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Volumn 170, Issue 2, 2005, Pages 225-235

The nuclear pore complex-associated protein, Mlp2p, binds to the yeast spindle pole body and promotes its efficient assembly

Author keywords

[No Author keywords available]

Indexed keywords

MUTANT PROTEIN; MYOSIN LIKE PROTEIN 2 P; NUCLEOPORIN; PROTEIN; PROTEIN MLP 1 P; PROTEIN SPC 10P; PROTEIN SPC 29P; PROTEIN SPC 42P; UNCLASSIFIED DRUG;

EID: 22944465779     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.200504140     Document Type: Article
Times cited : (69)

References (54)
  • 1
    • 0033577812 scopus 로고    scopus 로고
    • Localization of core spindle pole body (SPB) components during SPB duplication in Saccharomyces cerevisiae
    • Adams, I.R., and J.V. Kilmartin. 1999. Localization of core spindle pole body (SPB) components during SPB duplication in Saccharomyces cerevisiae. J. Cell Biol. 145:809-823.
    • (1999) J. Cell Biol. , vol.145 , pp. 809-823
    • Adams, I.R.1    Kilmartin, J.V.2
  • 2
    • 0029845118 scopus 로고    scopus 로고
    • Kap104p: A karyopherin involved in the nuclear transport of messenger RNA binding proteins
    • Aitchison, J.D., G. Blobel, and M.P. Rout. 1996. Kap104p: a karyopherin involved in the nuclear transport of messenger RNA binding proteins. Science. 274:624-627.
    • (1996) Science , vol.274 , pp. 624-627
    • Aitchison, J.D.1    Blobel, G.2    Rout, M.P.3
  • 4
    • 0037059611 scopus 로고    scopus 로고
    • Nuclear envelope breakdown proceeds by microtubule-induced tearing of the lamina
    • Beaudouin, J., D. Gerlich, N. Daigle, R. Eils, and J. Ellenberg. 2002. Nuclear envelope breakdown proceeds by microtubule-induced tearing of the lamina. Cell. 108:83-96.
    • (2002) Cell , vol.108 , pp. 83-96
    • Beaudouin, J.1    Gerlich, D.2    Daigle, N.3    Eils, R.4    Ellenberg, J.5
  • 5
    • 0031587852 scopus 로고    scopus 로고
    • The yeast spindle pole body is assembled around a central crystal of Spc42p
    • Bullitt, E., M.P. Rout, J.V. Kilmartin, and C.W. Akey. 1997. The yeast spindle pole body is assembled around a central crystal of Spc42p. Cell. 89:1077-1086.
    • (1997) Cell , vol.89 , pp. 1077-1086
    • Bullitt, E.1    Rout, M.P.2    Kilmartin, J.V.3    Akey, C.W.4
  • 6
    • 3042923653 scopus 로고
    • Electron microscopic observations on the meiotic karyotype of diploid and tetraploid Saccharomyces cerevisiae
    • Byers, B., and L. Goetsch. 1975. Electron microscopic observations on the meiotic karyotype of diploid and tetraploid Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA. 72:5056-5060.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 5056-5060
    • Byers, B.1    Goetsch, L.2
  • 7
    • 13444257509 scopus 로고    scopus 로고
    • Chromosome looping in yeast: Telomere pairing and coordinated movement reflect anchoring efficiency and territorial organization
    • Bystricky, K., T. Laroche, G. van Houwe, M. Blaszczyk, and S.M. Gasser. 2005. Chromosome looping in yeast: telomere pairing and coordinated movement reflect anchoring efficiency and territorial organization. J. Cell Biol. 168:375-387.
    • (2005) J. Cell Biol. , vol.168 , pp. 375-387
    • Bystricky, K.1    Laroche, T.2    Van Houwe, G.3    Blaszczyk, M.4    Gasser, S.M.5
  • 8
    • 0032576588 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae Ndc1p is a shared component of nuclear pore complexes and spindle pole bodies
    • Chial, H.J., M.P. Rout, T.H. Giddings, and M. Winey. 1998. Saccharomyces cerevisiae Ndc1p 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
  • 9
    • 0026629519 scopus 로고
    • A temperature-sensitive calmodulin mutant loses viability during mitosis
    • Davis, T.N. 1992. A temperature-sensitive calmodulin mutant loses viability during mitosis. J. Cell Biol. 118:607-617.
