the novel nucleoporin, Nup96
    • Fontoura B. M., Blobel G. and Matunis M. J. (1999) A conserved biogenesis pathway for nucleoporins: proteolytic processing of a 186-kilodalton precursor generates Nup98 and the novel nucleoporin, Nup96. J. Cell Biol. 144: 1097-1112
    • (1999) J. Cell Biol. , vol.144 , pp. 1097-1112
    • Fontoura, B.M.1    Blobel, G.2    Matunis, M.J.3
  • 41
    • 0035904235 scopus 로고    scopus 로고
    • An evolutionarily conserved NPC subcomplex, which redistributes in part to kinetochores in mammalian cells
    • Belgareh N., Rabut G., Bai S. W., van Overbeek M., Beaudouin J., Daigle N. et al. (2001) An evolutionarily conserved NPC subcomplex, which redistributes in part to kinetochores in mammalian cells. J. Cell Biol. 154: 1147-1160
    • (2001) J. Cell Biol. , vol.154 , pp. 1147-1160
    • Belgareh, N.1    Rabut, G.2    Bai, S.W.3    Van Overbeek, M.4    Beaudouin, J.5    Daigle, N.6
  • 42
    • 0035851914 scopus 로고    scopus 로고
    • Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA export
    • Vasu S., Shah S., Orjalo A., Park M., Fischer W. H. and Forbes D. J. (2001) Novel vertebrate nucleoporins Nup133 and Nup160 play a role in mRNA export. J. Cell Biol. 155: 339-354
    • (2001) J. Cell Biol. , vol.155 , pp. 339-354
    • Vasu, S.1    Shah, S.2    Orjalo, A.3    Park, M.4    Fischer, W.H.5    Forbes, D.J.6
  • 43
    • 0037547118 scopus 로고    scopus 로고
    • Removal of a single pore subcomplex results in vertebrate nuclei devoid of nuclear pores
    • Harel A., Orjalo A. V., Vincent T., Lachish-Zalait A., Vasu S., Shah S. et al. (2003) Removal of a single pore subcomplex results in vertebrate nuclei devoid of nuclear pores. Mol. Cell 11: 853-864
    • (2003) Mol. Cell , vol.11 , pp. 853-864
    • Harel, A.1    Orjalo, A.V.2    Vincent, T.3    Lachish-Zalait, A.4    Vasu, S.5    Shah, S.6
  • 44
    • 17044457744 scopus 로고    scopus 로고
    • The entire Nup 107-160 complex, including three new members, is targeted as one entity to kinetochores in mitosis
    • Loiodice I., Alves A., Rabut G., Van Overbeek M., Ellenberg J., Sibarita J. B. et al. (2004) The entire Nup 107-160 complex, including three new members, is targeted as one entity to kinetochores in mitosis. Mol. Biol. Cell 15: 3333-3344
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3333-3344
    • Loiodice, I.1    Alves, A.2    Rabut, G.3    Van Overbeek, M.4    Ellenberg, J.5    Sibarita, J.B.6
  • 45
    • 0037417808 scopus 로고    scopus 로고
    • Depletion of a single nucleoporin, Nup107, prevents the assembly of a subset of nucleoporins into the nuclear pore complex
    • USA
    • Boehmer T., Enninga J., Dales S., Blobel G. and Zhong H. (2003) Depletion of a single nucleoporin, Nup107, prevents the assembly of a subset of nucleoporins into the nuclear pore complex. Proc. Natl. Acad. Sci. USA 100: 981-985
    • (2003) Proc. Natl. Acad. Sci. , vol.100 , pp. 981-985
    • Boehmer, T.1    Enninga, J.2    Dales, S.3    Blobel, G.4    Zhong, H.5
  • 46
    • 0242668887 scopus 로고    scopus 로고
    • The conserved Nup107-160 complex is critical for nuclear pore complex assembly
    • Walther T. C., Alves A., Pickersgill H., Loiodice I., Hetzer M., Galy V. et al. (2003) The conserved Nup107-160 complex is critical for nuclear pore complex assembly. Cell 113: 195-206
    • (2003) Cell , vol.113 , pp. 195-206
    • Walther, T.C.1    Alves, A.2    Pickersgill, H.3    Loiodice, I.4    Hetzer, M.5    Galy, V.6
  • 47
    • 0027454503 scopus 로고
    • The Sec13p complex and reconstitution of vesicle budding from the ER with purified cytosolic proteins
    • Salama N. R., Yeung T. and Schekman R. W. (1993) The Sec13p complex and reconstitution of vesicle budding from the ER with purified cytosolic proteins. EMBO J. 12: 4073-4082
    • (1993) EMBO J. , vol.12 , pp. 4073-4082
    • Salama, N.R.1    Yeung, T.2    Schekman, R.W.3
  • 48
    • 9744266768 scopus 로고    scopus 로고
    • The N-terminal domain of Nup159 forms a beta-propeller that functions in mRNA export by tethering the helicase Dbp5 to the nuclear pore
    • Weirich C. S., Erzberger J. P., Berger J. M. and Weis K. (2004) The N-terminal domain of Nup159 forms a beta-propeller that functions in mRNA export by tethering the helicase Dbp5 to the nuclear pore. Mol. Cell 16: 749-760
    • (2004) Mol. Cell , vol.16 , pp. 749-760
    • Weirich, C.S.1    Erzberger, J.P.2    Berger, J.M.3    Weis, K.4
  • 49
    • 1842715846 scopus 로고    scopus 로고
    • The RanGAP1-RanBP2 complex is essential for microtubule-kinetochore interactions in vivo
    • Joseph J., Liu S. T., Jablonski S. A., Yen T. J. and Dasso M. (2004) The RanGAP1-RanBP2 complex is essential for microtubule-kinetochore interactions in vivo. Curr. Biol. 14: 611-617
    • (2004) Curr. Biol. , vol.14 , pp. 611-617
    • Joseph, J.1    Liu, S.T.2    Jablonski, S.A.3    Yen, T.J.4    Dasso, M.5
  • 51
    • 0033545869 scopus 로고    scopus 로고
    • Two distinct classes of Ran-binding sites on the nucleoporin Nup-358
    • USA
    • Yaseen N. R. and Blobel G. (1999) Two distinct classes of Ran-binding sites on the nucleoporin Nup-358. Proc. Natl. Acad. Sci. USA 96: 5516-5521
    • (1999) Proc. Natl. Acad. Sci. , vol.96 , pp. 5516-5521
    • Yaseen, N.R.1    Blobel, G.2
  • 54
    • 0037059619 scopus 로고    scopus 로고
    • The nucleoporin RanBP2 has SUMO1 E3 ligase activity
    • Pichler A., Gast A., Seeler J. S., Dejean A. and Melchior F. (2002) The nucleoporin RanBP2 has SUMO1 E3 ligase activity. Cell 108: 109-120
    • (2002) Cell , vol.108 , pp. 109-120
    • Pichler, A.1    Gast, A.2    Seeler, J.S.3    Dejean, A.4    Melchior, F.5
  • 56
    • 0035044364 scopus 로고    scopus 로고
    • Novel role for a Saccharomyces cerevisiae nucleoporin, Nup170p, in chromosome segregation
    • Kerscher O., Hieter P., Winey M. and Basrai M. A. (2001) Novel role for a Saccharomyces cerevisiae nucleoporin, Nup170p, in chromosome segregation. Genetics 157: 1543-1553
    • (2001) Genetics , vol.157 , pp. 1543-1553
    • Kerscher, O.1    Hieter, P.2    Winey, M.3    Basrai, M.A.4
  • 57
    • 27144544970 scopus 로고    scopus 로고
    • Nup155 regulates nuclear envelope and nuclear pore complex formation in nematodes and vertebrates
    • Franz C., Askjaer P., Antonin W., Iglesias C. L., Haselmann U., Schelder M. et al. (2005) Nup155 regulates nuclear envelope and nuclear pore complex formation in nematodes and vertebrates. EMBO J. 24: 3519-3531
    • (2005) EMBO J. , vol.24 , pp. 3519-3531
    • Franz, C.1    Askjaer, P.2    Antonin, W.3    Iglesias, C.L.4    Haselmann, U.5    Schelder, M.6
  • 58
    • 0042196107 scopus 로고    scopus 로고
    • The COPI complex functions in nuclear envelope breakdown and is recruited by the nucleoporin Nup153
    • Liu J., Pranuske A. J., Fager A. M. and Ullman K. S. (2003) The COPI complex functions in nuclear envelope breakdown and is recruited by the nucleoporin Nup153. Dev. Cell 5: 487-498
    • (2003) Dev. Cell , vol.5 , pp. 487-498
    • Liu, J.1    Pranuske, A.J.2    Fager, A.M.3    Ullman, K.S.4
  • 59
    • 0037128215 scopus 로고    scopus 로고
    • Tpr is localized within the nuclear basket of the pore complex and has a role in nuclear protein export
    • Frosst P., Guan T., Subauste C., Hahn K. and Gerace L. (2002) Tpr is localized within the nuclear basket of the pore complex and has a role in nuclear protein export. J. Cell Biol. 156: 617-630
    • (2002) J. Cell Biol. , vol.156 , pp. 617-630
    • Frosst, P.1    Guan, T.2    Subauste, C.3    Hahn, K.4    Gerace, L.5
  • 60
    • 4344700329 scopus 로고    scopus 로고
    • Nucleoporins as components of the nuclear pore complex core structure and tpr as the architectural element of the nuclear basket
    • Krull S., Thyberg J., Bjorkroth B., Rackwitz H. R. and Cordes V. C. (2004) Nucleoporins as components of the nuclear pore complex core structure and tpr as the architectural element of the nuclear basket. Mol. Biol. Cell 15: 4261-4277
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4261-4277
    • Krull, S.1    Thyberg, J.2    Bjorkroth, B.3    Rackwitz, H.R.4    Cordes, V.C.5
  • 61
    • 0033535342 scopus 로고    scopus 로고
    • Proteins connecting the nuclear pore complex with the nuclear interior
    • Strambio-de-Castillia C., Blobel G. and Rout M. P. (1999) Proteins connecting the nuclear pore complex with the nuclear interior. J. Cell Biol. 144: 839-855
    • (1999) J. Cell Biol. , vol.144 , pp. 839-855
    • Strambio-de-Castillia, C.1    Blobel, G.2    Rout, M.P.3
  • 62
    • 0033582411 scopus 로고    scopus 로고
    • Topology and functional domains of the yeast pore membrane protein Pom152p
    • Tcheperegine S. E., Marelli M. and Wozniak R. W. (1999) Topology and functional domains of the yeast pore membrane protein Pom152p. J. Biol. Chem. 274: 5252-5258
    • (1999) J. Biol. Chem. , vol.274 , pp. 5252-5258
    • Tcheperegine, S.E.1    Marelli, M.2    Wozniak, R.W.3
  • 63
    • 0032576588 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Ndclp is a shared component of nuclear pore complexes and spindle pole bodies
    • Chial H. J., Rout M. P., Giddings T. H. and Winey M. (1998) Saccharomyces cerevisiae Ndclp is a shared component of nuclear pore complexes and spindle pole bodies. J. Cell Biol. 143: 1789-1800
    • (1998) J. Cell Biol. , vol.143 , pp. 1789-1800
    • Chial, H.J.1    Rout, M.P.2    Giddings, T.H.3    Winey, M.4
  • 64
    • 8444225640 scopus 로고    scopus 로고
    • A novel allele of Saccharomyces cerevisiae NDC1 reveals a potential role for the spindle pole body component Ndclp in nuclear pore assembly
    • Lau C. K., Giddings T. H. Jr. and Winey M. (2004) A novel allele of Saccharomyces cerevisiae NDC1 reveals a potential role for the spindle pole body component Ndclp in nuclear pore assembly. Eukaryot. Cell 3: 447-458
    • (2004) Eukaryot. Cell , vol.3 , pp. 447-458
    • Lau, C.K.1    Giddings Jr., T.H.2    Winey, M.3
  • 65
    • 0027237823 scopus 로고
    • NDC1: A nuclear periphery component required for yeast spindle pole body duplication
    • Winey M., Hoyt M. A., Chan C., Goetsch L., Botstein D. and Byers B. (1993) NDC1: a nuclear periphery component required for yeast spindle pole body duplication. J. Cell Biol. 122: 743-751
    • (1993) J. Cell Biol. , vol.122 , pp. 743-751
    • Winey, M.1    Hoyt, M.A.2    Chan, C.3    Goetsch, L.4    Botstein, D.5    Byers, B.6
  • 66
    • 0022461695 scopus 로고
    • A gene required for the separation of chromosomes on the spindle apparatus in yeast
    • Thomas J. H. and Botstein D. (1986) A gene required for the separation of chromosomes on the spindle apparatus in yeast. Cell 44: 65-76
