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Volumn 16, Issue 8, 2015, Pages 17193-17230

Protein folding and mechanisms of proteostasis

Author keywords

Folding; Misfolding; Proteins; Proteostasis

Indexed keywords

4 (3 DIMETHYLAMINOPROPYLAMINO) 2 (4 METHOXYSTYRYL)QUINAZOLINE; 4 PHENYLBUTYRIC ACID; AMYLOID; CHAPERONE; GLUCOSE REGULATED PROTEIN 94; HEAT SHOCK TRANSCRIPTION FACTOR 1; INTRINSICALLY DISORDERED PROTEIN; PREALBUMIN; PROTEIN P53; TAFAMIDIS; TAUROURSODEOXYCHOLIC ACID;

EID: 84938117658     PISSN: 16616596     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms160817193     Document Type: Review
Times cited : (222)

References (256)
  • 1
    • 21844454763 scopus 로고    scopus 로고
    • Stress-induced variation in evolution: From behavioural plasticity to genetic assimilation
    • Badyaev, A.V. Stress-induced variation in evolution: From behavioural plasticity to genetic assimilation. Proc. Biol. Sci. 2005, 272, 877–886
    • (2005) Proc. Biol. Sci , vol.272 , pp. 877-886
    • Badyaev, A.V.1
  • 2
    • 84881493915 scopus 로고    scopus 로고
    • The spatial structure of cell signaling systems
    • Nussinov, R. The spatial structure of cell signaling systems. Phys. Biol. 2013, 10, 045004
    • (2013) Phys. Biol , vol.10
    • Nussinov, R.1
  • 3
    • 84896350648 scopus 로고    scopus 로고
    • A second molecular biology revolution? The energy landscapes of biomolecular function
    • Nussinov, R.; Wolynes, P.G. A second molecular biology revolution? The energy landscapes of biomolecular function. Phys. Chem. Chem. Phys. 2014, 16, 6321–6322
    • (2014) Phys. Chem. Chem. Phys , vol.16 , pp. 6321-6322
    • Nussinov, R.1    Wolynes, P.G.2
  • 4
    • 77953153048 scopus 로고    scopus 로고
    • Regulation of basal cellular physiology by the homeostatic unfolded protein response
    • Rutkowski, D.T.; Hegde, R.S. Regulation of basal cellular physiology by the homeostatic unfolded protein response. J. Cell Biol. 2010, 189, 783–794
    • (2010) J. Cell Biol , vol.189 , pp. 783-794
    • Rutkowski, D.T.1    Hegde, R.S.2
  • 5
    • 0033200063 scopus 로고    scopus 로고
    • Protein misfolding, evolution and disease
    • Dobson, C.M. Protein misfolding, evolution and disease. Trends Biochem. Sci. 1999, 24, 329–332
    • (1999) Trends Biochem. Sci , vol.24 , pp. 329-332
    • Dobson, C.M.1
  • 6
    • 2942627626 scopus 로고    scopus 로고
    • Hydrophobicity: An ancient damage-associated molecular pattern that initiates innate immune responses
    • Seong, S.Y.; Matzinger, P. Hydrophobicity: An ancient damage-associated molecular pattern that initiates innate immune responses. Nat. Rev. Immunol. 2004, 4, 469–478
    • (2004) Nat. Rev. Immunol , vol.4 , pp. 469-478
    • Seong, S.Y.1    Matzinger, P.2
  • 8
    • 34848929022 scopus 로고    scopus 로고
    • Favrin, G Structural reorganisation and potential toxicity of oligomeric species formed during the assembly of amyloid fibrils
    • Cheon, M.; Chang, I.; Mohanty, S.; Luheshi, L.M.; Dobson, C.M.; Vendruscolo, M.; Favrin, G Structural reorganisation and potential toxicity of oligomeric species formed during the assembly of amyloid fibrils. PLoS Comput. Biol. 2007, 3, 1727–1738
    • (2007) Plos Comput. Biol , vol.3 , pp. 1727-1738
    • Cheon, M.1    Chang, I.2    Mohanty, S.3    Luheshi, L.M.4    Dobson, C.M.5    Vendruscolo, M.6
  • 11
    • 79960066445 scopus 로고    scopus 로고
    • Proteostasis regulation at the endoplasmic reticulum: A new perturbation site for targeted cancer therapy
    • Liu, Y.; Ye, Y. Proteostasis regulation at the endoplasmic reticulum: A new perturbation site for targeted cancer therapy. Cell Res. 2011, 21, 867–883.
    • (2011) Cell Res , vol.21 , pp. 867-883
    • Liu, Y.1    Ye, Y.2
  • 13
    • 84863248733 scopus 로고    scopus 로고
    • Yang, P.; et al. Regular patterns for proteome-wide distribution of protein abundance across species
    • Zhong, F.; Yang, D.; Hao, Y.; Lin, C.; Jiang, Y.; Ying, W.; Wu, S.; Zhu, Y.; Liu, S.; Yang, P.; et al. Regular patterns for proteome-wide distribution of protein abundance across species PLoS ONE 2012, 7, e32423
    • (2012) Plos ONE , vol.7
    • Zhong, F.1    Yang, D.2    Hao, Y.3    Lin, C.4    Jiang, Y.5    Ying, W.6    Wu, S.7    Zhu, Y.8    Liu, S.9
  • 14
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: From stress pathway to homeostatic regulation
    • Walter, P.; Ron, D. The unfolded protein response: From stress pathway to homeostatic regulation. Science 2011, 334, 1081–1086
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 15
    • 84908018421 scopus 로고    scopus 로고
    • Cellular mechanisms of endoplasmic reticulum stress signaling in health and disease. 2. Protein misfolding and ER stress
    • Chambers, J.E.; Marciniak, S.J. Cellular mechanisms of endoplasmic reticulum stress signaling in health and disease. 2. Protein misfolding and ER stress. Am. J. Physiol. Cell Physiol. 2014, 307, C657–C670
    • (2014) "');">. , vol.307
    • Chambers, J.E.1    Marciniak, S.J.2
  • 16
    • 84922479583 scopus 로고    scopus 로고
    • Cellular mechanisms of endoplasmic reticulum stress signaling in health and disease. 3. Orchestrating the unfolded protein response in oncogenesis: An update
    • Manié, S.N.; Lebeau, J.; Chevet, E. Cellular mechanisms of endoplasmic reticulum stress signaling in health and disease. 3. Orchestrating the unfolded protein response in oncogenesis: An update. Am. J. Physiol. Cell Physiol. 2014, 307, C901–C907
    • (2014) "');">. , vol.307
    • Manié, S.N.1    Lebeau, J.2    Chevet, E.3
  • 17
    • 84887620237 scopus 로고    scopus 로고
    • ER stress-induced cell death mechanisms
    • Sano, R.; Reed, J.C. ER stress-induced cell death mechanisms. Biochim. Biophys. Acta 2013, 1833, 3460–3470
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 3460-3470
    • Sano, R.1    Reed, J.C.2
  • 18
    • 34147102801 scopus 로고    scopus 로고
    • Chaperones and proteases: Cellular fold-controlling factors of proteins in neurodegenerative diseases and aging
    • Hinault, M.P.; Ben-Zvi, A.; Goloubinoff, P. Chaperones and proteases: Cellular fold-controlling factors of proteins in neurodegenerative diseases and aging. J. Mol. Neurosci. 2006, 30, 249–265
    • (2006) J. Mol. Neurosci , vol.30 , pp. 249-265
    • Hinault, M.P.1    Ben-Zvi, A.2    Goloubinoff, P.3
  • 20
    • 2542530161 scopus 로고    scopus 로고
    • Protein chemistry: In the footsteps of alchemists
    • Dobson, M.C. Protein chemistry: In the footsteps of alchemists. Science 2004, 304, 1259–1262
    • (2004) Science , vol.304 , pp. 1259-1262
    • Dobson, M.C.1
  • 21
    • 0015859467 scopus 로고
    • Principles that govern folding of protein chains
    • Anfinsen, C.B. Principles that govern folding of protein chains. Science 1973, 181, 223–230
    • (1973) Science , vol.181 , pp. 223-230
    • Anfinsen, C.B.1
  • 22
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson, H.J.; Wright, P.E. Intrinsically unstructured proteins and their functions. Nat. Rev. Mol Cell Biol. 2005, 6, 197–208
    • (2005) Nat. Rev. Mol Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 23
  • 24
    • 84924854892 scopus 로고    scopus 로고
    • From local to global changes in proteins: A network view
    • Vuillon, L.; Lesieur, C. From local to global changes in proteins: A network view. Curr. Opin Struct. Biol. 2015, 31, 1–8
    • (2015) Curr. Opin Struct. Biol , vol.31 , pp. 1-8
    • Vuillon, L.1    Lesieur, C.2
  • 25
    • 84876266689 scopus 로고    scopus 로고
    • Allostery in disease and in drug discovery