    • (1992) J. Cell Biol. , vol.118 , pp. 607-617
    • Davis, T.N.1
  • 10
    • 0034681465 scopus 로고    scopus 로고
    • Convergent solutions to binding at a protein-protein interface
    • DeLano, W.L., M.H. Ultsch, A.M. de Vos, and J.A. Wells. 2000. Convergent solutions to binding at a protein-protein interface. Science. 287:1279-1283.
    • (2000) Science , vol.287 , pp. 1279-1283
    • DeLano, W.L.1    Ultsch, M.H.2    De Vos, A.M.3    Wells, J.A.4
  • 11
    • 0034089165 scopus 로고    scopus 로고
    • Large-scale screening of intracellular protein localization in living fission yeast cells by the use of a GFP-fusion genomic DNA library
    • Ding, D.Q., Y. Tomita, A. Yamamoto, Y. Chikashige, T. Haraguchi, and Y. Hiraoka. 2000. Large-scale screening of intracellular protein localization in living fission yeast cells by the use of a GFP-fusion genomic DNA library. Genes Cells. 5:169-190.
    • (2000) Genes Cells , vol.5 , pp. 169-190
    • Ding, D.Q.1    Tomita, Y.2    Yamamoto, A.3    Chikashige, Y.4    Haraguchi, T.5    Hiraoka, Y.6
  • 12
    • 0033023085 scopus 로고    scopus 로고
    • Spc29p is a component of the Spc110p subcomplex and is essential for spindle pole body duplication
    • Elliott, S., M. Knop, G. Schlenstedt, and E. Schiebel. 1999. Spc29p is a component of the Spc110p subcomplex and is essential for spindle pole body duplication. Proc. Natl. Acad. Sci. USA. 96:6205-6210.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6205-6210
    • Elliott, S.1    Knop, M.2    Schlenstedt, G.3    Schiebel, E.4
  • 13
    • 0026699308 scopus 로고
    • CLB5: A novel B cyclin from budding yeast with a role in S phase
    • Epstein, C.B., and F.R. Cross. 1992. CLB5: a novel B cyclin from budding yeast with a role in S phase. Genes Dev. 6:1695-1706.
    • (1992) Genes Dev. , vol.6 , pp. 1695-1706
    • Epstein, C.B.1    Cross, F.R.2
  • 15
    • 0036211823 scopus 로고    scopus 로고
    • RADARS, a bioinformatics solution that automates proteome mass spectral analysis, optimises protein identification, and archives data in a relational database
    • Field, H.I., D. Fenyo, and R.C. Beavis. 2002. RADARS, a bioinformatics solution that automates proteome mass spectral analysis, optimises protein identification, and archives data in a relational database. Proteomics. 2:36-47.
    • (2002) Proteomics , vol.2 , pp. 36-47
    • Field, H.I.1    Fenyo, D.2    Beavis, R.C.3
  • 16
    • 0035027807 scopus 로고    scopus 로고
    • Nuclear export of 60s ribosomal subunits depends on Xpo1p and requires a nuclear export sequence-containing factor, Nmd3p, that associates with the large subunit protein Rpl10p
    • Gadal, O., D. Strauss, J. Kessl, B. Trumpower, D. Tollervey, and E. Hurt. 2001. Nuclear export of 60s ribosomal subunits depends on Xpo1p and requires a nuclear export sequence-containing factor, Nmd3p, that associates with the large subunit protein Rpl10p. Mol. Cell. Biol. 21:3405-3415.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 3405-3415
    • Gadal, O.1    Strauss, D.2    Kessl, J.3    Trumpower, B.4    Tollervey, D.5    Hurt, E.6
  • 17
  • 18
    • 0742304306 scopus 로고    scopus 로고
    • Nuclear retention of unspliced mRNAs in yeast is mediated by perinuclear Mlp1
    • Galy, V., O. Gadal, M. Fromont-Racine, A. Romano, A. Jacquier, and U. Nehrbass. 2004. Nuclear retention of unspliced mRNAs in yeast is mediated by perinuclear Mlp1. Cell. 116:63-73.
