메뉴 건너뛰기




Volumn 2, Issue OCT, 2015, Pages

Metazoan Hsp70-based protein disaggregases: Emergence and mechanisms

Author keywords

Hsp110; Hsp70; J protein; Metazoan; Protein disaggregation

Indexed keywords


EID: 85014335951     PISSN: None     EISSN: 2296889X     Source Type: Journal    
DOI: 10.3389/fmolb.2015.00057     Document Type: Review
Times cited : (90)

References (124)
  • 1
    • 55949092734 scopus 로고    scopus 로고
    • Insights into the structural dynamics of the Hsp110-Hsp70 interaction reveal the mechanism for nucleotide exchange activity
    • Andréasson, C., Fiaux, J., Rampelt, H., Druffel-Augustin, S., and Bukau, B. (2008). Insights into the structural dynamics of the Hsp110-Hsp70 interaction reveal the mechanism for nucleotide exchange activity. Proc. Natl. Acad. Sci. U.S.A. 105, 16519-16524. doi: 10.1073/pnas.0804187105
    • (2008) Proc. Natl. Acad. Sci. U.S.A , vol.105 , pp. 16519-16524
    • Andréasson, C.1    Fiaux, J.2    Rampelt, H.3    Druffel-Augustin, S.4    Bukau, B.5
  • 2
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • Arrasate, M., Mitra, S., Schweitzer, E. S., Segal, M. R., and Finkbeiner, S. (2004). Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 431, 805-810. doi: 10.1038/nature02998
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 3
    • 4444288866 scopus 로고    scopus 로고
    • Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual hsp70 chaperones
    • Ben-Zvi, A., De Los Rios, P., Dietler, G., and Goloubinoff, P. (2004). Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual hsp70 chaperones. J. Biol. Chem. 279, 37298-37303. doi: 10.1074/jbc. M405627200
    • (2004) J. Biol. Chem , vol.279 , pp. 37298-37303
    • Ben-Zvi, A.1    De Los Rios, P.2    Dietler, G.3    Goloubinoff, P.4
  • 4
    • 0032489016 scopus 로고    scopus 로고
    • The Hsp70 and Hsp60 chaperone machines
    • Bukau, B., and Horwich, A. L. (1998). The Hsp70 and Hsp60 chaperone machines. Cell 92, 351-366. doi: 10.1016/S0092-8674(00)80928-9
    • (1998) Cell , vol.92 , pp. 351-366
    • Bukau, B.1    Horwich, A.L.2
  • 5
    • 84899854286 scopus 로고    scopus 로고
    • Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation
    • Carroni, M., Kummer, E., Oguchi, Y., Wendler, P., Clare, D. K., Sinning, I., et al. (2014). Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation. Elife 3:e02481. doi: 10.7554/eLife.02481
    • (2014) Elife , vol.3
    • Carroni, M.1    Kummer, E.2    Oguchi, Y.3    Wendler, P.4    Clare, D.K.5    Sinning, I.6
  • 6
    • 0031945665 scopus 로고    scopus 로고
    • Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function
    • Cheetham, M. E., and Caplan, A. J. (1998). Structure, function and evolution of DnaJ: conservation and adaptation of chaperone function. Cell Stress Chaperones 3, 28-36
    • (1998) Cell Stress Chaperones , vol.3 , pp. 28-36
    • Cheetham, M.E.1    Caplan, A.J.2
  • 7
    • 84989284335 scopus 로고    scopus 로고
    • Degradation of misfolded proteins in neurodegenerative diseases: therapeutic targets and strategies
    • Ciechanover, A., and Kwon, Y. T. (2015). Degradation of misfolded proteins in neurodegenerative diseases: therapeutic targets and strategies. Exp. Mol. Med. 47:e147. doi: 10.1038/emm.2014.117
    • (2015) Exp. Mol. Med , vol.47 , pp. e147
    • Ciechanover, A.1    Kwon, Y.T.2
  • 8
    • 33748792821 scopus 로고    scopus 로고
    • Opposing activities protect against age-onset proteotoxicity
    • Cohen, E., Bieschke, J., Perciavalle, R. M., Kelly, J. W., and Dillin, A. (2006). Opposing activities protect against age-onset proteotoxicity. Science 313, 1604-1610. doi: 10.1126/science.1124646
    • (2006) Science , vol.313 , pp. 1604-1610
    • Cohen, E.1    Bieschke, J.2    Perciavalle, R.M.3    Kelly, J.W.4    Dillin, A.5
  • 9
    • 4344659685 scopus 로고    scopus 로고
    • Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy
    • Cuervo, A. M., Stefanis, L., Fredenburg, R., Lansbury, P. T., and Sulzer, D. (2004). Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy. Science 305, 1292-1295. doi: 10.1126/science.1101738
    • (2004) Science , vol.305 , pp. 1292-1295
    • Cuervo, A.M.1    Stefanis, L.2    Fredenburg, R.3    Lansbury, P.T.4    Sulzer, D.5
  • 10
    • 33644557410 scopus 로고    scopus 로고
    • Eleven ancestral gene families lost in mammals and vertebrates while otherwise universally conserved in animals
    • Danchin, E. G., Gouret, P., and Pontarotti, P. (2006). Eleven ancestral gene families lost in mammals and vertebrates while otherwise universally conserved in animals. BMC Evol. Biol. 6:5. doi: 10.1186/1471-2148-6-5
    • (2006) BMC Evol. Biol , vol.6 , pp. 5
    • Danchin, E.G.1    Gouret, P.2    Pontarotti, P.3
  • 11
    • 33646557371 scopus 로고    scopus 로고
    • Hsp70 chaperones accelerate protein translocation and the unfolding of stable protein aggregates by entropic pulling
    • De Los Rios, P., Ben-Zvi, A., Slutsky, O., Azem, A., and Goloubinoff, P. (2006). Hsp70 chaperones accelerate protein translocation and the unfolding of stable protein aggregates by entropic pulling. Proc. Natl. Acad. Sci. U.S.A. 103, 6166-6171. doi: 10.1073/pnas.0510496103
    • (2006) Proc. Natl. Acad. Sci. U.S.A , vol.103 , pp. 6166-6171
    • De Los Rios, P.1    Ben-Zvi, A.2    Slutsky, O.3    Azem, A.4    Goloubinoff, P.5
  • 12
    • 84934767133 scopus 로고    scopus 로고
    • Misfolding, Aggregation, and Disordered Segments in c-Abl and p53 in Human Cancer
    • de Oliveira, G. A., Rangel, L. P., Costa, D. C., and Silva, J. L. (2015). Misfolding, Aggregation, and Disordered Segments in c-Abl and p53 in Human Cancer. Front. Oncol. 5:97. doi: 10.3389/fonc.2015.00097
    • (2015) Front. Oncol , vol.5 , pp. 97
    • de Oliveira, G.A.1    Rangel, L.P.2    Costa, D.C.3    Silva, J.L.4
  • 13
    • 0034647887 scopus 로고    scopus 로고
    • Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery
    • Diamant, S., Ben-Zvi, A. P., Bukau, B., and Goloubinoff, P. (2000). Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery. J. Biol. Chem. 275, 21107-21113. doi: 10.1074/jbc. M001293200
    • (2000) J. Biol. Chem , vol.275 , pp. 21107-21113
    • Diamant, S.1    Ben-Zvi, A.P.2    Bukau, B.3    Goloubinoff, P.4
  • 14
    • 67649306771 scopus 로고    scopus 로고
    • Molecular chaperones antagonize proteotoxicity by differentially modulating protein aggregation pathways
    • Douglas, P. M., Summers, D. W., and Cyr, D. M. (2009). Molecular chaperones antagonize proteotoxicity by differentially modulating protein aggregation pathways. Prion 3, 51-58. doi: 10.4161/pri.3.2.8587
    • (2009) Prion , vol.3 , pp. 51-58
    • Douglas, P.M.1    Summers, D.W.2    Cyr, D.M.3
  • 15
    • 84886446627 scopus 로고    scopus 로고
    • Protein rescue from aggregates by powerful molecular chaperone machines
    • Doyle, S. M., Genest, O., and Wickner, S. (2013). Protein rescue from aggregates by powerful molecular chaperone machines. Nat. Rev. Mol. Cell Biol. 14, 617-629. doi: 10.1038/nrm3660
    • (2013) Nat. Rev. Mol. Cell Biol , vol.14 , pp. 617-629
    • Doyle, S.M.1    Genest, O.2    Wickner, S.3
  • 16
    • 34547455220 scopus 로고    scopus 로고