    • (1986) Cell , vol.44 , pp. 65-76
    • Thomas, J.H.1    Botstein, D.2
  • 67
    • 0037439661 scopus 로고    scopus 로고
    • ANChors away: An actin based mechanism of nuclear positioning
    • Starr D. A. and Han M. (2003) ANChors away: an actin based mechanism of nuclear positioning. J. Cell. Sci. 116: 211-216
    • (2003) J. Cell. Sci. , vol.116 , pp. 211-216
    • Starr, D.A.1    Han, M.2
  • 68
    • 0033953888 scopus 로고    scopus 로고
    • Functional cooperation between the microtubule and actin cytoskeletons
    • Goode B. L., Drubin D. G. and Barnes G. (2000) Functional cooperation between the microtubule and actin cytoskeletons. Curr. Opin. Cell Biol. 12: 63-71
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 63-71
    • Goode, B.L.1    Drubin, D.G.2    Barnes, G.3
  • 69
    • 0037220989 scopus 로고    scopus 로고
    • Nuclear positioning: The means is at the ends
    • Morris N. R. (2003) Nuclear positioning: the means is at the ends. Curr. Opin. Cell Biol. 15: 54-59
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 54-59
    • Morris, N.R.1
  • 72
    • 0036155776 scopus 로고    scopus 로고
    • Myne-1, a spectrin repeat transmembrane protein of the myocyte inner nuclear membrane, interacts with lamin A/C
    • Mislow J. M., Kim M. S., Davis D. B. and McNally E. M. (2002) Myne-1, a spectrin repeat transmembrane protein of the myocyte inner nuclear membrane, interacts with lamin A/C. J. Cell. Sci. 115: 61-70
    • (2002) J. Cell. Sci. , vol.115 , pp. 61-70
    • Mislow, J.M.1    Kim, M.S.2    Davis, D.B.3    McNally, E.M.4
  • 73
    • 21844432667 scopus 로고    scopus 로고
    • Lamin A/C-dependent localization of Nesprin-2, a giant scaffolder at the nuclear envelope
    • Libotte T., Zaim H., Abraham S., Padmakumar V. C., Schneider M., Lu W. et al. (2005) Lamin A/C-dependent localization of Nesprin-2, a giant scaffolder at the nuclear envelope. Mol. Biol. Cell 16: 3411-3424
    • (2005) Mol. Biol. Cell , vol.16 , pp. 3411-3424
    • Libotte, T.1    Zaim, H.2    Abraham, S.3    Padmakumar, V.C.4    Schneider, M.5    Lu, W.6
  • 74
    • 0035694555 scopus 로고    scopus 로고
    • Nesprins: A novel family of spectrin-repeat-containing proteins that localize to the nuclear membrane in multiple tissues
    • Zhang Q., Skepper J. N., Yang F., Davies J. D., Hegyi L., Roberts R. G. et al. (2001) Nesprins: a novel family of spectrin-repeat-containing proteins that localize to the nuclear membrane in multiple tissues. J. Cell. Sci. 114: 4485-4498
    • (2001) J. Cell. Sci. , vol.114 , pp. 4485-4498
    • Zhang, Q.1    Skepper, J.N.2    Yang, F.3    Davies, J.D.4    Hegyi, L.5    Roberts, R.G.6
  • 76
    • 0036193442 scopus 로고    scopus 로고
    • Lamin-dependent localization of UNC-84, a protein required for nuclear migration in Caenorhabditis elegans
    • Lee K. K., Starr D., Cohen M., Liu J., Han M., Wilson K. L. et al. (2002) Lamin-dependent localization of UNC-84, a protein required for nuclear migration in Caenorhabditis elegans. Mol. Biol. Cell 13: 892-901
    • (2002) Mol. Biol. Cell , vol.13 , pp. 892-901
    • Lee, K.K.1    Starr, D.2    Cohen, M.3    Liu, J.4    Han, M.5    Wilson, K.L.6
  • 77
    • 0032772929 scopus 로고    scopus 로고
    • UNC-84 localizes to the nuclear envelope and is required for nuclear migration and anchoring during C. elegans development
    • Malone C. J., Fixsen W. D., Horvitz H. R. and Han M. (1999) UNC-84 localizes to the nuclear envelope and is required for nuclear migration and anchoring during C. elegans development. Development 126: 3171-3181
    • (1999) Development , vol.126 , pp. 3171-3181
    • Malone, C.J.1    Fixsen, W.D.2    Horvitz, H.R.3    Han, M.4
  • 78
    • 0035694702 scopus 로고    scopus 로고
    • unc-83 encodes a novel component of the nuclear envelope and is essential for proper nuclear migration
    • Starr D. A., Hermann G. J., Malone C. J., Fixsen W., Priess J. R., Horvitz H. R. et al. (2001 ) unc-83 encodes a novel component of the nuclear envelope and is essential for proper nuclear migration. Development 128: 5039-5050
    • (2001) Development , vol.128 , pp. 5039-5050
    • Starr, D.A.1    Hermann, G.J.2    Malone, C.J.3    Fixsen, W.4    Priess, J.R.5    Horvitz, H.R.6
  • 79
    • 2342466617 scopus 로고    scopus 로고
    • Matefin, a Caenorhabditis elegans germ line-specific SUN-domain nuclear membrane protein, is essential for early embryonic and germ cell development
    • USA
    • Fridkin A., Mills E., Margalit A., Neufeld E., Lee K. K., Feinstein N. et al. (2004) Matefin, a Caenorhabditis elegans germ line-specific SUN-domain nuclear membrane protein, is essential for early embryonic and germ cell development. Proc. Natl. Acad. Sci. USA 101: 6987-6992
    • (2004) Proc. Natl. Acad. Sci. , vol.101 , pp. 6987-6992
    • Fridkin, A.1    Mills, E.2    Margalit, A.3    Neufeld, E.4    Lee, K.K.5    Feinstein, N.6
  • 80
    • 0032537124 scopus 로고    scopus 로고
    • Integrin binding and mechanical tension induce movement of mRNA and ribosomes to focal adhesions
    • Chicurel M. E., Singer R. H., Meyer C. J. and Ingber D. E. (1998) Integrin binding and mechanical tension induce movement of mRNA and ribosomes to focal adhesions. Nature 392: 730-733
    • (1998) Nature , vol.392 , pp. 730-733
    • Chicurel, M.E.1    Singer, R.H.2    Meyer, C.J.3    Ingber, D.E.4
  • 81
    • 24144481867 scopus 로고    scopus 로고
    • Abnormal nuclear shape and impaired mechanotransduction in emerin-deficient cells
    • Lammerding J., Hsiao J., Schulze P. C., Kozlov S., Stewart C. L. and Lee R. T. (2005) Abnormal nuclear shape and impaired mechanotransduction in emerin-deficient cells. J. Cell Biol. 170: 781-791
    • (2005) J. Cell Biol. , vol.170 , pp. 781-791
    • Lammerding, J.1    Hsiao, J.2    Schulze, P.C.3    Kozlov, S.4    Stewart, C.L.5    Lee, R.T.6
  • 82
    • 0031017220 scopus 로고    scopus 로고
    • Demonstration of mechanical connections between integrins, cytoskeletal filaments and nucleoplasm that stabilize nuclear structure
    • USA
    • Maniotis A. J., Chen C. S. and Ingber D. E. (1997) Demonstration of mechanical connections between integrins, cytoskeletal filaments and nucleoplasm that stabilize nuclear structure. Proc. Natl. Acad. Sci. USA 94: 849-854
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 849-854
    • Maniotis, A.J.1    Chen, C.S.2    Ingber, D.E.3
  • 83
    • 0037133313 scopus 로고    scopus 로고
    • Engineering gene expression and protein synthesis by modulation of nuclear shape
    • USA
    • Thomas C. H., Collier J. H., Sfeir C. S. and Healy K. E. (2002) Engineering gene expression and protein synthesis by modulation of nuclear shape. Proc. Natl. Acad. Sci. USA 99: 1972-1977
    • (2002) Proc. Natl. Acad. Sci. , vol.99 , pp. 1972-1977
    • Thomas, C.H.1    Collier, J.H.2    Sfeir, C.S.3    Healy, K.E.4
  • 84
    • 0022638059 scopus 로고
    • Spatial organization of chromosomes in the salivary gland nuclei of Drosophila melanogaster
    • Hochstrasser M., Mathog D., Gruenbaum Y., Saumweber H. and Sedat J. W. (1986) Spatial organization of chromosomes in the salivary gland nuclei of Drosophila melanogaster. J. Cell Biol. 102: 112-123
    • (1986) J. Cell Biol. , vol.102 , pp. 112-123
    • Hochstrasser, M.1    Mathog, D.2    Gruenbaum, Y.3    Saumweber, H.4    Sedat, J.W.5
  • 85
    • 0037022862 scopus 로고    scopus 로고
    • Order and disorder in the nucleus
    • Marshall W. F. (2002) Order and disorder in the nucleus. Curr. Biol. 12: R185-R192
    • (2002) Curr. Biol. , vol.12
    • Marshall, W.F.1
  • 87
    • 9444281491 scopus 로고    scopus 로고
    • Higher order chromatin architecture in the cell nucleus: On the way from structure to function
    • Cremer T., Kupper K., Dietzel S. and Fakan S. (2004) Higher order chromatin architecture in the cell nucleus: on the way from structure to function. Biol Cell 96: 555-567
    • (2004) Biol Cell , vol.96 , pp. 555-567
    • Cremer, T.1    Kupper, K.2    Dietzel, S.3    Fakan, S.4
  • 89
    • 0037529048 scopus 로고    scopus 로고
    • Transcription and the territory: The ins and outs of gene positioning
    • Williams R. R. (2003) Transcription and the territory: the ins and outs of gene positioning. Trends Genet. 19: 298-302
    • (2003) Trends Genet. , vol.19 , pp. 298-302
    • Williams, R.R.1
  • 90
    • 0037282854 scopus 로고    scopus 로고
    • Visualizing chromatin and chromosomes in living cells
    • Zink D., Sadoni N. and Stelzer E. (2003) Visualizing chromatin and chromosomes in living cells. Methods 29: 42-50
    • (2003) Methods , vol.29 , pp. 42-50
    • Zink, D.1    Sadoni, N.2    Stelzer, E.3
  • 91
    • 0018331219 scopus 로고
    • Three-dimensional reconstruction of the chromatin bodies in the nuclei of mature erythrocytes from the newt Triturus cristatus: The number of nuclear envelope-attachment sites
    • Murray A. B. and Davies H. G. (1979) Three-dimensional reconstruction of the chromatin bodies in the nuclei of mature erythrocytes from the newt Triturus cristatus: the number of nuclear envelope-attachment sites. J. Cell. Sci. 35: 59-66
    • (1979) J. Cell. Sci. , vol.35 , pp. 59-66
    • Murray, A.B.1    Davies, H.G.2
  • 92
    • 0031972489 scopus 로고    scopus 로고
    • Mapping three-dimensional chromosome architecture in situ
    • Dernburg A. F. and Sedat J. W. (1998) Mapping three-dimensional chromosome architecture in situ. Methods Cell Biol. 53: 187-233
    • (1998) Methods Cell Biol. , vol.53 , pp. 187-233
    • Dernburg, A.F.1    Sedat, J.W.2
  • 93
    • 0029943141 scopus 로고    scopus 로고
    • Perturbation of nuclear architecture by long-distance chromosome interactions
    • Dernburg A. F., Broman K. W., Fung J. C., Marshall W. F., Philips J., Agard D. A. et al. (1996) Perturbation of nuclear architecture by long-distance chromosome interactions. Cell 85: 745-759
    • (1996) Cell , vol.85 , pp. 745-759
    • Dernburg, A.F.1    Broman, K.W.2    Fung, J.C.3    Marshall, W.F.4    Philips, J.5    Agard, D.A.6
  • 94
    • 4544228141 scopus 로고    scopus 로고
    • The nuclear envelope lamina network has elasticity and a compressibility limit suggestive of a molecular shock absorber
    • Dahl K. N., Kahn S. M., Wilson K. L. and Discher D. E. (2004) The nuclear envelope lamina network has elasticity and a compressibility limit suggestive of a molecular shock absorber. J. Cell. Sci. 117: 4779-4786
    • (2004) J. Cell. Sci. , vol.117 , pp. 4779-4786
    • Dahl, K.N.1    Kahn, S.M.2    Wilson, K.L.3    Discher, D.E.4
  • 95
    • 0035153087 scopus 로고    scopus 로고
    • Lamins in disease: Why do ubiquitously expressed nuclear envelope proteins give rise to tissue-specific disease phenotypes?
