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Volumn 408, Issue 3, 2011, Pages 432-448

Destabilization and recovery of a yeast prion after mild heat shock

Author keywords

Hsp; prion segregation; Saccharomyces cerevisiae; stress response; Sup35

Indexed keywords

CHAPERONE; CYCLOHEXIMIDE; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 104; HEAT SHOCK PROTEIN 70; PROTEIN; SUP35 PROTEIN; UNCLASSIFIED DRUG;

EID: 79953860164     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.02.034     Document Type: Article
Times cited : (70)

References (68)
  • 3
    • 77649202326 scopus 로고    scopus 로고
    • Protein aggregation diseases: Pathogenicity and therapeutic perspectives
    • Aguzzi A., and O'Connor T. Protein aggregation diseases: pathogenicity and therapeutic perspectives Nat. Rev., Drug Discov. 9 2010 237 248
    • (2010) Nat. Rev., Drug Discov. , vol.9 , pp. 237-248
    • Aguzzi, A.1    O'Connor, T.2
  • 6
    • 0034462603 scopus 로고    scopus 로고
    • [URE3] prion propagation in Saccharomyces cerevisiae: Requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p
    • DOI 10.1128/MCB.20.23.8916-8922.2000
    • Moriyama H., Edskes H.K., and Wickner R.B. [URE3] prion propagation in Saccharomyces cerevisiae: requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p Mol. Cell. Biol. 20 2000 8916 8922 (Pubitemid 32245922)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.23 , pp. 8916-8922
    • Moriyama, H.1    Edskes, H.K.2    Wickner, R.B.3
  • 8
    • 41349087784 scopus 로고    scopus 로고
    • Newly identified prion linked to the chromatin-remodeling factor Swi1 in Saccharomyces cerevisiae
    • DOI 10.1038/ng.112, PII NG112
    • Du Z., Park K.W., Yu H., Fan Q., and Li L. Newly identified prion linked to the chromatin-remodeling factor Swi1 in Saccharomyces cerevisiae Nat. Genet. 40 2008 460 465 (Pubitemid 351450881)
    • (2008) Nature Genetics , vol.40 , Issue.4 , pp. 460-465
    • Du, Z.1    Park, K.-W.2    Yu, H.3    Fan, Q.4    Li, L.5
  • 9
    • 61849091420 scopus 로고    scopus 로고
    • The yeast global transcriptional co-repressor protein Cyc8 can propagate as a prion
    • Patel B.K., Gavin-Smyth J., and Liebman S.W. The yeast global transcriptional co-repressor protein Cyc8 can propagate as a prion Nat. Cell Biol. 11 2009 344 349
    • (2009) Nat. Cell Biol. , vol.11 , pp. 344-349
    • Patel, B.K.1    Gavin-Smyth, J.2    Liebman, S.W.3
  • 10
    • 60549101873 scopus 로고    scopus 로고
    • A prion of yeast metacaspase homolog (Mca1p) detected by a genetic screen
    • Nemecek J., Nakayashiki T., and Wickner R.B. A prion of yeast metacaspase homolog (Mca1p) detected by a genetic screen Proc. Natl Acad. Sci. USA 106 2009 1892 1896
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , pp. 1892-1896
    • Nemecek, J.1    Nakayashiki, T.2    Wickner, R.B.3
  • 11
    • 0027996115 scopus 로고
    • Protein disaggregation mediated by heat-shock protein Hsp104
    • Parsell D.A., Kowal A.S., Singer M.A., and Lindquist S. Protein disaggregation mediated by heat-shock protein Hsp104 Nature 372 1994 475 478
    • (1994) Nature , vol.372 , pp. 475-478
    • Parsell, D.A.1    Kowal, A.S.2    Singer, M.A.3    Lindquist, S.4
  • 12
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70 and Hsp40: A novel chaperone system that rescues previously aggregated proteins
