메뉴 건너뛰기




Volumn 198, Issue 4, 2012, Pages 623-636

Hsp110 is required for spindle length control

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; GREEN FLUORESCENT PROTEIN; HEAT SHOCK PROTEIN 110; HEAT SHOCK PROTEIN 70; HYDROXYUREA; KINESIN 5;

EID: 84866395411     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201111105     Document Type: Article
Times cited : (18)

References (61)
  • 1
    • 30344462410 scopus 로고    scopus 로고
    • Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells
    • Albanèse, V., A.Y. Yam, J. Baughman, C. Parnot, and J. Frydman. 2006. Systems analyses reveal two chaperone networks with distinct functions in eukaryotic cells. Cell. 124:75-88. http://dx.doi.org/10.1016/j.cell.2005.11.039
    • (2006) Cell , vol.124 , pp. 75-88
    • Albanèse, V.1    Yam, A.Y.2    Baughman, J.3    Parnot, C.4    Frydman, J.5
  • 2
    • 35349022993 scopus 로고    scopus 로고
    • A suite of Gateway cloning vectors for high-throughput genetic analysis in Saccharomyces cerevisiae
    • Alberti, S., A.D. Gitler, and S. Lindquist. 2007. A suite of Gateway cloning vectors for high-throughput genetic analysis in Saccharomyces cerevisiae. Yeast. 24:913-919. http://dx.doi.org/10.1002/yea.1502
    • (2007) Yeast , vol.24 , pp. 913-919
    • Alberti, S.1    Gitler, A.D.2    Lindquist, S.3
  • 3
    • 0027968012 scopus 로고
    • The SAD1/RAD53 protein kinase controls multiple checkpoints and DNA damage-induced transcription in yeast
    • Allen, J.B., Z. Zhou, W. Siede, E.C. Friedberg, and S.J. Elledge. 1994. The SAD1/RAD53 protein kinase controls multiple checkpoints and DNA damage-induced transcription in yeast. Genes Dev. 8:2401-2415. http://dx.doi.org/10.1101/gad.8.20.2401
    • (1994) Genes Dev , vol.8 , pp. 2401-2415
    • Allen, J.B.1    Zhou, Z.2    Siede, W.3    Friedberg, E.C.4    Elledge, S.J.5
  • 4
    • 44049083594 scopus 로고    scopus 로고
    • Hsp110 is a nucleotide-activated exchange factor for Hsp70
    • Andréasson, C., J. Fiaux, H. Rampelt, M.P. Mayer, and B. Bukau. 2008. Hsp110 is a nucleotide-activated exchange factor for Hsp70. J. Biol. Chem. 283:8877-8884. http://dx.doi.org/10.1074/jbc.M710063200
    • (2008) J. Biol. Chem , vol.283 , pp. 8877-8884
    • Andréasson, C.1    Fiaux, J.2    Rampelt, H.3    Mayer, M.P.4    Bukau, B.5
  • 5
    • 0032579440 scopus 로고    scopus 로고
    • Designer deletion strains derived from Saccharomyces cerevisiae S288C: A useful set of strains and plasmids for PCR-mediated gene disruption and other applications
    • Brachmann, C.B., A. Davies, G.J. Cost, E. Caputo, J. Li, P. Hieter, and J.D. Boeke. 1998. Designer deletion strains derived from Saccharomyces cerevisiae S288C: A useful set of strains and plasmids for PCR-mediated gene disruption and other applications. Yeast. 14:115-132. http://dx.doi.org/10.1002/(SICI)1097-0061(19980130)14:2<115::AID-YEA204>3.0.CO;2-2
    • (1998) Yeast , vol.14 , pp. 115-132
    • Brachmann, C.B.1    Davies, A.2    Cost, G.J.3    Caputo, E.4    Li, J.5    Hieter, P.6    Boeke, J.D.7
  • 7
    • 33644753863 scopus 로고    scopus 로고
    • Diverse functions of spindle assembly checkpoint genes in Saccharomyces cerevisiae
    • Daniel, J.A., B.E. Keyes, Y.P. Ng, C.O. Freeman, and D.J. Burke. 2006. Diverse functions of spindle assembly checkpoint genes in Saccharomyces cerevisiae. Genetics. 172:53-65. http://dx.doi.org/10.1534/genetics.105.046441
    • (2006) Genetics , vol.172 , pp. 53-65
    • Daniel, J.A.1    Keyes, B.E.2    Ng, Y.P.3    Freeman, C.O.4    Burke, D.J.5
  • 8
    • 80053987011 scopus 로고    scopus 로고
