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Volumn 175, Issue 2, 2007, Pages 621-630

Importance of the Hsp70 ATPase domain in yeast prion propagation

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; CHAPERONE; HEAT SHOCK PROTEIN 70; PRION PROTEIN; PROTEIN SSA1P; PROTEIN SSA2P; UNCLASSIFIED DRUG; FUNGAL PROTEIN; HEAT SHOCK PROTEIN; HSP104 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN; SSA1 PROTEIN, S CEREVISIAE; SSA2 PROTEIN, FUNGAL; URE2 PROTEIN, S CEREVISIAE;

EID: 34247899009     PISSN: 00166731     EISSN: 00166731     Source Type: Journal    
DOI: 10.1534/genetics.106.066019     Document Type: Article
Times cited : (34)

References (56)
  • 1
    • 0016669719 scopus 로고
    • Genetical aspects of [URE3], a non-mitochondrial, cytoplasmically inherited mutation in yeast
    • AIGLE, M., and F. LACROUTE, 1975 Genetical aspects of [URE3], a non-mitochondrial, cytoplasmically inherited mutation in yeast. Mol. Gen. Genet. 136: 327-335.
    • (1975) Mol. Gen. Genet , vol.136 , pp. 327-335
    • AIGLE, M.1    LACROUTE, F.2
  • 2
    • 17444417025 scopus 로고    scopus 로고
    • Hsp70 chaperones as modulators of prion life cycle: Novel effects of Ssa and Ssb on the Saccharomyces cerevisiae prion [PSI1]
    • ALLEN, K. D., R. D. WEGRZYN, T. A. CHERNOVA, S. MULLER, G. P. NEWNAM et al., 2005 Hsp70 chaperones as modulators of prion life cycle: novel effects of Ssa and Ssb on the Saccharomyces cerevisiae prion [PSI1]. Genetics 169: 1227-1242.
    • (2005) Genetics , vol.169 , pp. 1227-1242
    • ALLEN, K.D.1    WEGRZYN, R.D.2    CHERNOVA, T.A.3    MULLER, S.4    NEWNAM, G.P.5
  • 3
    • 10744225913 scopus 로고    scopus 로고
    • Isolation of drugs active against mammalian prions using a yeast-based screening assay
    • BACH, S., N. TALAREK, T. ANDRIEU, J. M. VIERFOND, Y. METTEY et al., 2003 Isolation of drugs active against mammalian prions using a yeast-based screening assay. Nat. Biotechnol. 21: 1075-1081.
    • (2003) Nat. Biotechnol , vol.21 , pp. 1075-1081
    • BACH, S.1    TALAREK, N.2    ANDRIEU, T.3    VIERFOND, J.M.4    METTEY, Y.5
  • 4
    • 0029052468 scopus 로고
    • Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]
    • CHERNOFF, Y. O., S. L. LINDQUIST, B. ONO, S. G. INGE-VECHTOMOV and S. W. LIEBMAN, 1995 Role of the chaperone protein Hsp104 in propagation of the yeast prion-like factor [psi+]. Science 268: 880-884.
    • (1995) Science , vol.268 , pp. 880-884
    • CHERNOFF, Y.O.1    LINDQUIST, S.L.2    ONO, B.3    INGE-VECHTOMOV, S.G.4    LIEBMAN, S.W.5
  • 5
    • 0034916581 scopus 로고    scopus 로고
    • Prion diseases of humans and animals: Their causes and molecular basis
    • COLLINGE, J., 2001 Prion diseases of humans and animals: their causes and molecular basis. Annu. Rev. Neurosci. 24: 519-550.
    • (2001) Annu. Rev. Neurosci , vol.24 , pp. 519-550
    • COLLINGE, J.1
  • 6
    • 0030885650 scopus 로고    scopus 로고
    • The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog
    • COUSTOU, V., C. DELEU, S. SAUPE and J. BEGUERET, 1997 The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog. Proc. Natl. Acad. Sci. USA 94: 9773-9778.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 9773-9778
    • COUSTOU, V.1    DELEU, C.2    SAUPE, S.3    BEGUERET, J.4
  • 7
    • 84966138908 scopus 로고
    • PSI+], acytoplasmic suppressor of super-suppressors in yeast
    • COX, B. S., 1965 [PSI+], acytoplasmic suppressor of super-suppressors in yeast. Heredity 20: 505-521.
