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Volumn 16, Issue 9, 2005, Pages 3999-4012

Alanine scanning of Arp1 delineates a putative binding site for Jnm1/dynamitin and Nip100/p150Glued

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; DYNAMITIN; DYNEIN ADENOSINE TRIPHOSPHATASE; PROTEIN; PROTEIN ARP1; PROTEIN NIP100; PROTEIN P150 GLUED; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 24344440193     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E05-02-0093     Document Type: Article
Times cited : (11)

References (64)
  • 1
    • 0028928199 scopus 로고
    • Defining protein interactions with yeast actin in vivo
    • Amberg, D. C., Basart, E., and Botstein, D. (1995). Defining protein interactions with yeast actin in vivo. Nat. Struct. Biol. 2, 28-35.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 28-35
    • Amberg, D.C.1    Basart, E.2    Botstein, D.3
  • 2
    • 0032531024 scopus 로고    scopus 로고
    • Functional analysis of yeast essential genes using a promoter- substitution cassette and the tetracycline-regulatable dual expression system
    • Belli, G., Gari, E., Aldea, M., and Herrero, E. (1998a). Functional analysis of yeast essential genes using a promoter-substitution cassette and the tetracycline-regulatable dual expression system. Yeast 14, 1127-1138.
    • (1998) Yeast , vol.14 , pp. 1127-1138
    • Belli, G.1    Gari, E.2    Aldea, M.3    Herrero, E.4
  • 3
    • 0032519306 scopus 로고    scopus 로고
    • An activator/repressor dual system allows tight tetracycline-regulated gene expression in budding yeast
    • Belli, G., Gari, E., Piedrafita, L., Aldea, M., and Herrero, E. (1998b). An activator/repressor dual system allows tight tetracycline-regulated gene expression in budding yeast. Nucleic Acids Res. 26, 942-947.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 942-947
    • Belli, G.1    Gari, E.2    Piedrafita, L.3    Aldea, M.4    Herrero, E.5
  • 4
    • 0032494082 scopus 로고    scopus 로고
    • The yeast V159N actin mutant reveals roles for actin dynamics in vivo
    • Belmont, L. D., and Drubin, D. G. (1998). The yeast V159N actin mutant reveals roles for actin dynamics in vivo. J. Cell Biol. 742, 1289-1299.
    • (1998) J. Cell Biol. , vol.742 , pp. 1289-1299
    • Belmont, L.D.1    Drubin, D.G.2
  • 5
    • 0033524402 scopus 로고    scopus 로고
    • A change in actin conformation associated with filament instability after Pi release
    • Belmont, L. D., Orlova, A., Drubin, D. G., and Egelman, E. H. (1999a). A change in actin conformation associated with filament instability after Pi release. Proc. Natl. Acad. Sci. USA 96, 29-34.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 29-34
    • Belmont, L.D.1    Orlova, A.2    Drubin, D.G.3    Egelman, E.H.4
  • 6
    • 0033019429 scopus 로고    scopus 로고
    • New actin mutants allow further characterization of the nucleotide binding cleft and drug binding sites
    • Belmont, L. D., Patterson, G. M., and Drubin, D. G. (1999b). New actin mutants allow further characterization of the nucleotide binding cleft and drug binding sites. J. Cell Sci. 112, 1325-1336.
    • (1999) J. Cell Sci. , vol.112 , pp. 1325-1336
    • Belmont, L.D.1    Patterson, G.M.2    Drubin, D.G.3
  • 7
    • 0033602146 scopus 로고    scopus 로고
    • Self-regulated polymerization of the actin-related protein Arp1
    • Bingham, J. B., and Schroer, T. A. (1999). Self-regulated polymerization of the actin-related protein Arp1. Curr. Biol. 9, 223-226.
    • (1999) Curr. Biol. , vol.9 , pp. 223-226
    • Bingham, J.B.1    Schroer, T.A.2
  • 8
    • 0032214123 scopus 로고    scopus 로고
    • Two actin-related proteins are shared functional components of the chromatin-remodeling complexes RSC and SWI/SNF
    • Cairns, B. R., Erdjument-Bromage, H., Tempst, P., Winston, F., and Kornberg, R. D. (1998). Two actin-related proteins are shared functional components of the chromatin-remodeling complexes RSC and SWI/SNF. Mol. Cell 2, 639-651.