    • Expression of a mutant HSP110 sensitizes colorectal cancer cells to chemotherapy and improves disease prognosis
    • Dorard, C., A. de Thonel, A. Collura, L. Marisa, M. Svrcek, A. Lagrange, G. Jego, K. Wanherdrick, A.L. Joly, O. Buhard, et al. 2011. Expression of a mutant HSP110 sensitizes colorectal cancer cells to chemotherapy and improves disease prognosis. Nat. Med. 17:1283-1289. http://dx.doi.org/10.1038/nm.2457
    • (2011) Nat. Med , vol.17 , pp. 1283-1289
    • Dorard, C.1    de Thonel, A.2    Collura, A.3    Marisa, L.4    Svrcek, M.5    Lagrange, A.6    Jego, G.7    Wanherdrick, K.8    Joly, A.L.9    Buhard, O.10
  • 9
    • 0033625965 scopus 로고    scopus 로고
    • The hsp110 and Grp1 70 stress proteins: Newly recognized relatives of the Hsp70s
    • Easton, D.P., Y. Kaneko, and J.R. Subjeck. 2000. The hsp110 and Grp1 70 stress proteins: Newly recognized relatives of the Hsp70s. Cell Stress Chaperones. 5:276-290. http://dx.doi.org/10.1379/1466-1268(2000) 005<0276:THAGSP>2.0.CO;2
    • (2000) Cell Stress Chaperones , vol.5 , pp. 276-290
    • Easton, D.P.1    Kaneko, Y.2    Subjeck, J.R.3
  • 12
    • 67650681847 scopus 로고    scopus 로고
    • An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: Implications to protein folding pathways in the cell
    • Gong, Y., Y. Kakihara, N. Krogan, J. Greenblatt, A. Emili, Z. Zhang, and W.A. Houry. 2009. An atlas of chaperone-protein interactions in Saccharomyces cerevisiae: Implications to protein folding pathways in the cell. Mol. Syst. Biol. 5:275. http://dx.doi.org/10.1038/msb.2009.26
    • (2009) Mol. Syst. Biol. , vol.5 , pp. 275
    • Gong, Y.1    Kakihara, Y.2    Krogan, N.3    Greenblatt, J.4    Emili, A.5    Zhang, Z.6    Houry, W.A.7
  • 13
    • 0036678220 scopus 로고    scopus 로고
    • beta-Tubulin C354 mutations that severely decrease microtubule dynamics do not prevent nuclear migration in yeast
    • Gupta, M.L. Jr., C.J. Bode, D.A. Thrower, C.G. Pearson, K.A. Suprenant, K.S. Bloom, and R.H. Himes. 2002. beta-Tubulin C354 mutations that severely decrease microtubule dynamics do not prevent nuclear migration in yeast. Mol. Biol. Cell. 13:2919-2932. http://dx.doi.org/10.1091/mbc.E02-01-0003
    • (2002) Mol. Biol. Cell , vol.13 , pp. 2919-2932
    • Gupta Jr., M.L.1    Bode, C.J.2    Thrower, D.A.3    Pearson, C.G.4    Suprenant, K.A.5    Bloom, K.S.6    Himes, R.H.7
  • 14
    • 0035958556 scopus 로고    scopus 로고
    • Molecular analysis of kinetochore-microtubule attachment in budding yeast
    • He, X., D.R. Rines, C.W. Espelin, and P.K. Sorger. 2001. Molecular analysis of kinetochore-microtubule attachment in budding yeast. Cell. 106: 195-206. http://dx.doi.org/10.1016/S0092-8674(01)00438-X
    • (2001) Cell , vol.106 , pp. 195-206
    • He, X.1    Rines, D.R.2    Espelin, C.W.3    Sorger, P.K.4
  • 15
    • 0034677736 scopus 로고    scopus 로고
    • Mitotic motors in Saccharomyces cerevisiae
    • Hildebrandt, E.R., and M.A. Hoyt. 2000. Mitotic motors in Saccharomyces cerevisiae. Biochim. Biophys. Acta. 1496:99-116. http://dx.doi.org/10.1016/S0167-4889(00)00012-4
    • (2000) Biochim. Biophys. Acta , vol.1496 , pp. 99-116
    • Hildebrandt, E.R.1    Hoyt, M.A.2
  • 16
    • 0035196619 scopus 로고    scopus 로고
    • Cell cycle-dependent degradation of the Saccharomyces cerevisiae spindle motor Cin8p requires APC(Cdh1) and a bipartite destruction sequence
    • Hildebrandt, E.R., and M.A. Hoyt. 2001. Cell cycle-dependent degradation of the Saccharomyces cerevisiae spindle motor Cin8p requires APC(Cdh1) and a bipartite destruction sequence. Mol. Biol. Cell. 12:3402-3416.
