메뉴 건너뛰기




Volumn 12, Issue 11, 2014, Pages

Modulation of the Maladaptive Stress Response to Manage Diseases of Protein Folding

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA 1 ANTITRYPSIN; CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; HEAT SHOCK TRANSCRIPTION FACTOR 1; PROTEIN P23; ALKYLATING AGENT; CFTR PROTEIN, HUMAN; DITERPENE; DNA BINDING PROTEIN; EPOXIDE; HEAT SHOCK TRANSCRIPTION FACTOR; ISOMERASE; PHENANTHRENE DERIVATIVE; PROSTAGLANDIN E SYNTHASE; TRANSCRIPTION FACTOR; TRIPTOLIDE;

EID: 84912572110     PISSN: 15449173     EISSN: 15457885     Source Type: Journal    
DOI: 10.1371/journal.pbio.1001998     Document Type: Article
Times cited : (73)

References (121)
  • 1
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • Balch WE, Morimoto RI, Dillin A, Kelly JW, (2008) Adapting proteostasis for disease intervention. Science 319: 916–919.
    • (2008) Science , vol.319 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 3
    • 84892475033 scopus 로고    scopus 로고
    • Comparing protein folding in vitro and in vivo: foldability meets the fitness challenge
    • Hingorani KS, Gierasch LM, (2014) Comparing protein folding in vitro and in vivo: foldability meets the fitness challenge. Curr Opin Struct Biol 24C: 81–90.
    • (2014) Curr Opin Struct Biol , vol.24C , pp. 81-90
    • Hingorani, K.S.1    Gierasch, L.M.2
  • 4
    • 84885372912 scopus 로고    scopus 로고
    • Quinary protein structure and the consequences of crowding in living cells: Leaving the test-tube behind
    • Wirth AJ, Gruebele M, (2013) Quinary protein structure and the consequences of crowding in living cells: Leaving the test-tube behind. Bioessays 35: 984–993 doi:10.1002/bies.201300080
    • (2013) Bioessays , vol.35 , pp. 984-993
    • Wirth, A.J.1    Gruebele, M.2
  • 5
    • 84875461582 scopus 로고    scopus 로고
    • Diversity in the origins of proteostasis networks–a driver for protein function in evolution
    • Powers ET, Balch WE, (2013) Diversity in the origins of proteostasis networks–a driver for protein function in evolution. Nat Rev Mol Cell Biol 14: 237–248.
    • (2013) Nat Rev Mol Cell Biol , vol.14 , pp. 237-248
    • Powers, E.T.1    Balch, W.E.2
  • 6
    • 84885144353 scopus 로고    scopus 로고
    • Q-bodies monitor the quinary state of the protein fold
    • Roth DM, Balch WE, (2013) Q-bodies monitor the quinary state of the protein fold. Nat Cell Biol 15: 1137–1139.
    • (2013) Nat Cell Biol , vol.15 , pp. 1137-1139
    • Roth, D.M.1    Balch, W.E.2
  • 8
    • 84866488172 scopus 로고    scopus 로고
    • The heat shock response: systems biology of proteotoxic stress in aging and disease
    • Morimoto RI, (2011) The heat shock response: systems biology of proteotoxic stress in aging and disease. Cold Spring Harb Symp Quant Biol 76: 91–99.
    • (2011) Cold Spring Harb Symp Quant Biol , vol.76 , pp. 91-99
    • Morimoto, R.I.1
  • 9
    • 84875450858 scopus 로고    scopus 로고
    • Hutt DM, Balch WE (2013) Expanding proteostasis by membrane trafficking networks. Cold Spring Harb Perspect Biol. doi:10.1101/cshperspect.a013383
    • (2013)
    • Hutt, D.M.1
  • 10
    • 79954414554 scopus 로고    scopus 로고
    • Modeling general proteostasis: proteome balance in health and disease
    • Roth DM, Balch WE, (2011) Modeling general proteostasis: proteome balance in health and disease. Curr Opin Cell Biol 23: 126–134.
    • (2011) Curr Opin Cell Biol , vol.23 , pp. 126-134
    • Roth, D.M.1    Balch, W.E.2
  • 11
    • 84896923527 scopus 로고    scopus 로고
    • Small molecule probes to quantify the functional fraction of a specific protein in a cell with minimal folding equilibrium shifts
    • Liu Y, Tan YL, Zhang X, Bhabha G, Ekiert DC, et al. (2014) Small molecule probes to quantify the functional fraction of a specific protein in a cell with minimal folding equilibrium shifts. Proc Natl Acad Sci U S A 111: 4449–4454 doi:10.1073/pnas.1323268111
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 4449-4454
    • Liu, Y.1    Tan, Y.L.2    Zhang, X.3    Bhabha, G.4    Ekiert, D.C.5
  • 12
    • 84894254592 scopus 로고    scopus 로고
    • Proteostasis and longevity: when does aging really begin?
    • Labbadia J, Morimoto RI, (2014) Proteostasis and longevity: when does aging really begin? F1000Prime Rep 6: 7.
    • (2014) F1000Prime Rep , vol.6 , pp. 7
    • Labbadia, J.1    Morimoto, R.I.2
  • 13
    • 84863882374 scopus 로고    scopus 로고
    • Integrating protein homeostasis strategies in prokaryotes
    • Mogk A, Huber D, Bukau B (2011) Integrating protein homeostasis strategies in prokaryotes. Cold Spring Harb Perspect Biol 3. doi:10.1101/cshperspect.a004366
    • (2011) Cold Spring Harb Perspect Biol , pp. 3
    • Mogk, A.1    Huber, D.2    Bukau, B.3
  • 15
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: from stress pathway to homeostatic regulation
    • Walter P, Ron D, (2011) The unfolded protein response: from stress pathway to homeostatic regulation. Science 334: 1081–1086.
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 16
    • 84883210213 scopus 로고    scopus 로고
    • Principles of cotranslational ubiquitination and quality control at the ribosome
    • Duttler S, Pechmann S, Frydman J, (2013) Principles of cotranslational ubiquitination and quality control at the ribosome. Mol Cell 50: 379–393.
    • (2013) Mol Cell , vol.50 , pp. 379-393
    • Duttler, S.1    Pechmann, S.2    Frydman, J.3
  • 17
    • 68649100255 scopus 로고    scopus 로고
    • The proteostasis boundary in misfolding diseases of membrane traffic
    • Hutt DM, Powers ET, Balch WE, (2009) The proteostasis boundary in misfolding diseases of membrane traffic. FEBS Lett 583: 2639–2646.
    • (2009) FEBS Lett , vol.583 , pp. 2639-2646
    • Hutt, D.M.1    Powers, E.T.2    Balch, W.E.3
  • 18
    • 84885095437 scopus 로고    scopus 로고
    • Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress
    • Escusa-Toret S, Vonk WI, Frydman J, (2013) Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress. Nat Cell Biol 15: 1231–1243.