    • (1998) Mol. Cell , vol.2 , pp. 639-651
    • Cairns, B.R.1    Erdjument-Bromage, H.2    Tempst, P.3    Winston, F.4    Kornberg, R.D.5
  • 9
    • 0026686929 scopus 로고
    • Centractin is an actin homologue associated with the centrosome
    • Clark, S. W., and Meyer, D. I. (1992). Centractin is an actin homologue associated with the centrosome. Nature 359, 246-250.
    • (1992) Nature , vol.359 , pp. 246-250
    • Clark, S.W.1    Meyer, D.I.2
  • 10
    • 0030931849 scopus 로고    scopus 로고
    • Mitotic spindle positioning in Saccharomyces cerevisiae is accomplished by antagonistically acting microtubule motor proteins
    • Cottingham, F. R., and Hoyt, M. A. (1997). Mitotic spindle positioning in Saccharomyces cerevisiae is accomplished by antagonistically acting microtubule motor proteins. J. Cell Biol. 738, 1041-1053.
    • (1997) J. Cell Biol. , vol.738 , pp. 1041-1053
    • Cottingham, F.R.1    Hoyt, M.A.2
  • 11
    • 0030974313 scopus 로고    scopus 로고
    • Marker swap' plasmids: Convenient tools for budding yeast molecular genetics
    • Cross, F. R. (1997). 'Marker swap' plasmids: convenient tools for budding yeast molecular genetics. Yeast 73, 647-653.
    • (1997) Yeast , vol.73 , pp. 647-653
    • Cross, F.R.1
  • 12
    • 0030928162 scopus 로고    scopus 로고
    • Kinesin-related KIP3 of Saccharomyces cerevisiae is required for a distinct step in nuclear migration
    • DeZwaan, T. M., Ellingson, E., Pellman, D., and Roof, D. M. (1997). Kinesin-related KIP3 of Saccharomyces cerevisiae is required for a distinct step in nuclear migration. J. Cell Biol. 138, 1023-1040.
    • (1997) J. Cell Biol. , vol.138 , pp. 1023-1040
    • DeZwaan, T.M.1    Ellingson, E.2    Pellman, D.3    Roof, D.M.4
  • 13
    • 0027765526 scopus 로고
    • Actin structure and function: Roles in mitochondrial organization and morphogenesis in budding yeast and identification of the phalloidin-binding site
    • Drubin, D. G., Jones, H. D., and Wertman, K. F. (1993). Actin structure and function: roles in mitochondrial organization and morphogenesis in budding yeast and identification of the phalloidin-binding site. Mol. Biol. Cell 4, 1277-1294.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 1277-1294
    • Drubin, D.G.1    Jones, H.D.2    Wertman, K.F.3
  • 14
    • 0032728976 scopus 로고    scopus 로고
    • Analysis of dynactin subcomplexes reveals a novel actin-related protein associated with the arp1 minifilament pointed end
    • Eckley, D. M., Gill, S. R., Melkonian, K. A., Bingham, J. B., Goodson, H. V., Heuser, J. E., and Schroer, T. A. (1999). Analysis of dynactin subcomplexes reveals a novel actin-related protein associated with the arp1 minifilament pointed end. J. Cell Biol. 147, 307-320.