    • Collaboration between the ClpB AAA+ remodeling protein and the DnaK chaperone system
    • Doyle, S. M., Hoskins, J. R., and Wickner, S. (2007). Collaboration between the ClpB AAA+ remodeling protein and the DnaK chaperone system. Proc. Natl. Acad. Sci. U.S.A. 104, 11138-11144. doi: 10.1073/pnas.0703980104
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 11138-11144
    • Doyle, S.M.1    Hoskins, J.R.2    Wickner, S.3
  • 17
    • 84865220378 scopus 로고    scopus 로고
    • DnaK chaperone-dependent disaggregation by caseinolytic peptidase B (ClpB) mutants reveals functional overlap in the N-terminal domain and nucleotide-binding domain-1 pore tyrosine
    • Doyle, S. M., Hoskins, J. R., and Wickner, S. (2012). DnaK chaperone-dependent disaggregation by caseinolytic peptidase B (ClpB) mutants reveals functional overlap in the N-terminal domain and nucleotide-binding domain-1 pore tyrosine. J. Biol. Chem. 287, 28470-28479. doi: 10.1074/jbc. M112.383091
    • (2012) J. Biol. Chem , vol.287 , pp. 28470-28479
    • Doyle, S.M.1    Hoskins, J.R.2    Wickner, S.3
  • 18
    • 58149181486 scopus 로고    scopus 로고
    • Hsp104 and ClpB: protein disaggregating machines
    • Doyle, S. M., and Wickner, S. (2009). Hsp104 and ClpB: protein disaggregating machines. Trends Biochem. Sci. 34, 40-48. doi: 10.1016/j.tibs.2008.09.010
    • (2009) Trends Biochem. Sci , vol.34 , pp. 40-48
    • Doyle, S.M.1    Wickner, S.2
  • 19
    • 33745762927 scopus 로고    scopus 로고
    • Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s
    • Dragovic, Z., Broadley, S. A., Shomura, Y., Bracher, A., and Hartl, F. U. (2006). Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s. EMBO J. 25, 2519-2528. doi: 10.1038/sj.emboj.7601138
    • (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
  • 20
    • 78650944949 scopus 로고    scopus 로고
    • The cell-non-autonomous nature of electron transport chain-mediated longevity
    • Durieux, J., Wolff, S., and Dillin, A. (2011). The cell-non-autonomous nature of electron transport chain-mediated longevity. Cell 144, 79-91. doi: 10.1016/j.cell.2010.12.016
    • (2011) Cell , vol.144 , pp. 79-91
    • Durieux, J.1    Wolff, S.2    Dillin, A.3
  • 21
    • 0033625965 scopus 로고    scopus 로고
    • The hsp110 and Grp1 70 stress proteins: newly recognized relatives of the Hsp70s
    • Easton, D. P., Kaneko, Y., and Subjeck, J. R. (2000). The hsp110 and Grp1 70 stress proteins: newly recognized relatives of the Hsp70s. Cell Stress Chaper. 5, 276-290. doi: 10.1379/1466-1268(2000)005<0276:THAGSP>2.0.CO;2
    • (2000) Cell Stress Chaper , vol.5 , pp. 276-290
    • Easton, D.P.1    Kaneko, Y.2    Subjeck, J.R.3
  • 22
    • 84885095437 scopus 로고    scopus 로고
    • Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress
    • Escusa-Toret, S., Vonk, W. I. M., and Frydman, J. (2013). Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress. Nat. Cell Biol. 15, 1231-U1253. doi: 10.1038/ncb2838
    • (2013) Nat. Cell Biol , vol.15 , pp. 1231-U1253
    • Escusa-Toret, S.1    Vonk, W.I.M.2    Frydman, J.3
  • 23
    • 0742305339 scopus 로고    scopus 로고
    • Exchangeable chaperone modules contribute to specification of type I and type II Hsp40 cellular function
    • Fan, C. Y., Lee, S., Ren, H. Y., and Cyr, D. M. (2004). Exchangeable chaperone modules contribute to specification of type I and type II Hsp40 cellular function. Mol. Biol. Cell 15, 761-773. doi: 10.1091/mbc. E03-03-0146
    • (2004) Mol. Biol. Cell , vol.15 , pp. 761-773
    • Fan, C.Y.1    Lee, S.2    Ren, H.Y.3    Cyr, D.M.4
  • 24
    • 0026696625 scopus 로고
    • Physical Interaction between Heat-Shock Proteins Dnak, Dnaj, and Grpe and the Bacterial Heat-Shock Transcription Factor-Sigma(32)
    • Gamer, J., Bujard, H., and Bukau, B. (1992). Physical Interaction between Heat-Shock Proteins Dnak, Dnaj, and Grpe and the Bacterial Heat-Shock Transcription Factor-Sigma(32). Cell 69, 833-842. doi: 10.1016/0092-8674(92)90294-M
    • (1992) Cell , vol.69 , pp. 833-842
    • Gamer, J.1    Bujard, H.2    Bukau, B.3
  • 25
    • 84940897433 scopus 로고    scopus 로고
    • Human Hsp70 disaggregase reverses parkinson's-linked alpha-synuclein amyloid fibrils
    • Gao, X., Carroni, M., Nussbaum-Krammer, C., Mogk, A., Nillegoda, N. B., Szlachcic, A., et al. (2015). Human Hsp70 disaggregase reverses parkinson's-linked alpha-synuclein amyloid fibrils. Mol. Cell. 59, 781-793. doi: 10.1016/j.molcel.2015.07.012
    • (2015) Mol. Cell , vol.59 , pp. 781-793
    • Gao, X.1    Carroni, M.2    Nussbaum-Krammer, C.3    Mogk, A.4    Nillegoda, N.B.5    Szlachcic, A.6
  • 26
    • 79957730170 scopus 로고    scopus 로고
    • Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling
    • Genest, O., Hoskins, J. R., Camberg, J. L., Doyle, S. M., and Wickner, S. (2011). Heat shock protein 90 from Escherichia coli collaborates with the DnaK chaperone system in client protein remodeling. Proc. Natl. Acad. Sci. U.S.A. 108, 8206-8211. doi: 10.1073/pnas.1104703108
    • (2011) Proc. Natl. Acad. Sci. U.S.A , vol.108 , pp. 8206-8211
    • Genest, O.1    Hoskins, J.R.2    Camberg, J.L.3    Doyle, S.M.4    Wickner, S.5
  • 27
    • 0034806604 scopus 로고    scopus 로고
    • The djlA gene acts synergistically with dnaJ in promoting Escherichia coli growth
    • Genevaux, P., Schwager, F., Georgopoulos, C., and Kelley, W. L. (2001). The djlA gene acts synergistically with dnaJ in promoting Escherichia coli growth. J. Bacteriol. 183, 5747-5750. doi: 10.1128/JB.183.19.5747-5750.2001
    • (2001) J. Bacteriol , vol.183 , pp. 5747-5750
    • Genevaux, P.1    Schwager, F.2    Georgopoulos, C.3    Kelley, W.L.4
  • 28
    • 84863533791 scopus 로고    scopus 로고
    • The stress of protein misfolding: from single cells to multicellular organisms
    • Gidalevitz, T., Prahlad, V., and Morimoto, R. I. (2011). The stress of protein misfolding: from single cells to multicellular organisms. Cold Spring Harb. Perspect. Biol. 3:a009704. doi: 10.1101/cshperspect.a009704
    • (2011) Cold Spring Harb. Perspect. Biol , vol.3
    • Gidalevitz, T.1    Prahlad, V.2    Morimoto, R.I.3
  • 29
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins
    • Glover, J. R., and Lindquist, S. (1998). Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins. Cell 94, 73-82. doi: 10.1016/S0092-8674(00)81223-4
    • (1998) Cell , vol.94 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 30
    • 45549087972 scopus 로고    scopus 로고
    • The yeast Hsp110, Sse1p, exhibits high-affinity peptide binding
    • Goeckeler, J. L., Petruso, A. P., Aguirre, J., Clement, C. C., Chiosis, G., and Brodsky, J. L. (2008). The yeast Hsp110, Sse1p, exhibits high-affinity peptide binding. FEBS Lett. 582, 2393-2396. doi: 10.1016/j.febslet.2008.05.047
    • (2008) FEBS Lett , vol.582 , pp. 2393-2396
    • Goeckeler, J.L.1    Petruso, A.P.2    Aguirre, J.3    Clement, C.C.4    Chiosis, G.5    Brodsky, J.L.6
  • 31
    • 34547146401 scopus 로고    scopus 로고
    • The mechanism of Hsp70 chaperones: (entropic) pulling the models together
    • Goloubinoff, P., and De Los Rios, P. (2007). The mechanism of Hsp70 chaperones: (entropic) pulling the models together. Trends Biochem. Sci. 32, 372-380. doi: 10.1016/j.tibs.2007.06.008