    • (2013) Nat Cell Biol , vol.15 , pp. 1231-1243
    • Escusa-Toret, S.1    Vonk, W.I.2    Frydman, J.3
  • 19
    • 84878873702 scopus 로고    scopus 로고
    • Regulation of organismal proteostasis by transcellular chaperone signaling
    • van Oosten-Hawle P, Porter RS, Morimoto RI, (2013) Regulation of organismal proteostasis by transcellular chaperone signaling. Cell 153: 1366–1378.
    • (2013) Cell , vol.153 , pp. 1366-1378
    • van Oosten-Hawle, P.1    Porter, R.S.2    Morimoto, R.I.3
  • 20
    • 84857496780 scopus 로고    scopus 로고
    • Macro-level modeling of the response of C. elegans reproduction to chronic heat stress
    • McMullen PD, Aprison EZ, Winter PB, Amaral LA, Morimoto RI, et al. (2012) Macro-level modeling of the response of C. elegans reproduction to chronic heat stress. PLoS Comput Biol 8: e1002338.
    • (2012) PLoS Comput Biol , vol.8 , pp. e1002338
    • McMullen, P.D.1    Aprison, E.Z.2    Winter, P.B.3    Amaral, L.A.4    Morimoto, R.I.5
  • 21
    • 84879343155 scopus 로고    scopus 로고
    • XBP-1 is a cell-nonautonomous regulator of stress resistance and longevity
    • Taylor RC, Dillin A, (2013) XBP-1 is a cell-nonautonomous regulator of stress resistance and longevity. Cell 153: 1435–1447.
    • (2013) Cell , vol.153 , pp. 1435-1447
    • Taylor, R.C.1    Dillin, A.2
  • 23
    • 84891429025 scopus 로고    scopus 로고
    • The good and the bad of being connected: the integrons of aging
    • Dillin A, Gottschling DE, Nystrom T, (2014) The good and the bad of being connected: the integrons of aging. Curr Opin Cell Biol 26C: 107–112.
    • (2014) Curr Opin Cell Biol , vol.26C , pp. 107-112
    • Dillin, A.1    Gottschling, D.E.2    Nystrom, T.3
  • 24
    • 84894539428 scopus 로고    scopus 로고
    • Systemic stress signalling: understanding the cell non-autonomous control of proteostasis
    • Taylor RC, Berendzen KM, Dillin A, (2014) Systemic stress signalling: understanding the cell non-autonomous control of proteostasis. Nat Rev Mol Cell Biol 15: 211–217.
    • (2014) Nat Rev Mol Cell Biol , vol.15 , pp. 211-217
    • Taylor, R.C.1    Berendzen, K.M.2    Dillin, A.3
  • 25
    • 79959463520 scopus 로고    scopus 로고
    • Regulation of HSF1 function in the heat stress response: implications in aging and disease
    • Anckar J, Sistonen L, (2011) Regulation of HSF1 function in the heat stress response: implications in aging and disease. Annu Rev Biochem 80: 1089–1115.
    • (2011) Annu Rev Biochem , vol.80 , pp. 1089-1115
    • Anckar, J.1    Sistonen, L.2
  • 26
    • 0025737837 scopus 로고
    • Heat shock: the role of transient inducible responses in cell damage, transformation, and differentiation
    • Morimoto RI, (1991) Heat shock: the role of transient inducible responses in cell damage, transformation, and differentiation. Cancer Cells 3: 295–301.
    • (1991) Cancer Cells , vol.3 , pp. 295-301
    • Morimoto, R.I.1
  • 27
    • 77954955686 scopus 로고    scopus 로고
    • Heat shock factors: integrators of cell stress, development and lifespan
    • Akerfelt M, Morimoto RI, Sistonen L, (2010) Heat shock factors: integrators of cell stress, development and lifespan. Nat Rev Mol Cell Biol 11: 545–555.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 545-555
    • Akerfelt, M.1    Morimoto, R.I.2    Sistonen, L.3
  • 28
    • 84864585171 scopus 로고    scopus 로고
    • HSF1 drives a transcriptional program distinct from heat shock to support highly malignant human cancers
    • Mendillo ML, Santagata S, Koeva M, Bell GW, Hu R, et al. (2012) HSF1 drives a transcriptional program distinct from heat shock to support highly malignant human cancers. Cell 150: 549–562.
    • (2012) Cell , vol.150 , pp. 549-562
    • Mendillo, M.L.1    Santagata, S.2    Koeva, M.3    Bell, G.W.4    Hu, R.5
  • 29
    • 1542373742 scopus 로고    scopus 로고
    • The role of heat shock transcription factor 1 in the genome-wide regulation of the mammalian heat shock response
    • Trinklein ND, Murray JI, Hartman SJ, Botstein D, Myers RM, (2004) The role of heat shock transcription factor 1 in the genome-wide regulation of the mammalian heat shock response. Mol Biol Cell 15: 1254–1261.
    • (2004) Mol Biol Cell , vol.15 , pp. 1254-1261
    • Trinklein, N.D.1    Murray, J.I.2    Hartman, S.J.3    Botstein, D.4    Myers, R.M.5
  • 30
    • 33751092252 scopus 로고    scopus 로고
    • Genome-wide analysis of human HSF1 signaling reveals a transcriptional program linked to cellular adaptation and survival
    • Page TJ, Sikder D, Yang L, Pluta L, Wolfinger RD, et al. (2006) Genome-wide analysis of human HSF1 signaling reveals a transcriptional program linked to cellular adaptation and survival. Mol Biosyst 2: 627–639.
    • (2006) Mol Biosyst , vol.2 , pp. 627-639
    • Page, T.J.1    Sikder, D.2    Yang, L.3    Pluta, L.4    Wolfinger, R.D.5
  • 31
    • 84879829589 scopus 로고    scopus 로고
    • Biochemistry of Amyloid beta-Protein and Amyloid Deposits in Alzheimer Disease
    • Masters CL, Selkoe DJ, (2012) Biochemistry of Amyloid beta-Protein and Amyloid Deposits in Alzheimer Disease. Cold Spring Harb Perspect Med 2: a006262.
    • (2012) Cold Spring Harb Perspect Med , vol.2 , pp. a006262
    • Masters, C.L.1    Selkoe, D.J.2
  • 32
    • 79551604651 scopus 로고    scopus 로고
    • Alpha-1-antitrypsin deficiency: importance of proteasomal and autophagic degradative pathways in disposal of liver disease-associated protein aggregates
    • Perlmutter DH, (2011) Alpha-1-antitrypsin deficiency: importance of proteasomal and autophagic degradative pathways in disposal of liver disease-associated protein aggregates. Annu Rev Med 62: 333–345.
    • (2011) Annu Rev Med , vol.62 , pp. 333-345
    • Perlmutter, D.H.1
  • 33
    • 84868334619 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor (HDACi) suberoylanilide hydroxamic acid (SAHA)-mediated correction of alpha1-antitrypsin deficiency
    • Bouchecareilh M, Hutt DM, Szajner P, Flotte TR, Balch WE, (2012) Histone deacetylase inhibitor (HDACi) suberoylanilide hydroxamic acid (SAHA)-mediated correction of alpha1-antitrypsin deficiency. J Biol Chem 287: 38265–38278.