    • (1999) J. Cell Biol. , vol.147 , pp. 307-320
    • Eckley, D.M.1    Gill, S.R.2    Melkonian, K.A.3    Bingham, J.B.4    Goodson, H.V.5    Heuser, J.E.6    Schroer, T.A.7
  • 15
    • 0038107541 scopus 로고    scopus 로고
    • Interactions between the evolutionarily conserved, actin-related protein, Arp11, actin, and Arp1
    • Epub 2003 Mar 2620
    • Eckley, D. M., and Schroer, T. A. (2003). Interactions between the evolutionarily conserved, actin-related protein, Arp11, actin, and Arp1. Mol. Biol. Cell 14, 2645-2654. Epub 2003 Mar 2620.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2645-2654
    • Eckley, D.M.1    Schroer, T.A.2
  • 16
    • 0033576598 scopus 로고    scopus 로고
    • Interaction of the p62 subunit of dynactin with Arp1 and the cortical actin cytoskeleton
    • Garces, J. A., Clark, I. B., Meyer, D. I., and Vallee, R. B. (1999). Interaction of the p62 subunit of dynactin with Arp1 and the cortical actin cytoskeleton. Curr. Biol. 9, 1497-1500.
    • (1999) Curr. Biol. , vol.9 , pp. 1497-1500
    • Garces, J.A.1    Clark, I.B.2    Meyer, D.I.3    Vallee, R.B.4
  • 17
    • 0028685249 scopus 로고
    • Transforming yeast cells with DNA
    • Gietz, R. D., and Schiestl, R. H. (1995). Transforming yeast cells with DNA. Mol. Cell. Biol. 5, 255-269.
    • (1995) Mol. Cell. Biol. , vol.5 , pp. 255-269
    • Gietz, R.D.1    Schiestl, R.H.2
  • 18
    • 0036629334 scopus 로고    scopus 로고
    • Molecular evolution of the actin family
    • Goodson, H. V., and Hawse, W. F. (2002). Molecular evolution of the actin family. J. Cell Sci. 115, 2619-2622.
    • (2002) J. Cell Sci. , vol.115 , pp. 2619-2622
    • Goodson, H.V.1    Hawse, W.F.2
  • 19
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-Pdb-Viewer: An environment for comparative protein modeling
    • Guex, N., and Peitsch, M. C. (1997). SWISS-MODEL and the Swiss-Pdb-Viewer: an environment for comparative protein modeling. Electrophoresis 18, 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 20
    • 14844362866 scopus 로고    scopus 로고
    • Three-dimensional reconstruction of the dynactin complex by single-particle image analysis
    • Epub 2005 Feb 3628
    • Hodgkinson, J. L., Peters, C., Kuznetsov, S. A., and Steffen, W. (2005). Three-dimensional reconstruction of the dynactin complex by single-particle image analysis. Proc. Natl. Acad. Sci. USA 102, 3667-3672. Epub 2005 Feb 3628.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 3667-3672
    • Hodgkinson, J.L.1    Peters, C.2    Kuznetsov, S.A.3    Steffen, W.4
  • 21
    • 0031947483 scopus 로고    scopus 로고
    • The role of the dynactin complex in intracellular motility
    • Holleran, E. A., Karki, S., and Holzbaur, E. L. (1998). The role of the dynactin complex in intracellular motility. Int. Rev. Cytol. 182, 69-109.
    • (1998) Int. Rev. Cytol. , vol.182 , pp. 69-109
    • Holleran, E.A.1    Karki, S.2    Holzbaur, E.L.3
  • 22
    • 0026067071 scopus 로고
    • A simple and efficient method for direct cloning of PCR products using ddT-tailed vectors
    • Holton, T. A., and Graham, M. W. (1991). A simple and efficient method for direct cloning of PCR products using ddT-tailed vectors. Nucleic Acids Res. 19, 1156
    • (1991) Nucleic Acids Res. , vol.19 , pp. 1156
    • Holton, T.A.1    Graham, M.W.2
  • 23
    • 0028361816 scopus 로고
    • Mapping actin surfaces required for functional interactions in vivo
    • Holtzman, D. A., Wertman, K. F., and Drubin, D. G. (1994). Mapping actin surfaces required for functional interactions in vivo. J. Cell Biol. 126, 423-432.
    • (1994) J. Cell Biol. , vol.126 , pp. 423-432
    • Holtzman, D.A.1    Wertman, K.F.2    Drubin, D.G.3
  • 24
    • 0030455820 scopus 로고    scopus 로고
    • Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast
    • James, P., Halladay, J., and Craig, E. A. (1996). Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast. Genetics 144, 1425-1436.