    • (1965) Heredity , vol.20 , pp. 505-521
    • COX, B.S.1
  • 8
    • 0026739395 scopus 로고
    • Regulation of Hsp70 function by a eukaryotic DnaJ homolog
    • CYR, D. M., X. LU and M. G. DOUGLAS, 1992 Regulation of Hsp70 function by a eukaryotic DnaJ homolog. J. Biol. Chem. 267: 20927-20931.
    • (1992) J. Biol. Chem , vol.267 , pp. 20927-20931
    • CYR, D.M.1    LU, X.2    DOUGLAS, M.G.3
  • 9
    • 0030833388 scopus 로고    scopus 로고
    • Genetic and environmental factors affecting the de novo appearance of the [PSI1] prion in Saccharomyces cerevisiae
    • DERKATCH, I. L., M. E. BRADLEY, P. ZHOU, Y. O. CHERNOFF and S. W. LIEBMAN, 1997 Genetic and environmental factors affecting the de novo appearance of the [PSI1] prion in Saccharomyces cerevisiae. Genetics 147: 507-519.
    • (1997) Genetics , vol.147 , pp. 507-519
    • DERKATCH, I.L.1    BRADLEY, M.E.2    ZHOU, P.3    CHERNOFF, Y.O.4    LIEBMAN, S.W.5
  • 10
    • 0035958585 scopus 로고    scopus 로고
    • Prions affect the appearance of other prions: The story of [PIN(+)]
    • DERKATCH, I. L., M. E. BRADLEY, J. Y. HONG and S. W. LIEBMAN, 2001 Prions affect the appearance of other prions: the story of [PIN(+)]. Cell 106: 171-182.
    • (2001) Cell , vol.106 , pp. 171-182
    • DERKATCH, I.L.1    BRADLEY, M.E.2    HONG, J.Y.3    LIEBMAN, S.W.4
  • 11
    • 33745762927 scopus 로고    scopus 로고
    • Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s
    • DRAGOVIC, Z., S. A. BROADLEY, Y. SHOMURA, A. BRACHER and F. U. HARTL, 2006 Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s. EMBO J. 25: 2519-2528.
    • (2006) EMBO J , vol.25 , pp. 2519-2528
    • DRAGOVIC, Z.1    BROADLEY, S.A.2    SHOMURA, Y.3    BRACHER, A.4    HARTL, F.U.5
  • 12
    • 0034601056 scopus 로고    scopus 로고
    • The yeast prion [URE3] can be greatly induced by a functional mutated URE2 allele
    • FERNANDEZ-BELLOT, E., E. GUILLEMET and C. CULLIN, 2000 The yeast prion [URE3] can be greatly induced by a functional mutated URE2 allele. EMBO J. 19: 3215-3222.
    • (2000) EMBO J , vol.19 , pp. 3215-3222
    • FERNANDEZ-BELLOT, E.1    GUILLEMET, E.2    CULLIN, C.3
  • 13
    • 23644442282 scopus 로고    scopus 로고
    • Heat shock prevents alpha-synuclein-induced apoptosis in a yeast model of Parkinson's disease
    • FLOWER, T. R., L. S. CHESNOKOVA, C. A. FROELICH, C. DIXON and S. N. WITT, 2005 Heat shock prevents alpha-synuclein-induced apoptosis in a yeast model of Parkinson's disease. J. Mol. Biol. 351: 1081-1100.
    • (2005) J. Mol. Biol , vol.351 , pp. 1081-1100
    • FLOWER, T.R.1    CHESNOKOVA, L.S.2    FROELICH, C.A.3    DIXON, C.4    WITT, S.N.5
  • 14
    • 0242522907 scopus 로고    scopus 로고
    • The budding yeast Rad9 checkpoint complex: chaperone proteins are required for its function. EMBO Rep
    • GILBERT, C. S., M. VAN DEN BOSCH, C. M. GREEN, J. E. VIALARD, M. GRENON et al., 2003 The budding yeast Rad9 checkpoint complex: chaperone proteins are required for its function. EMBO Rep. 4: 953-958.
    • (2003) , vol.4 , pp. 953-958
    • GILBERT, C.S.1    VAN DEN BOSCH, M.2    GREEN, C.M.3    VIALARD, J.E.4    GRENON, M.5
  • 15
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins
    • GLOVER, J. R., and S. LINDQUIST, 1998 Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94: 73-82.