    • (2004) Cell , vol.116 , pp. 63-73
    • Galy, V.1    Gadal, O.2    Fromont-Racine, M.3    Romano, A.4    Jacquier, A.5    Nehrbass, U.6
  • 20
    • 0037417959 scopus 로고    scopus 로고
    • The C-terminal domain of myosin-like protein 1 (Mlp1p) is a docking site for heterogeneous nuclear ribonucleoproteins that are required for mRNA export
    • Green, D.M., C.P. Johnson, H. Hagan, and A.H. Corbett. 2003. The C-terminal domain of myosin-like protein 1 (Mlp1p) is a docking site for heterogeneous nuclear ribonucleoproteins that are required for mRNA export. Proc. Natl. Acad. Sci. USA. 100:1010-1015.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 1010-1015
    • Green, D.M.1    Johnson, C.P.2    Hagan, H.3    Corbett, A.H.4
  • 21
    • 0035146528 scopus 로고    scopus 로고
    • Multi-step control of spindle pole body duplication by cyclin-dependent kinase
    • Haase, S.B., M. Winey, and S.I. Reed. 2001. Multi-step control of spindle pole body duplication by cyclin-dependent kinase. Nat. Cell Biol. 3:38-42.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 38-42
    • Haase, S.B.1    Winey, M.2    Reed, S.I.3
  • 22
    • 0036968369 scopus 로고    scopus 로고
    • Myosin-like proteins 1 and 2 are not required for silencing or telomere anchoring, but act in the Tel1 pathway of telomere length control
    • Hediger, F., K. Dubrana, and S.M. Gasser. 2002a. Myosin-like proteins 1 and 2 are not required for silencing or telomere anchoring, but act in the Tel1 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
  • 23
    • 0037164718 scopus 로고    scopus 로고
    • Live imaging of telomeres: yKu and Sir proteins define redundant telomere-anchoring pathways in yeast
    • Hediger, F., F.R. Neumann, G. Van Houwe, K. Dubrana, and S.M. Gasser. 2002b. Live imaging of telomeres: yKu and Sir proteins define redundant telomere-anchoring pathways in yeast. Curr. Biol. 12:2076-2089.
    • (2002) Curr. Biol. , vol.12 , pp. 2076-2089
    • Hediger, F.1    Neumann, F.R.2    Van Houwe, G.3    Dubrana, K.4    Gasser, S.M.5
  • 24
    • 0037049550 scopus 로고    scopus 로고
    • The yeast nuclear pore complex functionally interacts with components of the spindle assembly checkpoint
    • Iouk, T., O. Kerscher, R.J. Scott, M.A. Basrai, and R.W. Wozniak. 2002. The yeast nuclear pore complex functionally interacts with components of the spindle assembly checkpoint. J. Cell Biol. 159:807-819.
    • (2002) J. Cell Biol. , vol.159 , pp. 807-819
    • Iouk, T.1    Kerscher, O.2    Scott, R.J.3    Basrai, M.A.4    Wozniak, R.W.5
  • 25
    • 0024094565 scopus 로고
    • Functions of microtubules in the Saccharomyces cerevisiae cell cycle
    • Jacobs, C.W., A.E. Adams, P.J. Szaniszlo, and J.R. Pringle. 1988. Functions of microtubules in the Saccharomyces cerevisiae cell cycle. J. Cell Biol. 107:1409-1426.
    • (1988) J. Cell Biol. , vol.107 , pp. 1409-1426
    • Jacobs, C.W.1    Adams, A.E.2    Szaniszlo, P.J.3    Pringle, J.R.4
  • 26
    • 4344705968 scopus 로고    scopus 로고
    • The budding yeast spindle pole body: Structure, duplication, and function
    • Jaspersen, S.L., and M. Winey. 2004. The budding yeast spindle pole body: structure, duplication, and function. Annu. Rev. Cell Dev. Biol. 20:1-28.