    • Hutchison C. J., Alvarez-Reyes M. and Vaughan O. A. (2001) Lamins in disease: why do ubiquitously expressed nuclear envelope proteins give rise to tissue-specific disease phenotypes? J. Cell. Sci. 114: 9-19
    • (2001) J. Cell. Sci. , vol.114 , pp. 9-19
    • Hutchison, C.J.1    Alvarez-Reyes, M.2    Vaughan, O.A.3
  • 96
    • 0032852110 scopus 로고    scopus 로고
    • Heart to heart: From nuclear proteins to Emery-Dreifuss muscular dystrophy
    • Morris G. E. and Manilal S. (1999) Heart to heart: from nuclear proteins to Emery-Dreifuss muscular dystrophy. Hum. Mol. Genet. 8: 1847-1851
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 1847-1851
    • Morris, G.E.1    Manilal, S.2
  • 97
    • 0033615969 scopus 로고    scopus 로고
    • Loss of A-type lamin expression compromises nuclear envelope integrity leading to muscular dystrophy
    • Sullivan T., Escalante-Alcalde D., Bhatt H., Anver M., Bhat N., Nagashima K. et al. (1999) Loss of A-type lamin expression compromises nuclear envelope integrity leading to muscular dystrophy. J. Cell Biol. 147: 913-920
    • (1999) J. Cell Biol. , vol.147 , pp. 913-920
    • Sullivan, T.1    Escalante-Alcalde, D.2    Bhatt, H.3    Anver, M.4    Bhat, N.5    Nagashima, K.6
  • 98
    • 0018840796 scopus 로고
    • The nuclear envelope lamina is reversibly depolymerized during mitosis
    • Gerace L. and Blobel G. (1980) The nuclear envelope lamina is reversibly depolymerized during mitosis. Cell 19: 277-287
    • (1980) Cell , vol.19 , pp. 277-287
    • Gerace, L.1    Blobel, G.2
  • 99
    • 0023032014 scopus 로고
    • cDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins
    • USA
    • Fisher D. Z., Chaudhary N. and Blobel G. (1986) cDNA sequencing of nuclear lamins A and C reveals primary and secondary structural homology to intermediate filament proteins. Proc. Natl. Acad. Sci. USA 83: 6450-6454
    • (1986) Proc. Natl. Acad. Sci , vol.83 , pp. 6450-6454
    • Fisher, D.Z.1    Chaudhary, N.2    Blobel, G.3
  • 100
    • 0028980645 scopus 로고
    • Expression of Drosophila lamin C is developmentally regulated: Analogies with vertebrate A-type lamins
    • Riemer D., Stuurman N., Berrios M., Hunter C., Fisher P. A. and Weber K. (1995) Expression of Drosophila lamin C is developmentally regulated: analogies with vertebrate A-type lamins. J. Cell. Sci. 108 (Pt 10): 3189-3198
    • (1995) J. Cell. Sci. , vol.108 , Issue.10 PART , pp. 3189-3198
    • Riemer, D.1    Stuurman, N.2    Berrios, M.3    Hunter, C.4    Fisher, P.A.5    Weber, K.6
  • 101
    • 0030004283 scopus 로고    scopus 로고
    • Characterization and quantitation of three B-type lamins in Xenopus oocytes and eggs: Increase of lamin LI protein synthesis during meiotic maturation
    • Lourim D., Kempf A. and Krohne G. (1996) Characterization and quantitation of three B-type lamins in Xenopus oocytes and eggs: increase of lamin LI protein synthesis during meiotic maturation. J. Cell. Sci. 109 (Pt 7): 1775-1785
    • (1996) J. Cell. Sci. , vol.109 , Issue.7 PART , pp. 1775-1785
    • Lourim, D.1    Kempf, A.2    Krohne, G.3
  • 103
    • 12344326099 scopus 로고    scopus 로고
    • The lamin CxM motif promotes nuclear membrane growth
    • Prufert K., Vogel A. and Krohne G. (2004) The lamin CxM motif promotes nuclear membrane growth. J. Cell. Sci. 117: 6105-6116
    • (2004) J. Cell. Sci. , vol.117 , pp. 6105-6116
    • Prufert, K.1    Vogel, A.2    Krohne, G.3
  • 104
    • 0025362748 scopus 로고
    • Isoprenylation is required for the processing of the lamin A precursor
    • Beck L. A., Hosick T. J. and Sinensky M. (1990) Isoprenylation is required for the processing of the lamin A precursor. J. Cell Biol. 110: 1489-1499
    • (1990) J. Cell Biol. , vol.110 , pp. 1489-1499
    • Beck, L.A.1    Hosick, T.J.2    Sinensky, M.3
  • 106
    • 0024828257 scopus 로고
    • Maturation of nuclear lamin A involves a specific carboxy-terminal trimming, which removes the polyisoprenylation site from the precursor; implications for the structure of the nuclear lamina
    • Weber K., Plessmann U. and Traub P. (1989) Maturation of nuclear lamin A involves a specific carboxy-terminal trimming, which removes the polyisoprenylation site from the precursor; implications for the structure of the nuclear lamina. FEBS Lett. 257: 411-414
    • (1989) FEBS Lett. , vol.257 , pp. 411-414
    • Weber, K.1    Plessmann, U.2    Traub, P.3
  • 107
    • 0035942736 scopus 로고    scopus 로고
    • Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells
    • Elbashir S. M., Harborth J., Lendeckel W., Yalcin A., Weber K. and Tuschl T. (2001) Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells. Nature 411: 494-498
    • (2001) Nature , vol.411 , pp. 494-498
    • Elbashir, S.M.1    Harborth, J.2    Lendeckel, W.3    Yalcin, A.4    Weber, K.5    Tuschl, T.6
  • 108
    • 0031562693 scopus 로고    scopus 로고
    • Peripheral framework of carrot cell nucleus contains a novel protein predicted to exhibit a long alpha-helical domain
    • Masuda K., Xu Z. J., Takahashi S., Ito A., Ono M., Nomura K. et al. (1997) Peripheral framework of carrot cell nucleus contains a novel protein predicted to exhibit a long alpha-helical domain. Exp. Cell Res. 232: 173-181
    • (1997) Exp. Cell Res. , vol.232 , pp. 173-181
    • Masuda, K.1    Xu, Z.J.2    Takahashi, S.3    Ito, A.4    Ono, M.5    Nomura, K.6
  • 109
    • 0002603505 scopus 로고    scopus 로고
    • Four signature motifs define the first class of structurally related large coiled-coil proteins in plants
    • Gindullis F., Rose A., Patel S. and Meier I. (2002) Four signature motifs define the first class of structurally related large coiled-coil proteins in plants. BMC Genomics 3: 9
    • (2002) BMC Genomics , vol.3 , pp. 9
    • Gindullis, F.1    Rose, A.2    Patel, S.3    Meier, I.4
  • 111
    • 0347134685 scopus 로고    scopus 로고
    • Profiling stage-dependent changes of protein expression in Caenorhabditis elegans by mass spectrometric proteome analysis leads to the identification of stage-specific marker proteins
    • Madi A., Mikkat S., Ringel B., Thiesen H. J. and Glocker M. O. (2003) Profiling stage-dependent changes of protein expression in Caenorhabditis elegans by mass spectrometric proteome analysis leads to the identification of stage-specific marker proteins. Electrophoresis 24: 1809-1817
    • (2003) Electrophoresis , vol.24 , pp. 1809-1817
    • Madi, A.1    Mikkat, S.2    Ringel, B.3    Thiesen, H.J.4    Glocker, M.O.5
  • 112
    • 0033749567 scopus 로고    scopus 로고
    • Essential roles for Caenorhabditis elegans lamin gene in nuclear organization, cell cycle progression and spatial organization of nuclear pore complexes
    • Liu J., Ben-Shahar T. R., Riemer D., Treinin M., Spann P., Weber K. et al. (2000) Essential roles for Caenorhabditis elegans lamin gene in nuclear organization, cell cycle progression and spatial organization of nuclear pore complexes. Mol. Biol. Cell 11: 3937-3947
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3937-3947
    • Liu, J.1    Ben-Shahar, T.R.2    Riemer, D.3    Treinin, M.4    Spann, P.5    Weber, K.6
  • 113
    • 0023840620 scopus 로고
    • Drosophila nuclear lamin precursor Dm0 is translated from either of two developmentally regulated mRNA species apparently encoded by a single gene
    • Gruenbaum Y., Landesman Y., Drees B., Bare J. W., Saumweber H., Paddy M. R. et al. (1988) Drosophila nuclear lamin precursor Dm0 is translated from either of two developmentally regulated mRNA species apparently encoded by a single gene. J. Cell Biol. 106: 585-596
    • (1988) J. Cell Biol. , vol.106 , pp. 585-596
    • Gruenbaum, Y.1    Landesman, Y.2    Drees, B.3    Bare, J.W.4    Saumweber, H.5    Paddy, M.R.6
  • 114
    • 0026694775 scopus 로고
    • Annulate lamellae: A last frontier in cellular organelles
    • Kessel R. G. (1992) Annulate lamellae: a last frontier in cellular organelles. Int. Rev. Cytol. 133: 43-120
    • (1992) Int. Rev. Cytol. , vol.133 , pp. 43-120
    • Kessel, R.G.1
  • 115
    • 0031005809 scopus 로고    scopus 로고
    • Insertional mutation of the Drosophila nuclear lamin Dm0 gene results in defective nuclear envelopes, clustering of nuclear pore complexes, and accumulation of annulate lamellae
    • Lenz-Bohme B., Wismar J., Fuchs S., Reifegerste R., Buchner E., Betz H. et al. (1997) Insertional mutation of the Drosophila nuclear lamin Dm0 gene results in defective nuclear envelopes, clustering of nuclear pore complexes, and accumulation of annulate lamellae. J. Cell Biol. 137: 1001-1016
    • (1997) J. Cell Biol. , vol.137 , pp. 1001-1016
    • Lenz-Bohme, B.1    Wismar, J.2    Fuchs, S.3    Reifegerste, R.4    Buchner, E.5    Betz, H.6
  • 117
    • 17544383469 scopus 로고    scopus 로고
    • Interaction between an integral protein of the nuclear envelope inner membrane and human chromodomain proteins homologous to Drosophila HP1
    • Ye Q. and Worman H. J. (1996) Interaction between an integral protein of the nuclear envelope inner membrane and human chromodomain proteins homologous to Drosophila HP1. J. Biol. Chem. 271: 14653-14656
    • (1996) J. Biol. Chem. , vol.271 , pp. 14653-14656
    • Ye, Q.1    Worman, H.J.2
  • 118
    • 1842584782 scopus 로고    scopus 로고
    • Proteins that bind A-type lamins: Integrating isolated clues
    • Zastrow M. S., Vlcek S. and Wilson K. L. (2004) Proteins that bind A-type lamins: integrating isolated clues. J. Cell. Sci. 117: 979-987
    • (2004) J. Cell. Sci. , vol.117 , pp. 979-987
    • Zastrow, M.S.1    Vlcek, S.2    Wilson, K.L.3
  • 119
    • 0027276759 scopus 로고
    • Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation
    • Foisner R. and Gerace L. (1993) Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation. Cell 73: 1267-1279
    • (1993) Cell , vol.73 , pp. 1267-1279
    • Foisner, R.1    Gerace, L.2
  • 120
    • 1642403318 scopus 로고    scopus 로고
    • Cell cycle dynamics of the nuclear envelope
    • Foisner R. (2003) Cell cycle dynamics of the nuclear envelope. Scientific World Journal 3: 1-20
    • (2003) Scientific World Journal , vol.3 , pp. 1-20
    • Foisner, R.1
  • 121
    • 2342463022 scopus 로고    scopus 로고
    • BAF: Roles in chromatin, nuclear structure and retrovirus integration
    • Segura-Totten M. and Wilson K. L. (2004) BAF: roles in chromatin, nuclear structure and retrovirus integration. Trends Cell Biol. 14: 261-266
    • (2004) Trends Cell Biol. , vol.14 , pp. 261-266
    • Segura-Totten, M.1    Wilson, K.L.2
  • 122
    • 1842578717 scopus 로고    scopus 로고
    • Dynamic interaction between BAF and emerin revealed by FRAP, FLIP and FRET analyses in living HeLa cells
    • Shimi T., Koujin T., Segura-Totten M., Wilson K. L., Haraguchi T. and Hiraoka Y. (2004) Dynamic interaction between BAF and emerin revealed by FRAP, FLIP and FRET analyses in living HeLa cells. J. Struct. Biol. 147: 31-41
    • (2004) J. Struct. Biol. , vol.147 , pp. 31-41
    • Shimi, T.1    Koujin, T.2    Segura-Totten, M.3    Wilson, K.L.4    Haraguchi, T.5    Hiraoka, Y.6
  • 123
    • 0037446880 scopus 로고    scopus 로고
    • MAN1 and emerin have overlapping function(s) essential for chromosome segregation and cell division in Caenorhabditis elegans