    • (2007) Trends Biochem. Sci , vol.32 , pp. 372-380
    • Goloubinoff, P.1    De Los Rios, P.2
  • 32
    • 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. (1999). Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Proc. Natl. Acad. Sci. U.S.A. 96, 13732-13737. doi: 10.1073/pnas.96.24.13732
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 13732-13737
    • Goloubinoff, P.1    Mogk, A.2    Zvi, A.P.3    Tomoyasu, T.4    Bukau, B.5
  • 33
    • 44849138934 scopus 로고    scopus 로고
    • Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments
    • Haslberger, T., Zdanowicz, A., Brand, I., Kirstein, J., Turgay, K., Mogk, A., et al. (2008). Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments. Nat. Struct. Mol. Biol. 15, 641-650. doi: 10.1038/nsmb.1425
    • (2008) Nat. Struct. Mol. Biol , vol.15 , pp. 641-650
    • Haslberger, T.1    Zdanowicz, A.2    Brand, I.3    Kirstein, J.4    Turgay, K.5    Mogk, A.6
  • 34
    • 75749101057 scopus 로고    scopus 로고
    • Cytoplasmic protein quality control degradation mediated by parallel actions of the E3 ubiquitin ligases Ubr1 and San1
    • Heck, J. W., Cheung, S. K., and Hampton, R. Y. (2010). Cytoplasmic protein quality control degradation mediated by parallel actions of the E3 ubiquitin ligases Ubr1 and San1. Proc. Natl. Acad. Sci. U.S.A. 107, 1106-1111. doi: 10.1073/pnas.0910591107
    • (2010) Proc. Natl. Acad. Sci. U.S.A , vol.107 , pp. 1106-1111
    • Heck, J.W.1    Cheung, S.K.2    Hampton, R.Y.3
  • 35
    • 21244480104 scopus 로고    scopus 로고
    • Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation
    • Hinnerwisch, J., Fenton, W. A., Furtak, K. J., Farr, G. W., and Horwich, A. L. (2005). Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation. Cell 121, 1029-1041. doi: 10.1016/j.cell.2005.04.012
    • (2005) Cell , vol.121 , pp. 1029-1041
    • Hinnerwisch, J.1    Fenton, W.A.2    Furtak, K.J.3    Farr, G.W.4    Horwich, A.L.5
  • 36
    • 84906794886 scopus 로고    scopus 로고
    • Proteostasis impairment in protein-misfolding and-aggregation diseases
    • Hipp, M. S., Park, S. H., and Hartl, F. U. (2014). Proteostasis impairment in protein-misfolding and-aggregation diseases. Trends Cell Biol. 24, 506-514. doi: 10.1016/j.tcb.2014.05.003
    • (2014) Trends Cell Biol , vol.24 , pp. 506-514
    • Hipp, M.S.1    Park, S.H.2    Hartl, F.U.3
  • 37
    • 0034636040 scopus 로고    scopus 로고
    • Mutants of Arabidopsis thaliana defective in the acquisition of tolerance to high temperature stress
    • Hong, S. W., and Vierling, E. (2000). Mutants of Arabidopsis thaliana defective in the acquisition of tolerance to high temperature stress. Proc. Natl. Acad. Sci. U.S.A. 97, 4392-4397. doi: 10.1073/pnas.97.8.4392
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 4392-4397
    • Hong, S.W.1    Vierling, E.2
  • 38
    • 0034895977 scopus 로고    scopus 로고
    • Hsp101 is necessary for heat tolerance but dispensable for development and germination in the absence of stress
    • Hong, S. W., and Vierling, E. (2001). Hsp101 is necessary for heat tolerance but dispensable for development and germination in the absence of stress. Plant J. 27, 25-35. doi: 10.1046/j.1365-313x.2001.01066.x
    • (2001) Plant J , vol.27 , pp. 25-35
    • Hong, S.W.1    Vierling, E.2
  • 39
    • 1842337450 scopus 로고    scopus 로고
    • Leishmania major Hsp100 is required chiefly in the mammalian stage of the parasite
    • Hübel, A., Krobitsch, S., Horauf, A., and Clos, J. (1997). Leishmania major Hsp100 is required chiefly in the mammalian stage of the parasite. Mol. Cell. Biol. 17, 5987-5995
    • (1997) Mol. Cell. Biol , vol.17 , pp. 5987-5995
    • Hübel, A.1    Krobitsch, S.2    Horauf, A.3    Clos, J.4
  • 40
    • 0042591262 scopus 로고    scopus 로고
    • Hsp105alpha suppresses the aggregation of truncated androgen receptor with expanded CAG repeats and cell toxicity
    • Ishihara, K., Yamagishi, N., Saito, Y., Adachi, H., Kobayashi, Y., Sobue, G., et al. (2003). Hsp105alpha suppresses the aggregation of truncated androgen receptor with expanded CAG repeats and cell toxicity. J. Biol. Chem. 278, 25143-25150. doi: 10.1074/jbc. M302975200
    • (2003) J. Biol. Chem , vol.278 , pp. 25143-25150
    • Ishihara, K.1    Yamagishi, N.2    Saito, Y.3    Adachi, H.4    Kobayashi, Y.5    Sobue, G.6
  • 41
    • 0027457953 scopus 로고
    • Thermotolerance in mammalian cells. Protein denaturation and aggregation, and stress proteins
    • Kampinga, H. H. (1993). Thermotolerance in mammalian cells. Protein denaturation and aggregation, and stress proteins. J. Cell Sci. 104 (Pt 1), 11-17
    • (1993) J. Cell Sci , vol.104 , pp. 11-17
    • Kampinga, H.H.1
  • 42
    • 77954947810 scopus 로고    scopus 로고
    • The HSP70 chaperone machinery: J proteins as drivers of functional specificity
    • Kampinga, H. H., and Craig, E. A. (2010). The HSP70 chaperone machinery: J proteins as drivers of functional specificity. Nat. Rev. Mol. Cell Biol. 11, 579-592. doi: 10.1038/nrm2941
    • (2010) Nat. Rev. Mol. Cell Biol , vol.11 , pp. 579-592
    • Kampinga, H.H.1    Craig, E.A.2
  • 43
    • 0031017476 scopus 로고    scopus 로고
    • A novel hsp110-related gene, apg-1, that is abundantly expressed in the testis responds to a low temperature heat shock rather than the traditional elevated temperatures
    • Kaneko, Y., Nishiyama, H., Nonoguchi, K., Higashitsuji, H., Kishishita, M., and Fujita, J. (1997). A novel hsp110-related gene, apg-1, that is abundantly expressed in the testis responds to a low temperature heat shock rather than the traditional elevated temperatures. J. Biol. Chem. 272, 2640-2645. doi: 10.1074/jbc.272.5.2640
    • (1997) J. Biol. Chem , vol.272 , pp. 2640-2645
    • Kaneko, Y.1    Nishiyama, H.2    Nonoguchi, K.3    Higashitsuji, H.4    Kishishita, M.5    Fujita, J.6
  • 44
    • 84907186821 scopus 로고    scopus 로고
    • Single-molecule spectroscopy reveals chaperone-mediated expansion of substrate protein
    • Kellner, R., Hofmann, H., Barducci, A., Wunderlich, B., Nettels, D., and Schuler, B. (2014). Single-molecule spectroscopy reveals chaperone-mediated expansion of substrate protein. Proc. Natl. Acad. Sci. U.S.A. 111, 13355-13360. doi: 10.1073/pnas.1407086111
    • (2014) Proc. Natl. Acad. Sci. U.S.A , vol.111 , pp. 13355-13360
    • Kellner, R.1    Hofmann, H.2    Barducci, A.3    Wunderlich, B.4    Nettels, D.5    Schuler, B.6
  • 45
    • 84878658572 scopus 로고    scopus 로고
    • The nascent polypeptide-associated complex is a key regulator of proteostasis
    • Kirstein-Miles, J., Scior, A., Deuerling, E., and Morimoto, R. I. (2013). The nascent polypeptide-associated complex is a key regulator of proteostasis. EMBO J. 32, 1451-1468. doi: 10.1038/emboj.2013.87
    • (2013) EMBO J , vol.32 , pp. 1451-1468
    • Kirstein-Miles, J.1    Scior, A.2    Deuerling, E.3    Morimoto, R.I.4
  • 46
    • 84901355639 scopus 로고    scopus 로고
    • The amyloid state and its association with protein misfolding diseases
    • Knowles, T. P., Vendruscolo, M., and Dobson, C. M. (2014). The amyloid state and its association with protein misfolding diseases. Nat. Rev. Mol. Cell Biol. 15, 384-396. doi: 10.1038/nrm3810