    • Glover J.R., and Lindquist S. Hsp104, Hsp70 and Hsp40: a novel chaperone system that rescues previously aggregated proteins Cell 94 1998 1 20
    • (1998) Cell , vol.94 , pp. 1-20
    • Glover, J.R.1    Lindquist, S.2
  • 13
    • 0033598703 scopus 로고    scopus 로고
    • Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network
    • Goloubinoff P., Mogk A., Zvi A.P., Tomoyasu T., and Bukau B. Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network Proc. Natl Acad. Sci. USA 96 2000 13732 13737
    • (2000) Proc. Natl Acad. Sci. USA , vol.96 , pp. 13732-13737
    • Goloubinoff, P.1    Mogk, A.2    Zvi, A.P.3    Tomoyasu, T.4    Bukau, B.5
  • 14
    • 34447526217 scopus 로고    scopus 로고
    • Stress and prions: Lessons from the yeast model
    • DOI 10.1016/j.febslet.2007.04.075, PII S0014579307004747, Cellular Stress
    • Chernoff Y.O. Stress and prions: lessons from the yeast model FEBS Lett. 581 2007 3695 3701 (Pubitemid 47081006)
    • (2007) FEBS Letters , vol.581 , Issue.19 , pp. 3695-3701
    • Chernoff, Y.O.1
  • 16
    • 62449229531 scopus 로고    scopus 로고
    • Chaperone effects on prion and non-prion aggregates
    • Rikhvanov E.G., Romanova N.V., and Chernoff Y.O. Chaperone effects on prion and non-prion aggregates Prion 1 2007 217 222
    • (2007) Prion , vol.1 , pp. 217-222
    • Rikhvanov, E.G.1    Romanova, N.V.2    Chernoff, Y.O.3
  • 18
    • 34948846000 scopus 로고    scopus 로고
    • Accelerated aging and failure to segregate damaged proteins in Sir2 mutants can be suppressed by overproducing the protein aggregation-remodeling factor Hsp104p
    • DOI 10.1101/gad.439307
    • Erjavec N., Larsson L., Grantham J., and Nyström T. Accelerated aging and failure to segregate damaged proteins in Sir2 mutants can be suppressed by overproducing the protein aggregation-remodeling factor Hsp104p Genes Dev. 21 2007 2410 2421 (Pubitemid 47529371)
    • (2007) Genes and Development , vol.21 , Issue.19 , pp. 2410-2421
    • Erjavec, N.1    Larsson, L.2    Grantham, J.3    Nystrom, T.4
  • 19
    • 67649326107 scopus 로고    scopus 로고
    • + chaperone Hsp104 is part of a network that links the actin cytoskeleton with the inheritance of damaged proteins
    • + chaperone Hsp104 is part of a network that links the actin cytoskeleton with the inheritance of damaged proteins Mol. Cell. Biol. 29 2009 3738 3745
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 3738-3745
    • Tessarz, P.1    Schwarz, M.2    Mogk, A.3    Bukau, B.4
  • 20
    • 33745419772 scopus 로고    scopus 로고
    • N-terminal domain of yeast Hsp104 chaperone is dispensable for thermotolerance and prion propagation but necessary for curing prions by Hsp104 overexpression
    • DOI 10.1534/genetics.106.056820
    • Hung G.C., and Masison D.C. N-terminal domain of yeast Hsp104 chaperone is dispensable for thermotolerance and prion propagation but necessary for curing prions by Hsp104 overexpression Genetics 173 2006 611 620 (Pubitemid 43945883)
    • (2006) Genetics , vol.173 , Issue.2 , pp. 611-620
    • Hung, G.-C.1    Masison, D.C.2
  • 21
    • 0032951475 scopus 로고    scopus 로고
    • Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing
    • Newnam G.P., Wegrzyn R.D., Lindquist S.L., and Chernoff Y.O. Antagonistic interactions between yeast chaperones Hsp104 and Hsp70 in prion curing Mol. Cell. Biol. 19 1999 1325 1333 (Pubitemid 29046874)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.2 , pp. 1325-1333
    • Newnam, G.P.1    Wegrzyn, R.D.2    Lindquist, S.L.3    Chernoff, Y.O.4
  • 23
    • 0035803490 scopus 로고    scopus 로고
    • Yeast prion protein derivative defective in aggregate shearing and production of new 'seeds'
    • DOI 10.1093/emboj/20.23.6683
    • Borchsenius A.S., Wegrzyn R.D., Newnam G.P., Inge-Vechtomov S.G., and Chernoff Y.O. Yeast prion protein derivative defective in aggregate shearing and production of new 'seeds' EMBO J. 20 2001 6683 6691 (Pubitemid 33134198)
    • (2001) EMBO Journal , vol.20 , Issue.23 , pp. 6683-6691
    • Borchsenius, A.S.1    Wegrzyn, R.D.2    Newnam, G.P.3    Inge-Vechtomov, S.G.4    Chernoff, Y.O.5
  • 24
    • 31044445005 scopus 로고    scopus 로고
    • Prion variant maintained only at high levels of the Hsp104 disaggregase
    • DOI 10.1007/s00294-005-0035-0
    • Borchsenius A.S., Müller S., Newnam G.P., Inge-Vechtomov S.G., and Chernoff Y.O. Prion variant maintained only at high levels of the Hsp104 disaggregase Curr. Genet. 49 2006 21 29 (Pubitemid 43118774)
    • (2006) Current Genetics , vol.49 , Issue.1 , pp. 21-29
    • Borchsenius, A.S.1    Muller, S.2    Newnam, G.P.3    Inge-Vechtomov, S.G.4    Chernoff, Y.O.5
  • 26
    • 0036096777 scopus 로고    scopus 로고
    • +] and [URE3] prions and curing of [URE3] by Hsp70 protein chaperone Ssa1p but not by Ssa2p
    • DOI 10.1128/MCB.22.11.3590-3598.2002
    • +] and [URE3] prions and curing of [URE3] by Hsp70 protein chaperone Ssa1p but not by Ssa2p Mol. Cell. Biol. 22 2002 3590 3598 (Pubitemid 34525203)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.11 , pp. 3590-3598
    • Schwimmer, C.1    Masison, D.C.2
  • 28
    • 52249119894 scopus 로고    scopus 로고
    • Prion-impairing mutations in Hsp70 chaperone Ssa1: Effects on ATPase and chaperone activities
    • Needham P.G., and Masison D.C. Prion-impairing mutations in Hsp70 chaperone Ssa1: effects on ATPase and chaperone activities Arch. Biochem. Biophys. 478 2008 167 174
    • (2008) Arch. Biochem. Biophys. , vol.478 , pp. 167-174
    • Needham, P.G.1    Masison, D.C.2
  • 29
    • 52049101761 scopus 로고    scopus 로고
    • Functionally redundant isoforms of a yeast Hsp70 chaperone subfamily have different antiprion effects
    • Sharma D., and Masison D.C. Functionally redundant isoforms of a yeast Hsp70 chaperone subfamily have different antiprion effects Genetics 179 2008 1301 1311
    • (2008) Genetics , vol.179 , pp. 1301-1311
    • Sharma, D.1    Masison, D.C.2
  • 31
    • 0033500152 scopus 로고    scopus 로고
    • Evidence for a protein mutator in yeast: Role of the Hsp70-related chaperone Ssb in formation, stability, and toxicity of the [PSI] prion
    • Chernoff Y.O., Newnam G.P., Kumar J., Allen K., and Zink A.D. Evidence for a protein mutator in yeast: role of the Hsp70-related chaperone Ssb in formation, stability, and toxicity of the [PSI] prion Mol. Cell. Biol. 19 1999 8103 8112 (Pubitemid 30414005)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.12 , pp. 8103-8112
    • Chernoff, Y.O.1    Newnam, G.P.2    Kumar, J.3    Allen, K.4    Zink, A.D.5
  • 35
    • 20744441099 scopus 로고    scopus 로고