    • USA
    • Liu J., Lee K. K., Segura-Totten M., Neufeld E., Wilson K. L. and Gruenbaum Y. (2003) MAN1 and emerin have overlapping function(s) essential for chromosome segregation and cell division in Caenorhabditis elegans. Proc. Natl. Acad. Sci. USA 100: 4598-4603
    • (2003) Proc. Natl. Acad. Sci. , vol.100 , pp. 4598-4603
    • Liu, J.1    Lee, K.K.2    Segura-Totten, M.3    Neufeld, E.4    Wilson, K.L.5    Gruenbaum, Y.6
  • 124
    • 0037470050 scopus 로고    scopus 로고
    • Transcriptional repressor germ cell-less (GCL) and barrier to autointegration factor (BAF) compete for binding to emerin in vitro
    • Holaska J. M., Lee K. K., Kowalski A. K. and Wilson K. L. (2003) Transcriptional repressor germ cell-less (GCL) and barrier to autointegration factor (BAF) compete for binding to emerin in vitro. J. Biol. Chem. 278: 6969-6975
    • (2003) J. Biol. Chem. , vol.278 , pp. 6969-6975
    • Holaska, J.M.1    Lee, K.K.2    Kowalski, A.K.3    Wilson, K.L.4
  • 125
    • 0036330001 scopus 로고    scopus 로고
    • Barrier-to-autointegration factor: Major roles in chromatin decondensation and nuclear assembly
    • Segura-Totten M., Kowalski A. K., Craigie R. and Wilson K. L. (2002) Barrier-to-autointegration factor: major roles in chromatin decondensation and nuclear assembly. J. Cell Biol. 158: 475-485
    • (2002) J. Cell Biol. , vol.158 , pp. 475-485
    • Segura-Totten, M.1    Kowalski, A.K.2    Craigie, R.3    Wilson, K.L.4
  • 127
    • 0035694820 scopus 로고    scopus 로고
    • Distinct functional domains in emerin bind lamin a and DNA-bridging protein BAF
    • Lee K. K., Haraguchi T., Lee R. S., Koujin T., Hiraoka Y. and Wilson K. L. (2001) Distinct functional domains in emerin bind lamin A and DNA-bridging protein BAF. J. Cell. Sci. 114: 4567-4573
    • (2001) J. Cell. Sci. , vol.114 , pp. 4567-4573
    • Lee, K.K.1    Haraguchi, T.2    Lee, R.S.3    Koujin, T.4    Hiraoka, Y.5    Wilson, K.L.6
  • 128
    • 0028077096 scopus 로고
    • Protection of retroviral DNA from autointegration: Involvement of a cellular factor
    • USA
    • Lee M. S. and Craigie R. (1994) Protection of retroviral DNA from autointegration: involvement of a cellular factor. Proc. Natl. Acad. Sci. USA 91: 9823-9827
    • (1994) Proc. Natl. Acad. Sci. , vol.91 , pp. 9823-9827
    • Lee, M.S.1    Craigie, R.2
  • 130
    • 0028923173 scopus 로고
    • Lamin proteins form an internal nucleoskeleton as well as a peripheral lamina in human cells
    • Hozak P., Sasseville A. M., Raymond Y. and Cook P. R. (1995) Lamin proteins form an internal nucleoskeleton as well as a peripheral lamina in human cells. J. Cell. Sci. 108 (Pt 2): 635-644
    • (1995) J. Cell. Sci. , vol.108 , Issue.2 PART , pp. 635-644
    • Hozak, P.1    Sasseville, A.M.2    Raymond, Y.3    Cook, P.R.4
  • 131
    • 0021702708 scopus 로고
    • Organization and modulation of nuclear lamina structure
    • Gerace L., Comeau C. and Benson M. (1984) Organization and modulation of nuclear lamina structure. J. Cell. Sci. Suppl. 1: 137-160
    • (1984) J. Cell. Sci. Suppl. , vol.1 , pp. 137-160
    • Gerace, L.1    Comeau, C.2    Benson, M.3
  • 132
    • 0033383769 scopus 로고    scopus 로고
    • The nuclear lamina: Molecular organization and interaction with chromatin
    • Goldberg M., Harel A. and Gruenbaum Y. (1999) The nuclear lamina: molecular organization and interaction with chromatin. Crit. Rev. Eukaryot. Gene Expr. 9: 285-293
    • (1999) Crit. Rev. Eukaryot. Gene Expr. , vol.9 , pp. 285-293
    • Goldberg, M.1    Harel, A.2    Gruenbaum, Y.3
  • 133
    • 0031686054 scopus 로고    scopus 로고
    • Nuclear lamins: Their structure, assembly and interactions
    • Stuurman N., Heins S. and Aebi U. (1998) Nuclear lamins: their structure, assembly and interactions. J. Struct. Biol. 122: 42-66
    • (1998) J. Struct. Biol. , vol.122 , pp. 42-66
    • Stuurman, N.1    Heins, S.2    Aebi, U.3
  • 134
    • 0242383489 scopus 로고    scopus 로고
    • Dynamic interactions of nuclear lamina proteins with chromatin and transcriptional machinery
    • Mattout-Drubezki A. and Gruenbaum Y. (2003) Dynamic interactions of nuclear lamina proteins with chromatin and transcriptional machinery. Cell. Mol. Life Sci. 60: 2053-2063
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 2053-2063
    • Mattout-Drubezki, A.1    Gruenbaum, Y.2
  • 135
    • 0037684765 scopus 로고    scopus 로고
    • The nucleoskeleton: Lamins and actin are major players in essential nuclear functions
    • Shumaker D. K., Kuczmarski E. R. and Goldman R. D. (2003) The nucleoskeleton: lamins and actin are major players in essential nuclear functions. Curr. Opin. Cell Biol. 15: 358-366
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 358-366
    • Shumaker, D.K.1    Kuczmarski, E.R.2    Goldman, R.D.3
  • 136
    • 0036843975 scopus 로고    scopus 로고
    • Lamins: Building blocks or regulators of gene expression?
    • Hutchison C. J. (2002) Lamins: building blocks or regulators of gene expression? Nat. Rev. Mol. Cell Biol. 3: 848-858
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 848-858
    • Hutchison, C.J.1
  • 137
    • 0025370462 scopus 로고
    • In vitro disassembly of the nuclear lamina and M phase-specific phosphorylation of lamins by cdc2 kinase
    • Peter M., Nakagawa J., Doree M., Labbe J. C. and Nigg E. A. (1990) In vitro disassembly of the nuclear lamina and M phase-specific phosphorylation of lamins by cdc2 kinase. Cell 61: 591-602
    • (1990) Cell , vol.61 , pp. 591-602
    • Peter, M.1    Nakagawa, J.2    Doree, M.3    Labbe, J.C.4    Nigg, E.A.5
  • 138
    • 0025924421 scopus 로고
    • p34cdc2 acts as a lamin kinase in fission yeast
    • Enoch T., Peter M., Nurse P. and Nigg E. A. (1991) p34cdc2 acts as a lamin kinase in fission yeast. J. Cell Biol. 112: 797-807
    • (1991) J. Cell Biol. , vol.112 , pp. 797-807
    • Enoch, T.1    Peter, M.2    Nurse, P.3    Nigg, E.A.4
  • 139
    • 0030669555 scopus 로고    scopus 로고
    • Identification of protein phosphatase 1 as a mitotic lamin phosphatase
    • Thompson L. J., Bollen M. and Fields A. P. (1997) Identification of protein phosphatase 1 as a mitotic lamin phosphatase. J. Biol. Chem. 272: 29693-29697
    • (1997) J. Biol. Chem. , vol.272 , pp. 29693-29697
    • Thompson, L.J.1    Bollen, M.2    Fields, A.P.3
  • 140
    • 0038348529 scopus 로고    scopus 로고
    • AKAP149 is a novel PP1 specifier required to maintain nuclear envelope integrity in G1 phase
    • Steen R. L., Beullens M., Landsverk H. B., Bollen M. and Collas P. (2003) AKAP149 is a novel PP1 specifier required to maintain nuclear envelope integrity in G1 phase. J. Cell. Sci. 116: 2237-2246
    • (2003) J. Cell. Sci. , vol.116 , pp. 2237-2246
    • Steen, R.L.1    Beullens, M.2    Landsverk, H.B.3    Bollen, M.4    Collas, P.5
  • 141
    • 0034638842 scopus 로고    scopus 로고
    • Nuclear lamins a and B1: Different pathways of assembly during nuclear envelope formation in living cells
    • Moir R. D., Yoon M., Khuon S. and Goldman R. D. (2000) Nuclear lamins A and B1: different pathways of assembly during nuclear envelope formation in living cells. J. Cell Biol. 151: 1155-1168
    • (2000) J. Cell Biol. , vol.151 , pp. 1155-1168
    • Moir, R.D.1    Yoon, M.2    Khuon, S.3    Goldman, R.D.4
  • 142
    • 0027275334 scopus 로고
    • Stepwise reassembly of the nuclear envelope at the end of mitosis
    • Chaudhary N. and Courvalin J. C. (1993) Stepwise reassembly of the nuclear envelope at the end of mitosis. J. Cell Biol. 122: 295-306
    • (1993) J. Cell Biol. , vol.122 , pp. 295-306
    • Chaudhary, N.1    Courvalin, J.C.2
  • 143
  • 144
    • 0022517260 scopus 로고
    • A cell free system to study reassembly of the nuclear envelope at the end of mitosis
    • Burke B. and Gerace L. (1986) A cell free system to study reassembly of the nuclear envelope at the end of mitosis. Cell 44: 639-652
    • (1986) Cell , vol.44 , pp. 639-652
    • Burke, B.1    Gerace, L.2
  • 145
    • 0030928058 scopus 로고    scopus 로고
    • Nuclear membrane vesicle targeting to chromatin in a Drosophila embryo cell-free system
    • Ulitzur N., Harel A., Goldberg M., Feinstein N. and Gruenbaum Y. (1997) Nuclear membrane vesicle targeting to chromatin in a Drosophila embryo cell-free system. Mol. Biol. Cell 8: 1439-1448
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1439-1448
    • Ulitzur, N.1    Harel, A.2    Goldberg, M.3    Feinstein, N.4    Gruenbaum, Y.5
  • 146
    • 0025612124 scopus 로고
    • A lamin-independent pathway for nuclear envelope assembly
    • Newport J. W., Wilson K. L. and Dunphy W. G. (1990) A lamin-independent pathway for nuclear envelope assembly. J. Cell Biol. 111: 2247-2259
    • (1990) J. Cell Biol. , vol.111 , pp. 2247-2259
    • Newport, J.W.1    Wilson, K.L.2    Dunphy, W.G.3
  • 147
    • 0026016285 scopus 로고
    • The role of lamin LIII in nuclear assembly and DNA replication, in cell-free extracts of Xenopus eggs
    • Meier J., Campbell K. H., Ford C. C., Stick R. and Hutchison C. J. (1991) The role of lamin LIII in nuclear assembly and DNA replication, in cell-free extracts of Xenopus eggs. J. Cell. Sci. 98 (Pt 3): 271-279
    • (1991) J. Cell. Sci. , vol.98 , Issue.3 PART , pp. 271-279
    • Meier, J.1    Campbell, K.H.2    Ford, C.C.3    Stick, R.4    Hutchison, C.J.5
  • 148
    • 0035972254 scopus 로고    scopus 로고
    • Mistargeting of B-type lamins at the end of mitosis: Implications on cell survival and regulation of lamins A/C expression
    • Steen R. L. and Collas P. (2001) Mistargeting of B-type lamins at the end of mitosis: implications on cell survival and regulation of lamins A/C expression. J. Cell Biol. 153: 621-626
    • (2001) J. Cell Biol. , vol.153 , pp. 621-626
    • Steen, R.L.1    Collas, P.2
  • 149
    • 0042691509 scopus 로고    scopus 로고
    • Nuclear membrane proteins with potential disease links found by subtractive proteomics
    • Schirmer E. C., Florens L., Guan T., Yates J. R. 3rd, and Gerace L. (2003) Nuclear membrane proteins with potential disease links found by subtractive proteomics. Science 301: 1380-1382
    • (2003) Science , vol.301 , pp. 1380-1382
    • Schirmer, E.C.1    Florens, L.2    Guan, T.3    Yates III, J.R.4    Gerace, L.5
  • 150
    • 21644480074 scopus 로고    scopus 로고
    • All in the family: Evidence for four new LEM-domain proteins Lem2 (NET-25), Lem3, Lem4 and Lem5 in the human genome
    • Lee K. K. and Wilson K. L. (2004) All in the family: evidence for four new LEM-domain proteins Lem2 (NET-25), Lem3, Lem4 and Lem5 in the human genome. Symp. Soc. Exp. Biol., 329-339
    • (2004) Symp. Soc. Exp. Biol. , pp. 329-339
    • Lee, K.K.1    Wilson, K.L.2
  • 151
    • 0027500249 scopus 로고
    • The amino-terminal domain of the lamin B receptor is a nuclear envelope targeting signal
    • Soullam B. and Worman H. J. (1993) The amino-terminal domain of the lamin B receptor is a nuclear envelope targeting signal. J. Cell Biol. 120: 1093-1100
    • (1993) J. Cell Biol. , vol.120 , pp. 1093-1100
    • Soullam, B.1    Worman, H.J.2
  • 152
    • 0029069183 scopus 로고
    • Signals and structural features involved in integral membrane protein targeting to the inner nuclear membrane