    • (1998) Cell , vol.94 , pp. 73-82
    • GLOVER, J.R.1    LINDQUIST, S.2
  • 16
    • 20744441099 scopus 로고    scopus 로고
    • Modulation of prion-dependent polyglutamine aggregation and toxicity by chaperone proteins in the yeast model
    • GOKHALE, K. C., G. P. NEWNAM, M. Y. SHERMAN and Y. O. CHERNOFF, 2005 Modulation of prion-dependent polyglutamine aggregation and toxicity by chaperone proteins in the yeast model. J. Biol. Chem. 280: 22809-22818.
    • (2005) J. Biol. Chem , vol.280 , pp. 22809-22818
    • GOKHALE, K.C.1    NEWNAM, G.P.2    SHERMAN, M.Y.3    CHERNOFF, Y.O.4
  • 17
    • 2542453964 scopus 로고    scopus 로고
    • Cns1 is an activator of the Ssa1 ATPase activity
    • HAINZL, O., H. WEGELE, K. RICHTER and J. BUCHNER, 2004 Cns1 is an activator of the Ssa1 ATPase activity. J. Biol. Chem. 279: 23267-23273.
    • (2004) J. Biol. Chem , vol.279 , pp. 23267-23273
    • HAINZL, O.1    WEGELE, H.2    RICHTER, K.3    BUCHNER, J.4
  • 18
    • 10044227566 scopus 로고    scopus 로고
    • Hsp104 binds to yeast Sup35 prion fiber but needs other factor(s) to sever it
    • INOUE, Y., H. TAGUCHI, A. KISHIMOTO and M. YOSHIDA, 2004 Hsp104 binds to yeast Sup35 prion fiber but needs other factor(s) to sever it. J. Biol. Chem. 279: 52319-52323.
    • (2004) J. Biol. Chem , vol.279 , pp. 52319-52323
    • INOUE, Y.1    TAGUCHI, H.2    KISHIMOTO, A.3    YOSHIDA, M.4
  • 19
    • 0031016469 scopus 로고    scopus 로고
    • JAMES, P., C. PFUND and E. A. CRAIG, 1997 Functional specificity among Hsp70 molecular chaperones. Science 275: 387-389.
    • JAMES, P., C. PFUND and E. A. CRAIG, 1997 Functional specificity among Hsp70 molecular chaperones. Science 275: 387-389.
  • 20
    • 27944436648 scopus 로고    scopus 로고
    • Structural basis of interdomain communication in the Hsc70 chaperone
    • JIANG, J., K. PRASAD, E.M. LAFER and R. SOUSA, 2005 Structural basis of interdomain communication in the Hsc70 chaperone. Mol. Cell 20: 513-524.
    • (2005) Mol. Cell , vol.20 , pp. 513-524
    • JIANG, J.1    PRASAD, K.2    LAFER, E.M.3    SOUSA, R.4
  • 22
    • 24644439320 scopus 로고    scopus 로고
    • Chaperonin prions: The cellular machinery for propagating an infectious protein?
    • JONES, G. W., and M. F. TUITE, 2005 Chaperonin prions: The cellular machinery for propagating an infectious protein? BioEssays 27: 823-832.
    • (2005) BioEssays , vol.27 , pp. 823-832
    • JONES, G.W.1    TUITE, M.F.2
  • 23
    • 1942518319 scopus 로고    scopus 로고
    • Propagation of Saccharomyces cerevisiae [PSI1] prion is impaired by factors that regulate Hsp70 substrate binding
    • JONES, G., Y. SONG, S. CHUNG and D. C. MASISON, 2004 Propagation of Saccharomyces cerevisiae [PSI1] prion is impaired by factors that regulate Hsp70 substrate binding. Mol. Cell. Biol. 24: 3928-3937.
    • (2004) Mol. Cell. Biol , vol.24 , pp. 3928-3937
    • JONES, G.1    SONG, Y.2    CHUNG, S.3    MASISON, D.C.4
  • 25
    • 0036275663 scopus 로고    scopus 로고
    • Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p
    • KABANI, M., J. M. BECKERICH and J. L. BRODSKY, 2002a Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p. Mol. Cell. Biol. 22: 4677-4689.