    • (2012) J Biol Chem , vol.287 , pp. 38265-38278
    • Bouchecareilh, M.1    Hutt, D.M.2    Szajner, P.3    Flotte, T.R.4    Balch, W.E.5
  • 34
    • 84863509037 scopus 로고    scopus 로고
    • Emergent properties of proteostasis in managing cystic fibrosis
    • Balch WE, Roth DM, Hutt DM (2011) Emergent properties of proteostasis in managing cystic fibrosis. Cold Spring Harb Perspect Biol 3: doi:10.1101/cshperspect.a004499
    • (2011)
    • Balch, W.E.1    Roth, D.M.2    Hutt, D.M.3
  • 35
    • 84863533791 scopus 로고    scopus 로고
    • The stress of protein misfolding: from single cells to multicellular organisms
    • Gidalevitz T, Prahlad V, Morimoto RI (2011) The stress of protein misfolding: from single cells to multicellular organisms. Cold Spring Harb Perspect Biol 3. doi:10.1101/cshperspect.a009704
    • (2011) Cold Spring Harb Perspect Biol , pp. 3
    • Gidalevitz, T.1    Prahlad, V.2    Morimoto, R.I.3
  • 36
    • 25844466597 scopus 로고    scopus 로고
    • Heat shock response modulators as therapeutic tools for diseases of protein conformation
    • Westerheide SD, Morimoto RI, (2005) Heat shock response modulators as therapeutic tools for diseases of protein conformation. J Biol Chem 280: 33097–33100.
    • (2005) J Biol Chem , vol.280 , pp. 33097-33100
    • Westerheide, S.D.1    Morimoto, R.I.2
  • 37
    • 84882386037 scopus 로고    scopus 로고
    • Heat shock response activation exacerbates inclusion body formation in a cellular model of Huntington disease
    • Bersuker K, Hipp MS, Calamini B, Morimoto RI, Kopito RR, (2013) Heat shock response activation exacerbates inclusion body formation in a cellular model of Huntington disease. J Biol Chem 288: 23633–23638.
    • (2013) J Biol Chem , vol.288 , pp. 23633-23638
    • Bersuker, K.1    Hipp, M.S.2    Calamini, B.3    Morimoto, R.I.4    Kopito, R.R.5
  • 39
    • 84880438841 scopus 로고    scopus 로고
    • Tight coordination of protein translation and HSF1 activation supports the anabolic malignant state
    • Santagata S, Mendillo ML, Tang YC, Subramanian A, Perley CC, et al. (2013) Tight coordination of protein translation and HSF1 activation supports the anabolic malignant state. Science 341: 1238303.
    • (2013) Science , vol.341 , pp. 1238303
    • Santagata, S.1    Mendillo, M.L.2    Tang, Y.C.3    Subramanian, A.4    Perley, C.C.5
  • 40
    • 84856089134 scopus 로고    scopus 로고
    • Small-molecule proteostasis regulators for protein conformational diseases
    • Calamini B, Silva MC, Madoux F, Hutt DM, Khanna S, et al. (2012) Small-molecule proteostasis regulators for protein conformational diseases. Nat Chem Biol 8: 185–196.
    • (2012) Nat Chem Biol , vol.8 , pp. 185-196
    • Calamini, B.1    Silva, M.C.2    Madoux, F.3    Hutt, D.M.4    Khanna, S.5
  • 41
    • 77955844171 scopus 로고    scopus 로고
    • Chaperone networks: tipping the balance in protein folding diseases
    • Voisine C, Pedersen JS, Morimoto RI, (2010) Chaperone networks: tipping the balance in protein folding diseases. Neurobiol Dis 40: 12–20.
    • (2010) Neurobiol Dis , vol.40 , pp. 12-20
    • Voisine, C.1    Pedersen, J.S.2    Morimoto, R.I.3
  • 42
  • 43
    • 0028150986 scopus 로고
    • Activation of the DNA-binding ability of human heat shock transcription factor 1 may involve the transition from an intramolecular to an intermolecular triple-stranded coiled-coil structure
    • Zuo J, Baler R, Dahl G, Voellmy R, (1994) Activation of the DNA-binding ability of human heat shock transcription factor 1 may involve the transition from an intramolecular to an intermolecular triple-stranded coiled-coil structure. Mol Cell Biol 14: 7557–7568.
    • (1994) Mol Cell Biol , vol.14 , pp. 7557-7568
    • Zuo, J.1    Baler, R.2    Dahl, G.3    Voellmy, R.4
  • 44
    • 0030049318 scopus 로고    scopus 로고
    • The regulatory domain of human heat shock factor 1 is sufficient to sense heat stress
    • Newton EM, Knauf U, Green M, Kingston RE, (1996) The regulatory domain of human heat shock factor 1 is sufficient to sense heat stress. Mol Cell Biol 16: 839–846.
    • (1996) Mol Cell Biol , vol.16 , pp. 839-846
    • Newton, E.M.1    Knauf, U.2    Green, M.3    Kingston, R.E.4
  • 45
    • 80053371954 scopus 로고    scopus 로고
    • Firefly luciferase mutants as sensors of proteome stress
    • Gupta R, Kasturi P, Bracher A, Loew C, Zheng M, et al. (2011) Firefly luciferase mutants as sensors of proteome stress. Nat Methods 8: 879–884.
    • (2011) Nat Methods , vol.8 , pp. 879-884
    • Gupta, R.1    Kasturi, P.2    Bracher, A.3    Loew, C.4    Zheng, M.5
  • 46
    • 77955655122 scopus 로고    scopus 로고
    • Trigger factor lacking the PPIase domain can enhance the folding of eukaryotic multi-domain proteins in Escherichia coli
    • Gupta R, Lakshmipathy SK, Chang HC, Etchells SA, Hartl FU, (2010) Trigger factor lacking the PPIase domain can enhance the folding of eukaryotic multi-domain proteins in Escherichia coli. FEBS Lett 584: 3620–3624.
    • (2010) FEBS Lett , vol.584 , pp. 3620-3624
    • Gupta, R.1    Lakshmipathy, S.K.2    Chang, H.C.3    Etchells, S.A.4    Hartl, F.U.5
  • 47
    • 77955559261 scopus 로고    scopus 로고
    • Interaction of the Hsp110 molecular chaperones from S. cerevisiae with substrate protein
    • Polier S, Hartl FU, Bracher A, (2010) Interaction of the Hsp110 molecular chaperones from S. cerevisiae with substrate protein. J Mol Biol 401: 696–707.
    • (2010) J Mol Biol , vol.401 , pp. 696-707
    • Polier, S.1    Hartl, F.U.2    Bracher, A.3
  • 48
    • 1942421714 scopus 로고    scopus 로고
    • Function of trigger factor and DnaK in multidomain protein folding: increase in yield at the expense of folding speed
    • Agashe VR, Guha S, Chang HC, Genevaux P, Hayer-Hartl M, et al. (2004) Function of trigger factor and DnaK in multidomain protein folding: increase in yield at the expense of folding speed. Cell 117: 199–209.
