메뉴 건너뛰기




Volumn 1843, Issue 4, 2014, Pages 746-757

Roles of Hsp104 and trehalose in solubilisation of mutant huntingtin in heat shocked Saccharomyces cerevisiae cells

Author keywords

Heat shock; Hsp104; Protein misfolding; Thermotolerance; Trehalose

Indexed keywords

CHAPERONE; HEAT SHOCK PROTEIN 104; HUNTINGTIN; POLYPEPTIDE; REACTIVE OXYGEN METABOLITE; TREHALOSE; TREHALOSE 6 PHOSPHATE SYNTHASES 1; UNCLASSIFIED DRUG;

EID: 84893497938     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2014.01.004     Document Type: Article
Times cited : (16)

References (63)
  • 1
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes
    • The Huntington's Disease Collaborative Research Group A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. Cell 1993, 72:971-983.
    • (1993) Cell , vol.72 , pp. 971-983
    • The Huntington's Disease Collaborative Research Group1
  • 2
    • 78650031174 scopus 로고    scopus 로고
    • Huntington's disease: from molecular pathogenesis to clinical treatment
    • Ross C.A., Tabrizi S.J. Huntington's disease: from molecular pathogenesis to clinical treatment. Lancet Neurol. 2011, 10:83-98.
    • (2011) Lancet Neurol. , vol.10 , pp. 83-98
    • Ross, C.A.1    Tabrizi, S.J.2
  • 3
    • 77950584656 scopus 로고    scopus 로고
    • Proteolysis of mutant huntingtin produces an exon 1 fragment that accumulates as an aggregated protein in neuronal nuclei in Huntington disease
    • Paganetti P., Bates G.P. Proteolysis of mutant huntingtin produces an exon 1 fragment that accumulates as an aggregated protein in neuronal nuclei in Huntington disease. J. Biol. Chem. 2012, 285:8808-8823.
    • (2012) J. Biol. Chem. , vol.285 , pp. 8808-8823
    • Paganetti, P.1    Bates, G.P.2
  • 4
    • 84868087531 scopus 로고    scopus 로고
    • Targeting mutant huntingtin for the development of disease-modifying therapy
    • Appl T., Kaltenbach L., Lo D.C., Terstappen G.C. Targeting mutant huntingtin for the development of disease-modifying therapy. Drug Discov. Today 2012, 17:1217-1223.
    • (2012) Drug Discov. Today , vol.17 , pp. 1217-1223
    • Appl, T.1    Kaltenbach, L.2    Lo, D.C.3    Terstappen, G.C.4
  • 7
    • 84863115461 scopus 로고    scopus 로고
    • Huntingtin aggregation kinetics and their pathological role in a Drosophila Huntington's disease model
    • Weiss K.R., Kimura Y., Lee W.C., Littleton J.T. Huntingtin aggregation kinetics and their pathological role in a Drosophila Huntington's disease model. Genetics 2012, 190:581-600.
    • (2012) Genetics , vol.190 , pp. 581-600
    • Weiss, K.R.1    Kimura, Y.2    Lee, W.C.3    Littleton, J.T.4
  • 8
    • 0037408279 scopus 로고    scopus 로고
    • Transcriptional abnormalities in Huntington disease
    • Sugars K.L., Rubinsztein D.C. Transcriptional abnormalities in Huntington disease. Trends Genet. 2003, 19:233-238.
    • (2003) Trends Genet. , vol.19 , pp. 233-238
    • Sugars, K.L.1    Rubinsztein, D.C.2
  • 9
    • 84862550502 scopus 로고    scopus 로고
    • Biology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system
    • Verghese J., Abrams J., Wang Y., Morano K.A. Biology of the heat shock response and protein chaperones: budding yeast (Saccharomyces cerevisiae) as a model system. Microbiol. Mol. Biol. Rev. 2012, 76:115-158.
    • (2012) Microbiol. Mol. Biol. Rev. , vol.76 , pp. 115-158
    • Verghese, J.1    Abrams, J.2    Wang, Y.3    Morano, K.A.4
  • 10
    • 57749116408 scopus 로고    scopus 로고
    • Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity
    • Duennwald M.L., Lindquist S. Impaired ERAD and ER stress are early and specific events in polyglutamine toxicity. Genes Dev. 2008, 22:3308-3319.