    • (2002) Mol. Cell. Biol , vol.22 , pp. 4677-4689
    • KABANI, M.1    BECKERICH, J.M.2    BRODSKY, J.L.3
  • 26
    • 0037032470 scopus 로고    scopus 로고
    • HspBP1, a homologue of the yeast Fes1 and Sls1 proteins, is an Hsc70 nucleotide exchange factor
    • KABANI, M., C. MCLELLAN, D. A. RAYNES, V. GUERRIERO and J. L. BRODSKY, 2002b HspBP1, a homologue of the yeast Fes1 and Sls1 proteins, is an Hsc70 nucleotide exchange factor. FEBS Lett. 531: 339-342.
    • (2002) FEBS Lett , vol.531 , pp. 339-342
    • KABANI, M.1    MCLELLAN, C.2    RAYNES, D.A.3    GUERRIERO, V.4    BRODSKY, J.L.5
  • 27
    • 0037189549 scopus 로고    scopus 로고
    • Increased expression of Hsp40 chaperones, transcripional factors, and ribosomal protein Rpp0 can cure yeast prions
    • KRYNDUSHKIN, D. S., V. N. SMIRNOV, M. D. TER-AVANESYAN and V. V. KUSHNIROV, 2002 Increased expression of Hsp40 chaperones, transcripional factors, and ribosomal protein Rpp0 can cure yeast prions. J. Biol. Chem. 277: 23702-23708.
    • (2002) J. Biol. Chem , vol.277 , pp. 23702-23708
    • KRYNDUSHKIN, D.S.1    SMIRNOV, V.N.2    TER-AVANESYAN, M.D.3    KUSHNIROV, V.V.4
  • 28
    • 33644555537 scopus 로고    scopus 로고
    • Molecular chaperones and the assembly of the prion Sup35p, an in vitro study
    • KRZEWSKA, J., and R. MELKI, 2006 Molecular chaperones and the assembly of the prion Sup35p, an in vitro study. EMBO J. 25: 822-833.
    • (2006) EMBO J , vol.25 , pp. 822-833
    • KRZEWSKA, J.1    MELKI, R.2
  • 32
    • 0034462603 scopus 로고    scopus 로고
    • URE3] prion propagation in Saccharomyces cerevisiae: Requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p
    • MORIYAMA, H., H. K. EDSKES and R. B. WICKNER, 2000 [URE3] prion propagation in Saccharomyces cerevisiae: requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p. Mol. Cell. Biol. 20: 8916-8922.
    • (2000) Mol. Cell. Biol , vol.20 , pp. 8916-8922
    • MORIYAMA, H.1    EDSKES, H.K.2    WICKNER, R.B.3
  • 33
    • 0032951475 scopus 로고    scopus 로고
    • Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing
    • NEWNAM, G. P., R. D. WEGRZYN, S. L. LINDQUIST and Y. O. CHERNOFF, 1999 Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing. Mol. Cell. Biol. 19: 1325-1333.
    • (1999) Mol. Cell. Biol , vol.19 , pp. 1325-1333
    • NEWNAM, G.P.1    WEGRZYN, R.D.2    LINDQUIST, S.L.3    CHERNOFF, Y.O.4
  • 34
    • 0029780647 scopus 로고    scopus 로고
    • Support for the prion hypothesis for inheritance of a phenotypic trait in yeast
    • PATINO, M. M., J. J. LIU, J. R. GLOVER and S. LINDQUIST, 1996 Support for the prion hypothesis for inheritance of a phenotypic trait in yeast. Science 273: 622-626.
    • (1996) Science , vol.273 , pp. 622-626
    • PATINO, M.M.1    LIU, J.J.2    GLOVER, J.R.3    LINDQUIST, S.4
  • 35
    • 0030907757 scopus 로고    scopus 로고
    • Interaction between yeast Sup45p (eRF1) and Sup35p (eRF3) polypeptide chain release factors: Implications for prion-dependent regulation
    • PAUSHKIN, S. V., V. V. KUSHNIROV, V. N. SMIRNOV and M. D. TER-AVANESYAN, 1997 Interaction between yeast Sup45p (eRF1) and Sup35p (eRF3) polypeptide chain release factors: implications for prion-dependent regulation. Mol. Cell. Biol. 17: 2798-2805.
    • (1997) Mol. Cell. Biol , vol.17 , pp. 2798-2805
    • PAUSHKIN, S.V.1    KUSHNIROV, V.V.2    SMIRNOV, V.N.3    TER-AVANESYAN, M.D.4
  • 36
    • 0020321767 scopus 로고
    • Novel proteinaceous infectious particles cause scrapie
    • PRUSINER, S. B., 1982 Novel proteinaceous infectious particles cause scrapie. Science 216: 136-144.