    • (2004) Cell , vol.117 , pp. 199-209
    • Agashe, V.R.1    Guha, S.2    Chang, H.C.3    Genevaux, P.4    Hayer-Hartl, M.5
  • 49
    • 84879996292 scopus 로고    scopus 로고
    • Noninvasive monitoring of oxidative stress in transplanted mesenchymal stromal cells
    • Psaltis PJ, Peterson KM, Xu R, Franchi F, Witt T, et al. (2013) Noninvasive monitoring of oxidative stress in transplanted mesenchymal stromal cells. JACC Cardiovasc Imaging 6: 795–802.
    • (2013) JACC Cardiovasc Imaging , vol.6 , pp. 795-802
    • Psaltis, P.J.1    Peterson, K.M.2    Xu, R.3    Franchi, F.4    Witt, T.5
  • 50
    • 39349083349 scopus 로고    scopus 로고
    • A highly sensitive assay for monitoring the secretory pathway and ER stress
    • Badr CE, Hewett JW, Breakefield XO, Tannous BA, (2007) A highly sensitive assay for monitoring the secretory pathway and ER stress. PLoS ONE 2: e571.
    • (2007) PLoS ONE , vol.2 , pp. e571
    • Badr, C.E.1    Hewett, J.W.2    Breakefield, X.O.3    Tannous, B.A.4
  • 51
    • 0033499798 scopus 로고    scopus 로고
    • Multiple components of the HSP90 chaperone complex function in regulation of heat shock factor 1 In vivo
    • Bharadwaj S, Ali A, Ovsenek N, (1999) Multiple components of the HSP90 chaperone complex function in regulation of heat shock factor 1 In vivo. Mol Cell Biol 19: 8033–8041.
    • (1999) Mol Cell Biol , vol.19 , pp. 8033-8041
    • Bharadwaj, S.1    Ali, A.2    Ovsenek, N.3
  • 52
    • 84934443868 scopus 로고    scopus 로고
    • Heat shock factor 1 as a coordinator of stress and developmental pathways
    • Anckar J, Sistonen L, (2007) Heat shock factor 1 as a coordinator of stress and developmental pathways. Adv Exp Med Biol 594: 78–88.
    • (2007) Adv Exp Med Biol , vol.594 , pp. 78-88
    • Anckar, J.1    Sistonen, L.2
  • 53
    • 53849149321 scopus 로고    scopus 로고
    • Chemical and biological folding contribute to temperature-sensitive DeltaF508 CFTR trafficking
    • Wang X, Koulov AV, Kellner WA, Riordan JR, Balch WE, (2008) Chemical and biological folding contribute to temperature-sensitive DeltaF508 CFTR trafficking. Traffic 9: 1878–1893.
    • (2008) Traffic , vol.9 , pp. 1878-1893
    • Wang, X.1    Koulov, A.V.2    Kellner, W.A.3    Riordan, J.R.4    Balch, W.E.5
  • 54
    • 0034102339 scopus 로고    scopus 로고
    • The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies
    • Freeman BC, Felts SJ, Toft DO, Yamamoto KR, (2000) The p23 molecular chaperones act at a late step in intracellular receptor action to differentially affect ligand efficacies. Genes Dev 14: 422–434.
    • (2000) Genes Dev , vol.14 , pp. 422-434
    • Freeman, B.C.1    Felts, S.J.2    Toft, D.O.3    Yamamoto, K.R.4
  • 55
    • 0037150683 scopus 로고    scopus 로고
    • Disassembly of transcriptional regulatory complexes by molecular chaperones
    • Freeman BC, Yamamoto KR, (2002) Disassembly of transcriptional regulatory complexes by molecular chaperones. Science 296: 2232–2235.
    • (2002) Science , vol.296 , pp. 2232-2235
    • Freeman, B.C.1    Yamamoto, K.R.2
  • 56
    • 77950428804 scopus 로고    scopus 로고
    • Reduced histone deacetylase 7 activity restores function to misfolded CFTR in cystic fibrosis
    • Hutt DM, Herman D, Rodrigues AP, Noel S, Pilewski JM, et al. (2010) Reduced histone deacetylase 7 activity restores function to misfolded CFTR in cystic fibrosis. Nat Chem Biol 6: 25–33.
    • (2010) Nat Chem Biol , vol.6 , pp. 25-33
    • Hutt, D.M.1    Herman, D.2    Rodrigues, A.P.3    Noel, S.4    Pilewski, J.M.5
  • 57
    • 81755163563 scopus 로고    scopus 로고
    • Correction of the F508del-CFTR protein processing defect in vitro by the investigational drug VX-809
    • Van Goor F, Hadida S, Grootenhuis PD, Burton B, Stack JH, et al. (2011) Correction of the F508del-CFTR protein processing defect in vitro by the investigational drug VX-809. Proc Natl Acad Sci U S A 108: 18843–18848.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 18843-18848
    • Van Goor, F.1    Hadida, S.2    Grootenhuis, P.D.3    Burton, B.4    Stack, J.H.5
  • 58
    • 84866137956 scopus 로고    scopus 로고
    • Progress in cystic fibrosis and the CF Therapeutics Development Network
    • Rowe SM, Borowitz DS, Burns JL, Clancy JP, Donaldson SH, et al. (2012) Progress in cystic fibrosis and the CF Therapeutics Development Network. Thorax 67: 882–890.
    • (2012) Thorax , vol.67 , pp. 882-890
    • Rowe, S.M.1    Borowitz, D.S.2    Burns, J.L.3    Clancy, J.P.4    Donaldson, S.H.5
  • 59
    • 84863511356 scopus 로고    scopus 로고
    • Proteostasis, an emerging therapeutic paradigm for managing inflammatory airway stress disease
    • Bouchecareilh M, Balch WE, (2012) Proteostasis, an emerging therapeutic paradigm for managing inflammatory airway stress disease. Curr Mol Med 12: 815–826.
    • (2012) Curr Mol Med , vol.12 , pp. 815-826
    • Bouchecareilh, M.1    Balch, W.E.2
  • 61
    • 0027465942 scopus 로고
    • The promoter region of the yeast KAR2 (BiP) gene contains a regulatory domain that responds to the presence of unfolded proteins in the endoplasmic reticulum
    • Kohno K, Normington K, Sambrook J, Gething MJ, Mori K, (1993) The promoter region of the yeast KAR2 (BiP) gene contains a regulatory domain that responds to the presence of unfolded proteins in the endoplasmic reticulum. Mol Cell Biol 13: 877–890.
    • (1993) Mol Cell Biol , vol.13 , pp. 877-890
    • Kohno, K.1    Normington, K.2    Sambrook, J.3    Gething, M.J.4    Mori, K.5
  • 62
    • 0035968205 scopus 로고    scopus 로고
    • Degradation of endoplasmic reticulum (ER) quality control substrates requires transport between the ER and Golgi
    • Caldwell SR, Hill KJ, Cooper AA, (2001) Degradation of endoplasmic reticulum (ER) quality control substrates requires transport between the ER and Golgi. J Biol Chem 276: 23296–23303.
    • (2001) J Biol Chem , vol.276 , pp. 23296-23303
    • Caldwell, S.R.1    Hill, K.J.2    Cooper, A.A.3
  • 63
    • 2942598422 scopus 로고    scopus 로고
    • Genome-wide analysis of the biology of stress responses through heat shock transcription factor
    • Hahn JS, Hu Z, Thiele DJ, Iyer VR, (2004) Genome-wide analysis of the biology of stress responses through heat shock transcription factor. Mol Cell Biol 24: 5249–5256.