    • (2001) Mol. Biol. Cell. , vol.12 , pp. 3402-3416
    • Hildebrandt, E.R.1    Hoyt, M.A.2
  • 17
    • 0031951035 scopus 로고    scopus 로고
    • The integral membrane protein snl1p is genetically linked to yeast nuclear pore complex function
    • Ho, A.K., G.A. Raczniak, E.B. Ives, and S.R. Wente. 1998. The integral membrane protein snl1p is genetically linked to yeast nuclear pore complex function. Mol. Biol. Cell. 9:355-373.
    • (1998) Mol. Biol. Cell. , vol.9 , pp. 355-373
    • Ho, A.K.1    Raczniak, G.A.2    Ives, E.B.3    Wente, S.R.4
  • 18
    • 0027181271 scopus 로고
    • Loss of function of Saccharomyces cerevisiae kinesin-related CIN8 and KIP1 is suppressed by KAR3 motor domain mutations
    • Hoyt, M.A., L. He, L. Totis, and W.S. Saunders. 1993. Loss of function of Saccharomyces cerevisiae kinesin-related CIN8 and KIP1 is suppressed by KAR3 motor domain mutations. Genetics. 135:35-44.
    • (1993) Genetics , vol.135 , pp. 35-44
    • Hoyt, M.A.1    He, L.2    Totis, L.3    Saunders, W.S.4
  • 19
    • 34147092780 scopus 로고    scopus 로고
    • Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae
    • Hu, Y., A. Rolfs, B. Bhullar, T.V. Murthy, C. Zhu, M.F. Berger, A.A. Camargo, F. Kelley, S. McCarron, D. Jepson, et al. 2007. Approaching a complete repository of sequence-verified protein-encoding clones for Saccharomyces cerevisiae. Genome Res. 17:536-543. http://dx.doi.org/10.1101/gr.6037607
    • (2007) Genome Res , vol.17 , pp. 536-543
    • Hu, Y.1    Rolfs, A.2    Bhullar, B.3    Murthy, T.V.4    Zhu, C.5    Berger, M.F.6    Camargo, A.A.7    Kelley, F.8    McCarron, S.9    Jepson, D.10
  • 20
    • 22444439361 scopus 로고    scopus 로고
    • The Hsp70 Ssz1 modulates the function of the ribosome-associated J-protein Zuo1
    • Huang, P., M. Gautschi, W. Walter, S. Rospert, and E.A. Craig. 2005. The Hsp70 Ssz1 modulates the function of the ribosome-associated J-protein Zuo1. Nat. Struct. Mol. Biol. 12:497-504. http://dx.doi.org/10.1038/nsmb942
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 497-504
    • Huang, P.1    Gautschi, M.2    Walter, W.3    Rospert, S.4    Craig, E.A.5
  • 22
    • 0037080986 scopus 로고    scopus 로고
    • Four new subunits of the Dam1-Duo1 complex reveal novel functions in sister kinetochore biorientation
    • Janke, C., J. Ortíz, T.U. Tanaka, J. Lechner, and E. Schiebel. 2002. Four new subunits of the Dam1-Duo1 complex reveal novel functions in sister kinetochore biorientation. EMBO J. 21:181-193. http://dx.doi.org/10.1093/emboj/21.1.181
    • (2002) EMBO J , vol.21 , pp. 181-193
    • Janke, C.1    Ortíz, J.2    Tanaka, T.U.3    Lechner, J.4    Schiebel, E.5
  • 23
    • 0036275663 scopus 로고    scopus 로고
    • Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p
    • Kabani, M., J.M. Beckerich, and J.L. Brodsky. 2002. Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p. Mol. Cell. Biol. 22:4677-4689. http://dx.doi.org/10.1128/MCB.22.13.4677-4689.2002
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4677-4689
    • Kabani, M.1    Beckerich, J.M.2    Brodsky, J.L.3
  • 24
    • 77954947810 scopus 로고    scopus 로고