    • Soullam B. and Worman H. J. (1995) Signals and structural features involved in integral membrane protein targeting to the inner nuclear membrane. J. Cell Biol. 130: 15-27
    • (1995) J. Cell Biol. , vol.130 , pp. 15-27
    • Soullam, B.1    Worman, H.J.2
  • 153
    • 11244316478 scopus 로고    scopus 로고
    • Energy- and temperature-dependent transport of integral proteins to the inner nuclear membrane via the nuclear pore
    • Ohba T., Schirmer E. C., Nishimoto T. and Gerace L. (2004) Energy- and temperature-dependent transport of integral proteins to the inner nuclear membrane via the nuclear pore. J. Cell Biol. 167: 1051-1062
    • (2004) J. Cell Biol. , vol.167 , pp. 1051-1062
    • Ohba, T.1    Schirmer, E.C.2    Nishimoto, T.3    Gerace, L.4
  • 154
    • 25444527940 scopus 로고    scopus 로고
    • Genome-wide screen for inner nuclear membrane protein targeting: Roles for N-acetylation and an integral membrane protein
    • Murthi A. and Hopper A. K. (2005) Genome-wide screen for inner nuclear membrane protein targeting: roles for N-acetylation and an integral membrane protein. Genetics 170: 1553-1560
    • (2005) Genetics , vol.170 , pp. 1553-1560
    • Murthi, A.1    Hopper, A.K.2
  • 155
    • 0030853497 scopus 로고    scopus 로고
    • Two proteins that cycle asynchronously between centrosomes and nuclear structures: Drosophila CP60 and CP190
    • Oegema K., Marshall W. F., Sedat J. W. and Alberts B. M. (1997) Two proteins that cycle asynchronously between centrosomes and nuclear structures: Drosophila CP60 and CP190. J. Cell. Sci. 110 (Pt 14): 1573-1583
    • (1997) J. Cell. Sci. , vol.110 , Issue.14 PART , pp. 1573-1583
    • Oegema, K.1    Marshall, W.F.2    Sedat, J.W.3    Alberts, B.M.4
  • 156
    • 0027516644 scopus 로고
    • A three-dimensional view of precursor messenger RNA metabolism within the mammalian nucleus
    • Carter K. C., Bowman D., Carrington W., Fogarty K., McNeil J. A., Fay F. S. et al. (1993) A three-dimensional view of precursor messenger RNA metabolism within the mammalian nucleus. Science 259: 1330-1335
    • (1993) Science , vol.259 , pp. 1330-1335
    • Carter, K.C.1    Bowman, D.2    Carrington, W.3    Fogarty, K.4    McNeil, J.A.5    Fay, F.S.6
  • 157
    • 0033553877 scopus 로고    scopus 로고
    • Differences in the localization and morphology of chromosomes in the human nucleus
    • Croft J. A., Bridger J. M., Boyle S., Perry P., Teague P. and Bickmore W. A. (1999) Differences in the localization and morphology of chromosomes in the human nucleus. J. Cell Biol. 145: 1119-1131
    • (1999) J. Cell Biol. , vol.145 , pp. 1119-1131
    • Croft, J.A.1    Bridger, J.M.2    Boyle, S.3    Perry, P.4    Teague, P.5    Bickmore, W.A.6
  • 158
    • 0034750744 scopus 로고    scopus 로고
    • Non-random radial higher-order chromatin arrangements in nuclei of diploid human cells
    • Cremer M., von Hase J., Volm T., Brero A., Kreth G., Walter J. et al. (2001) Non-random radial higher-order chromatin arrangements in nuclei of diploid human cells. Chromosome Res. 9: 541-567
    • (2001) Chromosome Res. , vol.9 , pp. 541-567
    • Cremer, M.1    Von Hase, J.2    Volm, T.3    Brero, A.4    Kreth, G.5    Walter, J.6
  • 159
    • 0035253606 scopus 로고    scopus 로고
    • The spatial organization of human chromosomes within the nuclei of normal and emerin-mutant cells
    • Boyle S., Gilchrist S., Bridger J. M., Mahy N. L., Ellis J. A. and Bickmore W. A. (2001) The spatial organization of human chromosomes within the nuclei of normal and emerin-mutant cells. Hum. Mol. Genet. 10: 211-219
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 211-219
    • Boyle, S.1    Gilchrist, S.2    Bridger, J.M.3    Mahy, N.L.4    Ellis, J.A.5    Bickmore, W.A.6
  • 160
    • 0032490917 scopus 로고    scopus 로고
    • Perinuclear localization of chromatin facilitates transcriptional silencing
    • Andrulis E. D., Neiman A. M., Zappulla D. C. and Sternglanz R. (1998) Perinuclear localization of chromatin facilitates transcriptional silencing. Nature 394: 592-595
    • (1998) Nature , vol.394 , pp. 592-595
    • Andrulis, E.D.1    Neiman, A.M.2    Zappulla, D.C.3    Sternglanz, R.4
  • 161
    • 0028064990 scopus 로고
    • Complex formation between lamin A and the retinoblastoma gene product: Identification of the domain on lamin A required for its interaction
    • Ozaki T., Saijo M., Murakami K., Enomoto H., Taya Y. and Sakiyama S. (1994) Complex formation between lamin A and the retinoblastoma gene product: identification of the domain on lamin A required for its interaction. Oncogene 9: 2649-2653
    • (1994) Oncogene , vol.9 , pp. 2649-2653
    • Ozaki, T.1    Saijo, M.2    Murakami, K.3    Enomoto, H.4    Taya, Y.5    Sakiyama, S.6
  • 162
    • 1842854443 scopus 로고    scopus 로고
    • Lamin A/C binding protein LAP2alpha is required for nuclear anchorage of retinoblastoma protein
    • Markiewicz E., Dechat T., Foisner R., Quinlan R. A. and Hutchison C. J. (2002) Lamin A/C binding protein LAP2alpha is required for nuclear anchorage of retinoblastoma protein. Mol. Biol. Cell 13: 4401-4413
    • (2002) Mol. Biol. Cell , vol.13 , pp. 4401-4413
    • Markiewicz, E.1    Dechat, T.2    Foisner, R.3    Quinlan, R.A.4    Hutchison, C.J.5
  • 163
    • 0027976913 scopus 로고
    • The retinoblastoma gene product is a cell cycle-dependent, nuclear matrix-associated protein
    • USA
    • Mancini M. A., Shan B., Nickerson J. A., Penman S. and Lee W. H. (1994) The retinoblastoma gene product is a cell cycle-dependent, nuclear matrix-associated protein. Proc. Natl. Acad. Sci. USA 91: 418-422
    • (1994) Proc. Natl. Acad. Sci. , vol.91 , pp. 418-422
    • Mancini, M.A.1    Shan, B.2    Nickerson, J.A.3    Penman, S.4    Lee, W.H.5
  • 165
    • 0034777991 scopus 로고    scopus 로고
    • Nuclear membrane protein LAP2beta mediates transcriptional repression alone and together with its binding partner GCL (germ-cell-less)
    • Nili E., Cojocaru G. S., Kalma Y., Ginsberg D., Copeland N. G., Gilbert D. J. et al. (2001) Nuclear membrane protein LAP2beta mediates transcriptional repression alone and together with its binding partner GCL (germ-cell-less) J. Cell. Sci. 114: 3297-3307
    • (2001) J. Cell. Sci. , vol.114 , pp. 3297-3307
    • Nili, E.1    Cojocaru, G.S.2    Kalma, Y.3    Ginsberg, D.4    Copeland, N.G.5    Gilbert, D.J.6
  • 166
    • 0033584403 scopus 로고    scopus 로고
    • Molecular cloning and genomic organization of mouse homologue of Drosophila germ cell-less and its expression in germ lineage cells
    • Kimura T., Yomogida K., Iwai N., Kato Y. and Nakano T. (1999) Molecular cloning and genomic organization of mouse homologue of Drosophila germ cell-less and its expression in germ lineage cells. Biochem. Biophys. Res. Commun. 262: 223-230
    • (1999) Biochem. Biophys. Res. Commun. , vol.262 , pp. 223-230
    • Kimura, T.1    Yomogida, K.2    Iwai, N.3    Kato, Y.4    Nakano, T.5
  • 167
    • 0033521615 scopus 로고    scopus 로고
    • Integration of a growth-suppressing BTB/POZ domain protein with the DP component of the E2F transcription factor
    • de la Luna S., Allen K. E., Mason S. E. and La Thangue N. B. (1999) Integration of a growth-suppressing BTB/POZ domain protein with the DP component of the E2F transcription factor. EMBO J. 18: 212-228
    • (1999) EMBO J. , vol.18 , pp. 212-228
    • De La Luna, S.1    Allen, K.E.2    Mason, S.E.3    La Thangue, N.B.4
  • 168
    • 0036537888 scopus 로고    scopus 로고
    • A novel interaction between lamin A and SREBP1: Implications for partial lipodystrophy and other laminopathies
    • Lloyd D. J., Trembath R. C. and Shackleton S. (2002) A novel interaction between lamin A and SREBP1: implications for partial lipodystrophy and other laminopathies. Hum. Mol. Genet. 11: 769-777
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 769-777
    • Lloyd, D.J.1    Trembath, R.C.2    Shackleton, S.3
  • 169
    • 0030681031 scopus 로고    scopus 로고
    • Dissociation of Oct-1 from the nuclear peripheral structure induces the cellular aging-associated collagenase gene expression
    • Imai S., Nishibayashi S., Takao K., Tomifuji M., Fujino T., Hasegawa M. et al. (1997) Dissociation of Oct-1 from the nuclear peripheral structure induces the cellular aging-associated collagenase gene expression. Mol. Biol. Cell 8: 2407-2419
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2407-2419
    • Imai, S.1    Nishibayashi, S.2    Takao, K.3    Tomifuji, M.4    Fujino, T.5    Hasegawa, M.6
  • 170
    • 0036848357 scopus 로고    scopus 로고
    • In vivo and in vitro interaction between human transcription factor MOK2 and nuclear lamin A/C
    • Dreuillet C., Tillit J., Kress M. and Ernoult-Lange M. (2002) In vivo and in vitro interaction between human transcription factor MOK2 and nuclear lamin A/C. Nucleic Acids Res. 30: 4634-4642
    • (2002) Nucleic Acids Res. , vol.30 , pp. 4634-4642
    • Dreuillet, C.1    Tillit, J.2    Kress, M.3    Ernoult-Lange, M.4
  • 171
    • 0037959860 scopus 로고    scopus 로고
    • XMAN1, an inner nuclear membrane protein, antagonizes BMP signaling by interacting with Smad1 in Xenopus embryos
    • Osada S., Ohmori S. Y. and Taira M. (2003) XMAN1, an inner nuclear membrane protein, antagonizes BMP signaling by interacting with Smad1 in Xenopus embryos. Development 130: 1783-1794
    • (2003) Development , vol.130 , pp. 1783-1794
    • Osada, S.1    Ohmori, S.Y.2    Taira, M.3
  • 172
    • 12444289583 scopus 로고    scopus 로고
    • Barrier-to-autointegration factor plays crucial roles in cell cycle progression and nuclear organization in Drosophila
    • Furukawa K., Sugiyama S., Osouda S., Goto H., Inagaki M., Horigome T. et al. (2003) Barrier-to-autointegration factor plays crucial roles in cell cycle progression and nuclear organization in Drosophila. J. Cell. Sci. 116: 3811-3823
    • (2003) J. Cell. Sci. , vol.116 , pp. 3811-3823
    • Furukawa, K.1    Sugiyama, S.2    Osouda, S.3    Goto, H.4    Inagaki, M.5    Horigome, T.6
  • 173
    • 0034255236 scopus 로고    scopus 로고
    • Barrier-to-autointegration factor (BAF) bridges DNA in a discrete, higher-order nucleoprotein complex
    • USA
    • Zheng R., Ghirlando R., Lee M. S., Mizuuchi K., Krause M. and Craigie R. (2000) Barrier-to-autointegration factor (BAF) bridges DNA in a discrete, higher-order nucleoprotein complex. Proc. Natl. Acad. Sci. USA 97: 8997-9002
    • (2000) Proc. Natl. Acad. Sci. , vol.97 , pp. 8997-9002
    • Zheng, R.1    Ghirlando, R.2    Lee, M.S.3    Mizuuchi, K.4    Krause, M.5    Craigie, R.6
  • 174
    • 0035794643 scopus 로고    scopus 로고
    • LAP2 binds to BAF.DNA complexes: Requirement for the LEM domain and modulation by variable regions
    • Shumaker D. K., Lee K. K., Tanhehco Y. C., Craigie R. and Wilson K. L. (2001) LAP2 binds to BAF.DNA complexes: requirement for the LEM domain and modulation by variable regions. EMBO J. 20: 1754-1764
    • (2001) EMBO J. , vol.20 , pp. 1754-1764
    • Shumaker, D.K.1    Lee, K.K.2    Tanhehco, Y.C.3    Craigie, R.4    Wilson, K.L.5
  • 175
    • 2142653551 scopus 로고    scopus 로고
    • Interphase chromosomes and the Rabl configuration: Does genome size matter?