    • Nussinov, R.; Tsai, C.J. Allostery in disease and in drug discovery. Cell 2013, 153, 293–305
    • (2013) Cell , vol.153 , pp. 293-305
    • Nussinov, R.1    Tsai, C.J.2
  • 26
    • 11144320699 scopus 로고    scopus 로고
    • Navigating chemical space for biology and medicine
    • Lipinski, C.; Hopkins, A. Navigating chemical space for biology and medicine. Nature 2004, 432, 855–861
    • (2004) Nature , vol.432 , pp. 855-861
    • Lipinski, C.1    Hopkins, A.2
  • 28
    • 84900410568 scopus 로고    scopus 로고
    • Multisteric regulation by structural disorder in modular signaling proteins: An extension of the concept of allostery
    • Tompa, P. Multisteric regulation by structural disorder in modular signaling proteins: An extension of the concept of allostery. Chem. Rev. 2014, 114, 6715–6732
    • (2014) Chem. Rev , vol.114 , pp. 6715-6732
    • Tompa, P.1
  • 29
    • 84925752002 scopus 로고    scopus 로고
    • Real-time dynamics of emerging actin networks in cell-mimicking compartments
    • Deshpande, S.; Pfohl, T. Real-time dynamics of emerging actin networks in cell-mimicking compartments. PLoS ONE 2015, 10, e011652
    • (2015) Plos ONE , vol.10
    • Deshpande, S.1    Pfohl, T.2
  • 30
    • 77951620965 scopus 로고    scopus 로고
    • Spatial organization and signal transduction at intercellular junctions
    • Manz, B.N.; Groves, J.T. Spatial organization and signal transduction at intercellular junctions Nat. Rev. Mol. Cell Biol. 2010, 11, 342–352
    • (2010) Nat. Rev. Mol. Cell Biol , vol.11 , pp. 342-352
    • Manz, B.N.1    Groves, J.T.2
  • 31
    • 33745712594 scopus 로고    scopus 로고
    • Why do hubs tend to be essential in protein networks?
    • He, X.; Zhang, J. Why do hubs tend to be essential in protein networks? PLoS Genet. 2006, 2, e88.
    • (2006) Plos Genet , vol.2
    • He, X.1    Zhang, J.2
  • 32
    • 84907646536 scopus 로고    scopus 로고
    • . Molecular crowding effects on conformation and stability of G-quadruplex DNA structure: Insights from molecular dynamics simulation
    • Verdian Doghaei, A.; Housaindokht, M.R.; Bozorgmehr, M.R. Molecular crowding effects on conformation and stability of G-quadruplex DNA structure: Insights from molecular dynamics simulation. J. Theor. Biol.2015, 364, 103–112
    • (2015) J. Theor. Biol , vol.364 , pp. 103-112
    • Verdian Doghaei, A.1    Housaindokht, M.R.2    Bozorgmehr, M.R.3
  • 33
    • 0036725277 scopus 로고    scopus 로고
    • Molecular dynamics simulations of biomolecules
    • Karplus, M.; McCammon, A.J. Molecular dynamics simulations of biomolecules. Nat. Struct. Biol 2002, 9, 646–652
    • (2002) Nat. Struct. Biol , vol.9 , pp. 646-652
    • Karplus, M.1    McCammon, A.J.2
  • 35
    • 84870065644 scopus 로고    scopus 로고
    • . Conditional disorder in chaperone action
    • Bardwell, J.C.; Jakob, U. Conditional disorder in chaperone action. Trends Biochem. Sci. 2012, 37, 517–525
    • (2012) Trends Biochem. Sci , vol.37 , pp. 517-525
    • Bardwell, J.C.1    Jakob, U.2
  • 37
    • 79953299218 scopus 로고    scopus 로고
    • Amyloidogenic properties of a D/N mutated 12 amino acid fragment of the C-terminal domain of the Cholesteryl-Ester Transfer Protein (CETP)
    • García-González, V.; Mas-Oliva, J. Amyloidogenic properties of a D/N mutated 12 amino acid fragment of the C-terminal domain of the Cholesteryl-Ester Transfer Protein (CETP). Int. J Mol. Sci. 2011, 12, 2019–2035
    • (2011) Int. J Mol. Sci , vol.12 , pp. 2019-2035
    • García-González, V.1    Mas-Oliva, J.2
  • 38
    • 84930225080 scopus 로고    scopus 로고
    • SnapShot: Intrinsic structural disorder
    • Guharoy, M.; Pauwels, K.; Tompa, P. SnapShot: Intrinsic structural disorder. Cell 2015, 161, 1230–1230
    • (2015) Cell , vol.161
    • Guharoy, M.1    Pauwels, K.2    Tompa, P.3
  • 39
    • 84883471917 scopus 로고    scopus 로고
    • From sequence and forces to structure, function, and evolution of intrinsically disordered proteins
    • Forman-Kay, J.D.; Mittag, T. From sequence and forces to structure, function, and evolution of intrinsically disordered proteins. Structure 2013, 21, 1492–1499
    • (2013) Structure , vol.21 , pp. 1492-1499
    • Forman-Kay, J.D.1    Mittag, T.2
  • 42
    • 65249102824 scopus 로고    scopus 로고
    • Close encounters of the third kind: Disordered domains and the interactions of proteins
    • Tompa, P.; Fuxreiter, M.; Oldfield, C.J.; Simon, I.; Dunker, A.K.; Uversky, V.N. Close encounters of the third kind: Disordered domains and the interactions of proteins. BioEssays 2009, 31, 328–335
    • (2009) Bioessays , vol.31 , pp. 328-335
    • Tompa, P.1    Fuxreiter, M.2    Oldfield, C.J.3    Simon, I.4    Dunker, A.K.5    Uversky, V.N.6
  • 44
    • 82655181911 scopus 로고    scopus 로고
    • Intrinsic disorder in cell signaling and gene transcription
    • Tantos, A.; Han, K.H.; Tompa, P. Intrinsic disorder in cell signaling and gene transcription Mol. Cell. Endocrinol. 2012, 348, 457–465
    • (2012) Mol. Cell. Endocrinol , vol.348 , pp. 457-465
    • Tantos, A.1    Han, K.H.2    Tompa, P.3
  • 45
    • 34347235156 scopus 로고    scopus 로고
    • Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins. Proc. Natl. Acad. Sci
    • Hilser, V.J.; Thompson, E.B. Intrinsic disorder as a mechanism to optimize allosteric coupling in proteins. Proc. Natl. Acad. Sci. USA 2007, 104, 8311–8315
    • (2007) USA , vol.104 , pp. 8311-8315
    • Hilser, V.J.1    Thompson, E.B.2
  • 46
    • 84879327823 scopus 로고    scopus 로고
    • Modulation of allostery by protein intrinsic disorder
    • Ferreon, A.C.; Ferreon, J.C.; Wright, P.E.; Deniz, A.A. Modulation of allostery by protein intrinsic disorder. Nature 2013, 498, 390–394
    • (2013) Nature , vol.498 , pp. 390-394
    • Ferreon, A.C.1    Ferreon, J.C.2    Wright, P.E.3    Deniz, A.A.4
  • 47
    • 23944514504 scopus 로고    scopus 로고
    • Structural disorder throws new light on moonlighting
    • Tompa, P.; Szász, C.; Buday, L. Structural disorder throws new light on moonlighting Trends Biochem. Sci. 2005, 30, 484–489
    • (2005) Trends Biochem. Sci , vol.30 , pp. 484-489
    • Tompa, P.1    Szász, C.2    Buday, L.3
  • 49
    • 49749117432 scopus 로고    scopus 로고
    • Contextual specificity in peptide-mediated protein interactions
    • Stein, A.; Aloy, P. Contextual specificity in peptide-mediated protein interactions. PLoS ONE 2008, 3, e2524
    • (2008) Plos ONE , vol.3
    • Stein, A.1    Aloy, P.2
  • 50
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • Ward, J.J.; Sodhi, J.S.; McGuffin, L.J.; Buxton, B.F.; Jones, D.T. Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J. Mol. Biol. 2004, 337, 635–645
    • (2004) J. Mol. Biol , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 53
    • 40949117264 scopus 로고    scopus 로고
    • Flexible nets: Disorder and induced fit in the associations of p53 and 14-3-3 with their partners
    • Oldfield, C.J.; Meng, J.; Yang, J.Y.; Yang, M.Q.; Uversky, V.N.; Dunker, A.K. Flexible nets: Disorder and induced fit in the associations of p53 and 14-3-3 with their partners. BMC Genomics 2008, 9, S1
    • (2008) BMC Genomics , vol.9
    • Oldfield, C.J.1    Meng, J.2    Yang, J.Y.3    Yang, M.Q.4    Uversky, V.N.5    Dunker, A.K.6
  • 55
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa, P. Intrinsically unstructured proteins. Trends Biochem. Sci. 2002, 27, 527–533
    • (2002) Trends Biochem. Sci , vol.27 , pp. 527-533
    • Tompa, P.1
  • 56
    • 0038148710 scopus 로고    scopus 로고
    • Conformational diversity and protein evolution—A 60-year-old hypothesis revisited