    • (2004) Annu. Rev. Cell Dev. Biol. , vol.20 , pp. 1-28
    • Jaspersen, S.L.1    Winey, M.2
  • 27
    • 1942452749 scopus 로고    scopus 로고
    • Proof and evolutionary analysis of ancient genome duplication in the yeast Saccharomyces cerevisiae
    • Kellis, M., B.W. Birren, and E.S. Lander. 2004. Proof and evolutionary analysis of ancient genome duplication in the yeast Saccharomyces cerevisiae. Nature. 428:617-624.
    • (2004) Nature , vol.428 , pp. 617-624
    • Kellis, M.1    Birren, B.W.2    Lander, E.S.3
  • 28
    • 0027382276 scopus 로고
    • A spacer protein in the Saccharomyces cerevisiae spindle pole body whose transcript is cell cycle-regulated
    • Kilmartin, J.V., S.L. Dyos, D. Kershaw, and J.T. Finch. 1993. A spacer protein in the Saccharomyces cerevisiae spindle pole body whose transcript is cell cycle-regulated. J. Cell Biol. 123:1175-1184.
    • (1993) J. Cell Biol. , vol.123 , pp. 1175-1184
    • Kilmartin, J.V.1    Dyos, S.L.2    Kershaw, D.3    Finch, J.T.4
  • 29
  • 30
    • 0035499655 scopus 로고    scopus 로고
    • Automatic identification of proteins with a MALDI-quadrupole ion trap mass spectrometer
    • Krutchinsky, A.N., M. Kalkum, and B.T. Chait. 2001. Automatic identification of proteins with a MALDI-quadrupole ion trap mass spectrometer. Anal. Chem. 73:5066-5077.
    • (2001) Anal. Chem. , vol.73 , pp. 5066-5077
    • Krutchinsky, A.N.1    Kalkum, M.2    Chait, B.T.3
  • 31
    • 0036870329 scopus 로고    scopus 로고
    • The evolutionarily conserved single-copy gene for murine Tpr encodes one prevalent isoform in somatic cells and lacks paralogs in higher eukaryotes
    • Kuznetsov, N.V., L. Sandblad, M.E. Hase, A. Hunziker, M. Hergt, and V.C. Cordes. 2002. The evolutionarily conserved single-copy gene for murine Tpr encodes one prevalent isoform in somatic cells and lacks paralogs in higher eukaryotes. Chromosoma. 111:236-255.
    • (2002) Chromosoma , vol.111 , pp. 236-255
    • Kuznetsov, N.V.1    Sandblad, L.2    Hase, M.E.3    Hunziker, A.4    Hergt, M.5    Cordes, V.C.6
  • 32
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • Longtine, M.S., A. McKenzie III, D.J. Demarini, N.G. Shah, A. Wach, A. Brachat, P. Philippsen, and J.R. Pringle. 1998. Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae. Yeast. 14:953-961.
    • (1998) Yeast , vol.14 , pp. 953-961
    • Longtine, M.S.1    McKenzie III, A.2    Demarini, D.J.3    Shah, N.G.4    Wach, A.5    Brachat, A.6    Philippsen, P.7    Pringle, J.R.8
  • 33
    • 0346094458 scopus 로고    scopus 로고
    • The C. elegans hook protein, ZYG-12, mediates the essential attachment between the centrosome and nucleus
    • Malone, C.J., L. Misner, N. Le Bot, M.C. Tsai, J.M. Campbell, J. Ahringer, and J.G. White. 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    White, J.G.7
  • 34
    • 0035725074 scopus 로고    scopus 로고
    • Mechanisms controlling subcellular localization of the G(1) cyclins Cln2p and Cln3p in budding yeast
    • Miller, M.E., and F.R. Cross. 2001. Mechanisms controlling subcellular localization of the G(1) cyclins Cln2p and Cln3p in budding yeast. Mol. Cell. Biol. 21:6292-6311.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 6292-6311
    • Miller, M.E.1    Cross, F.R.2
  • 35
    • 0018645212 scopus 로고
    • On the association of centrioles with the interphase nucleus
    • Nadezhdina, E.S., D. Fais, and Y.S. Chentsov. 1979. On the association of centrioles with the interphase nucleus. Eur. J. Cell Biol. 19:109-115.