    • (2008) Genes Dev. , vol.22 , pp. 3308-3319
    • Duennwald, M.L.1    Lindquist, S.2
  • 11
    • 84861369587 scopus 로고    scopus 로고
    • Impaired heat shock response in cells expressing full-length polyglutamine-expanded huntingtin
    • Chafekar S.M., Duennwald M.L. Impaired heat shock response in cells expressing full-length polyglutamine-expanded huntingtin. PLoS One 2012, 7:e37929.
    • (2012) PLoS One , vol.7
    • Chafekar, S.M.1    Duennwald, M.L.2
  • 12
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • Goldberg A.L. Protein degradation and protection against misfolded or damaged proteins. Nature 2003, 426:895-899.
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 15
    • 27944499891 scopus 로고    scopus 로고
    • Overexpression of yeast hsp104 reduces polyglutamine aggregation and prolongs survival of a transgenic mouse model of Huntington's disease
    • Vacher C., Garcia-Oroz L., Rubinsztein D.C. Overexpression of yeast hsp104 reduces polyglutamine aggregation and prolongs survival of a transgenic mouse model of Huntington's disease. Hum. Mol. Genet. 2005, 14:3425-3433.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 3425-3433
    • Vacher, C.1    Garcia-Oroz, L.2    Rubinsztein, D.C.3
  • 16
    • 21244466032 scopus 로고    scopus 로고
    • A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104
    • Cashikar A.G., Duennwald M., Lindquist S.L. A chaperone pathway in protein disaggregation. Hsp26 alters the nature of protein aggregates to facilitate reactivation by Hsp104. J. Biol. Chem. 2005, 280:23869-23875.
    • (2005) J. Biol. Chem. , vol.280 , pp. 23869-23875
    • Cashikar, A.G.1    Duennwald, M.2    Lindquist, S.L.3
  • 19
    • 0035363805 scopus 로고    scopus 로고
    • Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease
    • Sittler A., Lurz R., Lueder G., Priller J., Lehrach H., Hayer-Hartl M.K., Hartl F.U., Wanker E.E. Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease. Hum. Mol. Genet. 2001, 10:1307-1315.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 1307-1315
    • Sittler, A.1    Lurz, R.2    Lueder, G.3    Priller, J.4    Lehrach, H.5    Hayer-Hartl, M.K.6    Hartl, F.U.7    Wanker, E.E.8
  • 20
    • 84860123776 scopus 로고    scopus 로고
    • Suppression of protein aggregation by chaperone modification of high molecular weight complexes
    • Labbadia J., Novoselov S.S., Bett J.S., Weiss A., Paganetti P., Bates G.P., Cheetham M.E. Suppression of protein aggregation by chaperone modification of high molecular weight complexes. Brain 2012, 135:1180-1196.
    • (2012) Brain , vol.135 , pp. 1180-1196
    • Labbadia, J.1    Novoselov, S.S.2    Bett, J.S.3    Weiss, A.4    Paganetti, P.5    Bates, G.P.6    Cheetham, M.E.7
  • 21
    • 84872314860 scopus 로고    scopus 로고
    • TOR and RAS pathways regulate desiccation tolerance in Saccharomyces cerevisiae
    • Welch A.Z., Gibney P.A., Botstein D., Koshland D.E. TOR and RAS pathways regulate desiccation tolerance in Saccharomyces cerevisiae. Mol. Biol. Cell 2013, 24:115-128.
    • (2013) Mol. Biol. Cell , vol.24 , pp. 115-128
    • Welch, A.Z.1    Gibney, P.A.2    Botstein, D.3    Koshland, D.E.4
  • 22
    • 0032039542 scopus 로고    scopus 로고
    • Multiple effects of trehalose on protein folding in vitro and in vivo
    • Singer M.A., Lindquist S. Multiple effects of trehalose on protein folding in vitro and in vivo. Mol. Cell 1998, 1:639-648.
    • (1998) Mol. Cell , vol.1 , pp. 639-648
    • Singer, M.A.1    Lindquist, S.2
  • 23
    • 0032213339 scopus 로고    scopus 로고
    • Thermotolerance in Saccharomyces cerevisiae: the yin and yang of trehalose
    • Singer M.A., Lindquist S. Thermotolerance in Saccharomyces cerevisiae: the yin and yang of trehalose. Trends Biotechnol. 1998, 16:460-468.