    • The HSP70 chaperone machinery: J proteins as drivers of functional specificity
    • Kampinga, H.H., and E.A. Craig. 2010. The HSP70 chaperone machinery: J proteins as drivers of functional specificity. Nat. Rev. Mol. Cell Biol. 11:579-592. http://dx.doi.org/10.1038/nrm2941
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 579-592
    • Kampinga, H.H.1    Craig, E.A.2
  • 25
    • 34250789235 scopus 로고    scopus 로고
    • Cdc14-regulated midzone assembly controls anaphase B
    • Khmelinskii, A., C. Lawrence, J. Roostalu, and E. Schiebel. 2007. Cdc14-regulated midzone assembly controls anaphase B. J. Cell Biol. 177:981-993. http://dx.doi.org/10.1083/jcb.200702145
    • (2007) J. Cell Biol , vol.177 , pp. 981-993
    • Khmelinskii, A.1    Lawrence, C.2    Roostalu, J.3    Schiebel, E.4
  • 26
    • 68349122630 scopus 로고    scopus 로고
    • Phosphorylation-dependent protein interactions at the spindle midzone mediate cell cycle regulation of spindle elongation
    • Khmelinskii, A., J. Roostalu, H. Roque, C. Antony, and E. Schiebel. 2009. Phosphorylation-dependent protein interactions at the spindle midzone mediate cell cycle regulation of spindle elongation. Dev. Cell. 17:244-256. http://dx.doi.org/10.1016/j.devcel.2009.06.011
    • (2009) Dev. Cell , vol.17 , pp. 244-256
    • Khmelinskii, A.1    Roostalu, J.2    Roque, H.3    Antony, C.4    Schiebel, E.5
  • 27
    • 9744272519 scopus 로고    scopus 로고
    • DNA replication checkpoint prevents precocious chromosome segregation by regulating spindle behavior
    • Krishnan, V., S. Nirantar, K. Crasta, A.Y. Cheng, and U. Surana. 2004. DNA replication checkpoint prevents precocious chromosome segregation by regulating spindle behavior. Mol. Cell. 16:687-700. http://dx.doi.org/10.1016/j.molcel.2004.11.001
    • (2004) Mol. Cell. , vol.16 , pp. 687-700
    • Krishnan, V.1    Nirantar, S.2    Crasta, K.3    Cheng, A.Y.4    Surana, U.5
  • 30
    • 0026013226 scopus 로고
    • A 240 kd multisubunit protein complex, CBF3, is a major component of the budding yeast centromere
    • Lechner, J., and J. Carbon. 1991. A 240 kd multisubunit protein complex, CBF3, is a major component of the budding yeast centromere. Cell. 64:717-725. http://dx.doi.org/10.1016/0092-8674(91)90501-O
    • (1991) Cell , vol.64 , pp. 717-725
    • Lechner, J.1    Carbon, J.2
  • 31
    • 57149094026 scopus 로고    scopus 로고
    • The coordination of centromere replication, spindle formation, and kinetochore-microtubule interaction in budding yeast
    • Liu, H., F. Liang, F. Jin, and Y. Wang. 2008. The coordination of centromere replication, spindle formation, and kinetochore-microtubule interaction in budding yeast. PLoS Genet. 4:e1000262. http://dx.doi.org/10.1371/journal.pgen.1000262
    • (2008) PLoS Genet , vol.4
    • Liu, H.1    Liang, F.2    Jin, F.3    Wang, Y.4
  • 32
    • 0029764792 scopus 로고    scopus 로고
    • Members of the Hsp70 family of proteins in the cell wall of Saccharomyces cerevisiae
    • López-Ribot, J.L., and W.L. Chaffin. 1996. Members of the Hsp70 family of proteins in the cell wall of Saccharomyces cerevisiae. J. Bacteriol. 178:4724-4726.