    • James, C.; Tawfik, D.S. Conformational diversity and protein evolution—A 60-year-old hypothesis revisited. Trends Biochem. Sci. 2003, 28, 361–368
    • (2003) Trends Biochem. Sci , vol.28 , pp. 361-368
    • James, C.1    Tawfik, D.S.2
  • 57
    • 33645034035 scopus 로고    scopus 로고
    • Intrinsic disorder is a key characteristic in partners that bind 14-3-3 proteins
    • Bustos, D.M.; Iglesias, A.A. Intrinsic disorder is a key characteristic in partners that bind 14-3-3 proteins. Proteins 2006, 63, 35–42
    • (2006) Proteins , vol.63 , pp. 35-42
    • Bustos, D.M.1    Iglesias, A.A.2
  • 58
    • 0029662315 scopus 로고    scopus 로고
    • Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: Conformational disorder mediates binding diversity
    • Kriwacki, R.W.; Hengst, L.; Tennant, L.; Reed, S.I.; Wright, P.E. Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: Conformational disorder mediates binding diversity. Proc. Natl. Acad. Sci. USA1996, 93, 11504–11509
    • (1996) "');">. , vol.93 , pp. 11504-11509
    • Kriwacki, R.W.1    Hengst, L.2    Tennant, L.3    Reed, S.I.4    Wright, P.E.5
  • 59
    • 0033815822 scopus 로고    scopus 로고
    • Understanding the sequence determinants of conformational switching using protein design
    • Dalal, S.; Regan, L. Understanding the sequence determinants of conformational switching using protein design. Protein Sci. 2000, 9, 1651–1659
    • (2000) Protein Sci , vol.9 , pp. 1651-1659
    • Dalal, S.1    Regan, L.2
  • 62
    • 0031932169 scopus 로고    scopus 로고
    • Protein aggregation: Folding aggregates, inclusion bodies and amyloid
    • Fink, A.L. Protein aggregation: Folding aggregates, inclusion bodies and amyloid. Fold. Des 1998, 3, R9–R23
    • (1998) Fold. Des , vol.3
    • Fink, A.L.1
  • 63
    • 84858374665 scopus 로고    scopus 로고
    • The amyloid state of proteins in human diseases
    • Eisenberg, D.; Jucker, M. The amyloid state of proteins in human diseases. Cell 2012, 148, 1188–1203
    • (2012) Cell , vol.148 , pp. 1188-1203
    • Eisenberg, D.1    Jucker, M.2
  • 64
    • 33748688511 scopus 로고    scopus 로고
    • Protein denaturation and aggregation: Cellular responses to denatured and aggregated proteins
    • Meredith, S.C. Protein denaturation and aggregation: Cellular responses to denatured and aggregated proteins. Ann. N. Y. Acad. Sci. 2005, 1066, 181–221
    • (2005) Ann. N. Y. Acad. Sci , vol.1066 , pp. 181-221
    • Meredith, S.C.1
  • 65
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti, F.; Dobson, C.M. Protein misfolding, functional amyloid, and human disease Annu. Rev. Biochem. 2006, 75, 333–366
    • (2006) Annu. Rev. Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 66
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson, C.M. Protein folding and misfolding. Nature 2003, 426, 884–890.
    • (2003) Nature , vol.426 , pp. 884-890
    • Dobson, C.M.1
  • 70
    • 84937759580 scopus 로고    scopus 로고
    • Structure of a single-chain fv bound to the 17 N-terminal residues of huntingtin provides insights into pathogenic amyloid formation and suppression
    • De Genst, E.; Chirgadze, D.Y.; Klein, F.A.; Butler, D.C.; Matak-Vinković, D.; Trottier, Y.; Huston, J.S.; Messer, A.; Dobson, C.M. Structure of a single-chain fv bound to the 17 N-terminal residues of huntingtin provides insights into pathogenic amyloid formation and suppression J. Mol. Biol.2015, 427, 2166–2178
    • (2015) J. Mol. Biol , vol.427 , pp. 2166-2178
    • De Genst, E.1    Chirgadze, D.Y.2    Klein, F.A.3    Butler, D.C.4    Matak-Vinković, D.5    Trottier, Y.6    Huston, J.S.7    Messer, A.8    Dobson, C.M.9
  • 71
    • 84864288105 scopus 로고    scopus 로고
    • On the possible amyloid origin of protein folds
    • Greenwald, J.; Riek, R. On the possible amyloid origin of protein folds. J. Mol. Biol. 2012, 421, 417–426
    • (2012) J. Mol. Biol , vol.421 , pp. 417-426
    • Greenwald, J.1    Riek, R.2
  • 72
    • 21744439797 scopus 로고    scopus 로고
    • A model for the role of short self-assembled peptides in the very early stages of the origin of life
    • Carny, O.; Gazit, E. A model for the role of short self-assembled peptides in the very early stages of the origin of life. FASEB J. 2005, 19, 1051–1055
    • (2005) FASEB J , vol.19 , pp. 1051-1055
    • Carny, O.1    Gazit, E.2
  • 74
    • 0036845354 scopus 로고    scopus 로고
    • The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation
    • Fandrich, M.; Dobson, C.M. The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation. EMBO J. 2002, 21, 5682–5690
    • (2002) EMBO J , vol.21 , pp. 5682-5690
    • Fandrich, M.1    Dobson, C.M.2
  • 75
    • 0036468673 scopus 로고    scopus 로고
    • Hultgren, S.J. Role of Escherichia coli curli operons in directing amyloid fiber formation
    • Chapman, M.R.; Robinson, L.S.; Pinkner, J.S.; Roth, R.; Heuser, J.; Hammar, M.; Normark, S.; Hultgren, S.J. Role of Escherichia coli curli operons in directing amyloid fiber formation Science 2002, 295, 851–855
    • (2002) Science , vol.295 , pp. 851-855
    • Chapman, M.R.1    Robinson, L.S.2    Pinkner, J.S.3    Roth, R.4    Heuser, J.5    Hammar, M.6    Normark, S.7
  • 76
    • 0038004458 scopus 로고    scopus 로고
    • A novel class of secreted hydrophobic proteins is involved in aerial hyphae formation in Streptomyces coelicolor by forming amyloid-like fibrils
    • Claessen, D.; Rink, R.; de Jong, W.; Siebring, J.; de Vreugd, P.; Boersma, F.G.; Dijkhuizen, L.; Wosten, H.A. A novel class of secreted hydrophobic proteins is involved in aerial hyphae formation in Streptomyces coelicolor by forming amyloid-like fibrils. Genes Dev. 2003, 17, 1714–1726
    • (2003) Genes Dev , vol.17 , pp. 1714-1726
    • Claessen, D.1    Rink, R.2    De Jong, W.3    Siebring, J.4    De Vreugd, P.5    Boersma, F.G.6    Dijkhuizen, L.7    Wosten, H.A.8
  • 77
    • 0035089501 scopus 로고    scopus 로고
    • The hydrophobin EAS is largely unstructured in solution and functions by forming amyloid-like structures
    • Mackay, J.P.; Matthews, J.M.; Winefield, R.D.; Mackay, L.G.; Haverkamp, R.G.; Templeton, M.D The hydrophobin EAS is largely unstructured in solution and functions by forming amyloid-like structures. Structure 2001, 9, 83–91
    • (2001) Structure , vol.9 , pp. 83-91
    • Mackay, J.P.1    Matthews, J.M.2    Winefield, R.D.3    Mackay, L.G.4    Haverkamp, R.G.5    Templeton, M.D.6
  • 78
    • 0030885650 scopus 로고    scopus 로고
    • The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog
    • Coustou, V.; Deleu, C.; Saupe, S.; Begueret, J. The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog. Proc. Natl Acad. Sci. USA 1997, 94, 9773–9778
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 9773-9778
    • Coustou, V.1    Deleu, C.2    Saupe, S.3    Begueret, J.4
  • 79
    • 0030917006 scopus 로고    scopus 로고
    • Prion-inducing domain 2–114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments
    • King, C.Y.; Tittmann, P.; Gross, H.; Gebert, R.; Aebi, M.; Wüthrich, K. Prion-inducing domain 2–114 of yeast Sup35 protein transforms in vitro into amyloid-like filaments. Proc. Natl. Acad Sci. USA 1997, 94, 6618–6622
    • (1997) Proc. Natl. Acad Sci. USA , vol.94 , pp. 6618-6622
    • King, C.Y.1    Tittmann, P.2    Gross, H.3    Gebert, R.4    Aebi, M.5    Wüthrich, K.6
  • 80
    • 0034683126 scopus 로고    scopus 로고
    • Amyloids protect the silkmoth oocyte and embryo
    • Iconomidou, V.A.; Vriend, G.; Hamodrakas, S.J. Amyloids protect the silkmoth oocyte and embryo. FEBS Lett. 2000, 479, 141–145.