    • (1982) Science , vol.216 , pp. 136-144
    • PRUSINER, S.B.1
  • 37
    • 33745749328 scopus 로고    scopus 로고
    • Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor
    • RAVIOL, H., H. SADLISH, F. RODRIGUEZ, M. P. MAYER and B. BUKAU, 2006 Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor. EMBO J. 25: 2510-2518.
    • (2006) EMBO J , vol.25 , pp. 2510-2518
    • RAVIOL, H.1    SADLISH, H.2    RODRIGUEZ, F.3    MAYER, M.P.4    BUKAU, B.5
  • 38
    • 18144374138 scopus 로고    scopus 로고
    • NMR investigations of allosteric processes in a two-domain Thermus thermophilus Hsp70 molecular chaperone
    • REVINGTON, M., Y. ZHANG, G. N. YIP, A. V. KUROCHKIN and E. R. ZUIDERWEG, 2005 NMR investigations of allosteric processes in a two-domain Thermus thermophilus Hsp70 molecular chaperone. J. Mol. Biol. 349: 163-183.
    • (2005) J. Mol. Biol , vol.349 , pp. 163-183
    • REVINGTON, M.1    ZHANG, Y.2    YIP, G.N.3    KUROCHKIN, A.V.4    ZUIDERWEG, E.R.5
  • 39
    • 1242296312 scopus 로고    scopus 로고
    • URE3] prion propagation is abolished by a mutation of the primary cytosolic Hsp70 of budding yeast
    • ROBERTS, B. T., H. MORIYAMA and R. B. WICKNER, 2004 [URE3] prion propagation is abolished by a mutation of the primary cytosolic Hsp70 of budding yeast. Yeast 21: 107-117.
    • (2004) Yeast , vol.21 , pp. 107-117
    • ROBERTS, B.T.1    MORIYAMA, H.2    WICKNER, R.B.3
  • 40
    • 24644467295 scopus 로고    scopus 로고
    • Prion protein remodelling confers an immediate phenotypic switch
    • SATPUTE-KRISHNAN, P., and T. R. SERIO, 2005 Prion protein remodelling confers an immediate phenotypic switch. Nature 437: 262-265.
    • (2005) Nature , vol.437 , pp. 262-265
    • SATPUTE-KRISHNAN, P.1    SERIO, T.R.2
  • 41
    • 0023811994 scopus 로고
    • Isolation and characterization of conditional-lethal mutations in the TUB1 alphatubulin gene of the yeast Saccharomyces cerevisiae
    • SCHATZ, P. J., F. SOLOMON and D. BOTSTEIN, 1988 Isolation and characterization of conditional-lethal mutations in the TUB1 alphatubulin gene of the yeast Saccharomyces cerevisiae. Genetics 120: 681-695.
    • (1988) Genetics , vol.120 , pp. 681-695
    • SCHATZ, P.J.1    SOLOMON, F.2    BOTSTEIN, D.3
  • 42
    • 0036096777 scopus 로고    scopus 로고
    • Antagonistic interactions between yeast [PSI()] and [URE3] prions and curing of [URE3] by Hsp70 protein chaperone Ssa1p but not by Ssa2p
    • SCHWIMMER, C., and D. C. MASISON, 2002 Antagonistic interactions between yeast [PSI()] and [URE3] prions and curing of [URE3] by Hsp70 protein chaperone Ssa1p but not by Ssa2p. Mol. Cell. Biol. 22: 3590-3598.
    • (2002) Mol. Cell. Biol , vol.22 , pp. 3590-3598
    • SCHWIMMER, C.1    MASISON, D.C.2
  • 43
    • 13244278043 scopus 로고    scopus 로고
    • Regulation of Hsp70 function by HspBP1: Structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange
    • SHOMURA, Y., Z. DRAGOVIC, H. C. CHANG, N. TZVETKOV, J. C. YOUNG et al., 2005 Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange. Mol. Cell 17: 367-379.
    • (2005) Mol. Cell , vol.17 , pp. 367-379
    • SHOMURA, Y.1    DRAGOVIC, Z.2    CHANG, H.C.3    TZVETKOV, N.4    YOUNG, J.C.5
  • 44
    • 2942722444 scopus 로고    scopus 로고
    • Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers
    • SHORTER, J., and S. LINDQUIST, 2004 Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers. Science 304: 1793-1797.