    • (2014) Nat. Rev. Mol. Cell Biol , vol.15 , pp. 384-396
    • Knowles, T.P.1    Vendruscolo, M.2    Dobson, C.M.3
  • 47
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito, R. R. (2000). Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol. 10, 524-530. doi: 10.1016/S0962-8924(00)01852-3
    • (2000) Trends Cell Biol , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 48
    • 84887473021 scopus 로고    scopus 로고
    • Suppression of polyglutamine protein toxicity by co-expression of a heat-shock protein 40 and a heat-shock protein 110
    • Kuo, Y., Ren, S., Lao, U., Edgar, B. A., and Wang, T. (2013). Suppression of polyglutamine protein toxicity by co-expression of a heat-shock protein 40 and a heat-shock protein 110. Cell Death Dis. 4, e833. doi: 10.1038/cddis.2013.351
    • (2013) Cell Death Dis , vol.4 , pp. e833
    • Kuo, Y.1    Ren, S.2    Lao, U.3    Edgar, B.A.4    Wang, T.5
  • 50
  • 51
    • 0037077211 scopus 로고    scopus 로고
    • Identification of essential residues in the type II Hsp40 Sis1 that function in polypeptide binding
    • Lee, S., Fan, C. Y., Younger, J. M., Ren, H., and Cyr, D. M. (2002). Identification of essential residues in the type II Hsp40 Sis1 that function in polypeptide binding. J. Biol. Chem. 277, 21675-21682. doi: 10.1074/jbc. M111075200
    • (2002) J. Biol. Chem , vol.277 , pp. 21675-21682
    • Lee, S.1    Fan, C.Y.2    Younger, J.M.3    Ren, H.4    Cyr, D.M.5
  • 52
    • 33845641051 scopus 로고    scopus 로고
    • The Arabidopsis ClpB/Hsp100 family of proteins: chaperones for stress and chloroplast development
    • Lee, U., Rioflorido, I., Hong, S. W., Larkindale, J., Waters, E. R., and Vierling, E. (2007). The Arabidopsis ClpB/Hsp100 family of proteins: chaperones for stress and chloroplast development. Plant J. 49, 115-127. doi: 10.1111/j.1365-313x.2006.02940.x
    • (2007) Plant J , vol.49 , pp. 115-127
    • Lee, U.1    Rioflorido, I.2    Hong, S.W.3    Larkindale, J.4    Waters, E.R.5    Vierling, E.6
  • 53
    • 1542267796 scopus 로고    scopus 로고
    • Cytoplasmic aggregates trap polyglutamine-containing proteins and block axonal transport in a Drosophila model of Huntington's disease
    • Lee, W. C., Yoshihara, M., and Littleton, J. T. (2004). Cytoplasmic aggregates trap polyglutamine-containing proteins and block axonal transport in a Drosophila model of Huntington's disease. Proc. Natl. Acad. Sci. U.S.A. 101, 3224-3229. doi: 10.1073/pnas.0400243101
    • (2004) Proc. Natl. Acad. Sci. U.S.A , vol.101 , pp. 3224-3229
    • Lee, W.C.1    Yoshihara, M.2    Littleton, J.T.3
  • 54
    • 0029079045 scopus 로고
    • Identification of a major subfamily of large hsp70-like proteins through the cloning of the mammalian 110-kDa heat shock protein
    • Lee-Yoon, D., Easton, D., Murawski, M., Burd, R., and Subjeck, J. R. (1995). Identification of a major subfamily of large hsp70-like proteins through the cloning of the mammalian 110-kDa heat shock protein. J. Biol. Chem. 270, 15725-15733. doi: 10.1074/jbc.270.26.15725
    • (1995) J. Biol. Chem , vol.270 , pp. 15725-15733
    • Lee-Yoon, D.1    Easton, D.2    Murawski, M.3    Burd, R.4    Subjeck, J.R.5
  • 55
    • 0345299781 scopus 로고    scopus 로고
    • The crystal structure of the yeast Hsp40 Ydj1 complexed with its peptide substrate
    • Li, J., Qian, X., and Sha, B. (2003). The crystal structure of the yeast Hsp40 Ydj1 complexed with its peptide substrate. Structure 11, 1475-1483. doi: 10.1016/j.str.2003.10.012
    • (2003) Structure , vol.11 , pp. 1475-1483
    • Li, J.1    Qian, X.2    Sha, B.3
  • 56
    • 84873802635 scopus 로고    scopus 로고
    • Disruption of ionic interactions between the nucleotide binding domain 1 (NBD1) and middle (M) domain in Hsp100 disaggregase unleashes toxic hyperactivity and partial independence from Hsp70
    • Lipinska, N., Zietkiewicz, S., Sobczak, A., Jurczyk, A., Potocki, W., Morawiec, E., et al. (2013). Disruption of ionic interactions between the nucleotide binding domain 1 (NBD1) and middle (M) domain in Hsp100 disaggregase unleashes toxic hyperactivity and partial independence from Hsp70. J. Biol. Chem. 288, 2857-2869. doi: 10.1074/jbc. M112.387589
    • (2013) J. Biol. Chem , vol.288 , pp. 2857-2869
    • Lipinska, N.1    Zietkiewicz, S.2    Sobczak, A.3    Jurczyk, A.4    Potocki, W.5    Morawiec, E.6
  • 57
    • 34848869936 scopus 로고    scopus 로고
    • Insights into Hsp70 chaperone activity from a crystal structure of the yeast Hsp110 Sse1
    • Liu, Q., and Hendrickson, W. A. (2007). Insights into Hsp70 chaperone activity from a crystal structure of the yeast Hsp110 Sse1. Cell 131, 106-120. doi: 10.1016/j.cell.2007.08.039
    • (2007) Cell , vol.131 , pp. 106-120
    • Liu, Q.1    Hendrickson, W.A.2
  • 58
    • 33744964531 scopus 로고    scopus 로고
    • Tid1 isoforms are mitochondrial DnaJ-like chaperones with unique carboxyl termini that determine cytosolic fate
    • Lu, B., Garrido, N., Spelbrink, J. N., and Suzuki, C. K. (2006). Tid1 isoforms are mitochondrial DnaJ-like chaperones with unique carboxyl termini that determine cytosolic fate. J. Biol. Chem. 281, 13150-13158. doi: 10.1074/jbc. M509179200
    • (2006) J. Biol. Chem , vol.281 , pp. 13150-13158
    • Lu, B.1    Garrido, N.2    Spelbrink, J.N.3    Suzuki, C.K.4
  • 59
    • 84905491871 scopus 로고    scopus 로고
    • Autophagic clearance of polyQ proteins mediated by ubiquitin-Atg8 adaptors of the conserved CUET protein family
    • Lu, K., Psakhye, I., and Jentsch, S. (2014). Autophagic clearance of polyQ proteins mediated by ubiquitin-Atg8 adaptors of the conserved CUET protein family. Cell 158, 549-563. doi: 10.1016/j.cell.2014.05.048
    • (2014) Cell , vol.158 , pp. 549-563
    • Lu, K.1    Psakhye, I.2    Jentsch, S.3
  • 60
    • 0032561360 scopus 로고    scopus 로고
    • Protein folding activity of Hsp70 is modified differentially by the hsp40 co-chaperones Sis1 and Ydj1
    • Lu, Z., and Cyr, D. M. (1998). Protein folding activity of Hsp70 is modified differentially by the hsp40 co-chaperones Sis1 and Ydj1. J. Biol. Chem. 273, 27824-27830. doi: 10.1074/jbc.273.43.27824
    • (1998) J. Biol. Chem , vol.273 , pp. 27824-27830
    • Lu, Z.1    Cyr, D.M.2
  • 61
    • 3142657524 scopus 로고    scopus 로고
    • Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104
    • Lum, R., Tkach, J. M., Vierling, E., and Glover, J. R. (2004). Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104. J. Biol. Chem. 279, 29139-29146. doi: 10.1074/jbc. M403777200
    • (2004) J. Biol. Chem , vol.279 , pp. 29139-29146
    • Lum, R.1    Tkach, J.M.2    Vierling, E.3    Glover, J.R.4
  • 62
    • 84951908781 scopus 로고    scopus 로고
    • Large-Scale Conformational Transitions and Dimerization Are Encoded in the Amino-Acid Sequences of Hsp70 Chaperones
    • Malinverni, D., Marsili, S., Barducci, A., and De Los Rios, P. (2015). Large-Scale Conformational Transitions and Dimerization Are Encoded in the Amino-Acid Sequences of Hsp70 Chaperones. PLoS Comput. Biol. 11:e1004262. doi: 10.1371/journal.pcbi.1004262
    • (2015) PLoS Comput. Biol , vol.11
    • Malinverni, D.1    Marsili, S.2    Barducci, A.3    De Los Rios, P.4