    • (2000) FEBS Lett , vol.479 , pp. 141-145
    • Iconomidou, V.A.1    Vriend, G.2    Hamodrakas, S.J.3
  • 81
    • 33750994604 scopus 로고    scopus 로고
    • Amyloid fibril formation propensity is inherent into the hexapeptide tandemly repeating sequence of the central domain of silkmoth chorion proteins of the A-family
    • Iconomidou, V.A.; Chryssikos, G.D.; Gionis, V.; Galanis, A.S.; Cordopatis, P.; Hoenger, A.; Hamodrakas, S.J. Amyloid fibril formation propensity is inherent into the hexapeptide tandemly repeating sequence of the central domain of silkmoth chorion proteins of the A-family J. Struct. Biol.2006, 156, 480–488
    • (2006) J. Struct. Biol , vol.156 , pp. 480-488
    • Iconomidou, V.A.1    Chryssikos, G.D.2    Gionis, V.3    Galanis, A.S.4    Cordopatis, P.5    Hoenger, A.6    Hamodrakas, S.J.7
  • 82
    • 0037986392 scopus 로고    scopus 로고
    • Proprotein convertase cleavage liberates a fibrillogenic fragment of a resident glycoprotein to initiate melanosome biogenesis
    • Berson, J.F.; Theos, A.C.; Harper, D.C.; Tenza, D.; Raposo, G.; Marks, M.S. Proprotein convertase cleavage liberates a fibrillogenic fragment of a resident glycoprotein to initiate melanosome biogenesis. J. Cell Biol.2003, 161, 521–533
    • (2003) J. Cell Biol , vol.161 , pp. 521-533
    • Berson, J.F.1    Theos, A.C.2    Harper, D.C.3    Tenza, D.4    Raposo, G.5    Marks, M.S.6
  • 84
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
    • Stefani, M.; Dobson, C.M. Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution. J. Mol. Med. 2003, 81, 678–699
    • (2003) J. Mol. Med , vol.81 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 85
    • 84876807340 scopus 로고    scopus 로고
    • Amyloid fibril formation of peptides derived from the C-terminus of CETP modulated by lipids
    • García-González, V.; Mas-Oliva, J. Amyloid fibril formation of peptides derived from the C-terminus of CETP modulated by lipids. Biochem. Biophys. Res. Commun. 2013, 434, 54–59
    • (2013) Biochem. Biophys. Res. Commun , vol.434 , pp. 54-59
    • García-González, V.1    Mas-Oliva, J.2
  • 86
    • 5044235541 scopus 로고    scopus 로고
    • Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins
    • Fernandez-Escamilla, A.M.; Rousseau, F.; Schymkowitz, J.; Serrano, L. Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins Nat. Biotechnol. 2004, 22, 1302–1306
    • (2004) Nat. Biotechnol , vol.22 , pp. 1302-1306
    • Fernandez-Escamilla, A.M.1    Rousseau, F.2    Schymkowitz, J.3    Serrano, L.4
  • 87
    • 20444403757 scopus 로고    scopus 로고
    • Prediction of “aggregation-prone” and “aggregation-susceptible” regions in proteins associated with neurodegenerative diseases
    • Pawar, A.P.; Dubay, K.F.; Zurdo, J.; Chiti, F.; Vendruscolo, M.; Dobson, C.M. Prediction of “aggregation-prone” and “aggregation-susceptible” regions in proteins associated with neurodegenerative diseases. J. Mol. Biol.2005, 350, 379–392
    • (2005) J. Mol. Biol , vol.350 , pp. 379-392
    • Pawar, A.P.1    Dubay, K.F.2    Zurdo, J.3    Chiti, F.4    Vendruscolo, M.5    Dobson, C.M.6
  • 88
    • 33846990935 scopus 로고    scopus 로고
    • Friendly and dangerous signals: Is the tissue in control?
    • Matzinger, P. Friendly and dangerous signals: Is the tissue in control? Nat. Immunol.2007, 8, 11–13
    • (2007) Nat. Immunol , vol.8 , pp. 11-13
    • Matzinger, P.1
  • 89
    • 39349083915 scopus 로고    scopus 로고
    • . Adapting proteostasis for disease intervention
    • Balch, W.E.; Morimoto, R.I.; Dillin, A.; Kelly, J.W. Adapting proteostasis for disease intervention Science 2008, 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
  • 91
    • 84863958621 scopus 로고    scopus 로고
    • Protein solubility and protein homeostasis: A generic view of protein misfolding disorders
    • Vendruscolo, M.; Knowles, T.P.J.; Dobson, C.M. Protein solubility and protein homeostasis: A generic view of protein misfolding disorders. Cold Spring Harb. Perspect. Biol. 2011, 3, a010454
    • Cold Spring Harb. Perspect. Biol , vol.3
    • Vendruscolo, M.1    Knowles, T.2    Dobson, C.M.3
  • 92
    • 84901355639 scopus 로고    scopus 로고
    • The amyloid state and its association with protein misfolding diseases
    • Knowles, T.P.; Vendruscolo, M.; Dobson, C.M. The amyloid state and its association with protein misfolding diseases. Nat. Rev. Mol. Cell Biol. 2014, 15, 384–396
    • (2014) Nat. Rev. Mol. Cell Biol , vol.15 , pp. 384-396
    • Knowles, T.P.1    Vendruscolo, M.2    Dobson, C.M.3
  • 94
  • 95
    • 79551687316 scopus 로고    scopus 로고
    • Protein folding in the cell: Challenges and progress
    • Gershenson, A.; Gierasch, L.M. Protein folding in the cell: Challenges and progress. Curr. Opin Struct. Biol. 2011, 21, 32–41
    • (2011) Curr. Opin Struct. Biol , vol.21 , pp. 32-41
    • Gershenson, A.1    Gierasch, L.M.2
  • 96
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl, F.U.; Bracher, A.; Hayer-Hartl, M. Molecular chaperones in protein folding and proteostasis. Nature 2011, 475, 324–332
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 97
    • 4344568810 scopus 로고    scopus 로고
    • Protein crystallization and phase diagrams
    • Asherie, N. Protein crystallization and phase diagrams. Methods 2004, 34, 266–272.