    • (1996) J. Bacteriol , vol.178 , pp. 4724-4726
    • López-Ribot, J.L.1    Chaffin, W.L.2
  • 33
    • 34547752349 scopus 로고    scopus 로고
    • Spc24 and Stu2 promote spindle integrity when DNA replication is stalled
    • Ma, L., J. McQueen, L. Cuschieri, J. Vogel, and V. Measday. 2007. Spc24 and Stu2 promote spindle integrity when DNA replication is stalled. Mol. Biol. Cell. 18:2805-2816. http://dx.doi.org/10.1091/mbc.E06-09-0882
    • (2007) Mol. Biol. Cell , vol.18 , pp. 2805-2816
    • Ma, L.1    McQueen, J.2    Cuschieri, L.3    Vogel, J.4    Measday, V.5
  • 35
    • 0032491521 scopus 로고    scopus 로고
    • Loss of Hsp70-Hsp40 chaperone activity causes abnormal nuclear distribution and aberrant microtubule formation in M-phase of Saccharomyces cerevisiae
    • Oka, M., M. Nakai, T. Endo, C.R. Lim, Y. Kimata, and K. Kohno. 1998. Loss of Hsp70-Hsp40 chaperone activity causes abnormal nuclear distribution and aberrant microtubule formation in M-phase of Saccharomyces cerevisiae. J. Biol. Chem. 273:29727-29737. http://dx.doi.org/10.1074/jbc.273.45.29727
    • (1998) J. Biol. Chem , vol.273 , pp. 29727-29737
    • Oka, M.1    Nakai, M.2    Endo, T.3    Lim, C.R.4    Kimata, Y.5    Kohno, K.6
  • 36
    • 0036284778 scopus 로고    scopus 로고
    • The anaphase-promoting complex: Proteolysis in mitosis and beyond
    • Peters, J.M. 2002. The anaphase-promoting complex: Proteolysis in mitosis and beyond. Mol. Cell. 9:931-943. http://dx.doi.org/10.1016/S1097-2765(02)00540-3
    • (2002) Mol. Cell. , vol.9 , pp. 931-943
    • Peters, J.M.1
  • 37
    • 0032528301 scopus 로고    scopus 로고
    • The molecular chaperone Ssb from Saccharomyces cerevisiae is a component of the ribosomenascent chain complex
    • Pfund, C., N. Lopez-Hoyo, T. Ziegelhoffer, B.A. Schilke, P. Lopez-Buesa, W.A. Walter, M. Wiedmann, and E.A. Craig. 1998. The molecular chaperone Ssb from Saccharomyces cerevisiae is a component of the ribosomenascent chain complex. EMBO J. 17:3981-3989. http://dx.doi.org/10.1093/emboj/17.14.3981
    • (1998) EMBO J. , vol.17 , pp. 3981-3989
    • Pfund, C.1    Lopez-Hoyo, N.2    Ziegelhoffer, T.3    Schilke, B.A.4    Lopez-Buesa, P.5    Walter, W.A.6    Wiedmann, M.7    Craig, E.A.8
  • 38
    • 44649110104 scopus 로고    scopus 로고
    • Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding
    • Polier, S., Z. Dragovic, F.U. Hartl, and A. Bracher. 2008. Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding. Cell. 133:1068-1079. http://dx.doi.org/10.1016/j.cell.2008.05.022
    • (2008) Cell , vol.133 , pp. 1068-1079
    • Polier, S.1    Dragovic, Z.2    Hartl, F.U.3    Bracher, A.4
  • 39
    • 63349085550 scopus 로고    scopus 로고
    • Up-to-date catalogues of yeast protein complexes
    • Pu, S., J. Wong, B. Turner, E. Cho, and S.J. Wodak. 2009. Up-to-date catalogues of yeast protein complexes. Nucleic Acids Res. 37:825-831. http://dx.doi.org/10.1093/nar/gkn1005
    • (2009) Nucleic Acids Res , vol.37 , pp. 825-831
    • Pu, S.1    Wong, J.2    Turner, B.3    Cho, E.4    Wodak, S.J.5
  • 40
    • 0034841844 scopus 로고    scopus 로고