  • 63
    • 84880515581 scopus 로고    scopus 로고
    • Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates
    • Mattoo, R. U., Sharma, S. K., Priya, S., Finka, A., and Goloubinoff, P. (2013). Hsp110 is a bona fide chaperone using ATP to unfold stable misfolded polypeptides and reciprocally collaborate with Hsp70 to solubilize protein aggregates. J. Biol. Chem. 288, 21399-21411. doi: 10.1074/jbc. M113.479253
    • (2013) J. Biol. Chem , vol.288 , pp. 21399-21411
    • Mattoo, R.U.1    Sharma, S.K.2    Priya, S.3    Finka, A.4    Goloubinoff, P.5
  • 64
    • 17044387386 scopus 로고    scopus 로고
    • Hsp70 chaperones: cellular functions and molecular mechanism
    • Mayer, M. P., and Bukau, B. (2005). Hsp70 chaperones: cellular functions and molecular mechanism. Cell. Mol. Life Sci. 62, 670-684. doi: 10.1007/s00018-004-4464-6
    • (2005) Cell. Mol. Life Sci , vol.62 , pp. 670-684
    • Mayer, M.P.1    Bukau, B.2
  • 65
    • 84924251038 scopus 로고    scopus 로고
    • Spatially organized aggregation of misfolded proteins as cellular stress defense strategy
    • Miller, S. B., Mogk, A., and Bukau, B. (2015). Spatially organized aggregation of misfolded proteins as cellular stress defense strategy. J. Mol. Biol. 427, 1564-1574. doi: 10.1016/j.jmb.2015.02.006
    • (2015) J. Mol. Biol , vol.427 , pp. 1564-1574
    • Miller, S.B.1    Mogk, A.2    Bukau, B.3
  • 66
    • 0033573135 scopus 로고    scopus 로고
    • Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB
    • Mogk, A., Tomoyasu, T., Goloubinoff, P., Rudiger, S., Röder, D., Langen, H., et al. (1999). Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB. EMBO J. 18, 6934-6949. doi: 10.1093/emboj/18.24.6934
    • (1999) EMBO J , vol.18 , pp. 6934-6949
    • Mogk, A.1    Tomoyasu, T.2    Goloubinoff, P.3    Rudiger, S.4    Röder, D.5    Langen, H.6
  • 67
    • 84933675876 scopus 로고    scopus 로고
    • Hsp70 forms antiparallel dimers stabilized by post-translational modifications to position clients for transfer to Hsp90
    • Morgner, N., Schmidt, C., Beilsten-Edmands, V., Ebong, I. O., Patel, N. A., Clerico, E. M., et al. (2015). Hsp70 forms antiparallel dimers stabilized by post-translational modifications to position clients for transfer to Hsp90. Cell Rep. 11, 759-769. doi: 10.1016/j.celrep.2015.03.063
    • (2015) Cell Rep , vol.11 , pp. 759-769
    • Morgner, N.1    Schmidt, C.2    Beilsten-Edmands, V.3    Ebong, I.O.4    Patel, N.A.5    Clerico, E.M.6
  • 68
    • 44849094781 scopus 로고    scopus 로고
    • Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging
    • Morimoto, R. I. (2008). Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging. Genes Dev. 22, 1427-1438. doi: 10.1101/gad.1657108
    • (2008) Genes Dev , vol.22 , pp. 1427-1438
    • Morimoto, R.I.1
  • 69
    • 0033594880 scopus 로고    scopus 로고
    • Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones
    • Motohashi, K., Watanabe, Y., Yohda, M., and Yoshida, M. (1999). Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones. Proc. Natl. Acad. Sci. U.S.A. 96, 7184-7189
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 7184-7189
    • Motohashi, K.1    Watanabe, Y.2    Yohda, M.3    Yoshida, M.4
  • 70
    • 84933676860 scopus 로고    scopus 로고
    • Type 2 diabetes as a protein misfolding disease
    • Mukherjee, A., Morales-Scheihing, D., Butler, P. C., and Soto, C. (2015). Type 2 diabetes as a protein misfolding disease. Trends Mol. Med. 21, 439-449. doi: 10.1016/j.molmed.2015.04.005
    • (2015) Trends Mol. Med , vol.21 , pp. 439-449
    • Mukherjee, A.1    Morales-Scheihing, D.2    Butler, P.C.3    Soto, C.4
  • 71
    • 84892700864 scopus 로고    scopus 로고
    • Surface adsorption considerations when working with amyloid fibrils in multiwell plates and Eppendorf tubes
    • Murray, A. N., Palhano, F. L., Bieschke, J., and Kelly, J. W. (2013). Surface adsorption considerations when working with amyloid fibrils in multiwell plates and Eppendorf tubes. Prot. Sci. 22, 1531-1541. doi: 10.1002/pro.2339
    • (2013) Prot. Sci , vol.22 , pp. 1531-1541
    • Murray, A.N.1    Palhano, F.L.2    Bieschke, J.3    Kelly, J.W.4
  • 72
    • 84939559331 scopus 로고    scopus 로고
    • Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation
    • Nillegoda, N. B., Kirstein, J., Szlachcic, A., Berynskyy, M., Stank, A., Stengel, F., et al. (2015). Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation. Nature 524, 247-251. doi: 10.1038/nature14884
    • (2015) Nature , vol.524 , pp. 247-251
    • Nillegoda, N.B.1    Kirstein, J.2    Szlachcic, A.3    Berynskyy, M.4    Stank, A.5    Stengel, F.6
  • 73
    • 0001133526 scopus 로고    scopus 로고
    • Hsp110 protects heat-denatured proteins and confers cellular thermoresistance
    • Oh, H. J., Chen, X., and Subjeck, J. R. (1997). Hsp110 protects heat-denatured proteins and confers cellular thermoresistance. J. Biol. Chem. 272, 31636-31640. doi: 10.1074/jbc.272.50.31636
    • (1997) J. Biol. Chem , vol.272 , pp. 31636-31640
    • Oh, H.J.1    Chen, X.2    Subjeck, J.R.3
  • 74
    • 0000905027 scopus 로고    scopus 로고
    • The chaperoning activity of hsp110. Identification of functional domains by use of targeted deletions
    • Oh, H. J., Easton, D., Murawski, M., Kaneko, Y., and Subjeck, J. R. (1999). The chaperoning activity of hsp110. Identification of functional domains by use of targeted deletions. J. Biol. Chem. 274, 15712-15718. doi: 10.1074/jbc.274.22.15712
    • (1999) J. Biol. Chem , vol.274 , pp. 15712-15718
    • Oh, H.J.1    Easton, D.2    Murawski, M.3    Kaneko, Y.4    Subjeck, J.R.5
  • 75
    • 0033992538 scopus 로고    scopus 로고
    • Expression of APG-2 protein, a member of the heat shock protein 110 family, in developing rat brain
    • Okui, M., Ito, F., Ogita, K., Kuramoto, N., Kudoh, J., Shimizu, N., et al. (2000). Expression of APG-2 protein, a member of the heat shock protein 110 family, in developing rat brain. Neurochem. Int. 36, 35-43. doi: 10.1016/S0197-0186(99)00095-9
    • (2000) Neurochem. Int , vol.36 , pp. 35-43
    • Okui, M.1    Ito, F.2    Ogita, K.3    Kuramoto, N.4    Kudoh, J.5    Shimizu, N.6
  • 76
    • 78650963274 scopus 로고    scopus 로고
    • Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions
    • Olzscha, H., Schermann, S. M., Woerner, A. C., Pinkert, S., Hecht, M. H., Tartaglia, G. G., et al. (2011). Amyloid-like aggregates sequester numerous metastable proteins with essential cellular functions. Cell 144, 67-78. doi: 10.1016/j.cell.2010.11.050
    • (2011) Cell , vol.144 , pp. 67-78
    • Olzscha, H.1    Schermann, S.M.2    Woerner, A.C.3    Pinkert, S.4    Hecht, M.H.5    Tartaglia, G.G.6
  • 77
    • 84879920420 scopus 로고    scopus 로고
    • PolyQ proteins interfere with nuclear degradation of cytosolic proteins by sequestering the Sis1p chaperone
    • Park, S. H., Kukushkin, Y., Gupta, R., Chen, T., Konagai, A., Hipp, M. S., et al. (2013). PolyQ proteins interfere with nuclear degradation of cytosolic proteins by sequestering the Sis1p chaperone. Cell 154, 134-145. doi: 10.1016/j.cell.2013.06.003
    • (2013) Cell , vol.154 , pp. 134-145
    • Park, S.H.1    Kukushkin, Y.2    Gupta, R.3    Chen, T.4    Konagai, A.5    Hipp, M.S.6