    • (1996) Genetics , vol.144 , pp. 1425-1436
    • James, P.1    Halladay, J.2    Craig, E.A.3
  • 25
    • 0031580213 scopus 로고    scopus 로고
    • Partitioning of plasmid R1. The ParM protein exhibits ATPase activity and interacts with the centromere-like ParR-parC complex
    • Jensen, R. B., and Gerdes, K. (1997). Partitioning of plasmid R1. The ParM protein exhibits ATPase activity and interacts with the centromere-like ParR-parC complex. J. Mol. Biol. 269, 505-513.
    • (1997) J. Mol. Biol. , vol.269 , pp. 505-513
    • Jensen, R.B.1    Gerdes, K.2
  • 26
    • 0031845220 scopus 로고    scopus 로고
    • The yeast dynactin complex is involved in partitioning the mitotic spindle between mother and daughter cells during anaphase B
    • Kahana, J. A., Schlenstedt, G., Evanchuk, D. M., Geiser, J. R., Hoyt, M. A., and Silver, P. A. (1998). The yeast dynactin complex is involved in partitioning the mitotic spindle between mother and daughter cells during anaphase B. Mol. Biol. Cell 9, 1741-1756.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1741-1756
    • Kahana, J.A.1    Schlenstedt, G.2    Evanchuk, D.M.3    Geiser, J.R.4    Hoyt, M.A.5    Silver, P.A.6
  • 27
    • 0033004145 scopus 로고    scopus 로고
    • Cytoplasmic dynein and dynactin in cell division and intracellular transport
    • Karki, S., and Holzbaur, E. L. (1999). Cytoplasmic dynein and dynactin in cell division and intracellular transport. Curr. Opin. Cell Biol. 33, 45-53.
    • (1999) Curr. Opin. Cell Biol. , vol.33 , pp. 45-53
    • Karki, S.1    Holzbaur, E.L.2
  • 28
    • 0025329022 scopus 로고
    • The FUR1 gene of Saccharomyces cerevisiae: Cloning, structure and expression of wild-type and mutant alleles
    • Kern, L., de Montigny, J., Jund, R., and Lacroute, F. (1990). The FUR1 gene of Saccharomyces cerevisiae: cloning, structure and expression of wild-type and mutant alleles. Gene 88, 149-157.
    • (1990) Gene , vol.88 , pp. 149-157
    • Kern, L.1    De Montigny, J.2    Jund, R.3    Lacroute, F.4
  • 29
    • 0034708459 scopus 로고    scopus 로고
    • Molecular linkage underlying microtubule orientation toward cortical sites in yeast
    • Korinek, W. S., Copeland, M. J., Chaudhuri, A., and Chant, J. (2000). Molecular linkage underlying microtubule orientation toward cortical sites in yeast. Science 287, 2257-2259.
    • (2000) Science , vol.287 , pp. 2257-2259
    • Korinek, W.S.1    Copeland, M.J.2    Chaudhuri, A.3    Chant, J.4
  • 30
    • 0034764498 scopus 로고    scopus 로고
    • Dynactin-membrane interaction is regulated by the C-terminal domains of p150(Glued)
    • Epub 2001 Sep 2024
    • Kumar, S., Zhou, Y., and Plamann, M. (2001). Dynactin-membrane interaction is regulated by the C-terminal domains of p150(Glued). EMBO Rep. 2, 939-944. Epub 2001 Sep 2024.
    • (2001) EMBO Rep. , vol.2 , pp. 939-944
    • Kumar, S.1    Zhou, Y.2    Plamann, M.3
  • 31
    • 2642699794 scopus 로고
    • Rapid and efficient site-specific mutagenesis without phenotypic selection
    • Kunkel, T. A. (1985). Rapid and efficient site-specific mutagenesis without phenotypic selection. Proc. Natl. Acad. Sci. USA 82, 488-492.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 488-492
    • Kunkel, T.A.1
  • 32
    • 0035166330 scopus 로고    scopus 로고
    • Null mutants of the Neurospora actin-related protein 1 pointed-end complex show distinct phenotypes
    • Lee, I. H., Kumar, S., and Plamann, M. (2001). Null mutants of the Neurospora actin-related protein 1 pointed-end complex show distinct phenotypes. Mol. Biol. Cell 32, 2195-2206.