    • (2004) Methods , vol.34 , pp. 266-272
    • Asherie, N.1
  • 98
    • 84883049362 scopus 로고    scopus 로고
    • Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis
    • Finka, A.; Goloubinoff, P. Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis. Cell Stress Chaperones 2013, 18, 591–605
    • (2013) Cell Stress Chaperones , vol.18 , pp. 591-605
    • Finka, A.1    Goloubinoff, P.2
  • 101
    • 77955506092 scopus 로고    scopus 로고
    • Gymnastics of molecular chaperones
    • Mayer, M.P. Gymnastics of molecular chaperones. Mol. Cell 2010, 39, 321–331
    • (2010) Mol. Cell , vol.39 , pp. 321-331
    • Mayer, M.P.1
  • 102
    • 33745829795 scopus 로고    scopus 로고
    • Molecular chaperones: Assisting assembly in addition to folding
    • Ellis, R.J. Molecular chaperones: Assisting assembly in addition to folding. Trends Biochem. Sci 2006, 31, 395–401
    • (2006) Trends Biochem. Sci , vol.31 , pp. 395-401
    • Ellis, R.J.1
  • 103
    • 39149143645 scopus 로고    scopus 로고
    • Chaperone machines in action
    • Saibil, H.R. Chaperone machines in action. Curr. Opin. Struct. Biol. 2008, 18, 35–42
    • (2008) Curr. Opin. Struct. Biol , vol.18 , pp. 35-42
    • Saibil, H.R.1
  • 105
    • 66649132872 scopus 로고    scopus 로고
    • Chaperonin overexpression promotes genetic variation and enzyme evolution
    • Tokuriki, N.; Tawfik, D.S. Chaperonin overexpression promotes genetic variation and enzyme evolution. Nature 2009, 459, 668–671
    • (2009) Nature , vol.459 , pp. 668-671
    • Tokuriki, N.1    Tawfik, D.S.2
  • 106
    • 0032569851 scopus 로고    scopus 로고
    • Hsp90 as a capacitor for morphological evolution
    • Rutherford, S.L.; Lindquist, S. Hsp90 as a capacitor for morphological evolution. Nature 1998, 396, 336–342
    • (1998) Nature , vol.396 , pp. 336-342
    • Rutherford, S.L.1    Lindquist, S.2
  • 107
    • 0036049850 scopus 로고    scopus 로고
    • The unfolding story of the Escherichia coli Hsp70 DnaK: Is DnaK a holdase or an unfoldase?
    • Slepenkov, S.V.; Witt, S.N. The unfolding story of the Escherichia coli Hsp70 DnaK: Is DnaK a holdase or an unfoldase? Mol. Microbiol.2002, 45, 1197–1206
    • (2002) Mol. Microbiol , vol.45 , pp. 1197-1206
    • Slepenkov, S.V.1    Witt, S.N.2
  • 108
    • 33749244758 scopus 로고    scopus 로고
    • The molecular chaperone Hsp104—A molecular machine for protein disaggregation
    • Bosl, B.; Grimminger, V.; Walter, S. The molecular chaperone Hsp104—A molecular machine for protein disaggregation. J. Struct. Biol. 2006, 156, 139–148
    • (2006) J. Struct. Biol , vol.156 , pp. 139-148
    • Bosl, B.1    Grimminger, V.2    Walter, S.3
  • 109
    • 0026596223 scopus 로고
    • Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding
    • Langer, T.; Lu, C.; Echols, H.; Flanagan, J.; Hayer, M.K.; Hartl, F.U. Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding. Nature 1992, 356, 683–689
    • (1992) Nature , vol.356 , pp. 683-689
    • Langer, T.1    Lu, C.2    Echols, H.3    Flanagan, J.4    Hayer, M.K.5    Hartl, F.U.6
  • 110
    • 70350020881 scopus 로고    scopus 로고
    • Chaperonin-mediated protein folding: Using a central cavity to kinetically assist polypeptide chain folding
    • Horwich, A.L.; Fenton, W.A. Chaperonin-mediated protein folding: Using a central cavity to kinetically assist polypeptide chain folding. Q. Rev. Biophys.2009, 42, 83–116
    • (2009) Q. Rev. Biophys , vol.42 , pp. 83-116
    • Horwich, A.L.1    Fenton, W.A.2
  • 112
    • 80052177927 scopus 로고    scopus 로고
    • Structural analysis of the Sil1-Bip complex reveals the mechanism for Sil1 to function as a nucleotide-exchange factor
    • Yan, M.; Li, J.; Sha, B. Structural analysis of the Sil1-Bip complex reveals the mechanism for Sil1 to function as a nucleotide-exchange factor. Biochem. J. 2011, 438, 447–455
    • (2011) Biochem. J , vol.438 , pp. 447-455
    • Yan, M.1    Li, J.2    Sha, B.3
  • 113
    • 84866488172 scopus 로고    scopus 로고
    • The heat shock response: Systems biology of proteotoxic stress in aging and disease
    • Morimoto, R.I. The heat shock response: Systems biology of proteotoxic stress in aging and disease. Cold Spring Harb. Symp. Quant. Biol. 2011, 76, 91–99
    • (2011) Cold Spring Harb. Symp. Quant. Biol , vol.76 , pp. 91-99
    • Morimoto, R.I.1
  • 115
    • 60749101582 scopus 로고    scopus 로고
    • Stress-inducible regulation of heat shock factor 1 by the deacetylase SIRT1
    • Westerheide, S.D.; Anckar, J.; Stevens, S.M., Jr.; Sistonen, L.; Morimoto, R.I. Stress-inducible regulation of heat shock factor 1 by the deacetylase SIRT1. Science 2009, 323, 1063–1066
    • (2009) Science , vol.323 , pp. 1063-1066
    • Westerheide, S.D.1    Anckar, J.2    Stevens, S.M.3    Sistonen, L.4    Morimoto, R.I.5
  • 116
    • 84866644698 scopus 로고    scopus 로고
    • Diverse functional manifestations of intrinsic structural disorder in molecular chaperones
    • Kovacs, D.; Tompa, P. Diverse functional manifestations of intrinsic structural disorder in molecular chaperones. Biochem. Soc. Trans. 2012, 40, 963–968
    • (2012) Biochem. Soc. Trans , vol.40 , pp. 963-968
    • Kovacs, D.1    Tompa, P.2
  • 117
    • 84969577902 scopus 로고    scopus 로고
    • Unfolded protein responses with or without unfolded proteins?
    • Snapp, E.L. Unfolded protein responses with or without unfolded proteins? Cells 2012, 1, 926–950.