    • Modulation of prion-dependent polyglutamine aggregation and toxicity by chaperone proteins in the yeast model
    • DOI 10.1074/jbc.M500390200
    • Gokhale K.C., Newnam G.P., Sherman M.Y., and Chernoff Y.O. Modulation of prion-dependent polyglutamine aggregation and toxicity by chaperone proteins in the yeast model J. Biol. Chem. 280 2005 22809 22818 (Pubitemid 40853187)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.24 , pp. 22809-22818
    • Gokhale, K.C.1    Newnam, G.P.2    Sherman, M.Y.3    Chernoff, Y.O.4
  • 36
    • 55949109442 scopus 로고    scopus 로고
    • In vivo monitoring of the prion replication cycle reveals a critical role for Sis1 in delivering substrates to Hsp104
    • Tipton K.A., Verges K.J., and Weissman J.S. In vivo monitoring of the prion replication cycle reveals a critical role for Sis1 in delivering substrates to Hsp104 Mol. Cell 32 2008 584 591
    • (2008) Mol. Cell , vol.32 , pp. 584-591
    • Tipton, K.A.1    Verges, K.J.2    Weissman, J.S.3
  • 37
    • 33744481323 scopus 로고    scopus 로고
    • +] are regulated by the heat-shock transcription factor
    • DOI 10.1534/genetics.105.054221
    • +] are regulated by the heat-shock transcription factor Genetics 173 2006 35 47 (Pubitemid 43800182)
    • (2006) Genetics , vol.173 , Issue.1 , pp. 35-47
    • Park, K.-W.1    Hahn, J.-S.2    Fan, Q.3    Thiele, D.J.4    Li, L.5
  • 38
    • 0024085209 scopus 로고
    • The Ψ factor of yeast: A problem in inheritance
    • Cox B.S., Tuite M.F., and McLaughlin C.S. The Ψ factor of yeast: a problem in inheritance Yeast 4 1988 159 178
    • (1988) Yeast , vol.4 , pp. 159-178
    • Cox, B.S.1    Tuite, M.F.2    McLaughlin, C.S.3
  • 39
    • 0026523626 scopus 로고
    • Hsp104 is required for tolerance to many forms of stress
    • Sanchez Y., Taulien J., Borkovich K.A., and Lindquist S. Hsp104 is required for tolerance to many forms of stress EMBO J. 11 1992 2357 2364
    • (1992) EMBO J. , vol.11 , pp. 2357-2364
    • Sanchez, Y.1    Taulien, J.2    Borkovich, K.A.3    Lindquist, S.4
  • 41
    • 0025193343 scopus 로고
    • HSP104 required for induced thermotolerance
    • Sanchez Y., and Lindquist S.L. Hsp104 required for induced thermotolerance Science 248 1990 1112 1115 (Pubitemid 120031537)
    • (1990) Science , vol.248 , Issue.4959 , pp. 1112-1115
    • Sanchez, Y.1    Lindquist, S.L.2
  • 42
    • 0033118934 scopus 로고    scopus 로고
    • Translation termination efficiency can be regulated in Saccharomyces cerevisiae by environmental stress through a prion-mediated mechanism
    • Eaglestone S.S., Cox B.S., and Tuite M.F. Translation termination efficiency can be regulated in Saccharomyces cerevisiae by environmental stress through a prion-mediated mechanism EMBO J. 18 1999 1974 1981 (Pubitemid 29158540)
    • (1999) EMBO Journal , vol.18 , Issue.7 , pp. 1974-1981
    • Eaglestone, S.S.1    Cox, B.S.2    Tuite, M.F.3
  • 43
    • 0034727077 scopus 로고    scopus 로고
    • A yeast prion provides a mechanism for genetic variation and phenotypic diversity
    • True H.L., and Lindquist S.L. A yeast prion provides a mechanism for genetic variation and phenotypic diversity Nature 407 2000 477 483
    • (2000) Nature , vol.407 , pp. 477-483
    • True, H.L.1    Lindquist, S.L.2
  • 45
    • 0034974996 scopus 로고    scopus 로고