    • (1998) Trends Biotechnol. , vol.16 , pp. 460-468
    • Singer, M.A.1    Lindquist, S.2
  • 24
    • 27844585463 scopus 로고    scopus 로고
    • Trehalose and glycerol stabilize and renature yeast inorganic pyrophosphatase inactivated by very high temperatures
    • Zancan P., Sola-Penna M. Trehalose and glycerol stabilize and renature yeast inorganic pyrophosphatase inactivated by very high temperatures. Arch. Biochem. Biophys. 2005, 444:52-60.
    • (2005) Arch. Biochem. Biophys. , vol.444 , pp. 52-60
    • Zancan, P.1    Sola-Penna, M.2
  • 25
    • 40949151538 scopus 로고    scopus 로고
    • Effects of drought on water content and photosynthetic parameters in potato plants expressing the trehalose-6-phosphate synthase gene of Saccharomyces cerevisiae
    • Stiller I., Dulai S., Kondrák M., Tarnai R., Szabó L., Toldi O., Bánfalvi Z. Effects of drought on water content and photosynthetic parameters in potato plants expressing the trehalose-6-phosphate synthase gene of Saccharomyces cerevisiae. Planta 2008, 227:299-308.
    • (2008) Planta , vol.227 , pp. 299-308
    • Stiller, I.1    Dulai, S.2    Kondrák, M.3    Tarnai, R.4    Szabó, L.5    Toldi, O.6    Bánfalvi, Z.7
  • 29
    • 0026562884 scopus 로고
    • Improved method for high efficiency transformation of intact yeast cells
    • Gietz D., St.Jean A., Woods R.A., Schiestl R.H. Improved method for high efficiency transformation of intact yeast cells. Nucleic Acids Res. 1992, 20:1425-1431.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 1425-1431
    • Gietz, D.1    St Jean, A.2    Woods, R.A.3    Schiestl, R.H.4
  • 30
    • 0036447573 scopus 로고    scopus 로고
    • Expression and purification of homogenous proteins in Saccharomyces cerevisiae based on ubiquitin-FLAG fusion
    • Einhauer A., Schuster M., Wasserbauer E., Jungbauer A. Expression and purification of homogenous proteins in Saccharomyces cerevisiae based on ubiquitin-FLAG fusion. Protein Expr. Purif. 2002, 24:497-504.
    • (2002) Protein Expr. Purif. , vol.24 , pp. 497-504
    • Einhauer, A.1    Schuster, M.2    Wasserbauer, E.3    Jungbauer, A.4
  • 31
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 32
    • 0019187844 scopus 로고
    • Reserve carbohydrate metabolism in Saccharomyces cerevisiae: responses to nutrient limitation
    • Lillie S.H., Pringle J.R. Reserve carbohydrate metabolism in Saccharomyces cerevisiae: responses to nutrient limitation. J. Bacteriol. 1980, 143:1384-1394.
    • (1980) J. Bacteriol. , vol.143 , pp. 1384-1394
    • Lillie, S.H.1    Pringle, J.R.2
  • 33
    • 0030958532 scopus 로고    scopus 로고
    • Comparison of three different methods for trehalose determination in yeast extracts
    • Ferreira J.C., Paschoalin V.M.F., Panek A.D., Trugo L.C. Comparison of three different methods for trehalose determination in yeast extracts. Food Chem. 1997, 60:251-254.
    • (1997) Food Chem. , vol.60 , pp. 251-254
    • Ferreira, J.C.1    Paschoalin, V.M.F.2    Panek, A.D.3    Trugo, L.C.4
  • 34
    • 0037085384 scopus 로고    scopus 로고
    • Cooperation of yeast peroxiredoxins Tsa1p and Tsa2p in the cellular defense against oxidative and nitrosative stress
    • Wong C.M., Zhou Y., Ng R.W.M., Kung H., Jin D.Y. Cooperation of yeast peroxiredoxins Tsa1p and Tsa2p in the cellular defense against oxidative and nitrosative stress. J. Biol. Chem. 2002, 277:5385-5394.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5385-5394
    • Wong, C.M.1    Zhou, Y.2    Ng, R.W.M.3    Kung, H.4    Jin, D.Y.5
  • 35
    • 34247885929 scopus 로고    scopus 로고
    • Cellular processes and pathways that protect Saccharomyces cerevisiae cells against the plasma membrane-perturbing compound chitosan
    • Zakrzewska A., Boorsma A., Delneri D., Brul S., Oliver S.G., Klis F.M. Cellular processes and pathways that protect Saccharomyces cerevisiae cells against the plasma membrane-perturbing compound chitosan. Eukaryot. Cell 2007, 6:600-608.