    • Santos A. P. and Shaw P. (2004) Interphase chromosomes and the Rabl configuration: does genome size matter? J. Microsc. 214: 201-206
    • (2004) J. Microsc. , vol.214 , pp. 201-206
    • Santos, A.P.1    Shaw, P.2
  • 176
    • 0031044199 scopus 로고    scopus 로고
    • 2+ stores are not required for nuclear envelope assembly or nuclear protein import in Xenopus egg extracts
    • 2+ stores are not required for nuclear envelope assembly or nuclear protein import in Xenopus egg extracts. Cell Calcium 21: 151-161
    • (1997) Cell Calcium , vol.21 , pp. 151-161
    • Marshall, I.C.1    Gant, T.M.2    Wilson, K.L.3
  • 177
    • 1942503933 scopus 로고    scopus 로고
    • Separation of silencing from perinuclear anchoring functions in yeast Ku80, Sir4 and Esc1 proteins
    • Taddei A., Hediger F., Neumann F. R., Bauer C. and Gasser S. M. (2004) Separation of silencing from perinuclear anchoring functions in yeast Ku80, Sir4 and Esc1 proteins. EMBO J. 23: 1301-1312
    • (2004) EMBO J. , vol.23 , pp. 1301-1312
    • Taddei, A.1    Hediger, F.2    Neumann, F.R.3    Bauer, C.4    Gasser, S.M.5
  • 178
    • 0347683485 scopus 로고    scopus 로고
    • Separation-of-function mutants of yeast Ku80 reveal a Yku80p-Sir4p interaction involved in telomeric silencing
    • Roy R., Meier B., McAinsh A. D., Feldmann H. M. and Jackson S. P. (2004) Separation-of-function mutants of yeast Ku80 reveal a Yku80p-Sir4p interaction involved in telomeric silencing. J. Biol. Chem. 279: 86-94
    • (2004) J. Biol. Chem. , vol.279 , pp. 86-94
    • Roy, R.1    Meier, B.2    McAinsh, A.D.3    Feldmann, H.M.4    Jackson, S.P.5
  • 179
    • 0037097940 scopus 로고    scopus 로고
    • Rap1-Sir4 binding independent of other Sir, yKu or histone interactions initiates the assembly of telomeric heterochromatin in yeast
    • Luo K., Vega-Palas M. A. and Grunstein M. (2002) Rap1-Sir4 binding independent of other Sir, yKu or histone interactions initiates the assembly of telomeric heterochromatin in yeast. Genes Dev. 16: 1528-1539
    • (2002) Genes Dev. , vol.16 , pp. 1528-1539
    • Luo, K.1    Vega-Palas, M.A.2    Grunstein, M.3
  • 180
  • 181
    • 0036968369 scopus 로고    scopus 로고
    • Myosin-like proteins 1 and 2 are not required for silencing or telomere anchoring, but act in the Tell pathway of telomere length control
    • Hediger F., Dubrana K. and Gasser S. M. (2002) Myosin-like proteins 1 and 2 are not required for silencing or telomere anchoring, but act in the Tell pathway of telomere length control. J. Struct. Biol. 140: 79-91
    • (2002) J. Struct. Biol. , vol.140 , pp. 79-91
    • Hediger, F.1    Dubrana, K.2    Gasser, S.M.3
  • 182
  • 183
    • 11144296359 scopus 로고    scopus 로고
    • Sir-mediated repression can occur independently of chromosomal and subnuclear contexts
    • Gartenberg M. R., Neumann F. R., Laroche T., Blaszczyk M. and Gasser S. M. (2004) Sir-mediated repression can occur independently of chromosomal and subnuclear contexts. Cell 119: 955-967
    • (2004) Cell , vol.119 , pp. 955-967
    • Gartenberg, M.R.1    Neumann, F.R.2    Laroche, T.3    Blaszczyk, M.4    Gasser, S.M.5
  • 184
    • 0037205232 scopus 로고    scopus 로고
    • Chromatin boundaries in budding yeast: The nuclear pore connection
    • Ishii K., Arib G., Lin C., Van Houwe G. and Laemmli U. K. (2002) Chromatin boundaries in budding yeast: the nuclear pore connection. Cell 109: 551-562
    • (2002) Cell , vol.109 , pp. 551-562
    • Ishii, K.1    Arib, G.2    Lin, C.3    Van Houwe, G.4    Laemmli, U.K.5
  • 185
    • 14044266853 scopus 로고    scopus 로고
    • Gene recruitment of the activated INO1 locus to the nuclear membrane
    • Brickner J. H. and Walter P. (2004) Gene recruitment of the activated INO1 locus to the nuclear membrane. PLoS Biol. 2: e342
    • (2004) PLoS Biol. , vol.2
    • Brickner, J.H.1    Walter, P.2
  • 186
    • 2342501365 scopus 로고    scopus 로고
    • Genome-wide localization of the nuclear transport machinery couples transcriptional status and nuclear organization
    • Casolari J. M., Brown C. R., Komili S., West J., Hieronymus H. and Silver P. A. (2004) Genome-wide localization of the nuclear transport machinery couples transcriptional status and nuclear organization. Cell 117: 427-439
    • (2004) Cell , vol.117 , pp. 427-439
    • Casolari, J.M.1    Brown, C.R.2    Komili, S.3    West, J.4    Hieronymus, H.5    Silver, P.A.6
  • 187
    • 0344338368 scopus 로고
    • Gene gating: A hypothesis
    • USA
    • Blobel G. (1985) Gene gating: a hypothesis. Proc. Natl. Acad. Sci. USA 82: 8527-8529
    • (1985) Proc. Natl. Acad. Sci. , vol.82 , pp. 8527-8529
    • Blobel, G.1
  • 188
    • 0033523949 scopus 로고    scopus 로고
    • Transcribed genes are localized according to chromosomal position within polarized Drosophila embryonic nuclei
    • Wilkie G. S., Shermoen A. W., O'Farrell P. H. and Davis I. (1999) Transcribed genes are localized according to chromosomal position within polarized Drosophila embryonic nuclei. Curr. Biol. 9: 1263-1266
    • (1999) Curr. Biol. , vol.9 , pp. 1263-1266
    • Wilkie, G.S.1    Shermoen, A.W.2    O'Farrell, P.H.3    Davis, I.4
  • 189
    • 0344378215 scopus 로고    scopus 로고
    • The intranuclear movement of Balbiani ring premessenger ribonucleoprotein particles
    • Singh O. P., Bjorkroth B., Masich S., Wieslander L. and Daneholt B. (1999) The intranuclear movement of Balbiani ring premessenger ribonucleoprotein particles. Exp. Cell Res. 251: 135-146
    • (1999) Exp. Cell Res. , vol.251 , pp. 135-146
    • Singh, O.P.1    Bjorkroth, B.2    Masich, S.3    Wieslander, L.4    Daneholt, B.5
  • 190
    • 0035234534 scopus 로고    scopus 로고
    • Ire1p: A kinase and site-specific endoribonuclease
    • Gonzalez T. N. and Walter P. (2001) Ire1p: a kinase and site-specific endoribonuclease. Methods Mol Biol 160: 25-36
    • (2001) Methods Mol Biol , vol.160 , pp. 25-36
    • Gonzalez, T.N.1    Walter, P.2
  • 191
    • 0035370949 scopus 로고    scopus 로고
    • Intracellular signaling from the endoplasmic reticulum to the nucleus: The unfolded protein response in yeast and mammals
    • Patil C. and Walter P. (2001) Intracellular signaling from the endoplasmic reticulum to the nucleus: the unfolded protein response in yeast and mammals. Curr. Opin. Cell Biol. 13: 349-355
    • (2001) Curr. Opin. Cell Biol. , vol.13 , pp. 349-355
    • Patil, C.1    Walter, P.2
  • 192
    • 0030297537 scopus 로고    scopus 로고
    • A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response
    • Cox J. S. and Walter P. (1996) A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response. Cell 87: 391-404
    • (1996) Cell , vol.87 , pp. 391-404
    • Cox, J.S.1    Walter, P.2
  • 193
    • 22244446505 scopus 로고    scopus 로고
    • The mammalian unfolded protein response
    • Schroder M. and Kaufman R. J. (2005) The mammalian unfolded protein response. Annu. Rev. Biochem. 74: 739-789
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 739-789
    • Schroder, M.1    Kaufman, R.J.2
  • 194
    • 3242772325 scopus 로고    scopus 로고
    • Molecular aspects of diagnostic nucleolar and nuclear envelope changes in prostate cancer
    • Fischer A. H., Bardarov S. Jr. and Jiang Z. (2004) Molecular aspects of diagnostic nucleolar and nuclear envelope changes in prostate cancer. J. Cell. Biochem. 91: 170-184
    • (2004) J. Cell. Biochem. , vol.91 , pp. 170-184
    • Fischer, A.H.1    Bardarov Jr., S.2    Jiang, Z.3
  • 195
    • 9044249724 scopus 로고    scopus 로고
    • The t(7;11)(p15;p15) translocation in acute myeloid leukaemia fuses the genes for nucleoporin NUP98 and class I homeoprotein HOXA9
    • Borrow J., Shearman A. M., Stanton V. P. Jr., Becher R., Collins T., Williams A. J. et al. (1996) The t(7;11)(p15;p15) translocation in acute myeloid leukaemia fuses the genes for nucleoporin NUP98 and class I homeoprotein HOXA9. Nat. Genet. 12: 159-167
    • (1996) Nat. Genet. , vol.12 , pp. 159-167
    • Borrow, J.1    Shearman, A.M.2    Stanton Jr., V.P.3    Becher, R.4    Collins, T.5    Williams, A.J.6
  • 196
    • 9044241254 scopus 로고    scopus 로고
    • Fusion of the nucleoporin gene NUP98 to HOXA9 by the chromosome translocation t(7;11)(p15;p15) in human myeloid leukaemia
    • Nakamura T., Largaespada D. A., Lee M. P., Johnson L. A., Ohyashiki K., Toyama K. et al. (1996) Fusion of the nucleoporin gene NUP98 to HOXA9 by the chromosome translocation t(7;11)(p15;p15) in human myeloid leukaemia. Nat. Genet. 12: 154-158
    • (1996) Nat. Genet. , vol.12 , pp. 154-158
    • Nakamura, T.1    Largaespada, D.A.2    Lee, M.P.3    Johnson, L.A.4    Ohyashiki, K.5    Toyama, K.6
  • 197
    • 0029008267 scopus 로고
    • Relocation of the carboxyterminal part of CAN from the nuclear envelope to the nucleus as a result of leukemia-specific chromosome rearrangements
    • Fornerod M., Boer J., van Baal S., Jaegle M., von Lindern M., Murti K. G. et al. (1995) Relocation of the carboxyterminal part of CAN from the nuclear envelope to the nucleus as a result of leukemia-specific chromosome rearrangements. Oncogene 10: 1739-1748
    • (1995) Oncogene , vol.10 , pp. 1739-1748
    • Fornerod, M.1    Boer, J.2    Van Baal, S.3    Jaegle, M.4    Von Lindern, M.5    Murti, K.G.6
  • 198
    • 0029860596 scopus 로고    scopus 로고
    • Interaction of cellular proteins with the leukemia specific fusion proteins DEK-CAN and SET-CAN and their normal counterpart, the nucleoporin CAN
    • Fornerod M., Boer J., van Baal S., Morreau H. and Grosveld G. (1996) Interaction of cellular proteins with the leukemia specific fusion proteins DEK-CAN and SET-CAN and their normal counterpart, the nucleoporin CAN. Oncogene 13: 1801-1808
    • (1996) Oncogene , vol.13 , pp. 1801-1808
    • Fornerod, M.1    Boer, J.2    Van Baal, S.3    Morreau, H.4    Grosveld, G.5
  • 199
    • 1542609480 scopus 로고    scopus 로고
    • Minimal nuclear pore complexes define FG repeat domains essential for transport
    • Strawn L. A., Shen T., Shulga N., Goldfarb D. S. and Wente S. R. (2004) Minimal nuclear pore complexes define FG repeat domains essential for transport. Nat. Cell Biol. 6: 197-206
    • (2004) Nat. Cell Biol. , vol.6 , pp. 197-206
    • Strawn, L.A.1    Shen, T.2    Shulga, N.3    Goldfarb, D.S.4    Wente, S.R.5
  • 200
    • 0034698683 scopus 로고    scopus 로고
    • Binding of the Mex67p/Mtr2p heterodimer to FXFG, GLFG and FG repeat nucleoporins is essential for nuclear mRNA export
    • Strasser K., Bassler J. and Hurt E. (2000) Binding of the Mex67p/Mtr2p heterodimer to FXFG, GLFG and FG repeat nucleoporins is essential for nuclear mRNA export. J. Cell Biol. 150: 695-706
    • (2000) J. Cell Biol. , vol.150 , pp. 695-706
    • Strasser, K.1    Bassler, J.2    Hurt, E.3
  • 201
    • 0033785391 scopus 로고    scopus 로고
    • The molecular genetics of recurring chromosome abnormalities in acute myeloid leukemia
    • Hayashi Y. (2000) The molecular genetics of recurring chromosome abnormalities in acute myeloid leukemia. Semin. Hematol. 37: 368-380
    • (2000) Semin. Hematol. , vol.37 , pp. 368-380
    • Hayashi, Y.1
  • 202
    • 0032927877 scopus 로고    scopus 로고