    • (1979) Eur. J. Cell Biol. , vol.19 , pp. 109-115
    • Nadezhdina, E.S.1    Fais, D.2    Chentsov, Y.S.3
  • 36
    • 0033053359 scopus 로고    scopus 로고
    • High-voltage electron tomography of spindle pole bodies and early mitotic spindles in the yeast Saccharomyces cerevisiae
    • O'Toole, E.T., M. Winey, and J.R. McIntosh. 1999. High-voltage electron tomography of spindle pole bodies and early mitotic spindles in the yeast Saccharomyces cerevisiae. Mol. Biol. Cell. 10:2017-2031.
    • (1999) Mol. Biol. Cell. , vol.10 , pp. 2017-2031
    • O'Toole, E.T.1    Winey, M.2    McIntosh, J.R.3
  • 38
    • 0036270546 scopus 로고    scopus 로고
    • Cloning-free genome alterations in Saccharomyces cerevisiae using adaptamer-mediated PCR
    • Reid, R.J., M. Lisby, and R. Rothstein. 2002. Cloning-free genome alterations in Saccharomyces cerevisiae using adaptamer-mediated PCR. Methods Enzymol. 350:258-277.
    • (2002) Methods Enzymol. , vol.350 , pp. 258-277
    • Reid, R.J.1    Lisby, M.2    Rothstein, R.3
  • 39
    • 0027366167 scopus 로고
    • Isolation of the yeast nuclear pore complex
    • Rout, M.P., and G. Blobel. 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
  • 40
    • 0025013883 scopus 로고
    • Components of the yeast spindle and spindle pole body
    • Rout, M.P., and J.V. Kilmartin. 1990. Components of the yeast spindle and spindle pole body. J. Cell Biol. 111:1913-1927.
    • (1990) J. Cell Biol. , vol.111 , pp. 1913-1927
    • Rout, M.P.1    Kilmartin, J.V.2
  • 41
    • 0034695924 scopus 로고    scopus 로고
    • The yeast nuclear pore complex: Composition, architecture, and transport mechanism
    • Rout, M.P., J.D. Aitchison, A. Suprapto, K. Hjertaas, Y. Zhao, and B.T. Chait. 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
  • 42
    • 0035163724 scopus 로고    scopus 로고
    • Cnm67p is a spacer protein of the Saccharomyces cerevisiae spindle pole body outer plaque
    • Schaerer, F., G. Morgan, M. Winey, and P. Philippsen. 2001. Cnm67p is a spacer protein of the Saccharomyces cerevisiae spindle pole body outer plaque. Mol. Biol. Cell. 12:2519-2533.
    • (2001) Mol. Biol. Cell. , vol.12 , pp. 2519-2533
    • Schaerer, F.1    Morgan, G.2    Winey, M.3    Philippsen, P.4
  • 44
    • 0027366227 scopus 로고
    • The calcium-binding protein cell division cycle 31 of Saccharomyces cerevisiae is a component of the half bridge of the spindle pole body
    • Spang, A., I. Courtney, U. Fackler, M. Matzner, and E. Schiebel. 1993. The calcium-binding protein cell division cycle 31 of Saccharomyces cerevisiae is a component of the half bridge of the spindle pole body. J. Cell Biol. 123:405-416.
    • (1993) J. Cell Biol. , vol.123 , pp. 405-416
    • Spang, A.1    Courtney, I.2    Fackler, U.3    Matzner, M.4    Schiebel, E.5
  • 45
    • 0034639234 scopus 로고    scopus 로고
    • Mutations in SPC110, encoding the yeast spindle pole body calmodulin-binding protein, cause defects in cell integrity as well as spindle formation
    • Stirling, D.A., and M.J. Stark. 2000. Mutations in SPC110, encoding the yeast spindle pole body calmodulin-binding protein, cause defects in cell integrity as well as spindle formation. Biochim. Biophys. Acta. 1499:85-100.