    • (2004) Mol Cell Biol , vol.24 , pp. 5249-5256
    • Hahn, J.S.1    Hu, Z.2    Thiele, D.J.3    Iyer, V.R.4
  • 64
    • 43749115379 scopus 로고    scopus 로고
    • Niemann-Pick type C1 I1061T mutant encodes a functional protein that is selected for endoplasmic reticulum-associated degradation due to protein misfolding
    • Gelsthorpe ME, Baumann N, Millard E, Gale SE, Langmade SJ, et al. (2008) Niemann-Pick type C1 I1061T mutant encodes a functional protein that is selected for endoplasmic reticulum-associated degradation due to protein misfolding. J Biol Chem 283: 8229–8236.
    • (2008) J Biol Chem , vol.283 , pp. 8229-8236
    • Gelsthorpe, M.E.1    Baumann, N.2    Millard, E.3    Gale, S.E.4    Langmade, S.J.5
  • 65
    • 84876000270 scopus 로고    scopus 로고
    • Spreading of a prion domain from cell-to-cell by vesicular transport in Caenorhabditis elegans
    • Nussbaum-Krammer CI, Park KW, Li L, Melki R, Morimoto RI, (2013) Spreading of a prion domain from cell-to-cell by vesicular transport in Caenorhabditis elegans. PLoS Genet 9: e1003351.
    • (2013) PLoS Genet , vol.9 , pp. e1003351
    • Nussbaum-Krammer, C.I.1    Park, K.W.2    Li, L.3    Melki, R.4    Morimoto, R.I.5
  • 66
    • 84883063789 scopus 로고    scopus 로고
    • The TFEB orthologue HLH-30 regulates autophagy and modulates longevity in Caenorhabditis elegans
    • Lapierre LR, De Magalhaes Filho CD, McQuary PR, Chu CC, Visvikis O, et al. (2013) The TFEB orthologue HLH-30 regulates autophagy and modulates longevity in Caenorhabditis elegans. Nat Commun 4: 2267.
    • (2013) Nat Commun , vol.4 , pp. 2267
    • Lapierre, L.R.1    De Magalhaes Filho, C.D.2    McQuary, P.R.3    Chu, C.C.4    Visvikis, O.5
  • 67
    • 0037418731 scopus 로고    scopus 로고
    • Transcriptional activity and DNA binding of heat shock factor-1 involve phosphorylation on threonine 142 by CK2
    • Soncin F, Zhang X, Chu B, Wang X, Asea A, et al. (2003) Transcriptional activity and DNA binding of heat shock factor-1 involve phosphorylation on threonine 142 by CK2. Biochem Biophys Res Commun 303: 700–706.
    • (2003) Biochem Biophys Res Commun , vol.303 , pp. 700-706
    • Soncin, F.1    Zhang, X.2    Chu, B.3    Wang, X.4    Asea, A.5
  • 68
    • 0028952749 scopus 로고
    • Aggregation of secreted amyloid beta-protein into sodium dodecyl sulfate-stable oligomers in cell culture
    • Podlisny MB, Ostaszewski BL, Squazzo SL, Koo EH, Rydell RE, et al. (1995) Aggregation of secreted amyloid beta-protein into sodium dodecyl sulfate-stable oligomers in cell culture. J Biol Chem 270: 9564–9570.
    • (1995) J Biol Chem , vol.270 , pp. 9564-9570
    • Podlisny, M.B.1    Ostaszewski, B.L.2    Squazzo, S.L.3    Koo, E.H.4    Rydell, R.E.5
  • 69
    • 77954358003 scopus 로고    scopus 로고
    • Progressive accumulation of amyloid-beta oligomers in Alzheimer's disease and in amyloid precursor protein transgenic mice is accompanied by selective alterations in synaptic scaffold proteins
    • Pham E, Crews L, Ubhi K, Hansen L, Adame A, et al. (2010) Progressive accumulation of amyloid-beta oligomers in Alzheimer's disease and in amyloid precursor protein transgenic mice is accompanied by selective alterations in synaptic scaffold proteins. FEBS J 277: 3051–3067.
    • (2010) FEBS J , vol.277 , pp. 3051-3067
    • Pham, E.1    Crews, L.2    Ubhi, K.3    Hansen, L.4    Adame, A.5
  • 70
    • 79960721785 scopus 로고    scopus 로고
    • A longitudinal study of behavioral deficits in an AbetaPP transgenic mouse model of Alzheimer's disease
    • Havas D, Hutter-Paier B, Ubhi K, Rockenstein E, Crailsheim K, et al. (2011) A longitudinal study of behavioral deficits in an AbetaPP transgenic mouse model of Alzheimer's disease. J Alzheimers Dis 25: 231–243.
    • (2011) J Alzheimers Dis , vol.25 , pp. 231-243
    • Havas, D.1    Hutter-Paier, B.2    Ubhi, K.3    Rockenstein, E.4    Crailsheim, K.5
  • 71
    • 84906220352 scopus 로고    scopus 로고
    • Altered proteostasis in aging and heat shock response in C. elegans revealed by analysis of the global and de novo synthesized proteome
    • Liang V, Ullrich M, Lam H, Chew YL, Banister S, et al. (2014) Altered proteostasis in aging and heat shock response in C. elegans revealed by analysis of the global and de novo synthesized proteome. Cell Mol Life Sci 71: 3339–3361 doi:10.1007/s00018-014-1558-7
    • (2014) Cell Mol Life Sci , vol.71 , pp. 3339-3361
    • Liang, V.1    Ullrich, M.2    Lam, H.3    Chew, Y.L.4    Banister, S.5
  • 72
    • 40649129442 scopus 로고    scopus 로고
    • Nonenzymatic posttranslational protein modifications in ageing
    • Soskic V, Groebe K, Schrattenholz A, (2008) Nonenzymatic posttranslational protein modifications in ageing. Exp Gerontol 43: 247–257.
    • (2008) Exp Gerontol , vol.43 , pp. 247-257
    • Soskic, V.1    Groebe, K.2    Schrattenholz, A.3
  • 74
    • 0027476419 scopus 로고
    • Stress-induced inhibition of protein synthesis initiation: modulation of initiation factor 2 and guanine nucleotide exchange factor activities following transient cerebral ischemia in the rat
    • Hu BR, Wieloch T, (1993) Stress-induced inhibition of protein synthesis initiation: modulation of initiation factor 2 and guanine nucleotide exchange factor activities following transient cerebral ischemia in the rat. J Neurosci 13: 1830–1838.
    • (1993) J Neurosci , vol.13 , pp. 1830-1838
    • Hu, B.R.1    Wieloch, T.2
  • 75
    • 78649775607 scopus 로고    scopus 로고
    • The primary folding defect and rescue of DeltaF508 CFTR emerge during translation of the mutant domain
    • Hoelen H, Kleizen B, Schmidt A, Richardson J, Charitou P, et al. (2010) The primary folding defect and rescue of DeltaF508 CFTR emerge during translation of the mutant domain. PLoS ONE 5: e15458.