    • CREB binding protein interacts with nucleoporin-specific FG repeats that activate transcription and mediate NUP98-HOXA9 oncogenicity
    • Kasper L. H., Brindle P. K., Schnabel C. A., Pritchard C. E., Cleary M. L. and van Deursen J. M. (1999) CREB binding protein interacts with nucleoporin-specific FG repeats that activate transcription and mediate NUP98-HOXA9 oncogenicity. Mol. Cell. Biol. 19: 764-776
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 764-776
    • Kasper, L.H.1    Brindle, P.K.2    Schnabel, C.A.3    Pritchard, C.E.4    Cleary, M.L.5    Van Deursen, J.M.6
  • 204
    • 0023134788 scopus 로고
    • Characterization of the rearranged tpr-met oncogene breakpoint
    • Dean M., Park M. and Vande Woude G. F. (1987) Characterization of the rearranged tpr-met oncogene breakpoint. Mol. Cell. Biol. 7: 921-924
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 921-924
    • Dean, M.1    Park, M.2    Vande Woude, G.F.3
  • 205
    • 0037947770 scopus 로고    scopus 로고
    • The nuclear pore complex protein ALADIN is mislocalized in triple A syndrome
    • USA
    • Cronshaw J. M. and Matunis M. J. (2003) The nuclear pore complex protein ALADIN is mislocalized in triple A syndrome. Proc. Natl. Acad. Sci. USA 100: 5823-5827
    • (2003) Proc. Natl. Acad. Sci. , vol.100 , pp. 5823-5827
    • Cronshaw, J.M.1    Matunis, M.J.2
  • 206
    • 36348978046 scopus 로고    scopus 로고
    • The nuclear pore complex: Disease associations and functional correlations
    • Cronshaw J. M. and Matunis M. J. (2004) The nuclear pore complex: disease associations and functional correlations. Trends Endocrinol. Metab. 15: 34-39
    • (2004) Trends Endocrinol. Metab. , vol.15 , pp. 34-39
    • Cronshaw, J.M.1    Matunis, M.J.2
  • 208
    • 0035194146 scopus 로고    scopus 로고
    • The role of the nuclear envelope in Emery-Dreifuss muscular dystrophy
    • Morris G. E. (2001) The role of the nuclear envelope in Emery-Dreifuss muscular dystrophy. Trends Mol. Med. 7: 572-577
    • (2001) Trends Mol. Med. , vol.7 , pp. 572-577
    • Morris, G.E.1
  • 209
    • 0035201307 scopus 로고    scopus 로고
    • The structure and function of nuclear lamins: Implications for disease
    • Moir R. D. and Spann T. P. (2001) The structure and function of nuclear lamins: implications for disease. Cell. Mol. Life Sci. 58: 1748-1757
    • (2001) Cell. Mol. Life Sci. , vol.58 , pp. 1748-1757
    • Moir, R.D.1    Spann, T.P.2
  • 210
    • 7244239317 scopus 로고    scopus 로고
    • Hutchinson-Gilford progeria syndrome
    • Pollex R. L. and Hegele R. A. (2004) Hutchinson-Gilford progeria syndrome. Clin. Genet. 66: 375-381
    • (2004) Clin. Genet. , vol.66 , pp. 375-381
    • Pollex, R.L.1    Hegele, R.A.2
  • 211
    • 5644250530 scopus 로고    scopus 로고
    • The stability of the nuclear lamina polymer changes with the composition of lamin subtypes according to their individual binding strengths
    • Schirmer E. C. and Gerace L. (2004) The stability of the nuclear lamina polymer changes with the composition of lamin subtypes according to their individual binding strengths. J. Biol. Chem. 279: 42811-42817
    • (2004) J. Biol. Chem. , vol.279 , pp. 42811-42817
    • Schirmer, E.C.1    Gerace, L.2
  • 212
    • 0030903041 scopus 로고    scopus 로고
    • Nuclear envelope protein autoantibodies in primary biliary cirrhosis
    • Courvalin J. C. and Worman H. J. (1997) Nuclear envelope protein autoantibodies in primary biliary cirrhosis. Semin. Liver Dis. 17: 79-90
    • (1997) Semin. Liver Dis. , vol.17 , pp. 79-90
    • Courvalin, J.C.1    Worman, H.J.2
  • 214
    • 2542609838 scopus 로고    scopus 로고
    • Autoantibodies from primary biliary cirrhosis patients with anti-p95c antibodies bind to recombinant p97/VCP and inhibit in vitro nuclear envelope assembly
    • Miyachi K., Hirano Y., Horigome T., Mimori T., Miyakawa H., Onozuka Y. et al. (2004) Autoantibodies from primary biliary cirrhosis patients with anti-p95c antibodies bind to recombinant p97/VCP and inhibit in vitro nuclear envelope assembly. Clin. Exp. Immunol. 136: 568-573
    • (2004) Clin. Exp. Immunol. , vol.136 , pp. 568-573
    • Miyachi, K.1    Hirano, Y.2    Horigome, T.3    Mimori, T.4    Miyakawa, H.5    Onozuka, Y.6
  • 215
    • 0028545385 scopus 로고
    • Primary biliary cirrhosis and the molecular cell biology of the nuclear envelope
    • Worman H. J. (1994) Primary biliary cirrhosis and the molecular cell biology of the nuclear envelope. Mt. Sinai J. Med. 61: 461-475
    • (1994) Mt. Sinai J. Med. , vol.61 , pp. 461-475
    • Worman, H.J.1
  • 216
    • 0036337963 scopus 로고    scopus 로고
    • Inhibition of nuclear import and alteration of nuclear pore complex composition by rhinovirus
    • Gustin K. E. and Sarnow P. (2002) Inhibition of nuclear import and alteration of nuclear pore complex composition by rhinovirus. J. Virol. 76: 8787-8796
    • (2002) J. Virol. , vol.76 , pp. 8787-8796
    • Gustin, K.E.1    Sarnow, P.2
  • 217
    • 0030065385 scopus 로고    scopus 로고
    • Autoantibodies against nucleoporin p62 constitute a novel marker of primary biliary cirrhosis
    • Wesierska-Gadek J., Hohenuer H., Hitchman E. and Penner E. (1996) Autoantibodies against nucleoporin p62 constitute a novel marker of primary biliary cirrhosis. Gastroenterology 110: 840-847
    • (1996) Gastroenterology , vol.110 , pp. 840-847
    • Wesierska-Gadek, J.1    Hohenuer, H.2    Hitchman, E.3    Penner, E.4
  • 218
    • 0027985787 scopus 로고
    • Identification of a novel X-linked gene responsible for Emery-Dreifuss muscular dystrophy
    • Bione S., Maestrini E., Rivella S., Mancini M., Regis S., Romeo G. et al. (1994) Identification of a novel X-linked gene responsible for Emery-Dreifuss muscular dystrophy. Nat. Genet. 8: 323-327
    • (1994) Nat. Genet. , vol.8 , pp. 323-327
    • Bione, S.1    Maestrini, E.2    Rivella, S.3    Mancini, M.4    Regis, S.5    Romeo, G.6
  • 219
    • 0010397284 scopus 로고    scopus 로고
    • The Emery-Dreifuss muscular dystrophy protein, emerin, is a nuclear membrane protein
    • Manilal S., Nguyen T. M., Sewry C. A. and Morris G. E. (1996) The Emery-Dreifuss muscular dystrophy protein, emerin, is a nuclear membrane protein. Hum. Mol. Genet. 5: 801-808
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 801-808
    • Manilal, S.1    Nguyen, T.M.2    Sewry, C.A.3    Morris, G.E.4
  • 220
    • 0033865686 scopus 로고    scopus 로고
    • Clinical and molecular genetic spectrum of autosomal dominant Emery-Dreifuss muscular dystrophy due to mutations of the lamin A/C gene
    • Bonne G., Mercuri E., Muchir A., Urtizberea A., Becane H. M., Recan D. et al. (2000) Clinical and molecular genetic spectrum of autosomal dominant Emery-Dreifuss muscular dystrophy due to mutations of the lamin A/C gene. Ann. Neurol. 48: 170-180
    • (2000) Ann. Neurol. , vol.48 , pp. 170-180
    • Bonne, G.1    Mercuri, E.2    Muchir, A.3    Urtizberea, A.4    Becane, H.M.5    Recan, D.6
  • 221
    • 0032977685 scopus 로고    scopus 로고
    • Mutations in the gene encoding lamin A/C cause autosomal dominant Emery-Dreifuss muscular dystrophy
    • Bonne G., Di Barletta M. R., Varnous S., Becane H. M., Hammouda E. H., Merlini L. et al. (1999) Mutations in the gene encoding lamin A/C cause autosomal dominant Emery-Dreifuss muscular dystrophy. Nat. Genet. 21: 285-288
    • (1999) Nat. Genet. , vol.21 , pp. 285-288
    • Bonne, G.1    Di Barletta, M.R.2    Varnous, S.3    Becane, H.M.4    Hammouda, E.H.5    Merlini, L.6
  • 222
    • 0037382801 scopus 로고    scopus 로고
    • Nuclear envelope proteins and neuromuscular diseases
    • Ostlund C. and Worman H. J. (2003) Nuclear envelope proteins and neuromuscular diseases. Muscle Nerve 27: 393-406
    • (2003) Muscle Nerve , vol.27 , pp. 393-406
    • Ostlund, C.1    Worman, H.J.2
  • 224
    • 0034820958 scopus 로고    scopus 로고
    • Novel lamin A/C mutations in two families with dilated cardiomyopathy and conduction system disease
    • Jakobs P. M., Hanson E. L., Crispell K. A., Toy W., Keegan H., Schilling K. et al. (2001 ) Novel lamin A/C mutations in two families with dilated cardiomyopathy and conduction system disease. J. Card. Fail. 7: 249-256
    • (2001) J. Card. Fail. , vol.7 , pp. 249-256
    • Jakobs, P.M.1    Hanson, E.L.2    Crispell, K.A.3    Toy, W.4    Keegan, H.5    Schilling, K.6
  • 226
    • 2342458205 scopus 로고    scopus 로고
    • Aging and nuclear organization: Lamins and progeria
    • Mounkes L. C. and Stewart C. L. (2004) Aging and nuclear organization: lamins and progeria. Curr. Opin. Cell Biol. 16: 322-327
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 322-327
    • Mounkes, L.C.1    Stewart, C.L.2
  • 227
    • 12244285280 scopus 로고    scopus 로고
    • Mutations at the mouse ichthyosis locus are within the lamin B receptor gene: A single gene model for human Pelger-Huet anomaly
    • Shultz L. D., Lyons B. L., Burzenski L. M., Gott B., Samuels R., Schweitzer P. A. et al. (2003) Mutations at the mouse ichthyosis locus are within the lamin B receptor gene: a single gene model for human Pelger-Huet anomaly. Hum. Mol. Genet. 12: 61-69
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 61-69
    • Shultz, L.D.1    Lyons, B.L.2    Burzenski, L.M.3    Gott, B.4    Samuels, R.5    Schweitzer, P.A.6
  • 228
    • 0036699522 scopus 로고    scopus 로고
    • Mutations in the gene encoding the lamin B receptor produce an altered nuclear morphology in granulocytes (Pelger-Huet anomaly)
    • Hoffmann K., Dreger C. K., Olins A. L., Olins D. E., Shultz L. D., Lucke B. et al. (2002) Mutations in the gene encoding the lamin B receptor produce an altered nuclear morphology in granulocytes (Pelger-Huet anomaly) Nat. Genet. 31: 410-414
    • (2002) Nat. Genet. , vol.31 , pp. 410-414
    • Hoffmann, K.1    Dreger, C.K.2    Olins, A.L.3    Olins, D.E.4    Shultz, L.D.5    Lucke, B.6
  • 229
    • 0034176682 scopus 로고    scopus 로고
    • The nuclear envelope, muscular dystrophy and gene expression
    • Wilson K. L. (2000) The nuclear envelope, muscular dystrophy and gene expression. Trends Cell Biol. 10: 125-129
    • (2000) Trends Cell Biol. , vol.10 , pp. 125-129
    • Wilson, K.L.1
  • 230
    • 0345084450 scopus 로고    scopus 로고
    • Ultrastructural abnormality of sarcolemmal nuclei in Emery-Dreifuss muscular dystrophy (EDMD)
    • Fidzianska A., Toniolo D. and Hausmanowa-Petrusewicz I. (1998) Ultrastructural abnormality of sarcolemmal nuclei in Emery-Dreifuss muscular dystrophy (EDMD) J. Neurol. Sci. 159: 88-93
    • (1998) J. Neurol. Sci. , vol.159 , pp. 88-93
    • Fidzianska, A.1    Toniolo, D.2    Hausmanowa-Petrusewicz, I.3
  • 231
    • 0037624625 scopus 로고    scopus 로고
    • Architectural abnormalities in muscle nuclei. Ultrastructural differences between X-linked and autosomal dominant forms of EDMD
    • Fidzianska A. and Hausmanowa-Petrusewicz I. (2003) Architectural abnormalities in muscle nuclei. Ultrastructural differences between X-linked and autosomal dominant forms of EDMD. J. Neurol. Sci. 210: 47-51
    • (2003) J. Neurol. Sci. , vol.210 , pp. 47-51
    • Fidzianska, A.1    Hausmanowa-Petrusewicz, I.2