    • (2007) Eukaryot. Cell , vol.6 , pp. 600-608
    • Zakrzewska, A.1    Boorsma, A.2    Delneri, D.3    Brul, S.4    Oliver, S.G.5    Klis, F.M.6
  • 37
    • 0033990048 scopus 로고    scopus 로고
    • Primer3 on the WWW for general users and for biologist programmers
    • Rozen S., Skaletsky H. Primer3 on the WWW for general users and for biologist programmers. Methods Mol. Biol. 2000, 132:365-386.
    • (2000) Methods Mol. Biol. , vol.132 , pp. 365-386
    • Rozen, S.1    Skaletsky, H.2
  • 38
    • 44949231424 scopus 로고    scopus 로고
    • Analyzing real-time PCR data by the comparative CT method
    • Schmittgen T.D., Livak K.J. Analyzing real-time PCR data by the comparative CT method. Nat. Protoc. 2008, 3:1101-1108.
    • (2008) Nat. Protoc. , vol.3 , pp. 1101-1108
    • Schmittgen, T.D.1    Livak, K.J.2
  • 39
    • 47049121708 scopus 로고    scopus 로고
    • Regulation of thermotolerance by stress-induced transcription factors in Saccharomyces cerevisiae
    • Yamamoto N., Maeda Y., Ikeda A., Sakurai H. Regulation of thermotolerance by stress-induced transcription factors in Saccharomyces cerevisiae. Eukaryot. Cell 2008, 7:783-790.
    • (2008) Eukaryot. Cell , vol.7 , pp. 783-790
    • Yamamoto, N.1    Maeda, Y.2    Ikeda, A.3    Sakurai, H.4
  • 40
    • 0023650350 scopus 로고
    • Trehalose accumulates in Saccharomyces cerevisiae during exposure to agents that induce heat shock response
    • Attfield P.V. Trehalose accumulates in Saccharomyces cerevisiae during exposure to agents that induce heat shock response. FEBS Lett. 1987, 225:259-263.
    • (1987) FEBS Lett. , vol.225 , pp. 259-263
    • Attfield, P.V.1
  • 41
    • 84455173005 scopus 로고    scopus 로고
    • In vitro and in vivo aggregation of a fragment of huntingtin protein directly causes free radical production
    • Hands S., Sajjad M.U., Newton M.J., Wyttenbach A. In vitro and in vivo aggregation of a fragment of huntingtin protein directly causes free radical production. J. Biol. Chem. 2011, 286:44512-44520.
    • (2011) J. Biol. Chem. , vol.286 , pp. 44512-44520
    • Hands, S.1    Sajjad, M.U.2    Newton, M.J.3    Wyttenbach, A.4
  • 43
    • 84859586432 scopus 로고    scopus 로고
    • The response to heat shock and oxidative stress in Saccharomyces cerevisiae
    • Morano K.A., Grant C.M., Moye-Rowley W.S. The response to heat shock and oxidative stress in Saccharomyces cerevisiae. Genetics 2012, 190:1157-1195.
    • (2012) Genetics , vol.190 , pp. 1157-1195
    • Morano, K.A.1    Grant, C.M.2    Moye-Rowley, W.S.3
  • 44
    • 0037053566 scopus 로고    scopus 로고
    • Huntington toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1
    • Meriin A.B., Zhang X., He X., Newnam G.P., Chernoff Y.O., Sherman M.Y. Huntington toxicity in yeast model depends on polyglutamine aggregation mediated by a prion-like protein Rnq1. J. Cell Biol. 2002, 157:997-1004.