    • Guanidine hydrochloride inhibits Hsp104 activity in vivo: A possible explanation for its effect in curing yeast prions
    • DOI 10.1007/s002840010251
    • Jung G., and Masison D.C. Guanidine hydrochloride inhibits Hsp104 activity in vivo: a possible explanation for its effect in curing yeast prions Curr. Microbiol. 43 2001 7 10 (Pubitemid 32549917)
    • (2001) Current Microbiology , vol.43 , Issue.1 , pp. 7-10
    • Jung, G.1    Masison, D.C.2
  • 46
  • 47
    • 0030482356 scopus 로고    scopus 로고
    • Genesis and variability of [PSI] prion factors in Saccharomyces cerevisiae
    • Derkatch I.L., Chernoff Y.O., Kushnirov V.V., Inge-Vechtomov S.G., and Liebman S.W. Genesis and variability of [PSI] prion factors in Saccharomyces cerevisiae Genetics 144 1996 1375 1386 (Pubitemid 26427888)
    • (1996) Genetics , vol.144 , Issue.4 , pp. 1375-1386
    • Derkatch, I.L.1    Chernoff, Y.O.2    Kushnirov, V.V.3    Inge-Vechtomov, S.G.4    Liebman, S.W.5
  • 48
    • 0023375806 scopus 로고
    • Complex interactions among members of an essential subfamily of hsp70 genes in Saccharomyces cerevisiae
    • Werner-Washburne M., Stone D.E., and Craig E.A. Complex interactions among members of an essential subfamily of hsp70 genes in Saccharomyces cerevisiae Mol. Cell. Biol. 7 1987 2568 2577
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 2568-2577
    • Werner-Washburne, M.1    Stone, D.E.2    Craig, E.A.3
  • 50
    • 1242296312 scopus 로고    scopus 로고
    • [URE3] prion propagation is abolished by a mutation of the primary cytosolic Hsp70 of budding yeast
    • DOI 10.1002/yea.1062
    • Roberts B.T., Moriyama H., and Wickner R.B. [URE3] prion propagation is abolished by a mutation of the primary cytosolic Hsp70 of budding yeast Yeast 21 2004 107 117 (Pubitemid 38219964)
    • (2004) Yeast , vol.21 , Issue.2 , pp. 107-117
    • Roberts, B.T.1    Moriyama, H.2    Wickner, R.B.3
  • 52
    • 33745615836 scopus 로고    scopus 로고
    • Purification and analysis of prion and amyloid aggregates
    • DOI 10.1016/j.ymeth.2006.04.007, PII S1046202306000570
    • Kushnirov V.V., Alexandrov I.M., Mitkevich O.V., Shkundina I.S., and Ter- Avanesyan M.D. Purification and analysis of prion and amyloid aggregates Methods 39 2006 50 55 (Pubitemid 43994494)
    • (2006) Methods , vol.39 , Issue.1 , pp. 50-55
    • Kushnirov, V.V.1    Alexandrov, I.M.2    Mitkevich, O.V.3    Shkundina, I.S.4    Ter-Avanesyan, M.D.5
  • 54
    • 0141455115 scopus 로고    scopus 로고
    • +] prion in yeast
    • +] prion in yeast Genetics 165 2003 23 33 (Pubitemid 37204053)
    • (2003) Genetics , vol.165 , Issue.1 , pp. 23-33
    • Cox, B.1    Ness, F.2    Tuite, M.3
  • 55
    • 0029780647 scopus 로고    scopus 로고
    • Support for the prion hypothesis for inheritance of a phenotypic trait in yeast
    • Patino M.M., Liu J.J., Glover J.R., and Lindquist S. Support for the prion hypothesis for inheritance of a phenotypic trait in yeast Science 273 1996 622 626 (Pubitemid 26262109)
    • (1996) Science , vol.273 , Issue.5275 , pp. 622-626
    • Patino, M.M.1    Liu, J.-J.2    Glover, J.R.3    Lindquist, S.4
  • 56
    • 0029888121 scopus 로고    scopus 로고
    • +] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor
    • +] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor EMBO J. 15 1996 3127 3134 (Pubitemid 26187760)