    • The tandem affinity purification (TAP) method: A general procedure of protein complex purification
    • Puig, O., F. Caspary, G. Rigaut, B. Rutz, E. Bouveret, E. Bragado-Nilsson, M. Wilm, and B. Séraphin. 2001. The tandem affinity purification (TAP) method: A general procedure of protein complex purification. Methods. 24:218-229. http://dx.doi.org/10.1006/meth.2001.1183
    • (2001) Methods , vol.24 , pp. 218-229
    • Puig, O.1    Caspary, F.2    Rigaut, G.3    Rutz, B.4    Bouveret, E.5    Bragado-Nilsson, E.6    Wilm, M.7    Séraphin, B.8
  • 41
    • 79953285218 scopus 로고    scopus 로고
    • Directional switching of the kinesin Cin8 through motor coupling
    • Roostalu, J., C. Hentrich, P. Bieling, I.A. Telley, E. Schiebel, and T. Surrey. 2011. Directional switching of the kinesin Cin8 through motor coupling. Science. 332:94-99. http://dx.doi.org/10.1126/science.1199945
    • (2011) Science , vol.332 , pp. 94-99
    • Roostalu, J.1    Hentrich, C.2    Bieling, P.3    Telley, I.A.4    Schiebel, E.5    Surrey, T.6
  • 42
    • 46149116088 scopus 로고    scopus 로고
    • Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities
    • Sadlish, H., H. Rampelt, J. Shorter, R.D. Wegrzyn, C. Andréasson, S. Lindquist, and B. Bukau. 2008. Hsp110 chaperones regulate prion formation and propagation in S. cerevisiae by two discrete activities. PLoS ONE. 3:e1763. http://dx.doi.org/10.1371/journal.pone.0001763
    • (2008) PLoS ONE , vol.3
    • Sadlish, H.1    Rampelt, H.2    Shorter, J.3    Wegrzyn, R.D.4    Andréasson, C.5    Lindquist, S.6    Bukau, B.7
  • 43
    • 10844237288 scopus 로고    scopus 로고
    • Uncovering novel cell cycle players through the inactivation of securin in budding yeast
    • Sarin, S., K.E. Ross, L. Boucher, Y. Green, M. Tyers, and O. Cohen-Fix. 2004. Uncovering novel cell cycle players through the inactivation of securin in budding yeast. Genetics. 168:1763-1771. http://dx.doi.org/10.1534/genetics.104.029033
    • (2004) Genetics , vol.168 , pp. 1763-1771
    • Sarin, S.1    Ross, K.E.2    Boucher, L.3    Green, Y.4    Tyers, M.5    Cohen-Fix, O.6
  • 44
    • 0030933383 scopus 로고    scopus 로고
    • The Saccharomyces cerevisiae kinesin-related motor Kar3p acts at preanaphase spindle poles to limit the number and length of cytoplasmic microtubules
    • Saunders, W., D. Hornack, V. Lengyel, and C.C. Deng. 1997a. The Saccharomyces cerevisiae kinesin-related motor Kar3p acts at preanaphase spindle poles to limit the number and length of cytoplasmic microtubules. J. Cell Biol. 137:417-431. http://dx.doi.org/10.1083/jcb.137.2.417
    • (1997) J. Cell Biol , vol.137 , pp. 417-431
    • Saunders, W.1    Hornack, D.2    Lengyel, V.3    Deng, C.C.4
  • 45
    • 0030974461 scopus 로고    scopus 로고
    • Mitotic spindle function in Saccharomyces cerevisiae requires a balance between different types of kinesin-related motors
    • Saunders, W., V. Lengyel, and M.A. Hoyt. 1997b. Mitotic spindle function in Saccharomyces cerevisiae requires a balance between different types of kinesin-related motors. Mol. Biol. Cell. 8:1025-1033.