    • (2004) Science , vol.304 , pp. 1793-1797
    • SHORTER, J.1    LINDQUIST, S.2
  • 45
    • 33746405081 scopus 로고    scopus 로고
    • Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities
    • SHORTER, J., and S. LINDQUIST, 2006 Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities. Mol. Cell 23: 425-438.
    • (2006) Mol. Cell , vol.23 , pp. 425-438
    • SHORTER, J.1    LINDQUIST, S.2
  • 46
    • 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 P. HIETER, 1989 A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122: 19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
    • SIKORSKI, R.S.1    HIETER, P.2
  • 47
    • 13844313010 scopus 로고    scopus 로고
    • Role for Hsp70 chaperone in Saccharomyces cerevisiae prion seed replication
    • SONG, Y., Y. X. WU, G. JUNG, Y. TUTAR, E. EISENBERG et al., 2005 Role for Hsp70 chaperone in Saccharomyces cerevisiae prion seed replication. Eukaryot. Cell 4: 289-297.
    • (2005) Eukaryot. Cell , vol.4 , pp. 289-297
    • SONG, Y.1    WU, Y.X.2    JUNG, G.3    TUTAR, Y.4    EISENBERG, E.5
  • 48
    • 0035749733 scopus 로고    scopus 로고
    • URE3] and [PSI]: Prions of Saccharomyces cerevisiae
    • TAYLOR, K. L., and R. B. WICKNER, 2001 [URE3] and [PSI]: prions of Saccharomyces cerevisiae. Contrib. Microbiol. 7: 21-31.
    • (2001) Contrib. Microbiol , vol.7 , pp. 21-31
    • TAYLOR, K.L.1    WICKNER, R.B.2
  • 49
    • 31444452768 scopus 로고    scopus 로고
    • The battle of the fold: Chaperones take on prions
    • TRUE, H. L., 2006 The battle of the fold: chaperones take on prions. Trends Genet. 22: 110-117.
    • (2006) Trends Genet , vol.22 , pp. 110-117
    • TRUE, H.L.1
  • 50
    • 0034603218 scopus 로고    scopus 로고
    • Yeast prions and their prion-folding domain
    • TUITE, M. F., 2000 Yeast prions and their prion-folding domain. Cell 100: 289-292.
    • (2000) Cell , vol.100 , pp. 289-292
    • TUITE, M.F.1
  • 51
    • 0035890264 scopus 로고    scopus 로고
    • Strains of [PSI(1)] are distinguished by their efficiencies of prion-mediated conformational conversion
    • UPTAIN, S. M., G. J. SAWICKI, B. CAUGHEY and S. LINDQUIST, 2001 Strains of [PSI(1)] are distinguished by their efficiencies of prion-mediated conformational conversion. EMBO J. 20: 6236-6245.
    • (2001) EMBO J , vol.20 , pp. 6236-6245
    • UPTAIN, S.M.1    SAWICKI, G.J.2    CAUGHEY, B.3    LINDQUIST, S.4
  • 52
    • 31544442176 scopus 로고    scopus 로고
    • Allosteric regulation of Hsp70 chaperones by a proline switch
    • VOGEL, M., B. BUKAU and M. P. MAYER, 2006 Allosteric regulation of Hsp70 chaperones by a proline switch. Mol. Cell 21: 359-367.
    • (2006) Mol. Cell , vol.21 , pp. 359-367
    • VOGEL, M.1    BUKAU, B.2    MAYER, M.P.3
  • 55
    • 0024670024 scopus 로고
    • Yeast Hsp70 RNA levels vary in response to the physiological status of the cell
    • WERNER-WASHBURNE, M., J. BECKER, J. KOSIC-SMITHERS and E. A. CRAIG, 1989 Yeast Hsp70 RNA levels vary in response to the physiological status of the cell. J. Bacteriol. 171: 2680-2688.
    • (1989) J. Bacteriol , vol.171 , pp. 2680-2688
    • WERNER-WASHBURNE, M.1    BECKER, J.2    KOSIC-SMITHERS, J.3    CRAIG, E.A.4
  • 56
    • 0028308104 scopus 로고
    • URE3] as an altered URE2 protein: Evidence for a prion analog in Saccharomyces cerevisiae
    • WICKNER, R. B., 1994 [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science 264: 566-569.
    • (1994) Science , vol.264 , pp. 566-569
    • WICKNER, R.B.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.