    • (2001) Mol. Biol. Cell , vol.32 , pp. 2195-2206
    • Lee, I.H.1    Kumar, S.2    Plamann, M.3
  • 33
    • 0034708606 scopus 로고    scopus 로고
    • Positioning of the mitotic spindle by a cortical-microtubule capture mechanism
    • Lee, L., Tirnauer, J. S., Li, J., Schuyler, S. C., Liu, J. Y., and Pellman, D. (2000). Positioning of the mitotic spindle by a cortical-microtubule capture mechanism. Science 287, 2260-2262.
    • (2000) Science , vol.287 , pp. 2260-2262
    • Lee, L.1    Tirnauer, J.S.2    Li, J.3    Schuyler, S.C.4    Liu, J.Y.5    Pellman, D.6
  • 34
    • 0026783380 scopus 로고
    • A vertebrate actin-related protein is a component of a multisubunit complex involved in microrubule-based vesicle motility
    • Lees-Miller, J. P., Helfman, D. M., and Schroer, T. A. (1992). A vertebrate actin-related protein is a component of a multisubunit complex involved in microrubule-based vesicle motility. Nature 359, 244-246.
    • (1992) Nature , vol.359 , pp. 244-246
    • Lees-Miller, J.P.1    Helfman, D.M.2    Schroer, T.A.3
  • 35
    • 0027131941 scopus 로고
    • Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm
    • Lorenz, M., Popp, D., and Holmes, K. C. (1993). Refinement of the F-actin model against X-ray fiber diffraction data by the use of a directed mutation algorithm. J. Mol. Biol. 234, 826-836.
    • (1993) J. Mol. Biol. , vol.234 , pp. 826-836
    • Lorenz, M.1    Popp, D.2    Holmes, K.C.3
  • 37
    • 0034490532 scopus 로고    scopus 로고
    • Bim1p/Yeb1p mediates the Kar9p-dependent cortical attachment of cytoplasmic microtubules
    • Miller, R. K., Cheng, S. C., and Rose, M. D. (2000). Bim1p/Yeb1p mediates the Kar9p-dependent cortical attachment of cytoplasmic microtubules. Mol. Biol. Cell 33, 2949-2959.
    • (2000) Mol. Biol. Cell , vol.33 , pp. 2949-2959
    • Miller, R.K.1    Cheng, S.C.2    Rose, M.D.3
  • 38
    • 0031878092 scopus 로고    scopus 로고
    • The kinesin-related proteins, Kip2p and Kip3p, function differently in nuclear migration in yeast
    • Miller, R. K., Heller, K. K., Frisen, L., Wallack, D. L., Loayza, D., Gammie, A. E., and Rose, M. D. (1998). The kinesin-related proteins, Kip2p and Kip3p, function differently in nuclear migration in yeast. Mol. Biol. Cell 9, 2051-2068.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 2051-2068
    • Miller, R.K.1    Heller, K.K.2    Frisen, L.3    Wallack, D.L.4    Loayza, D.5    Gammie, A.E.6    Rose, M.D.7
  • 39
    • 0030048070 scopus 로고    scopus 로고
    • Protein-protein interactions in the rigor actomyosin complex
    • Milligan, R. A. (1996). Protein-protein interactions in the rigor actomyosin complex. Proc. Natl. Acad. Sci. USA 93, 21-26.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 21-26
    • Milligan, R.A.1
  • 40
    • 0032984997 scopus 로고    scopus 로고
    • Neurospora crassa ro-10 and ro-11 genes encode novel proteins required for nuclear distribution
    • Minke, P. F., Lee, I. H., Tinsley, J. H., Bruno, K. S., and Plamann, M. (1999). Neurospora crassa ro-10 and ro-11 genes encode novel proteins required for nuclear distribution. Mol. Microbiol. 32, 1065-1076.