    • (2000) Biochim. Biophys. Acta , vol.1499 , pp. 85-100
    • Stirling, D.A.1    Stark, M.J.2
  • 46
    • 0029943427 scopus 로고    scopus 로고
    • Mutations which block the binding of calmodulin to Spc110p cause multiple mitotic defects
    • Stirling, D.A., T.F. Rayner, A.R. Prescott, and M.J. Stark. 1996. Mutations which block the binding of calmodulin to Spc110p cause multiple mitotic defects. J. Cell Sci. 109:1297-1310.
    • (1996) J. Cell Sci. , vol.109 , pp. 1297-1310
    • Stirling, D.A.1    Rayner, T.F.2    Prescott, A.R.3    Stark, M.J.4
  • 47
    • 0033535342 scopus 로고    scopus 로고
    • Proteins connecting the nuclear pore complex with the nuclear interior
    • Strambio-de-Castillia, C., G. Blobel, and M.P. Rout. 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
  • 48
    • 0030660673 scopus 로고    scopus 로고
    • A mutational analysis identifies three functional regions of the spindle pole component Spc110p in Saccharomyces cerevisiae
    • Sundberg, H.A., and T.N. Davis. 1997. A mutational analysis identifies three functional regions of the spindle pole component Spc110p in Saccharomyces cerevisiae. Mol. Biol. Cell. 8:2575-2590.
    • (1997) Mol. Biol. Cell. , vol.8 , pp. 2575-2590
    • Sundberg, H.A.1    Davis, T.N.2
  • 49
    • 0029997448 scopus 로고    scopus 로고
    • Role of calmodulin and Spc110p interaction in the proper assembly of spindle pole body compenents
    • Sundberg, H.A., L. Goetsch, B. Byers, and T.N. Davis. 1996. Role of calmodulin and Spc110p interaction in the proper assembly of spindle pole body compenents. J. Cell Biol. 133:111-124.
    • (1996) J. Cell Biol. , vol.133 , pp. 111-124
    • Sundberg, H.A.1    Goetsch, L.2    Byers, B.3    Davis, T.N.4
  • 51
    • 15444368318 scopus 로고    scopus 로고
    • Perinuclear Mlp proteins downregulate gene expression in response to a defect in mRNA export
    • Vinciguerra, P., N. Iglesias, J. Camblong, D. Zenklusen, and F. Stutz. 2005. Perinuclear Mlp proteins downregulate gene expression in response to a defect in mRNA export. EMBO J. 24:813-823.
    • (2005) EMBO J. , vol.24 , pp. 813-823
    • Vinciguerra, P.1    Iglesias, N.2    Camblong, J.3    Zenklusen, D.4    Stutz, F.5
  • 52
    • 0026463881 scopus 로고
    • A new family of yeast nuclear pore complex proteins
    • Wente, S.R., M.P. Rout, and G. Blobel. 1992. A new family of yeast nuclear pore complex proteins. J. Cell Biol. 119:705-723.
    • (1992) J. Cell Biol. , vol.119 , pp. 705-723
    • Wente, S.R.1    Rout, M.P.2    Blobel, G.3
  • 53
    • 0024708867 scopus 로고
    • Higher order structure is present in the yeast nucleus: Autoantibody probes demonstrate that the nucleolus lies opposite the spindle pole body
    • Yang, C.H., E.J. Lambie, J. Hardin, J. Craft, and M. Snyder. 1989. Higher order structure is present in the yeast nucleus: autoantibody probes demonstrate that the nucleolus lies opposite the spindle pole body. Chromosoma. 98:123-128.
    • (1989) Chromosoma , vol.98 , pp. 123-128
    • Yang, C.H.1    Lambie, E.J.2    Hardin, J.3    Craft, J.4    Snyder, M.5
  • 54
    • 0042970575 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae spindle pole body is a dynamic structure
    • Yoder, T.J., C.G. Pearson, K. Bloom, and T.N. Davis. 2003. The Saccharomyces cerevisiae spindle pole body is a dynamic structure. Mol. Biol. Cell. 14:3494-3505.
    • (2003) Mol. Biol. Cell. , vol.14 , pp. 3494-3505
    • Yoder, T.J.1    Pearson, C.G.2    Bloom, K.3    Davis, T.N.4


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