  • 78
    • 0027996115 scopus 로고
    • Protein disaggregation mediated by heat-shock protein Hsp104
    • Parsell, D. A., Kowal, A. S., Singer, M. A., and Lindquist, S. (1994). Protein disaggregation mediated by heat-shock protein Hsp104. Nature 372, 475-478. doi: 10.1038/372475a0
    • (1994) Nature , vol.372 , pp. 475-478
    • Parsell, D.A.1    Kowal, A.S.2    Singer, M.A.3    Lindquist, S.4
  • 79
    • 0028283985 scopus 로고
    • Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases
    • Perutz, M. F., Johnson, T., Suzuki, M., and Finch, J. T. (1994). Glutamine repeats as polar zippers: their possible role in inherited neurodegenerative diseases. Proc. Natl. Acad. Sci. U.S.A. 91, 5355-5358. doi: 10.1073/pnas.91.12.5355
    • (1994) Proc. Natl. Acad. Sci. U.S.A , vol.91 , pp. 5355-5358
    • Perutz, M.F.1    Johnson, T.2    Suzuki, M.3    Finch, J.T.4
  • 80
    • 77955559261 scopus 로고    scopus 로고
    • Interaction of the Hsp110 molecular chaperones from S. cerevisiae with substrate protein
    • Polier, S., Hartl, F. U., and Bracher, A. (2010). Interaction of the Hsp110 molecular chaperones from S. cerevisiae with substrate protein. J. Mol. Biol. 401, 696-707. doi: 10.1016/j.jmb.2010.07.004
    • (2010) J. Mol. Biol , vol.401 , pp. 696-707
    • Polier, S.1    Hartl, F.U.2    Bracher, A.3
  • 81
    • 84863808563 scopus 로고    scopus 로고
    • Prion-like spread of protein aggregates in neurodegeneration
    • Polymenidou, M., and Cleveland, D. W. (2012). Prion-like spread of protein aggregates in neurodegeneration. J. Exp. Med. 209, 889-893. doi: 10.1084/jem.20120741
    • (2012) J. Exp. Med , vol.209 , pp. 889-893
    • Polymenidou, M.1    Cleveland, D.W.2
  • 82
    • 0034119621 scopus 로고    scopus 로고
    • Heat shock protein 101 plays a crucial role in thermotolerance in Arabidopsis
    • Queitsch, C., Hong, S. W., Vierling, E., and Lindquist, S. (2000). Heat shock protein 101 plays a crucial role in thermotolerance in Arabidopsis. Plant Cell 12, 479-492. doi: 10.1105/tpc.12.4.479
    • (2000) Plant Cell , vol.12 , pp. 479-492
    • Queitsch, C.1    Hong, S.W.2    Vierling, E.3    Lindquist, S.4
  • 83
    • 84868525116 scopus 로고    scopus 로고
    • Metazoan Hsp70 machines use Hsp110 to power protein disaggregation
    • Rampelt, H., Kirstein-Miles, J., Nillegoda, N. B., Chi, K., Scholz, S. R., Morimoto, R. I., et al. (2012). Metazoan Hsp70 machines use Hsp110 to power protein disaggregation. EMBO J. 31, 4221-4235. doi: 10.1038/emboj.2012.264
    • (2012) EMBO J , vol.31 , pp. 4221-4235
    • Rampelt, H.1    Kirstein-Miles, J.2    Nillegoda, N.B.3    Chi, K.4    Scholz, S.R.5    Morimoto, R.I.6
  • 84
    • 84934444265 scopus 로고    scopus 로고
    • Clearance of mutant aggregate-prone proteins by autophagy
    • Ravikumar, B., Sarkar, S., and Rubinsztein, D. C. (2008). Clearance of mutant aggregate-prone proteins by autophagy. Methods Mol. Biol. 445, 195-211. doi: 10.1007/978-1-59745-157-4_13
    • (2008) Methods Mol. Biol , vol.445 , pp. 195-211
    • Ravikumar, B.1    Sarkar, S.2    Rubinsztein, D.C.3
  • 85
    • 29344449706 scopus 로고    scopus 로고
    • Human and yeast Hsp110 chaperones exhibit functional differences
    • Raviol, H., Bukau, B., and Mayer, M. P. (2006a). Human and yeast Hsp110 chaperones exhibit functional differences. FEBS Lett. 580, 168-174. doi: 10.1016/j.febslet.2005.11.069
    • (2006) FEBS Lett , vol.580 , pp. 168-174
    • Raviol, H.1    Bukau, B.2    Mayer, M.P.3
  • 86
    • 33745749328 scopus 로고    scopus 로고
    • Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor
    • Raviol, H., Sadlish, H., Rodriguez, F., Mayer, M. P., and Bukau, B. (2006b). Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor. EMBO J. 25, 2510-2518. doi: 10.1038/sj.emboj.7601139
    • (2006) EMBO J , vol.25 , pp. 2510-2518
    • Raviol, H.1    Sadlish, H.2    Rodriguez, F.3    Mayer, M.P.4    Bukau, B.5
  • 87
    • 84892859905 scopus 로고    scopus 로고
    • Interactions between autophagy receptors and ubiquitin-like proteins form the molecular basis for selective autophagy
    • Rogov, V., Dötsch, V., Johansen, T., and Kirkin, V. (2014). Interactions between autophagy receptors and ubiquitin-like proteins form the molecular basis for selective autophagy. Mol. Cell 53, 167-178. doi: 10.1016/j.molcel.2013.12.014
    • (2014) Mol. Cell , vol.53 , pp. 167-178
    • Rogov, V.1    Dötsch, V.2    Johansen, T.3    Kirkin, V.4
  • 88
    • 84874393637 scopus 로고    scopus 로고
    • Unraveling the mechanism of protein disaggregation through a ClpB-DnaK interaction
    • Rosenzweig, R., Moradi, S., Zarrine-Afsar, A., Glover, J. R., and Kay, L. E. (2013). Unraveling the mechanism of protein disaggregation through a ClpB-DnaK interaction. Science 339, 1080-1083. doi: 10.1126/science.1233066
    • (2013) Science , vol.339 , pp. 1080-1083
    • Rosenzweig, R.1    Moradi, S.2    Zarrine-Afsar, A.3    Glover, J.R.4    Kay, L.E.5
  • 89
    • 34648857577 scopus 로고    scopus 로고
    • Different localization of Hsp105 family proteins in mammalian cells
    • Saito, Y., Yamagishi, N., and Hatayama, T. (2007). Different localization of Hsp105 family proteins in mammalian cells. Exp. Cell Res. 313, 3707-3717. doi: 10.1016/j.yexcr.2007.06.009
    • (2007) Exp. Cell Res , vol.313 , pp. 3707-3717
    • Saito, Y.1    Yamagishi, N.2    Hatayama, T.3
  • 90
    • 59449103206 scopus 로고    scopus 로고
    • Nuclear localization mechanism of Hsp105beta and its possible function in mammalian cells
    • Saito, Y., Yamagishi, N., and Hatayama, T. (2009). Nuclear localization mechanism of Hsp105beta and its possible function in mammalian cells. J. Biochem. 145, 185-191. doi: 10.1093/jb/mvn155
    • (2009) J. Biochem , vol.145 , pp. 185-191
    • Saito, Y.1    Yamagishi, N.2    Hatayama, T.3
  • 91
    • 0025193343 scopus 로고
    • HSP104 required for induced thermotolerance
    • Sanchez, Y., and Lindquist, S. L. (1990). HSP104 required for induced thermotolerance. Science 248, 1112-1115. doi: 10.1126/science.2188365
    • (1990) Science , vol.248 , pp. 1112-1115
    • Sanchez, Y.1    Lindquist, S.L.2
  • 92
    • 84926432180 scopus 로고    scopus 로고
    • A functional DnaK dimer is essential for the efficient interaction with Hsp40 heat shock protein
    • Sarbeng, E. B., Liu, Q., Tian, X., Yang, J., Li, H., Wong, J. L., et al. (2015). A functional DnaK dimer is essential for the efficient interaction with Hsp40 heat shock protein. J. Biol. Chem. 290, 8849-8862. doi: 10.1074/jbc. M114.596288
    • (2015) J. Biol. Chem , vol.290 , pp. 8849-8862
    • Sarbeng, E.B.1    Liu, Q.2    Tian, X.3    Yang, J.4    Li, H.5    Wong, J.L.6
  • 93
    • 84861749562 scopus 로고    scopus 로고
    • Human heat shock protein 105/110 kDa (Hsp105/110) regulates biogenesis and quality control of misfolded cystic fibrosis transmembrane conductance regulator at multiple levels
    • Saxena, A., Banasavadi-Siddegowda, Y. K., Fan, Y., Bhattacharya, S., Roy, G., Giovannucci, D. R., et al. (2012). Human heat shock protein 105/110 kDa (Hsp105/110) regulates biogenesis and quality control of misfolded cystic fibrosis transmembrane conductance regulator at multiple levels. J. Biol. Chem. 287, 19158-19170. doi: 10.1074/jbc. M111.297580