    • (1999) Mol. Microbiol. , vol.32 , pp. 1065-1076
    • Minke, P.F.1    Lee, I.H.2    Tinsley, J.H.3    Bruno, K.S.4    Plamann, M.5
  • 41
    • 0033737971 scopus 로고    scopus 로고
    • A Neurospora crassa Arp1 mutation affecting cytoplasmic dynein and dynactin localization
    • Minke, P. F., Lee, I. H., Tinsley, J. H., and Plamann, M. (2000). A Neurospora crassa Arp1 mutation affecting cytoplasmic dynein and dynactin localization. Mol. Gen. Genet. 264, 433-440.
    • (2000) Mol. Gen. Genet. , vol.264 , pp. 433-440
    • Minke, P.F.1    Lee, I.H.2    Tinsley, J.H.3    Plamann, M.4
  • 42
    • 0035104723 scopus 로고    scopus 로고
    • Dynactin-dependent, dynein-driven vesicle transport in the absence of membrane proteins: A role for spectrin and acidic phospholipids
    • Muresan, V., Stankewich, M. C., Steffen, W., Morrow, J. S., Holzbaur, E. L., and Schnapp, B. J. (2001). Dynactin-dependent, dynein-driven vesicle transport in the absence of membrane proteins: a role for spectrin and acidic phospholipids. Mol. Cell 7, 173-183.
    • (2001) Mol. Cell , vol.7 , pp. 173-183
    • Muresan, V.1    Stankewich, M.C.2    Steffen, W.3    Morrow, J.S.4    Holzbaur, E.L.5    Schnapp, B.J.6
  • 43
    • 0030053370 scopus 로고    scopus 로고
    • ProMod and Swiss-Model: Internet-based tools for automated comparative protein modelling
    • Peitsch, M. C. (1996). ProMod and Swiss-Model: Internet-based tools for automated comparative protein modelling. Biochem. Soc. Trans. 24, 274-279.
    • (1996) Biochem. Soc. Trans. , vol.24 , pp. 274-279
    • Peitsch, M.C.1
  • 44
    • 0030754347 scopus 로고    scopus 로고
    • Who's who among the Saccharomyces cerevisiae actin-related proteins? A classification and nomenclature proposal for a large family
    • Poch, O., and Winsor, B. (1997). Who's who among the Saccharomyces cerevisiae actin-related proteins? A classification and nomenclature proposal for a large family. Yeast 33, 1053-1058.
    • (1997) Yeast , vol.33 , pp. 1053-1058
    • Poch, O.1    Winsor, B.2
  • 45
    • 0022555884 scopus 로고
    • Actin and actin-binding proteins. A critical evaluation of mechanisms and functions
    • Pollard, T. D., and Cooper, J. A. (1986). Actin and actin-binding proteins. A critical evaluation of mechanisms and functions. Annu. Rev. Biochem. 55, 987-1035.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 987-1035
    • Pollard, T.D.1    Cooper, J.A.2
  • 46
    • 0037382240 scopus 로고    scopus 로고
    • Mutant dynactin in motor neuron disease
    • Puls, I., et al. (2003). Mutant dynactin in motor neuron disease. Nat. Genet. 33, 455-456.
    • (2003) Nat. Genet. , vol.33 , pp. 455-456
    • Puls, I.1
  • 48
    • 0028123401 scopus 로고
    • Systematic mutational analysis of the yeast beta-tubulin gene
    • Reijo, R. A., Cooper, E. M., Beagle, G. J., and Huffaker, T. C. (1994). Systematic mutational analysis of the yeast beta-tubulin gene. Mol. Biol. Cell 5, 29-43.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 29-43
    • Reijo, R.A.1    Cooper, E.M.2    Beagle, G.J.3    Huffaker, T.C.4
  • 50
    • 0023545322 scopus 로고
    • A Saccharomyces cerevisiae genomic plasmid bank based on a centromere-containing shuttle vector
    • Rose, M. D., Novick, P., Thomas, J. H., Botstein, D., and Fink, G. R. (1987). A Saccharomyces cerevisiae genomic plasmid bank based on a centromere-containing shuttle vector. Gene 60, 237-243.