    • (2012) Cells , vol.1 , pp. 926-950
    • Snapp, E.L.1
  • 118
    • 84964698311 scopus 로고    scopus 로고
    • Noncanonical binding of BiP ATPase domain to Ire1 and Perk is dissociated by unfolded protein CH1 to initiate ER stress signaling
    • Carrara, M.; Prischi, F.; Nowak, P.R.; Kopp, M.C.; Ali, M.M. Noncanonical binding of BiP ATPase domain to Ire1 and Perk is dissociated by unfolded protein CH1 to initiate ER stress signaling. Elife 2015, 4, doi:10.7554/eLife.03522
    • (2015) Elife , vol.4
    • Carrara, M.1    Prischi, F.2    Nowak, P.R.3    Kopp, M.C.4    Ali, M.M.5
  • 120
    • 84855966721 scopus 로고    scopus 로고
    • Role of endoplasmic reticulum stress in metabolic disease and other disorders
    • Ozcan, L.; Tabas, I. Role of endoplasmic reticulum stress in metabolic disease and other disorders. Annu. Rev. Med. 2012, 63, 317–328
    • (2012) Annu. Rev. Med , vol.63 , pp. 317-328
    • Ozcan, L.1    Tabas, I.2
  • 121
    • 0037336295 scopus 로고    scopus 로고
    • Quality control in the endoplasmic reticulum
    • Ellgaard, L.; Helenius, A. Quality control in the endoplasmic reticulum. Nat. Rev. Mol. Cell Biol 2003, 4, 181–191
    • (2003) Nat. Rev. Mol. Cell Biol , vol.4 , pp. 181-191
    • Ellgaard, L.1    Helenius, A.2
  • 122
    • 84870159094 scopus 로고    scopus 로고
    • Structural basis of the unfolded protein response
    • Korennykh, A.; Walter, P. Structural basis of the unfolded protein response. Annu. Rev. Cell Dev. Biol. 2012, 28, 251–277
    • (2012) Annu. Rev. Cell Dev. Biol , vol.28 , pp. 251-277
    • Korennykh, A.1    Walter, P.2
  • 123
    • 33749233991 scopus 로고    scopus 로고
    • The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response
    • Zhou, J.; Liu, C.Y.; Back, S.H.; Clark, R.L.; Peisach, D.; Xu, Z.; Kaufman, R.J. The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response. Proc. Natl. Acad. Sci. USA 2006, 103, 14343–14348
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 14343-14348
    • Zhou, J.1    Liu, C.Y.2    Back, S.H.3    Clark, R.L.4    Peisach, D.5    Xu, Z.6    Kaufman, R.J.7
  • 124
    • 82255161944 scopus 로고    scopus 로고
    • Road to ruin: Targeting proteins for degradation in the endoplasmic reticulum
    • Smith, M.H.; Ploegh, H.L.; Weissman, J.S. Road to ruin: Targeting proteins for degradation in the endoplasmic reticulum. Science 2011, 334, 1086–1090
    • (2011) Science , vol.334 , pp. 1086-1090
    • Smith, M.H.1    Ploegh, H.L.2    Weissman, J.S.3
  • 125
    • 0036776098 scopus 로고    scopus 로고
    • Structural organization of the endoplasmic reticulum
    • Voeltz, G.K.; Rolls, M.M.; Rapoport, T.A. Structural organization of the endoplasmic reticulum EMBO Rep. 2002, 3, 944–950
    • (2002) EMBO Rep , vol.3 , pp. 944-950
    • Voeltz, G.K.1    Rolls, M.M.2    Rapoport, T.A.3
  • 126
    • 70449577164 scopus 로고    scopus 로고
    • . In vitro reconstitution of ER-stress induced ATF6 transport in COPII vesicles
    • Schindler, A.J.; Schekman, R. In vitro reconstitution of ER-stress induced ATF6 transport in COPII vesicles. Proc. Natl. Acad. Sci. USA 2009, 106, 17775–17780
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 17775-17780
    • Schindler, A.J.1    Schekman, R.2
  • 127
    • 0032693671 scopus 로고    scopus 로고
    • Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress
    • Haze, K.; Yoshida, H.; Yanagi, H.; Yura, T.; Mori, K. Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress. Mol. Biol. Cell 1999, 10, 3787–3799
    • (1999) Mol. Biol. Cell , vol.10 , pp. 3787-3799
    • Haze, K.1    Yoshida, H.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 130
    • 79953288480 scopus 로고    scopus 로고
    • Selective inhibition of a regulatory subunit of protein phosphatase 1 restores proteostasis
    • Tsaytler, P.; Harding, H.P.; Ron, D.; Bertolotti, A. Selective inhibition of a regulatory subunit of protein phosphatase 1 restores proteostasis. Science 2011, 332, 91–94
    • (2011) Science , vol.332 , pp. 91-94
    • Tsaytler, P.1    Harding, H.P.2    Ron, D.3    Bertolotti, A.4
  • 131
    • 0037011917 scopus 로고    scopus 로고
    • IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA
    • Calfon, M.; Zeng, H.; Urano, F.; Till, J.H.; Hubbard, S.R.; Harding, H.P.; Clark, S.G.; Ron, D IRE1 couples endoplasmic reticulum load to secretory capacity by processing the XBP-1 mRNA Nature 2002, 415, 92–96
    • (2002) Nature , vol.415 , pp. 92-96
    • Calfon, M.1    Zeng, H.2    Urano, F.3    Till, J.H.4    Hubbard, S.R.5    Harding, H.P.6    Clark, S.G.7    Ron, D.8
  • 132
    • 0035966269 scopus 로고    scopus 로고
    • XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor
    • Yoshida, H.; Matsui, T.; Yamamoto, A.; Okada, T.; Mori, K. XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor. Cell 2001, 107, 881–891
    • (2001) Cell , vol.107 , pp. 881-891
    • Yoshida, H.1    Matsui, T.2    Yamamoto, A.3    Okada, T.4    Mori, K.5
  • 134
    • 0037083755 scopus 로고    scopus 로고
    • IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response
    • Lee, K.; Tirasophon, W.; Shen, X.; Michalak, M.; Prywes, R.; Okada, T.; Yoshida, H.; Mori, K.; Kaufman, R.J. IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response. Genes Dev. 2002, 16, 452–466
    • (2002) Genes Dev , vol.16 , pp. 452-466
    • Lee, K.1    Tirasophon, W.2    Shen, X.3    Michalak, M.4    Prywes, R.5    Okada, T.6    Yoshida, H.7    Mori, K.8    Kaufman, R.J.9
  • 135
    • 0037320265 scopus 로고    scopus 로고
    • A time-dependent phase shift in the mammalian unfolded protein response
    • Yoshida, H.; Matsui, T.; Hosokawa, N.; Kaufman, R.J.; Nagata, K.; Mori, K. A time-dependent phase shift in the mammalian unfolded protein response. Dev. Cell 2003, 4, 265–271
    • (2003) Dev. Cell , vol.4 , pp. 265-271
    • Yoshida, H.1    Matsui, T.2    Hosokawa, N.3    Kaufman, R.J.4    Nagata, K.5    Mori, K.6
  • 138
    • 84896706762 scopus 로고    scopus 로고
    • Regulatory crosstalk within the mammalian unfolded protein response
    • Brewer, J.W. Regulatory crosstalk within the mammalian unfolded protein response. Cell Mol Life Sci. 2014, 71, 1067–1079
    • (2014) Cell Mol Life Sci , vol.71 , pp. 1067-1079
    • Brewer, J.W.1
  • 139
    • 84856111924 scopus 로고    scopus 로고
    • The unfolded protein response: Controlling cell fate decisions under ER stress and beyond
    • Hetz, C. The unfolded protein response: Controlling cell fate decisions under ER stress and beyond. Nat. Rev. Mol. Cell Biol. 2012, 13, 89–102
    • (2012) Nat. Rev. Mol. Cell Biol , vol.13 , pp. 89-102
    • Hetz, C.1
  • 141
    • 77958016968 scopus 로고    scopus 로고
    • Mammalian endoplasmic reticulum stress sensor IRE1 signals by dynamic clustering
    • Li, H.; Korennykh, A.V.; Behrman, S.L.; Walter, P. Mammalian endoplasmic reticulum stress sensor IRE1 signals by dynamic clustering. Proc. Natl. Acad. Sci. USA 2010, 107, 16113–16118
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 16113-16118
    • Li, H.1    Korennykh, A.V.2    Behrman, S.L.3    Walter, P.4
  • 142
    • 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.; Frydman, J. Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress. Nat. Cell Biol. 2013, 15, 1231–1243
    • (2013) Nat. Cell Biol , vol.15 , pp. 1231-1243
    • Escusa-Toret, S.1    Vonk, W.I.2    Frydman, J.3
  • 143
    • 84883210213 scopus 로고    scopus 로고
    • Principles of cotranslational ubiquitination and quality control at the ribosome
    • Duttler, S.; Pechmann, S.; Frydman, J. Principles of cotranslational ubiquitination and quality control at the ribosome. Mol. Cell 2013, 50, 379–393
    • (2013) Mol. Cell , vol.50 , pp. 379-393
    • Duttler, S.1    Pechmann, S.2    Frydman, J.3
  • 144
    • 84883229070 scopus 로고    scopus 로고
    • A cotranslational ubiquitination pathway for quality control of misfolded proteins
    • Wang, F.; Durfee, L.A.; Huibregtse, J.M. A cotranslational ubiquitination pathway for quality control of misfolded proteins. Mol. Cell 2013, 50, 368–378
    • (2013) Mol. Cell , vol.50 , pp. 368-378
    • Wang, F.1    Durfee, L.A.2    Huibregtse, J.M.3
  • 145
    • 84925553022 scopus 로고    scopus 로고
    • Local slowdown of translation by nonoptimal codons promotes nascent-chain recognition by SRP in vivo
    • Pechmann, S.; Chartron, J.W.; Frydman, J. Local slowdown of translation by nonoptimal codons promotes nascent-chain recognition by SRP in vivo. Nat. Struct. Mol. Biol. 2014, 21, 1100–1105
    • (2014) Nat. Struct. Mol. Biol , vol.21 , pp. 1100-1105
    • Pechmann, S.1    Chartron, J.W.2    Frydman, J.3
  • 146
    • 84897129156 scopus 로고    scopus 로고
    • Differential scales of protein quality control
    • Wolff, S.; Weissman, J.S.; Dillin, A. Differential scales of protein quality control. Cell 2014, 157, 52–64
    • (2014) Cell , vol.157 , pp. 52-64
    • Wolff, S.1    Weissman, J.S.2    Dillin, A.3
  • 147
    • 67649306771 scopus 로고    scopus 로고
    • Molecular chaperones antagonize proteotoxicity by differentially modulating protein aggregation pathways
    • Douglas, P.M.; Summers, D.W.; Cyr, D.M. Molecular chaperones antagonize proteotoxicity by differentially modulating protein aggregation pathways. Prion 2009, 3, 51–58
    • (2009) Prion , vol.3 , pp. 51-58
    • Douglas, P.M.1    Summers, D.W.2    Cyr, D.M.3
  • 148
    • 33748792821 scopus 로고    scopus 로고
    • Opposing activities protect against age-onset proteotoxicity
    • Cohen, E.; Bieschke, J.; Perciavalle, R.M.; Kelly, J.W.; Dillin, A. Opposing activities protect against age-onset proteotoxicity. Science 2006, 313, 1604–1610
    • (2006) Science , vol.313 , pp. 1604-1610
    • Cohen, E.1    Bieschke, J.2    Perciavalle, R.M.3    Kelly, J.W.4    Dillin, A.5
  • 149
    • 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.; Finkbeiner, S. Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 2004, 431, 805–810
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 150
    • 50649116818 scopus 로고    scopus 로고
    • Misfolded proteins partition between two distinct quality control compartments
    • Kaganovich, D.; Kopito, R.; Frydman, J. Misfolded proteins partition between two distinct quality control compartments. Nature 2008, 454, 1088–1095.