    • (2012) J. Biol. Chem , vol.287 , pp. 19158-19170
    • Saxena, A.1    Banasavadi-Siddegowda, Y.K.2    Fan, Y.3    Bhattacharya, S.4    Roy, G.5    Giovannucci, D.R.6
  • 95
    • 45849091944 scopus 로고    scopus 로고
    • Structure of the Hsp110:Hsc70 nucleotide exchange machine
    • Schuermann, J. P., Jiang, J., Cuellar, J., Llorca, O., Wang, L., Gimenez, L. E., et al. (2008). Structure of the Hsp110:Hsc70 nucleotide exchange machine. Mol. Cell 31, 232-243. doi: 10.1016/j.molcel.2008.05.006
    • (2008) Mol. Cell , vol.31 , pp. 232-243
    • Schuermann, J.P.1    Jiang, J.2    Cuellar, J.3    Llorca, O.4    Wang, L.5    Gimenez, L.E.6
  • 96
    • 84870792675 scopus 로고    scopus 로고
    • Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA+ disaggregase at aggregate surfaces
    • Seyffer, F., Kummer, E., Oguchi, Y., Winkler, J., Kumar, M., Zahn, R., et al. (2012). Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA+ disaggregase at aggregate surfaces. Nat. Struct. Mol. Biol. 19, 1347-1355. doi: 10.1038/nsmb.2442
    • (2012) Nat. Struct. Mol. Biol , vol.19 , pp. 1347-1355
    • Seyffer, F.1    Kummer, E.2    Oguchi, Y.3    Winkler, J.4    Kumar, M.5    Zahn, R.6
  • 97
    • 33845587149 scopus 로고    scopus 로고
    • Characterization of Hsp70 binding and nucleotide exchange by the yeast Hsp110 chaperone Sse1
    • Shaner, L., Sousa, R., and Morano, K. A. (2006). Characterization of Hsp70 binding and nucleotide exchange by the yeast Hsp110 chaperone Sse1. Biochemistry 45, 15075-15084. doi: 10.1021/bi061279k
    • (2006) Biochemistry , vol.45 , pp. 15075-15084
    • Shaner, L.1    Sousa, R.2    Morano, K.A.3
  • 98
    • 2542435778 scopus 로고    scopus 로고
    • The function of the yeast molecular chaperone Sse1 is mechanistically distinct from the closely related hsp70 family
    • Shaner, L., Trott, A., Goeckeler, J. L., Brodsky, J. L., and Morano, K. A. (2004). The function of the yeast molecular chaperone Sse1 is mechanistically distinct from the closely related hsp70 family. J. Biol. Chem. 279, 21992-22001. doi: 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
  • 99
    • 79955724860 scopus 로고    scopus 로고
    • Probing the different chaperone activities of the bacterial HSP70-HSP40 system using a thermolabile luciferase substrate
    • Sharma, S. K., De Los Rios, P., and Goloubinoff, P. (2011). Probing the different chaperone activities of the bacterial HSP70-HSP40 system using a thermolabile luciferase substrate. Proteins 79, 1991-1998. doi: 10.1002/prot.23024
    • (2011) Proteins , vol.79 , pp. 1991-1998
    • Sharma, S.K.1    De Los Rios, P.2    Goloubinoff, P.3
  • 100
    • 80054699747 scopus 로고    scopus 로고
    • The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system
    • Shorter, J. (2011). The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system. PLoS ONE 6:e26319. doi: 10.1371/journal.pone.0026319
    • (2011) PLoS ONE , vol.6
    • Shorter, J.1
  • 101
    • 0035936826 scopus 로고    scopus 로고
    • Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors
    • Sondermann, H., Scheufler, C., Schneider, C., Hohfeld, J., Hartl, F. U., and Moarefi, I. (2001). Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors. Science 291, 1553-1557. doi: 10.1126/science.1057268
    • (2001) Science , vol.291 , pp. 1553-1557
    • Sondermann, H.1    Scheufler, C.2    Schneider, C.3    Hohfeld, J.4    Hartl, F.U.5    Moarefi, I.6
  • 102
    • 84875845592 scopus 로고    scopus 로고
    • Molecular chaperone Hsp110 rescues a vesicle transport defect produced by an ALS-associated mutant SOD1 protein in squid axoplasm
    • Song, Y., Nagy, M., Ni, W., Tyagi, N. K., Fenton, W. A., Lopez-Giráldez, F., et al. (2013). Molecular chaperone Hsp110 rescues a vesicle transport defect produced by an ALS-associated mutant SOD1 protein in squid axoplasm. Proc. Natl. Acad. Sci. U.S.A. 110, 5428-5433. doi: 10.1073/pnas.1303279110
    • (2013) Proc. Natl. Acad. Sci. U.S.A , vol.110 , pp. 5428-5433
    • Song, Y.1    Nagy, M.2    Ni, W.3    Tyagi, N.K.4    Fenton, W.A.5    Lopez-Giráldez, F.6
  • 103
    • 33750996168 scopus 로고    scopus 로고
    • Keep the traffic moving: mechanism of the Hsp70 motor
    • Sousa, R., and Lafer, E. M. (2006). Keep the traffic moving: mechanism of the Hsp70 motor. Traffic 7, 1596-1603. doi: 10.1111/j.1600-0854.2006.00497.x
    • (2006) Traffic , vol.7 , pp. 1596-1603
    • Sousa, R.1    Lafer, E.M.2
  • 104
    • 0025799542 scopus 로고
    • ClpB is the Escherichia coli heat shock protein F84.1
    • Squires, C. L., Pedersen, S., Ross, B. M., and Squires, C. (1991). ClpB is the Escherichia coli heat shock protein F84.1. J. Bacteriol. 173, 4254-4262
    • (1991) J. Bacteriol , vol.173 , pp. 4254-4262
    • Squires, C.L.1    Pedersen, S.2    Ross, B.M.3    Squires, C.4
  • 105
    • 0041734594 scopus 로고    scopus 로고
    • Structural features required for the interaction of the Hsp70 molecular chaperone DnaK with its cochaperone DnaJ
    • Suh, W. C., Lu, C. Z., and Gross, C. A. (1999). Structural features required for the interaction of the Hsp70 molecular chaperone DnaK with its cochaperone DnaJ. J. Biol. Chem. 274, 30534-30539. doi: 10.1074/jbc.274.43.30534
    • (1999) J. Biol. Chem , vol.274 , pp. 30534-30539
    • Suh, W.C.1    Lu, C.Z.2    Gross, C.A.3
  • 106
    • 0037388418 scopus 로고    scopus 로고
    • Aggresomes protect cells by enhancing the degradation of toxic polyglutamine-containing protein
    • Taylor, J. P., Tanaka, F., Robitschek, J., Sandoval, C. M., Taye, A., Markovic-Plese, S., et al. (2003). Aggresomes protect cells by enhancing the degradation of toxic polyglutamine-containing protein. Hum. Mol. Genet. 12, 749-757. doi: 10.1093/hmg/ddg074
    • (2003) Hum. Mol. Genet , vol.12 , pp. 749-757
    • Taylor, J.P.1    Tanaka, F.2    Robitschek, J.3    Sandoval, C.M.4    Taye, A.5    Markovic-Plese, S.6
  • 107
    • 0034637603 scopus 로고    scopus 로고
    • Human DnaJ homologs dj2 and dj3, and bag-1 are positive cochaperones of hsc70
    • Terada, K., and Mori, M. (2000). Human DnaJ homologs dj2 and dj3, and bag-1 are positive cochaperones of hsc70. J. Biol. Chem. 275, 24728-24734. doi: 10.1074/jbc. M002021200
    • (2000) J. Biol. Chem , vol.275 , pp. 24728-24734
    • Terada, K.1    Mori, M.2
  • 108
    • 77952773873 scopus 로고    scopus 로고
    • Multiple molecules of Hsc70 and a dimer of DjA1 independently bind to an unfolded protein
    • Terada, K., and Oike, Y. (2010). Multiple molecules of Hsc70 and a dimer of DjA1 independently bind to an unfolded protein. J. Biol. Chem. 285, 16789-16797. doi: 10.1074/jbc. M110.101501
    • (2010) J. Biol. Chem , vol.285 , pp. 16789-16797
    • Terada, K.1    Oike, Y.2
  • 109
    • 40649098449 scopus 로고    scopus 로고
    • Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation
    • Tessarz, P., Mogk, A., and Bukau, B. (2008). Substrate threading through the central pore of the Hsp104 chaperone as a common mechanism for protein disaggregation and prion propagation. Mol. Microbiol. 68, 87-97. doi: 10.1111/j.1365-2958.2008.06135.x
    • (2008) Mol. Microbiol , vol.68 , pp. 87-97