    • (2010) PLoS ONE , vol.5 , pp. e15458
    • Hoelen, H.1    Kleizen, B.2    Schmidt, A.3    Richardson, J.4    Charitou, P.5
  • 76
    • 71949095400 scopus 로고    scopus 로고
    • Identification of inhibitors of HSF1 functional activity by high-content target-based screening
    • Au Q, Zhang Y, Barber JR, Ng SC, Zhang B, (2009) Identification of inhibitors of HSF1 functional activity by high-content target-based screening. J Biomol Screen 14: 1165–1175.
    • (2009) J Biomol Screen , vol.14 , pp. 1165-1175
    • Au, Q.1    Zhang, Y.2    Barber, J.R.3    Ng, S.C.4    Zhang, B.5
  • 78
    • 84869137686 scopus 로고    scopus 로고
    • Fixing cystic fibrosis by correcting CFTR domain assembly
    • Okiyoneda T, Lukacs GL, (2012) Fixing cystic fibrosis by correcting CFTR domain assembly. J Cell Biol 199: 199–204.
    • (2012) J Cell Biol , vol.199 , pp. 199-204
    • Okiyoneda, T.1    Lukacs, G.L.2
  • 79
    • 84862909346 scopus 로고    scopus 로고
    • Requirements for efficient correction of DeltaF508 CFTR revealed by analyses of evolved sequences
    • Mendoza JL, Schmidt A, Li Q, Nuvaga E, Barrett T, et al. (2012) Requirements for efficient correction of DeltaF508 CFTR revealed by analyses of evolved sequences. Cell 148: 164–174.
    • (2012) Cell , vol.148 , pp. 164-174
    • Mendoza, J.L.1    Schmidt, A.2    Li, Q.3    Nuvaga, E.4    Barrett, T.5
  • 80
    • 0026091893 scopus 로고
    • Increased synthesis and accumulation of heat shock 70 proteins in Alzheimer's disease
    • Perez N, Sugar J, Charya S, Johnson G, Merril C, et al. (1991) Increased synthesis and accumulation of heat shock 70 proteins in Alzheimer's disease. Brain Res Mol Brain Res 11: 249–254.
    • (1991) Brain Res Mol Brain Res , vol.11 , pp. 249-254
    • Perez, N.1    Sugar, J.2    Charya, S.3    Johnson, G.4    Merril, C.5
  • 81
    • 0032585829 scopus 로고    scopus 로고
    • Heat-shock protein 70 levels in brain of patients with Down syndrome and Alzheimer's disease
    • Yoo BC, Seidl R, Cairns N, Lubec G (1999) Heat-shock protein 70 levels in brain of patients with Down syndrome and Alzheimer's disease. J Neural Transm Suppl 57: 315–322.
    • (1999) J Neural Transm Suppl , vol.57 , pp. 315-322
    • Yoo, B.C.1    Seidl, R.2    Cairns, N.3    Lubec, G.4
  • 83
    • 0027376485 scopus 로고
    • Increased expression of heat-shock protein 27 kDa in Alzheimer disease: a preliminary study
    • Renkawek K, Bosman GJ, Gaestel M, (1993) Increased expression of heat-shock protein 27 kDa in Alzheimer disease: a preliminary study. Neuroreport 5: 14–16.
    • (1993) Neuroreport , vol.5 , pp. 14-16
    • Renkawek, K.1    Bosman, G.J.2    Gaestel, M.3
  • 84
    • 84885567675 scopus 로고    scopus 로고
    • Increased expression of heat shock protein 70 in chronic obstructive pulmonary disease
    • Dong J, Guo L, Liao Z, Zhang M, Zhang M, et al. (2013) Increased expression of heat shock protein 70 in chronic obstructive pulmonary disease. Int Immunopharmacol 17: 885–893.
    • (2013) Int Immunopharmacol , vol.17 , pp. 885-893
    • Dong, J.1    Guo, L.2    Liao, Z.3    Zhang, M.4    Zhang, M.5
  • 85
    • 84856629737 scopus 로고    scopus 로고
    • CFTR: folding, misfolding and correcting the DeltaF508 conformational defect
    • Lukacs GL, Verkman AS, (2012) CFTR: folding, misfolding and correcting the DeltaF508 conformational defect. Trends Mol Med 18: 81–91.
    • (2012) Trends Mol Med , vol.18 , pp. 81-91
    • Lukacs, G.L.1    Verkman, A.S.2
  • 86
    • 23144442469 scopus 로고    scopus 로고
    • A new pharmacology–drugging stressed folding pathways
    • Wiseman RL, Balch WE, (2005) A new pharmacology–drugging stressed folding pathways. Trends Mol Med 11: 347–350.
    • (2005) Trends Mol Med , vol.11 , pp. 347-350
    • Wiseman, R.L.1    Balch, W.E.2
  • 87
    • 36049032748 scopus 로고    scopus 로고
    • An adaptable standard for protein export from the endoplasmic reticulum
    • Wiseman RL, Powers ET, Buxbaum JN, Kelly JW, Balch WE, (2007) An adaptable standard for protein export from the endoplasmic reticulum. Cell 131: 809–821.
    • (2007) Cell , vol.131 , pp. 809-821
    • Wiseman, R.L.1    Powers, E.T.2    Buxbaum, J.N.3    Kelly, J.W.4    Balch, W.E.5
  • 88
  • 89
    • 71449108913 scopus 로고    scopus 로고
    • Reduced IGF-1 signaling delays age-associated proteotoxicity in mice
    • Cohen E, Paulsson JF, Blinder P, Burstyn-Cohen T, Du D, et al. (2009) Reduced IGF-1 signaling delays age-associated proteotoxicity in mice. Cell 139: 1157–1169.
    • (2009) Cell , vol.139 , pp. 1157-1169
    • Cohen, E.1    Paulsson, J.F.2    Blinder, P.3    Burstyn-Cohen, T.4    Du, D.5
  • 90
    • 0036678146 scopus 로고    scopus 로고
    • The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans
    • Morley JF, Brignull HR, Weyers JJ, Morimoto RI, (2002) The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans. Proc Natl Acad Sci U S A 99: 10417–10422.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 10417-10422
    • Morley, J.F.1    Brignull, H.R.2    Weyers, J.J.3    Morimoto, R.I.4
  • 91
    • 33745167938 scopus 로고    scopus 로고
    • Protein-misfolding diseases and chaperone-based therapeutic approaches
    • Chaudhuri TK, Paul S, (2006) Protein-misfolding diseases and chaperone-based therapeutic approaches. FEBS J 273: 1331–1349.
    • (2006) FEBS J , vol.273 , pp. 1331-1349
    • Chaudhuri, T.K.1    Paul, S.2
  • 92
    • 59649097036 scopus 로고    scopus 로고
    • Rab11a and HSP90 regulate recycling of extracellular alpha-synuclein
    • Liu J, Zhang JP, Shi M, Quinn T, Bradner J, et al. (2009) Rab11a and HSP90 regulate recycling of extracellular alpha-synuclein. J Neurosci 29: 1480–1485.