    • (2008) Nature , vol.454 , pp. 1088-1095
    • Kaganovich, D.1    Kopito, R.2    Frydman, J.3
  • 152
    • 84896779318 scopus 로고    scopus 로고
    • Misfolded polyglutamine, polyalanine, and superoxide dismutase 1 aggregate via distinct pathways in the cell
    • Polling, S.; Mok, Y.F.; Ramdzan, Y.M.; Turner, B.J.; Yerbury, J.J.; Hill, A.F.; Hatters, D.M Misfolded polyglutamine, polyalanine, and superoxide dismutase 1 aggregate via distinct pathways in the cell. J. Biol. Chem. 2014, 289, 6669–6690
    • (2014) J. Biol. Chem , vol.289 , pp. 6669-6690
    • Polling, S.1    Mok, Y.F.2    Ramdzan, Y.M.3    Turner, B.J.4    Yerbury, J.J.5    Hill, A.F.6    Hatters, D.M.7
  • 153
    • 84866883258 scopus 로고    scopus 로고
    • Kaganovich, D Compartmentalization of superoxide dismutase 1 (SOD1G93A) aggregates determines their toxicity
    • Weisberg, S.J.; Lyakhovetsky, R.; Werdiger, A.-C.; Gitler, A.D.; Soen, Y.; Kaganovich, D Compartmentalization of superoxide dismutase 1 (SOD1G93A) aggregates determines their toxicity. Proc. Natl. Acad. Sci. USA 2012, 109, 15811–15816
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 15811-15816
    • Weisberg, S.J.1    Lyakhovetsky, R.2    Werdiger, A.-C.3    Gitler, A.D.4    Soen, Y.5
  • 155
    • 84886440159 scopus 로고    scopus 로고
    • Protein folding: Misfolded proteins join the Q
    • Wrighton, K.H. Protein folding: Misfolded proteins join the Q. Nat. Rev. Mol. Cell Biol. 2013, 14, 608
    • (2013) Nat. Rev. Mol. Cell Biol , vol.14 , pp. 608
    • Wrighton, K.H.1
  • 156
    • 84930746830 scopus 로고    scopus 로고
    • The biology of proteostasis in aging and disease
    • Labbadia, J.; Morimoto, R.I. The biology of proteostasis in aging and disease. Annu. Rev. Biochem2015, doi:10.1146/annurev-biochem-060614-033955
    • (2015) Annu. Rev. Biochem
    • Labbadia, J.1    Morimoto, R.I.2
  • 157
    • 77955844171 scopus 로고    scopus 로고
    • Chaperone networks: Tipping the balance in protein folding diseases
    • Voisine, C.; Pedersen, J.S.; Morimoto, R.I. Chaperone networks: Tipping the balance in protein folding diseases. Neurobiol. Dis. 2010, 40, 12–20
    • (2010) Neurobiol. Dis , vol.40 , pp. 12-20
    • Voisine, C.1    Pedersen, J.S.2    Morimoto, R.I.3
  • 158
    • 84863723691 scopus 로고    scopus 로고
    • Selective destruction of abnormal proteins by ubiquitin-mediated protein quality control degradation
    • Fredrickson, E.K.; Gardner, R.G. Selective destruction of abnormal proteins by ubiquitin-mediated protein quality control degradation. Semin. Cell Dev. Biol. 2012, 23, 530–537
    • (2012) Semin. Cell Dev. Biol , vol.23 , pp. 530-537
    • Fredrickson, E.K.1    Gardner, R.G.2
  • 159
    • 72549095406 scopus 로고    scopus 로고
    • Regulation mechanisms and signaling pathways of autophagy
    • He, C.; Klionsky, D.J. Regulation mechanisms and signaling pathways of autophagy Annu. Rev. Genet. 2009, 43, 67–93
    • (2009) Annu. Rev. Genet , vol.43 , pp. 67-93
    • He, C.1    Klionsky, D.J.2
  • 160
    • 84890203542 scopus 로고    scopus 로고
    • Regulation of proteasome activity in health and disease
    • Schmidt, M.; Finley, D. Regulation of proteasome activity in health and disease Biochim. Biophys. Acta 2014, 1843, 13–25
    • (2014) Biochim. Biophys. Acta , vol.1843 , pp. 13-25
    • Schmidt, M.1    Finley, D.2
  • 164
    • 84859702750 scopus 로고    scopus 로고
    • Molecular model of the human 26S proteasome
    • Da Fonseca, P.C.A.; He, J.; Morris, E.P. Molecular model of the human 26S proteasome Mol. Cell 2012, 46, 54–66
    • (2012) Mol. Cell , vol.46 , pp. 54-66
    • Da Fonseca, P.1    He, J.2    Morris, E.P.3
  • 167
    • 59249084491 scopus 로고    scopus 로고
    • The proteasome: Overview of structure and functions
    • Tanaka, K. The proteasome: Overview of structure and functions. Proc. Jpn. Acad. Ser. B 2009, 85, 12–36.