    • (1997) Mol. Biol. Cell. , vol.8 , pp. 1025-1033
    • Saunders, W.1    Lengyel, V.2    Hoyt, M.A.3
  • 46
    • 0026638269 scopus 로고
    • Kinesin-related proteins required for structural integrity of the mitotic spindle
    • Saunders, W.S., and M.A. Hoyt. 1992. Kinesin-related proteins required for structural integrity of the mitotic spindle. Cell. 70:451-458. http://dx.doi.org/10.1016/0092-8674(92)90169-D
    • (1992) Cell , vol.70 , pp. 451-458
    • Saunders, W.S.1    Hoyt, M.A.2
  • 47
    • 0034646511 scopus 로고    scopus 로고
    • Structure of TPR domainpeptide complexes: Critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
    • Scheufler, C., A. Brinker, G. Bourenkov, S. Pegoraro, L. Moroder, H. Bartunik, F.U. Hartl, and I. Moarefi. 2000. Structure of TPR domainpeptide complexes: Critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine. Cell. 101:199-210. http://dx.doi.org/10.1016/S0092-8674(00)80830-2
    • (2000) Cell , vol.101 , pp. 199-210
    • Scheufler, C.1    Brinker, A.2    Bourenkov, G.3    Pegoraro, S.4    Moroder, L.5    Bartunik, H.6    Hartl, F.U.7    Moarefi, I.8
  • 49
    • 2542435778 scopus 로고    scopus 로고
    • The function of the yeast molecular chaperone Sse1 is mechanistically distinct from the closely related hsp70 family
    • Shaner, L., A. Trott, J.L. Goeckeler, J.L. Brodsky, and K.A. Morano. 2004. The function of the yeast molecular chaperone Sse1 is mechanistically distinct from the closely related hsp70 family. J. Biol. Chem. 279:21992-22001. http://dx.doi.org/10.1074/jbc.M313739200
    • (2004) J. Biol. Chem. , vol.279 , pp. 21992-22001
    • Shaner, L.1    Trott, A.2    Goeckeler, J.L.3    Brodsky, J.L.4    Morano, K.A.5
  • 50
    • 29244467709 scopus 로고    scopus 로고
    • The yeast Hsp110 Sse1 functionally interacts with the Hsp70 chaperones Ssa and Ssb
    • Shaner, L., H. Wegele, J. Buchner, and K.A. Morano. 2005. The yeast Hsp110 Sse1 functionally interacts with the Hsp70 chaperones Ssa and Ssb. J. Biol. Chem. 280:41262-41269. http://dx.doi.org/10.1074/jbc.M503614200
    • (2005) J. Biol. Chem. , vol.280 , pp. 41262-41269
    • Shaner, L.1    Wegele, H.2    Buchner, J.3    Morano, K.A.4
  • 51
    • 0032473568 scopus 로고    scopus 로고
    • The Polo-like kinase Cdc5p and the WD-repeat protein Cdc20p/fizzy are regulators and substrates of the anaphase promoting complex in Saccharomyces cerevisiae
    • Shirayama, M., W. Zachariae, R. Ciosk, and K. Nasmyth. 1998. The Polo-like kinase Cdc5p and the WD-repeat protein Cdc20p/fizzy are regulators and substrates of the anaphase promoting complex in Saccharomyces cerevisiae. EMBO J. 17:1336-1349. http://dx.doi.org/10.1093/emboj/17.5.1336
    • (1998) EMBO J. , vol.17 , pp. 1336-1349
    • Shirayama, M.1    Zachariae, W.2    Ciosk, R.3    Nasmyth, K.4
  • 52
    • 0037031902 scopus 로고    scopus 로고
    • Prediction of novel Bag-1 homologs based on structure/function analysis identifies Snl1p as an Hsp70 co-chaperone in Saccharomyces cerevisiae
    • Sondermann, H., A.K. Ho, L.L. Listenberger, K. Siegers, I. Moarefi, S.R. Wente, F.U. Hartl, and J.C. Young. 2002. Prediction of novel Bag-1 homologs based on structure/function analysis identifies Snl1p as an Hsp70 co-chaperone in Saccharomyces cerevisiae. J. Biol. Chem. 277:33220-33227. http://dx.doi.org/10.1074/jbc.M204624200
    • (2002) J. Biol. Chem. , vol.277 , pp. 33220-33227