    • (2002) J. Cell Biol. , vol.157 , pp. 997-1004
    • Meriin, A.B.1    Zhang, X.2    He, X.3    Newnam, G.P.4    Chernoff, Y.O.5    Sherman, M.Y.6
  • 45
    • 0034055242 scopus 로고    scopus 로고
    • Cell cycle arrest enhances the in vitro cellular toxicity of the truncated Machado-Joseph disease gene product with an expanded polyglutamine stretch
    • Yoshizawa T., Yamagishi Y., Koseki N., Goto J., Yoshida H., Shibasaki F., Shoji S., Kanazawa I. Cell cycle arrest enhances the in vitro cellular toxicity of the truncated Machado-Joseph disease gene product with an expanded polyglutamine stretch. Hum. Mol. Genet. 2000, 9:69-78.
    • (2000) Hum. Mol. Genet. , vol.9 , pp. 69-78
    • Yoshizawa, T.1    Yamagishi, Y.2    Koseki, N.3    Goto, J.4    Yoshida, H.5    Shibasaki, F.6    Shoji, S.7    Kanazawa, I.8
  • 46
    • 58049217323 scopus 로고    scopus 로고
    • Unexpected link between anaphase promoting complex and the toxicity of expanded polyglutamines expressed in yeast
    • Bocharova N.A., Sokolov S.S., Knorre D.A., Skulachev V.P., Severin F.F. Unexpected link between anaphase promoting complex and the toxicity of expanded polyglutamines expressed in yeast. Cell Cycle 2008, 7:3943-3946.
    • (2008) Cell Cycle , vol.7 , pp. 3943-3946
    • Bocharova, N.A.1    Sokolov, S.S.2    Knorre, D.A.3    Skulachev, V.P.4    Severin, F.F.5
  • 47
    • 0033959218 scopus 로고    scopus 로고
    • Induction of neutral trehalase Nth1 by heat and osmotic stress is controlled by STRE elements and Msn2/Msn4 transcription factors: variations of PKA effect during stress and growth
    • Zähringer H., Thevelein J.M., Nwaka S. Induction of neutral trehalase Nth1 by heat and osmotic stress is controlled by STRE elements and Msn2/Msn4 transcription factors: variations of PKA effect during stress and growth. Mol. Microbiol. 2000, 35:397-406.
    • (2000) Mol. Microbiol. , vol.35 , pp. 397-406
    • Zähringer, H.1    Thevelein, J.M.2    Nwaka, S.3
  • 48
    • 0027981247 scopus 로고
    • Saccharomyces cerevisiae Hsp104 protein. Purification and characterization of ATP-induced structural changes
    • Parsell D.A., Kowal A.S., Lindquist S. Saccharomyces cerevisiae Hsp104 protein. Purification and characterization of ATP-induced structural changes. J. Biol. Chem. 1994, 269:4480-4487.
    • (1994) J. Biol. Chem. , vol.269 , pp. 4480-4487
    • Parsell, D.A.1    Kowal, A.S.2    Lindquist, S.3
  • 49
    • 33846909430 scopus 로고    scopus 로고
    • The natural osmolyte trehalose is a positive regulator of the heat-induced activity of yeast heat shock transcription factor
    • Conlin L.K., Nelson H.C. The natural osmolyte trehalose is a positive regulator of the heat-induced activity of yeast heat shock transcription factor. Mol. Cell. Biol. 2007, 27:1505-1515.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 1505-1515
    • Conlin, L.K.1    Nelson, H.C.2
  • 50
    • 0034974996 scopus 로고    scopus 로고
    • Guanidine hydrochloride inhibits Hsp104 activity in vivo: a possible explanation for its effect in curing yeast prions
    • Jung G., Masison D.C. Guanidine hydrochloride inhibits Hsp104 activity in vivo: a possible explanation for its effect in curing yeast prions. Curr. Microbiol. 2001, 43:7-10.
    • (2001) Curr. Microbiol. , vol.43 , pp. 7-10
    • Jung, G.1    Masison, D.C.2
  • 51
    • 1542380028 scopus 로고    scopus 로고
    • The prion curing agent guanidinium chloride specifically inhibits ATP hydrolysis by Hsp104
    • Grimminger V., Richter K., Imhof A., Buchner J., Walter S. The prion curing agent guanidinium chloride specifically inhibits ATP hydrolysis by Hsp104. J. Biol. Chem. 2004, 279:7378-7383.