    • Tessarz, P.1    Mogk, A.2    Bukau, B.3
  • 110
    • 0029871766 scopus 로고    scopus 로고
    • A conserved HPD sequence of the J-domain is necessary for YDJ1 stimulation of Hsp70 ATPase activity at a site distinct from substrate binding
    • Tsai, J., and Douglas, M. G. (1996). A conserved HPD sequence of the J-domain is necessary for YDJ1 stimulation of Hsp70 ATPase activity at a site distinct from substrate binding. J. Biol. Chem. 271, 9347-9354. doi: 10.1074/jbc.271.16.9347
    • (1996) J. Biol. Chem , vol.271 , pp. 9347-9354
    • Tsai, J.1    Douglas, M.G.2
  • 111
    • 77958487260 scopus 로고    scopus 로고
    • Cellular strategies for controlling protein aggregation
    • Tyedmers, J., Mogk, A., and Bukau, B. (2010). Cellular strategies for controlling protein aggregation. Nat. Rev. Mol. Cell Biol. 11, 777-788. doi: 10.1038/nrm2993
    • (2010) Nat. Rev. Mol. Cell Biol , vol.11 , pp. 777-788
    • Tyedmers, J.1    Mogk, A.2    Bukau, B.3
  • 112
    • 84878873702 scopus 로고    scopus 로고
    • Regulation of organismal proteostasis by transcellular chaperone signaling
    • Van Oosten-Hawle, P., Porter, R. S., and Morimoto, R. I. (2013). Regulation of organismal proteostasis by transcellular chaperone signaling. Cell 153, 1366-1378. doi: 10.1016/j.cell.2013.05.015
    • (2013) Cell , vol.153 , pp. 1366-1378
    • Van Oosten-Hawle, P.1    Porter, R.S.2    Morimoto, R.I.3
  • 113
    • 8844251486 scopus 로고    scopus 로고
    • Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB
    • Weibezahn, J., Tessarz, P., Schlieker, C., Zahn, R., Maglica, Z., Lee, S., et al. (2004). Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB. Cell 119, 653-665. doi: 10.1016/j.cell.2004.11.027
    • (2004) Cell , vol.119 , pp. 653-665
    • Weibezahn, J.1    Tessarz, P.2    Schlieker, C.3    Zahn, R.4    Maglica, Z.5    Lee, S.6
  • 114
    • 84864387363 scopus 로고    scopus 로고
    • Chaperone networks in protein disaggregation and prion propagation
    • Winkler, J., Tyedmers, J., Bukau, B., and Mogk, A. (2012a). Chaperone networks in protein disaggregation and prion propagation. J. Struct. Biol. 179, 152-160. doi: 10.1016/j.jsb.2012.05.002
    • (2012) J. Struct. Biol , vol.179 , pp. 152-160
    • Winkler, J.1    Tyedmers, J.2    Bukau, B.3    Mogk, A.4
  • 115
    • 84866438776 scopus 로고    scopus 로고
    • Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation
    • Winkler, J., Tyedmers, J., Bukau, B., and Mogk, A. (2012b). Hsp70 targets Hsp100 chaperones to substrates for protein disaggregation and prion fragmentation. J. Cell Biol. 198, 387-404. doi: 10.1083/jcb.201201074
    • (2012) J. Cell Biol , vol.198 , pp. 387-404
    • Winkler, J.1    Tyedmers, J.2    Bukau, B.3    Mogk, A.4
  • 116
    • 84863155446 scopus 로고    scopus 로고
    • Unique peptide substrate binding properties of 110-kDa heat-shock protein (Hsp110) determine its distinct chaperone activity
    • Xu, X., Sarbeng, E. B., Vorvis, C., Kumar, D. P., Zhou, L., and Liu, Q. (2012). Unique peptide substrate binding properties of 110-kDa heat-shock protein (Hsp110) determine its distinct chaperone activity. J. Biol. Chem. 287, 5661-5672. doi: 10.1074/jbc. M111.275057
    • (2012) J. Biol. Chem , vol.287 , pp. 5661-5672
    • Xu, X.1    Sarbeng, E.B.2    Vorvis, C.3    Kumar, D.P.4    Zhou, L.5    Liu, Q.6
  • 117
    • 0344009436 scopus 로고    scopus 로고
    • Hsp105 but not Hsp70 family proteins suppress the aggregation of heat-denatured protein in the presence of ADP
    • Yamagishi, N., Ishihara, K., Saito, Y., and Hatayama, T. (2003). Hsp105 but not Hsp70 family proteins suppress the aggregation of heat-denatured protein in the presence of ADP. FEBS Lett. 555, 390-396. doi: 10.1016/S0014-5793(03)01292-4
    • (2003) FEBS Lett , vol.555 , pp. 390-396
    • Yamagishi, N.1    Ishihara, K.2    Saito, Y.3    Hatayama, T.4
  • 118
    • 0034674304 scopus 로고    scopus 로고
    • Modulation of the chaperone activities of Hsc70/Hsp40 by Hsp105alpha and Hsp105beta
    • Yamagishi, N., Nishihori, H., Ishihara, K., Ohtsuka, K., and Hatayama, T. (2000). Modulation of the chaperone activities of Hsc70/Hsp40 by Hsp105alpha and Hsp105beta. Biochem. Biophys. Res. Commun. 272, 850-855. doi: 10.1006/bbrc.2000.2864
    • (2000) Biochem. Biophys. Res. Commun , vol.272 , pp. 850-855
    • Yamagishi, N.1    Nishihori, H.2    Ishihara, K.3    Ohtsuka, K.4    Hatayama, T.5
  • 119
    • 79956207695 scopus 로고    scopus 로고
    • Characterization of stress sensitivity and chaperone activity of Hsp105 in mammalian cells
    • Yamagishi, N., Yokota, M., Yasuda, K., Saito, Y., Nagata, K., and Hatayama, T. (2011). Characterization of stress sensitivity and chaperone activity of Hsp105 in mammalian cells. Biochem. Biophys. Res. Commun. 409, 90-95. doi: 10.1016/j.bbrc.2011.04.114
    • (2011) Biochem. Biophys. Res. Commun , vol.409 , pp. 90-95
    • Yamagishi, N.1    Yokota, M.2    Yasuda, K.3    Saito, Y.4    Nagata, K.5    Hatayama, T.6
  • 120
    • 34547893834 scopus 로고    scopus 로고
    • Heat-shock protein 105 interacts with and suppresses aggregation of mutant Cu/Zn superoxide dismutase: clues to a possible strategy for treating ALS
    • Yamashita, H., Kawamata, J., Okawa, K., Kanki, R., Nakamizo, T., Hatayama, T., et al. (2007). Heat-shock protein 105 interacts with and suppresses aggregation of mutant Cu/Zn superoxide dismutase: clues to a possible strategy for treating ALS. J. Neurochem. 102, 1497-1505. doi: 10.1111/j.1471-4159.2007.04534.x
    • (2007) J. Neurochem , vol.102 , pp. 1497-1505
    • Yamashita, H.1    Kawamata, J.2    Okawa, K.3    Kanki, R.4    Nakamizo, T.5    Hatayama, T.6
  • 121
    • 0029564092 scopus 로고
    • Cloning and expression of murine high molecular mass heat shock proteins, HSP105
    • Yasuda, K., Nakai, A., Hatayama, T., and Nagata, K. (1995). Cloning and expression of murine high molecular mass heat shock proteins, HSP105. J. Biol. Chem. 270, 29718-29723. doi: 10.1074/jbc.270.50.29718
    • (1995) J. Biol. Chem , vol.270 , pp. 29718-29723
    • Yasuda, K.1    Nakai, A.2    Hatayama, T.3    Nagata, K.4
  • 122
  • 123
    • 7244247277 scopus 로고    scopus 로고
    • Successive and synergistic action of the Hsp70 and Hsp100 chaperones in protein disaggregation
    • Zietkiewicz, S., Krzewska, J., and Liberek, K. (2004). Successive and synergistic action of the Hsp70 and Hsp100 chaperones in protein disaggregation. J. Biol. Chem. 279, 44376-44383. doi: 10.1074/jbc. M402405200
    • (2004) J. Biol. Chem , vol.279 , pp. 44376-44383
    • Zietkiewicz, S.1    Krzewska, J.2    Liberek, K.3
  • 124
    • 33646354916 scopus 로고    scopus 로고
    • Hsp70 chaperone machine remodels protein aggregates at the initial step of Hsp70-Hsp100-dependent disaggregation
    • Zietkiewicz, S., Lewandowska, A., Stocki, P., and Liberek, K. (2006). Hsp70 chaperone machine remodels protein aggregates at the initial step of Hsp70-Hsp100-dependent disaggregation. J. Biol. Chem. 281, 7022-7029. doi: 10.1074/jbc. M507893200
    • (2006) J. Biol. Chem , vol.281 , pp. 7022-7029
    • Zietkiewicz, S.1    Lewandowska, A.2    Stocki, P.3    Liberek, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.