    • (1987) Gene , vol.60 , pp. 237-243
    • Rose, M.D.1    Novick, P.2    Thomas, J.H.3    Botstein, D.4    Fink, G.R.5
  • 52
    • 0037059618 scopus 로고    scopus 로고
    • Cytoplasmic dynein as a facilitator of nuclear envelope breakdown
    • Salina, D., Bodoor, K., Eckley, D. M., Schroer, T. A., Rattner, J. B., and Burke, B. (2002). Cytoplasmic dynein as a facilitator of nuclear envelope breakdown. Cell 308, 97-107.
    • (2002) Cell , vol.308 , pp. 97-107
    • Salina, D.1    Bodoor, K.2    Eckley, D.M.3    Schroer, T.A.4    Rattner, J.B.5    Burke, B.6
  • 53
    • 0031672952 scopus 로고    scopus 로고
    • Structure-mutation analysis of the ATPase site of Dictyostelium discoideum myosin II
    • Sasaki, N., and Sutoh, K. (1998). Structure-mutation analysis of the ATPase site of Dictyostelium discoideum myosin II. Adv. Biophys. 35, 1-24.
    • (1998) Adv. Biophys. , vol.35 , pp. 1-24
    • Sasaki, N.1    Sutoh, K.2
  • 54
    • 0028304474 scopus 로고
    • Ultrastructural analysis of the dynactin complex: An actin-related protein is a component of a filament that resembles F-actin
    • Schafer, D. A., Gill, S. R., Cooper, J. A., Heuser, J. E., and Schroer, T. A. (1994). Ultrastructural analysis of the dynactin complex: an actin-related protein is a component of a filament that resembles F-actin. J. Cell Biol. 126, 403-412.
    • (1994) J. Cell Biol. , vol.126 , pp. 403-412
    • Schafer, D.A.1    Gill, S.R.2    Cooper, J.A.3    Heuser, J.E.4    Schroer, T.A.5
  • 58
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R. S., and Hieter, P. (1989). A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 322, 19-27.
    • (1989) Genetics , vol.322 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 59
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier, F. W., and Moffatt, B. A. (1986). Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 389, 113-130.
    • (1986) J. Mol. Biol. , vol.389 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 60
    • 0028676232 scopus 로고
    • New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae
    • Wach, A., Brachat, A., Pohlmann, R., and Philippsen, P. (1994). New heterologous modules for classical or PCR-based gene disruptions in Saccharomyces cerevisiae. Yeast 10, 1793-1808.
    • (1994) Yeast , vol.10 , pp. 1793-1808
    • Wach, A.1    Brachat, A.2    Pohlmann, R.3    Philippsen, P.4
  • 61
    • 0026737363 scopus 로고
    • Systematic mutational analysis of the yeast ACT1 gene
    • Wertman, K. F., Drubin, D. G., and Botstein, D. (1992). Systematic mutational analysis of the yeast ACT1 gene. Genetics 332, 337-350.
    • (1992) Genetics , vol.332 , pp. 337-350
    • Wertman, K.F.1    Drubin, D.G.2    Botstein, D.3
  • 62
    • 0035109067 scopus 로고    scopus 로고
    • Generation of an isogenic collection of yeast actin mutants and identification of three interrelated phenotypes
    • Whitacre, J., Davis, D., Toenjes, K., Brower, S., and Adams, A. (2001). Generation of an isogenic collection of yeast actin mutants and identification of three interrelated phenotypes. Genetics 357, 533-543.
    • (2001) Genetics , vol.357 , pp. 533-543
    • Whitacre, J.1    Davis, D.2    Toenjes, K.3    Brower, S.4    Adams, A.5
  • 64
    • 0034739004 scopus 로고    scopus 로고
    • Myosin V orientates the mitotic spindle in yeast
    • Yin, H., Pruyne, D., Huffaker, T. C., and Bretscher, A. (2000). Myosin V orientates the mitotic spindle in yeast. Nature 406, 1013-1015.
    • (2000) Nature , vol.406 , pp. 1013-1015
    • Yin, H.1    Pruyne, D.2    Huffaker, T.C.3    Bretscher, A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.