    • (2009) J Neurosci , vol.29 , pp. 1480-1485
    • Liu, J.1    Zhang, J.P.2    Shi, M.3    Quinn, T.4    Bradner, J.5
  • 93
    • 34247390079 scopus 로고    scopus 로고
    • Polyglutamine-mediated neurodegeneration: use of chaperones as prevention strategy
    • Paul S, (2007) Polyglutamine-mediated neurodegeneration: use of chaperones as prevention strategy. Biochemistry (Mosc) 72: 359–366.
    • (2007) Biochemistry (Mosc) , vol.72 , pp. 359-366
    • Paul, S.1
  • 94
    • 67849111948 scopus 로고    scopus 로고
    • Binding of Hsp90 to tau promotes a conformational change and aggregation of tau protein
    • Tortosa E, Santa-Maria I, Moreno F, Lim F, Perez M, et al. (2009) Binding of Hsp90 to tau promotes a conformational change and aggregation of tau protein. J Alzheimers Dis 17: 319–325.
    • (2009) J Alzheimers Dis , vol.17 , pp. 319-325
    • Tortosa, E.1    Santa-Maria, I.2    Moreno, F.3    Lim, F.4    Perez, M.5
  • 95
    • 84896837095 scopus 로고    scopus 로고
    • Hsp90-tau complex reveals molecular basis for specificity in chaperone action
    • Karagoz GE, Duarte AM, Akoury E, Ippel H, Biernat J, et al. (2014) Hsp90-tau complex reveals molecular basis for specificity in chaperone action. Cell 156: 963–974.
    • (2014) Cell , vol.156 , pp. 963-974
    • Karagoz, G.E.1    Duarte, A.M.2    Akoury, E.3    Ippel, H.4    Biernat, J.5
  • 96
    • 84879920420 scopus 로고    scopus 로고
    • PolyQ proteins interfere with nuclear degradation of cytosolic proteins by sequestering the Sis1p chaperone
    • Park SH, Kukushkin Y, Gupta R, Chen T, Konagai A, et al. (2013) PolyQ proteins interfere with nuclear degradation of cytosolic proteins by sequestering the Sis1p chaperone. Cell 154: 134–145.
    • (2013) Cell , vol.154 , pp. 134-145
    • Park, S.H.1    Kukushkin, Y.2    Gupta, R.3    Chen, T.4    Konagai, A.5
  • 97
    • 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, et al. (2001) Geldanamycin activates a heat shock response and inhibits huntingtin aggregation in a cell culture model of Huntington's disease. Hum Mol Genet 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
  • 99
    • 34547183507 scopus 로고    scopus 로고
    • Roles of heat-shock protein 90 in maintaining and facilitating the neurodegenerative phenotype in tauopathies
    • Luo W, Dou F, Rodina A, Chip S, Kim J, et al. (2007) Roles of heat-shock protein 90 in maintaining and facilitating the neurodegenerative phenotype in tauopathies. Proc Natl Acad Sci U S A 104: 9511–9516.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 9511-9516
    • Luo, W.1    Dou, F.2    Rodina, A.3    Chip, S.4    Kim, J.5
  • 100
    • 78649767505 scopus 로고    scopus 로고
    • Hsp90 regulates tau pathology through co-chaperone complexes in Alzheimer's disease
    • Salminen A, Ojala J, Kaarniranta K, Hiltunen M, Soininen H, (2011) Hsp90 regulates tau pathology through co-chaperone complexes in Alzheimer's disease. Prog Neurobiol 93: 99–110.
    • (2011) Prog Neurobiol , vol.93 , pp. 99-110
    • Salminen, A.1    Ojala, J.2    Kaarniranta, K.3    Hiltunen, M.4    Soininen, H.5
  • 101
    • 33644850056 scopus 로고    scopus 로고
    • Progressive disruption of cellular protein folding in models of polyglutamine diseases
    • Gidalevitz T, Ben-Zvi A, Ho KH, Brignull HR, Morimoto RI, (2006) Progressive disruption of cellular protein folding in models of polyglutamine diseases. Science 311: 1471–1474.
    • (2006) Science , vol.311 , pp. 1471-1474
    • Gidalevitz, T.1    Ben-Zvi, A.2    Ho, K.H.3    Brignull, H.R.4    Morimoto, R.I.5
  • 102
    • 33747053662 scopus 로고    scopus 로고
    • Polyglutamine proteins at the pathogenic threshold display neuron-specific aggregation in a pan-neuronal Caenorhabditis elegans model
    • Brignull HR, Moore FE, Tang SJ, Morimoto RI, (2006) Polyglutamine proteins at the pathogenic threshold display neuron-specific aggregation in a pan-neuronal Caenorhabditis elegans model. J Neurosci 26: 7597–7606.
    • (2006) J Neurosci , vol.26 , pp. 7597-7606
    • Brignull, H.R.1    Moore, F.E.2    Tang, S.J.3    Morimoto, R.I.4
  • 103
    • 84877309346 scopus 로고    scopus 로고
    • DAF-16 employs the chromatin remodeller SWI/SNF to promote stress resistance and longevity
    • Riedel CG, Dowen RH, Lourenco GF, Kirienko NV, Heimbucher T, et al. (2013) DAF-16 employs the chromatin remodeller SWI/SNF to promote stress resistance and longevity. Nat Cell Biol 15: 491–501.
    • (2013) Nat Cell Biol , vol.15 , pp. 491-501
    • Riedel, C.G.1    Dowen, R.H.2    Lourenco, G.F.3    Kirienko, N.V.4    Heimbucher, T.5
  • 104
    • 84860885335 scopus 로고    scopus 로고
    • Temporal requirements of heat shock factor-1 for longevity assurance
    • Volovik Y, Maman M, Dubnikov T, Bejerano-Sagie M, Joyce D, et al. (2012) Temporal requirements of heat shock factor-1 for longevity assurance. Aging Cell 11: 491–499.
    • (2012) Aging Cell , vol.11 , pp. 491-499
    • Volovik, Y.1    Maman, M.2    Dubnikov, T.3    Bejerano-Sagie, M.4    Joyce, D.5
  • 105
    • 84866182143 scopus 로고    scopus 로고
    • RPN-6 determines C. elegans longevity under proteotoxic stress conditions
    • Vilchez D, Morantte I, Liu Z, Douglas PM, Merkwirth C, et al. (2012) RPN-6 determines C. elegans longevity under proteotoxic stress conditions. Nature 489: 263–268.
    • (2012) Nature , vol.489 , pp. 263-268
    • Vilchez, D.1    Morantte, I.2    Liu, Z.3    Douglas, P.M.4    Merkwirth, C.5
  • 106
    • 79551678082 scopus 로고    scopus 로고
    • The endoplasmic reticulum-associated Hsp40 DNAJB12 and Hsc70 cooperate to facilitate RMA1 E3-dependent degradation of nascent CFTRDeltaF508
    • Grove DE, Fan CY, Ren HY, Cyr DM, (2011) The endoplasmic reticulum-associated Hsp40 DNAJB12 and Hsc70 cooperate to facilitate RMA1 E3-dependent degradation of nascent CFTRDeltaF508. Mol Biol Cell 22: 301–314.