    • Sondermann, H.1    Ho, A.K.2    Listenberger, L.L.3    Siegers, K.4    Moarefi, I.5    Wente, S.R.6    Hartl, F.U.7    Young, J.C.8
  • 54
    • 0034069495 scopus 로고    scopus 로고
    • Gene ontology: Tool for the unification of biology
    • The Gene Ontology Consortium
    • The Gene Ontology Consortium. 2000. Gene ontology: Tool for the unification of biology. Nat. Genet. 25:25-29. http://dx.doi.org/10.1038/75556
    • (2000) Nat. Genet , vol.25 , pp. 25-29
  • 55
    • 0034388026 scopus 로고    scopus 로고
    • LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum
    • Tyson, J.R., and C.J. Stirling. 2000. LHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulum. EMBO J. 19:6440-6452. http://dx.doi.org/10.1093/emboj/19.23.6440
    • (2000) EMBO J , vol.19 , pp. 6440-6452
    • Tyson, J.R.1    Stirling, C.J.2
  • 56
    • 33644894727 scopus 로고    scopus 로고
    • Analysis of kinesin motor function at budding yeast kinetochores
    • Tytell, J.D., and P.K. Sorger. 2006. Analysis of kinesin motor function at budding yeast kinetochores. J. Cell Biol. 172:861-874. http://dx.doi.org/10.1083/jcb.200509101
    • (2006) J. Cell Biol , vol.172 , pp. 861-874
    • Tytell, J.D.1    Sorger, P.K.2
  • 57
    • 3843078831 scopus 로고    scopus 로고
    • Remodelling the Rad9 checkpoint complex: preparing Rad53 for action
    • van den Bosch, M., and N.F. Lowndes. 2004. Remodelling the Rad9 checkpoint complex: preparing Rad53 for action. Cell Cycle. 3:119-122.
    • (2004) Cell Cycle , vol.3 , pp. 119-122
    • van den Bosch, M.1    Lowndes, N.F.2
  • 58
    • 0037830586 scopus 로고    scopus 로고
    • Sti1 is a novel activator of the Ssa proteins
    • Wegele, H., M. Haslbeck, J. Reinstein, and J. Buchner. 2003. Sti1 is a novel activator of the Ssa proteins. J. Biol. Chem. 278:25970-25976. http://dx.doi.org/10.1074/jbc.M301548200
    • (2003) J. Biol. Chem , vol.278 , pp. 25970-25976
    • Wegele, H.1    Haslbeck, M.2    Reinstein, J.3    Buchner, J.4
  • 59
    • 0031750102 scopus 로고    scopus 로고
    • Analysis of the Saccharomyces spindle pole by matrix-assisted laser desorption/ionization (MALDI) mass spectrometry
    • Wigge, P.A., O.N. Jensen, S. Holmes, S. Souès, M. Mann, and J.V. Kilmartin. 1998. Analysis of the Saccharomyces spindle pole by matrix-assisted laser desorption/ionization (MALDI) mass spectrometry. J. Cell Biol. 141:967-977. http://dx.doi.org/10.1083/jcb.141.4.967
    • (1998) J. Cell Biol , vol.141 , pp. 967-977
    • Wigge, P.A.1    Jensen, O.N.2    Holmes, S.3    Souès, S.4    Mann, M.5    Kilmartin, J.V.6
  • 60
    • 29244432181 scopus 로고    scopus 로고
    • Hsp110 cooperates with different cytosolic HSP70 systems in a pathway for de novo folding
    • Yam, A.Y., V. Albanèse, H.T. Lin, and J. Frydman. 2005. Hsp110 cooperates with different cytosolic HSP70 systems in a pathway for de novo folding. J. Biol. Chem. 280:41252-41261. http://dx.doi.org/10.1074/jbc.M503615200
    • (2005) J. Biol. Chem , vol.280 , pp. 41252-41261
    • Yam, A.Y.1    Albanèse, V.2    Lin, H.T.3    Frydman, J.4
  • 61
    • 77950600645 scopus 로고    scopus 로고
    • Mechanisms of the Hsp70 chaperone system
    • Young, J.C. 2010. Mechanisms of the Hsp70 chaperone system. Biochem. Cell Biol. 88:291-300. http://dx.doi.org/10.1139/O09-175
    • (2010) Biochem. Cell Biol , vol.88 , pp. 291-300
    • Young, J.C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.