    • (2004) J. Biol. Chem. , vol.279 , pp. 7378-7383
    • Grimminger, V.1    Richter, K.2    Imhof, A.3    Buchner, J.4    Walter, S.5
  • 52
    • 0023649963 scopus 로고
    • Rapid changes of heat and desiccation tolerance correlated with changes of trehalose content in Saccharomyces cerevisiae cells subjected to temperature shifts
    • Hottiger T., Boller T., Wiemken A. Rapid changes of heat and desiccation tolerance correlated with changes of trehalose content in Saccharomyces cerevisiae cells subjected to temperature shifts. FEBS Lett. 1987, 220:113-115.
    • (1987) FEBS Lett. , vol.220 , pp. 113-115
    • Hottiger, T.1    Boller, T.2    Wiemken, A.3
  • 53
    • 68549139856 scopus 로고    scopus 로고
    • The induction of trehalose and glycerol in Saccharomyces cerevisiae in response to various stresses
    • Li L., Ye Y., Pan L., Zhu Y., Zheng S., Lin Y. The induction of trehalose and glycerol in Saccharomyces cerevisiae in response to various stresses. Biochem. Biophys. Res. Commun. 2009, 387:778-783.
    • (2009) Biochem. Biophys. Res. Commun. , vol.387 , pp. 778-783
    • Li, L.1    Ye, Y.2    Pan, L.3    Zhu, Y.4    Zheng, S.5    Lin, Y.6
  • 54
    • 0029861940 scopus 로고    scopus 로고
    • Synergy between trehalose and Hsp104 for thermotolerance in Saccharomyces cerevisiae
    • Elliott B., Haltiwanger R.S., Futcher B. Synergy between trehalose and Hsp104 for thermotolerance in Saccharomyces cerevisiae. Genetics 1996, 144:923-933.
    • (1996) Genetics , vol.144 , pp. 923-933
    • Elliott, B.1    Haltiwanger, R.S.2    Futcher, B.3
  • 55
    • 0031764272 scopus 로고    scopus 로고
    • Evidence for the interplay between trehalose metabolism and Hsp104 in yeast
    • Iwahashi H., Nwaka S., Obuchi K., Komatsu Y. Evidence for the interplay between trehalose metabolism and Hsp104 in yeast. Appl. Environ. Microbiol. 1998, 64:4614-4617.
    • (1998) Appl. Environ. Microbiol. , vol.64 , pp. 4614-4617
    • Iwahashi, H.1    Nwaka, S.2    Obuchi, K.3    Komatsu, Y.4
  • 56
    • 50649116818 scopus 로고    scopus 로고
    • Misfolded proteins partition between two distinct quality control compartments
    • Kaganovich D., Kopito R., Frydman J. Misfolded proteins partition between two distinct quality control compartments. Nature 2008, 454:1088-1095.
    • (2008) Nature , vol.454 , pp. 1088-1095
    • Kaganovich, D.1    Kopito, R.2    Frydman, J.3
  • 58
    • 0028912106 scopus 로고
    • Phenotypic features of trehalase mutants in Saccharomyces cerevisiae
    • Nwaka S., Mechler B., Destruelle M., Holzer H. Phenotypic features of trehalase mutants in Saccharomyces cerevisiae. FEBS Lett. 1995, 360:286-290.
    • (1995) FEBS Lett. , vol.360 , pp. 286-290
    • Nwaka, S.1    Mechler, B.2    Destruelle, M.3    Holzer, H.4
  • 60
    • 84865277422 scopus 로고    scopus 로고
    • Molecular chaperones and stress-inducible protein-sorting factors coordinate the spatiotemporal distribution of protein aggregates
    • Malinovska L., Kroschwald S., Munder M.C., Richter D., Alberti S. Molecular chaperones and stress-inducible protein-sorting factors coordinate the spatiotemporal distribution of protein aggregates. Cell 2012, 23:3041-3056.
    • (2012) Cell , vol.23 , pp. 3041-3056
    • Malinovska, L.1    Kroschwald, S.2    Munder, M.C.3    Richter, D.4    Alberti, S.5
  • 61
    • 54349128824 scopus 로고    scopus 로고
    • Curing of the [URE3] prion by Btn2p, a Batten disease-related protein
    • Kryndushkin D.S., Shewmaker F., Wickner R.B. Curing of the [URE3] prion by Btn2p, a Batten disease-related protein. EMBO J. 2008, 27:2725-2735.
    • (2008) EMBO J. , vol.27 , pp. 2725-2735
    • Kryndushkin, D.S.1    Shewmaker, F.2    Wickner, R.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.