    • (1996) EMBO Journal , vol.15 , Issue.12 , pp. 3127-3134
    • Paushkin, S.V.1    Kushnirov, V.V.2    Smirnov, V.N.3    Ter-Avanesyan, M.D.4
  • 57
    • 78049408567 scopus 로고    scopus 로고
    • A size threshold limits prion transmission and establishes phenotypic diversity
    • Derdowski A., Sindi S.S., Klaips C.L., DiSalvo S., and Serio T.R. A size threshold limits prion transmission and establishes phenotypic diversity Science 330 2010 680 683
    • (2010) Science , vol.330 , pp. 680-683
    • Derdowski, A.1    Sindi, S.S.2    Klaips, C.L.3    Disalvo, S.4    Serio, T.R.5
  • 58
    • 0003108549 scopus 로고    scopus 로고
    • Prions of fungi: [URE3], [PSI] and [Het-s] discovered as heritable traits
    • Wickner R.B., and Chernoff Y.O. Prions of fungi: [URE3], [PSI] and [Het-s] discovered as heritable traits S.B. Prusiner, Prion Biology and Diseases 1999 Cold Spring Harbor Laboratory Press Cold Spring Harbor, NY 229 272
    • (1999) Prion Biology and Diseases , pp. 229-272
    • Wickner, R.B.1    Chernoff, Y.O.2
  • 60
    • 56849099636 scopus 로고    scopus 로고
    • Prion switching in response to environmental stress
    • Tyedmers J., Madariaga M., and Lindquist S. Prion switching in response to environmental stress PLoS Biol. 6 2008 e294
    • (2008) PLoS Biol. , vol.6 , pp. 294
    • Tyedmers, J.1    Madariaga, M.2    Lindquist, S.3
  • 61
    • 0032832981 scopus 로고    scopus 로고
    • Genetic study of interactions between the cytoskeletal assembly protein Sla1 and prion-forming domain of the release factor Sup35 (eRF3) in Saccharomyces cerevisiae
    • Bailleul P.A., Newnam G.P., Steenbergen J.N., and Chernoff Y.O. Genetic study of interactions between the cytoskeletal assembly protein sla1 and prion-forming domain of the release factor Sup35 (eRF3) in Saccharomyces cerevisiae Genetics 153 1999 81 94 (Pubitemid 29434770)
    • (1999) Genetics , vol.153 , Issue.1 , pp. 81-94
    • Bailleul, P.A.1    Newnam, G.P.2    Steenbergen, J.N.3    Chernoff, Y.O.4
  • 63
    • 0022656534 scopus 로고
    • Isolation of a chromosomal DNA fragment containing sup2 gene of the yeast Saccharomyces cerevisiae
    • Telckov M.V., Surguchov A.P., Dagkesamanskaya A.R., and Ter-Avanesyan M.D. Isolation of a chromosomal DNA fragment containing SUP2 gene of the yeast Saccharomyces cerevisiae Genetika (Moscow) 22 1986 17 25 (Pubitemid 16168653)
    • (1986) Genetika , vol.22 , Issue.1 , pp. 17-25
    • Telckov, M.V.1    Surguchov, A.P.2    Dagckesamanskaya, A.R.3    Ter-Avanesyan, M.D.4
  • 65
    • 0031820288 scopus 로고    scopus 로고
    • Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae
    • DOI 10.1002/(SICI)1097-0061(199807) 14:10<953::AID-YEA293>3.0.CO;2- U
    • Longtine M.S., McKenzie A., DeMarini D.J., Shah N.G., Wach A., and Brachat A. Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae Yeast 14 1998 953 961 (Pubitemid 28328001)
    • (1998) Yeast , vol.14 , Issue.10 , 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
  • 66
    • 0036275447 scopus 로고    scopus 로고
    • Getting started with yeast
    • DOI 10.1016/S0076-6879(02)50954-X
    • Sherman F. Getting started with yeast Methods Enzymol. 350 2002 3 41 (Pubitemid 34619482)
    • (2002) Methods in Enzymology , vol.350 , pp. 3-41
    • Sherman, F.1


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