  • 232
    • 13544274478 scopus 로고    scopus 로고
    • Loss-of-function mutations in LEMD3 result in osteopoikilosis, Buschke-Ollendorff syndrome and melorheostosis
    • Hellemans J., Preobrazhenska O., Willaert A., Debeer P., Verdonk P. C., Costa T. et al. (2004) Loss-of-function mutations in LEMD3 result in osteopoikilosis, Buschke-Ollendorff syndrome and melorheostosis. Nat. Genet. 36: 1213-1218
    • (2004) Nat. Genet. , vol.36 , pp. 1213-1218
    • Hellemans, J.1    Preobrazhenska, O.2    Willaert, A.3    Debeer, P.4    Verdonk, P.C.5    Costa, T.6
  • 233
    • 13544264752 scopus 로고    scopus 로고
    • MAN1, an integral protein of the inner nuclear membrane, binds Smad2 and Smad3 and antagonizes transforming growth factor-{beta} signaling
    • Lin F., Morrison J. M., Wu W. and Worman H. J. (2004) MAN1, an integral protein of the inner nuclear membrane, binds Smad2 and Smad3 and antagonizes transforming growth factor-{beta} signaling. Hum. Mol. Genet. 14: 437-445
    • (2004) Hum. Mol. Genet. , vol.14 , pp. 437-445
    • Lin, F.1    Morrison, J.M.2    Wu, W.3    Worman, H.J.4
  • 234
    • 0024993332 scopus 로고
    • Identification and characterization of autoantibodies against the nuclear envelope lamin B receptor from patients with primary biliary cirrhosis
    • Courvalin J. C., Lassoued K., Worman H. J. and Blobel G. (1990) Identification and characterization of autoantibodies against the nuclear envelope lamin B receptor from patients with primary biliary cirrhosis. J. Exp. Med. 172: 961-967
    • (1990) J. Exp. Med. , vol.172 , pp. 961-967
    • Courvalin, J.C.1    Lassoued, K.2    Worman, H.J.3    Blobel, G.4
  • 235
    • 0345535128 scopus 로고    scopus 로고
    • Autosomal recessive HEM/Greenberg skeletal dysplasia is caused by 3 beta-hydroxysterol delta 14-reductase deficiency due to mutations in the lamin B receptor gene
    • Waterham H. R., Koster J., Mooyer P., Noort GvG., Kelley R. I., Wilcox W. R. et al. (2003) Autosomal recessive HEM/Greenberg skeletal dysplasia is caused by 3 beta-hydroxysterol delta 14-reductase deficiency due to mutations in the lamin B receptor gene. Am. J. Hum. Genet. 72: 1013-1017
    • (2003) Am. J. Hum. Genet. , vol.72 , pp. 1013-1017
    • Waterham, H.R.1    Koster, J.2    Mooyer, P.3    Noort, Gv.G.4    Kelley, R.I.5    Wilcox, W.R.6
  • 236
    • 0028859201 scopus 로고
    • Integral membrane proteins associated with the nuclear lamina are novel autoimmune antigens of the nuclear envelope
    • Konstantinov K., Foisner R., Byrd D., Liu F. T., Tsai W. M., Wiik A. et al. (1995) Integral membrane proteins associated with the nuclear lamina are novel autoimmune antigens of the nuclear envelope. Clin. Immunol. Immunopathol. 74: 89-99
    • (1995) Clin. Immunol. Immunopathol. , vol.74 , pp. 89-99
    • Konstantinov, K.1    Foisner, R.2    Byrd, D.3    Liu, F.T.4    Tsai, W.M.5    Wiik, A.6
  • 237
    • 0037636737 scopus 로고    scopus 로고
    • Clinicopathological significance of Nup88 expression in patients with colorectal cancer
    • Emterling A., Skoglund J., Arbman G., Schneider J., Evertsson S., Carstensen, J. et al. (2003) Clinicopathological significance of Nup88 expression in patients with colorectal cancer. Oncology 64: 361-369
    • (2003) Oncology , vol.64 , pp. 361-369
    • Emterling, A.1    Skoglund, J.2    Arbman, G.3    Schneider, J.4    Evertsson, S.5    Carstensen, J.6
  • 238
    • 1342331426 scopus 로고    scopus 로고
    • Clinicopathological significance of microsatellite instability and mutated RIZ in colorectal cancer
    • Emterling A., Wallin A., Arbman G. and Sun X. F. (2004) Clinicopathological significance of microsatellite instability and mutated RIZ in colorectal cancer. Ann. Oncol. 15: 242-246
    • (2004) Ann. Oncol. , vol.15 , pp. 242-246
    • Emterling, A.1    Wallin, A.2    Arbman, G.3    Sun, X.F.4
  • 239
    • 0031935821 scopus 로고    scopus 로고
    • Overexpression of the nucleoporin CAN/NUP214 induces growth arrest, nucleocytoplasmic transport defects and apoptosis
    • Boer J., Bonten-Surtel J. and Grosveld G. (1998) Overexpression of the nucleoporin CAN/NUP214 induces growth arrest, nucleocytoplasmic transport defects and apoptosis. Mol. Cell. Biol. 18: 1236-1247
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1236-1247
    • Boer, J.1    Bonten-Surtel, J.2    Grosveld, G.3
  • 240
    • 6944252248 scopus 로고    scopus 로고
    • Fusion of NUP214 to ABL1 on amplified episomes in T-cell acute lymphoblastic leukemia
    • Graux C., Cools J., Melotte C., Quentmeier H., Ferrando A., Levine R. et al. (2004) Fusion of NUP214 to ABL1 on amplified episomes in T-cell acute lymphoblastic leukemia. Nat. Genet. 36: 1084-1089
    • (2004) Nat. Genet. , vol.36 , pp. 1084-1089
    • Graux, C.1    Cools, J.2    Melotte, C.3    Quentmeier, H.4    Ferrando, A.5    Levine, R.6
  • 241
    • 0027979480 scopus 로고
    • The human CAN protein, a putative oncogene product associated with myeloid leukemogenesis, is a nuclear pore complex protein that faces the cytoplasm
    • USA
    • Kraemer D., Wozniak R. W., Blobel G. and Radu A. (1994) The human CAN protein, a putative oncogene product associated with myeloid leukemogenesis, is a nuclear pore complex protein that faces the cytoplasm. Proc. Natl. Acad. Sci. USA 91: 1519-1523
    • (1994) Proc. Natl. Acad. Sci. , vol.91 , pp. 1519-1523
    • Kraemer, D.1    Wozniak, R.W.2    Blobel, G.3    Radu, A.4
  • 242
    • 3843075545 scopus 로고    scopus 로고
    • Aberrant intracellular localization of SET-CAN fusion protein, associated with a leukemia, disorganizes nuclear export
    • Saito S., Miyaji-Yamaguchi M. and Nagata K. (2004) Aberrant intracellular localization of SET-CAN fusion protein, associated with a leukemia, disorganizes nuclear export. Int. J. Cancer 111: 501-507
    • (2004) Int. J. Cancer , vol.111 , pp. 501-507
    • Saito, S.1    Miyaji-Yamaguchi, M.2    Nagata, K.3
  • 243
    • 0037402562 scopus 로고    scopus 로고
    • Fusion of ALK to the Ran-binding protein 2 (RANBP2) gene in inflammatory myofibroblastic tumor
    • Ma Z., Hill D. A., Collins M. H., Morris S. W., Sumegi J., Zhou M. et al. (2003) Fusion of ALK to the Ran-binding protein 2 (RANBP2) gene in inflammatory myofibroblastic tumor. Genes Chromosomes Cancer 37: 98-105
    • (2003) Genes Chromosomes Cancer , vol.37 , pp. 98-105
    • Ma, Z.1    Hill, D.A.2    Collins, M.H.3    Morris, S.W.4    Sumegi, J.5    Zhou, M.6
  • 245
    • 0242365630 scopus 로고    scopus 로고
    • Failure of lamin A/C to functionally assemble in R482L mutated familial partial lipodystrophy fibroblasts: Altered intermolecular interaction with emerin and implications for gene transcription
    • Capanni C., Cenni V., Mattioli E., Sabatelli P., Ognibene A., Columbaro M. et al. (2003) Failure of lamin A/C to functionally assemble in R482L mutated familial partial lipodystrophy fibroblasts: altered intermolecular interaction with emerin and implications for gene transcription. Exp. Cell Res. 291: 122-134
    • (2003) Exp. Cell Res. , vol.291 , pp. 122-134
    • Capanni, C.1    Cenni, V.2    Mattioli, E.3    Sabatelli, P.4    Ognibene, A.5    Columbaro, M.6
  • 247
    • 0033518282 scopus 로고    scopus 로고
    • Missense mutations in the rod domain of the lamin A/C gene as causes of dilated cardiomyopathy and conduction-system disease
    • Fatkin D., MacRae C., Sasaki T., Wolff M. R., Porcu M., Frenneaux M. et al. (1999) Missense mutations in the rod domain of the lamin A/C gene as causes of dilated cardiomyopathy and conduction-system disease. N. Engl. J. Med. 341: 1715-1724
    • (1999) N. Engl. J. Med. , vol.341 , pp. 1715-1724
    • Fatkin, D.1    MacRae, C.2    Sasaki, T.3    Wolff, M.R.4    Porcu, M.5    Frenneaux, M.6
  • 248
    • 0037225049 scopus 로고    scopus 로고
    • Expression of lamin a mutated in the carboxyl-terminal tail generates an aberrant nuclear phenotype similar to that observed in cells from patients with Dunnigan-type partial lipodystrophy and Emery-Dreifuss muscular dystrophy
    • Favreau C., Dubosclard E., Ostlund C., Vigouroux C., Capeau J., Wehnert M. et al. (2003) Expression of lamin A mutated in the carboxyl-terminal tail generates an aberrant nuclear phenotype similar to that observed in cells from patients with Dunnigan-type partial lipodystrophy and Emery-Dreifuss muscular dystrophy. Exp. Cell Res. 282: 14-23
    • (2003) Exp. Cell Res. , vol.282 , pp. 14-23
    • Favreau, C.1    Dubosclard, E.2    Ostlund, C.3    Vigouroux, C.4    Capeau, J.5    Wehnert, M.6
  • 249
    • 0036098280 scopus 로고    scopus 로고
    • Multi-system dystrophy syndrome due to novel missense mutations in the amino-terminal head and alpha-helical rod domains of the lamm A/C gene
    • Garg A., Speckman R. A. and Bowcock A. M. (2002) Multi-system dystrophy syndrome due to novel missense mutations in the amino-terminal head and alpha-helical rod domains of the lamm A/C gene. Am. J. Med. 112: 549-555
    • (2002) Am. J. Med. , vol.112 , pp. 549-555
    • Garg, A.1    Speckman, R.A.2    Bowcock, A.M.3
  • 250
    • 0036911038 scopus 로고    scopus 로고
    • A novel lamin A/C mutation in a family with dilated cardiomyopathy, prominent conduction system disease and need for permanent pacemaker implantation
    • Hershberger R. E., Hanson E. L., Jakobs P. M., Keegan H., Coates K., Bousman S. et al. (2002) A novel lamin A/C mutation in a family with dilated cardiomyopathy, prominent conduction system disease and need for permanent pacemaker implantation. Am. Heart J. 144: 1081-1086
    • (2002) Am. Heart J. , vol.144 , pp. 1081-1086
    • Hershberger, R.E.1    Hanson, E.L.2    Jakobs, P.M.3    Keegan, H.4    Coates, K.5    Bousman, S.6
  • 251
    • 0035715144 scopus 로고    scopus 로고
    • Subcutaneous abdominal adipocyte size, a predictor of type 2 diabetes, is linked to chromosome Iq2-q23 and is associated with a common polymorphism in LMNA in Pima Indians
    • Weyer C., Wolford J. K., Hanson R. L., Foley J. E., Tataranni P. A., Bogardus C. et al. (2001) Subcutaneous abdominal adipocyte size, a predictor of type 2 diabetes, is linked to chromosome Iq2-q23 and is associated with a common polymorphism in LMNA in Pima Indians. Mol. Genet. Metab. 72: 231-238
    • (2001) Mol. Genet. Metab. , vol.72 , pp. 231-238
    • Weyer, C.1    Wolford, J.K.2    Hanson, R.L.3    Foley, J.E.4    Tataranni, P.A.5    Bogardus, C.6
  • 253
    • 0034702027 scopus 로고    scopus 로고
    • Identification of mutations in the gene encoding lamins A/C in autosomal dominant limb girdle muscular dystrophy with atrioventricular conduction disturbances (LGMD1B)
    • Muchir A., Bonne G., van der Kooi A. J., van Meegen M., Baas F., Bolhuis P. A. et al. (2000) Identification of mutations in the gene encoding lamins A/C in autosomal dominant limb girdle muscular dystrophy with atrioventricular conduction disturbances (LGMD1B) Hum. Mol. Genet. 9: 1453-1459
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 1453-1459
    • Muchir, A.1    Bonne, G.2    Van Der Kooi, A.J.3    Van Meegen, M.4    Baas, F.5    Bolhuis, P.A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.