    • (2011) Mol Biol Cell , vol.22 , pp. 301-314
    • Grove, D.E.1    Fan, C.Y.2    Ren, H.Y.3    Cyr, D.M.4
  • 107
    • 84896843332 scopus 로고    scopus 로고
    • Interplay of acetyltransferase EP300 and the proteasome system in regulating heat shock transcription factor 1
    • Raychaudhuri S, Loew C, Korner R, Pinkert S, Theis M, et al. (2014) Interplay of acetyltransferase EP300 and the proteasome system in regulating heat shock transcription factor 1. Cell 156: 975–985.
    • (2014) Cell , vol.156 , pp. 975-985
    • Raychaudhuri, S.1    Loew, C.2    Korner, R.3    Pinkert, S.4    Theis, M.5
  • 108
    • 84906794886 scopus 로고    scopus 로고
    • Proteostasis impairment in protein-misfolding and -aggregation diseases
    • Hipp MS, Park SH, Hartl FU, (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
  • 109
    • 84866167976 scopus 로고    scopus 로고
    • Increased proteasome activity in human embryonic stem cells is regulated by PSMD11
    • Vilchez D, Boyer L, Morantte I, Lutz M, Merkwirth C, et al. (2012) Increased proteasome activity in human embryonic stem cells is regulated by PSMD11. Nature 489: 304–308.
    • (2012) Nature , vol.489 , pp. 304-308
    • Vilchez, D.1    Boyer, L.2    Morantte, I.3    Lutz, M.4    Merkwirth, C.5
  • 110
    • 84892399560 scopus 로고    scopus 로고
    • Caenorhabditis elegans as a model system for studying non-cell-autonomous mechanisms in protein-misfolding diseases
    • Nussbaum-Krammer CI, Morimoto RI, (2014) Caenorhabditis elegans as a model system for studying non-cell-autonomous mechanisms in protein-misfolding diseases. Dis Model Mech 7: 31–39.
    • (2014) Dis Model Mech , vol.7 , pp. 31-39
    • Nussbaum-Krammer, C.I.1    Morimoto, R.I.2
  • 111
    • 78149452881 scopus 로고    scopus 로고
    • Protein homeostasis and the phenotypic manifestation of genetic diversity: principles and mechanisms
    • Jarosz DF, Taipale M, Lindquist S, (2010) Protein homeostasis and the phenotypic manifestation of genetic diversity: principles and mechanisms. Annu Rev Genet 44: 189–216.
    • (2010) Annu Rev Genet , vol.44 , pp. 189-216
    • Jarosz, D.F.1    Taipale, M.2    Lindquist, S.3
  • 112
    • 67649217159 scopus 로고    scopus 로고
    • Inhibiting the transcription factor HSF1 as an anticancer strategy
    • Whitesell L, Lindquist S, (2009) Inhibiting the transcription factor HSF1 as an anticancer strategy. Expert Opin Ther Targets 13: 469–478.
    • (2009) Expert Opin Ther Targets , vol.13 , pp. 469-478
    • Whitesell, L.1    Lindquist, S.2
  • 113
    • 84873419140 scopus 로고    scopus 로고
    • The ribosome as a hub for protein quality control
    • Pechmann S, Willmund F, Frydman J, (2013) The ribosome as a hub for protein quality control. Mol Cell 49: 411–421.
    • (2013) Mol Cell , vol.49 , pp. 411-421
    • Pechmann, S.1    Willmund, F.2    Frydman, J.3
  • 114
    • 84876406925 scopus 로고    scopus 로고
    • The role of mutational robustness in RNA virus evolution
    • Lauring AS, Frydman J, Andino R, (2013) The role of mutational robustness in RNA virus evolution. Nat Rev Microbiol 11: 327–336.
    • (2013) Nat Rev Microbiol , vol.11 , pp. 327-336
    • Lauring, A.S.1    Frydman, J.2    Andino, R.3
  • 115
    • 33846471075 scopus 로고    scopus 로고
    • Evolutionary constraints on chaperone-mediated folding provide an antiviral approach refractory to development of drug resistance
    • Geller R, Vignuzzi M, Andino R, Frydman J, (2007) Evolutionary constraints on chaperone-mediated folding provide an antiviral approach refractory to development of drug resistance. Genes Dev 21: 195–205.
    • (2007) Genes Dev , vol.21 , pp. 195-205
    • Geller, R.1    Vignuzzi, M.2    Andino, R.3    Frydman, J.4
  • 116
    • 77957740228 scopus 로고    scopus 로고
    • Protein folding sculpting evolutionary change
    • Lindquist S, (2009) Protein folding sculpting evolutionary change. Cold Spring Harb Symp Quant Biol 74: 103–108.
    • (2009) Cold Spring Harb Symp Quant Biol , vol.74 , pp. 103-108
    • Lindquist, S.1
  • 118
    • 84862641651 scopus 로고    scopus 로고
    • FK506 Binding Protein 8 Peptidylprolyl Isomerase Activity Manages a Late Stage of Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) Folding and Stability
    • Hutt DM, Roth DM, Chalfant MA, Youker RT, Matteson J, et al. (2012) FK506 Binding Protein 8 Peptidylprolyl Isomerase Activity Manages a Late Stage of Cystic Fibrosis Transmembrane Conductance Regulator (CFTR) Folding and Stability. J Biol Chem 287: 21914–21925.
    • (2012) J Biol Chem , vol.287 , pp. 21914-21925
    • Hutt, D.M.1    Roth, D.M.2    Chalfant, M.A.3    Youker, R.T.4    Matteson, J.5
  • 119
    • 33750842131 scopus 로고    scopus 로고
    • Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis
    • Wang X, Venable J, LaPointe P, Hutt DM, Koulov AV, et al. (2006) Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis. Cell 127: 803–815.
    • (2006) Cell , vol.127 , pp. 803-815
    • Wang, X.1    Venable, J.2    LaPointe, P.3    Hutt, D.M.4    Koulov, A.V.5
  • 120
    • 0035200620 scopus 로고    scopus 로고
    • Cell-based assay for high-throughput quantitative screening of CFTR chloride transport agonists
    • Galietta LV, Jayaraman S, Verkman AS, (2001) Cell-based assay for high-throughput quantitative screening of CFTR chloride transport agonists. Am J Physiol Cell Physiol 281: C1734–1742.
    • (2001) Am J Physiol Cell Physiol , vol.281 , pp. 1734-1742
    • Galietta, L.V.1    Jayaraman, S.2    Verkman, A.S.3
  • 121
    • 0035889404 scopus 로고    scopus 로고
    • Early formation of mature amyloid-beta protein deposits in a mutant APP transgenic model depends on levels of Abeta(1–42)
    • Rockenstein E, Mallory M, Mante M, Sisk A, Masliaha E, (2001) Early formation of mature amyloid-beta protein deposits in a mutant APP transgenic model depends on levels of Abeta(1–42). J Neurosci Res 66: 573–582.
    • (2001) J Neurosci Res , vol.66 , pp. 573-582
    • Rockenstein, E.1    Mallory, M.2    Mante, M.3    Sisk, A.4    Masliaha, E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.