    • (2009) Proc. Jpn. Acad. Ser. B , vol.85 , pp. 12-36
    • Tanaka, K.1
  • 168
    • 69249241853 scopus 로고    scopus 로고
    • Variably modulated gating of the 26S proteasome by ATP and polyubiquitin
    • Li, X.; Demartino, G.N. Variably modulated gating of the 26S proteasome by ATP and polyubiquitin. Biochem. J. 2009, 421, 397–404
    • (2009) Biochem. J , vol.421 , pp. 397-404
    • Li, X.1    Demartino, G.N.2
  • 169
    • 84876412543 scopus 로고    scopus 로고
    • Allosteric effects in the regulation of 26S proteasome activities
    • Sledź, P.; Förster, F.; Baumeister, W.J. Allosteric effects in the regulation of 26S proteasome activities. Mol. Biol. 2013, 425, 1415–1423
    • (2013) Mol. Biol , vol.425 , pp. 1415-1423
    • Sledź, P.1    Förster, F.2    Baumeister, W.J.3
  • 170
    • 0025770134 scopus 로고
    • The distribution of tangles, plaques and related immunohistochemical markers in healthy aging and Alzheimer’s disease
    • Price, J.L.; Davis, P.B.; Morris, J.C.; White, D.L. The distribution of tangles, plaques and related immunohistochemical markers in healthy aging and Alzheimer’s disease. Neurobiol. Aging 1991, 12, 295–312
    • (1991) Neurobiol. Aging , vol.12 , pp. 295-312
    • Price, J.L.1    Davis, P.B.2    Morris, J.C.3    White, D.L.4
  • 174
    • 0037383052 scopus 로고    scopus 로고
    • Relationship between β-amyloid degradation and the 26S proteasome in neural cells
    • Lopez Salon, M.; Pasquini, L.; Besio Moreno, M.; Pasquini, J.M.; Soto, E. Relationship between β-amyloid degradation and the 26S proteasome in neural cells. Exp. Neurol. 2003, 180, 131–143
    • (2003) Exp. Neurol , vol.180 , pp. 131-143
    • Lopez Salon, M.1    Pasquini, L.2    Besio Moreno, M.3    Pasquini, J.M.4    Soto, E.5
  • 176
    • 84873660610 scopus 로고    scopus 로고
    • Autophagy in human health and disease
    • Choi, A.M.; Ryter, S.W.; Levine, B. Autophagy in human health and disease. N. Engl. J. Med 2013, 368, 651–662
    • (2013) N. Engl. J. Med , vol.368 , pp. 651-662
    • Choi, A.M.1    Ryter, S.W.2    Levine, B.3
  • 177
    • 84922946917 scopus 로고    scopus 로고
    • . Protein quality control and metabolism: Bidirectional control in the heart
    • Wang, Z.V.; Hill, J.A. Protein quality control and metabolism: Bidirectional control in the heart Cell Metab. 2015, 21, 215–226
    • (2015) Cell Metab , vol.21 , pp. 215-226
    • Wang, Z.V.1    Hill, J.A.2
  • 178
    • 84878562770 scopus 로고    scopus 로고
    • Autophagic processes in yeast: Mechanism, machinery and regulation
    • Reggiori, F.; Klionsky, D.J. Autophagic processes in yeast: Mechanism, machinery and regulation. Genetics 2013, 194, 341–361
    • (2013) Genetics , vol.194 , pp. 341-361
    • Reggiori, F.1    Klionsky, D.J.2
  • 179
    • 84937431778 scopus 로고    scopus 로고
    • Mechanisms of autophagy
    • Noda, N.N.; Inagaki, F. Mechanisms of autophagy. Annu. Rev. Biophys. 2015, doi:10.1146/ annurev-biophys-060414-034248
    • (2015) Annu. Rev. Biophys
    • Noda, N.N.1    Inagaki, F.2
  • 180
    • 84891741302 scopus 로고    scopus 로고
    • Chaperone-mediated autophagy: Roles in disease and aging
    • Cuervo, A.M.; Wong, E. Chaperone-mediated autophagy: Roles in disease and aging. Cell Res2014, 24, 92–104
    • (2014) Cell Res , vol.24 , pp. 92-104
    • Cuervo, A.M.1    Wong, E.2
  • 181
    • 77951214016 scopus 로고    scopus 로고
    • Mammalian autophagy: Core molecular machinery and signaling regulation
    • Yang, Z.; Klionsky, D.J. Mammalian autophagy: Core molecular machinery and signaling regulation. Curr. Opin. Cell Biol. 2010, 22, 124–131
    • (2010) Curr. Opin. Cell Biol , vol.22 , pp. 124-131
    • Yang, Z.1    Klionsky, D.J.2
  • 182
    • 78649338141 scopus 로고    scopus 로고
    • Autophagy and the integrated stress response
    • Kroemer, G.; Mariño, G.; Levine, B. Autophagy and the integrated stress response. Mol. Cell 2010, 40, 280–293
    • (2010) Mol. Cell , vol.40 , pp. 280-293
    • Kroemer, G.1    Mariño, G.2    Levine, B.3
  • 183
    • 37649005234 scopus 로고    scopus 로고
    • Autophagy in the pathogenesis of disease
    • Levine, B.; Kroemer, G. Autophagy in the pathogenesis of disease. Cell 2008, 132, 27–42
    • (2008) Cell , vol.132 , pp. 27-42
    • Levine, B.1    Kroemer, G.2
  • 186
    • 34249798692 scopus 로고    scopus 로고
    • Autophagic and apoptotic response to stress signals in mammalian cells
    • Ferraro, E.; Cecconi, F. Autophagic and apoptotic response to stress signals in mammalian cells Arch. Biochem. Biophys. 2007, 462, 210–219.
    • (2007) Arch. Biochem. Biophys , vol.462 , pp. 210-219
    • Ferraro, E.1    Cecconi, F.2
  • 187
    • 84871650725 scopus 로고    scopus 로고
    • Small molecules that target protein misfolding
    • Gavrin, L.K.; Denny, R.A.; Saiah, E. Small molecules that target protein misfolding. J. Med. Chem 2012, 55, 10823–10843
    • (2012) J. Med. Chem , vol.55 , pp. 10823-10843
    • Gavrin, L.K.1    Denny, R.A.2    Saiah, E.3
  • 188
    • 84887606872 scopus 로고    scopus 로고
    • Widespread aggregation and neurodegenerative diseases are associated with supersaturated proteins
    • Ciryam, P.; Tartaglia, G.G.; Morimoto, R.I.; Dobson, C.M.; Vendruscolo, M. Widespread aggregation and neurodegenerative diseases are associated with supersaturated proteins. Cell Rep 2013, 5, 781–790
    • (2013) Cell Rep , vol.5 , pp. 781-790
    • Ciryam, P.1    Tartaglia, G.G.2    Morimoto, R.I.3    Dobson, C.M.4    Vendruscolo, M.5
  • 189
    • 20444453307 scopus 로고    scopus 로고
    • Protein length in eukaryotic and prokaryotic proteomes
    • Brocchieri, L.; Karlin, S. Protein length in eukaryotic and prokaryotic proteomes. Nucleic Acids Res 2005, 33, 3390–3400
    • (2005) Nucleic Acids Res , vol.33 , pp. 3390-3400
    • Brocchieri, L.1    Karlin, S.2
  • 190
    • 18844413446 scopus 로고    scopus 로고
    • Structural insights into translational fidelity
    • Ogle, J.M.; Ramakrishnan, V. Structural insights into translational fidelity. Annu. Rev. Biochem 2005, 74, 129–177
    • (2005) Annu. Rev. Biochem , vol.74 , pp. 129-177
    • Ogle, J.M.1    Ramakrishnan, V.2
  • 191
    • 84873419140 scopus 로고    scopus 로고
    • The ribosome as a hub for protein quality control
    • Pechmann, S.; Willmund, F.; Frydman, J. The ribosome as a hub for protein quality control Mol. Cell 2013, 49, 411–421
    • (2013) Mol. Cell , vol.49 , pp. 411-421
    • Pechmann, S.1    Willmund, F.2    Frydman, J.3
  • 192
    • 34547638958 scopus 로고    scopus 로고
    • High expression rates of human islet amyloid polypeptide induce endoplasmic reticulum stress mediated β-cell apoptosis, a characteristic of humans with type 2 but not type 1 diabetes
    • Huang, C.J.; Lin, C.Y.; Haataja, L.; Gurlo, T.; Butler, A.E.; Rizza, R.A.; Butler, P.C. High expression rates of human islet amyloid polypeptide induce endoplasmic reticulum stress mediated β-cell apoptosis, a characteristic of humans with type 2 but not type 1 diabetes Diabetes 2007, 56, 2016–2027
    • (2007) Diabetes , vol.56 , pp. 2016-2027
    • Huang, C.J.1    Lin, C.Y.2    Haataja, L.3    Gurlo, T.4    Butler, A.E.5    Rizza, R.A.6    Butler, P.C.7
  • 194
    • 77958487260 scopus 로고    scopus 로고
    • Cellular strategies for controlling protein aggregation
    • Tyedmers, J.; Mogk, A.; Bukau, B. Cellular strategies for controlling protein aggregation Nat. Rev. Mol. Cell Biol. 2010, 11, 777–788
    • (2010) Nat. Rev. Mol. Cell Biol , vol.11 , pp. 777-788
    • Tyedmers, J.1    Mogk, A.2    Bukau, B.3
  • 195
    • 0035947372 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome system by protein aggregation
    • Bence, N.F.; Sampat, R.M.; Kopito, R.R. Impairment of the ubiquitin-proteasome system by protein aggregation. Science 2001, 292, 1552–1555
    • (2001) Science , vol.292 , pp. 1552-1555
    • Bence, N.F.1    Sampat, R.M.2    Kopito, R.R.3
  • 196
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • Ross, C.A.; Poirier, M.A. Protein aggregation and neurodegenerative disease. Nat. Med. 2004, 10, S10–S17
    • (2004) Nat. Med , vol.10
    • Ross, C.A.1    Poirier, M.A.2
  • 197
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman, M.H.; Ciechanover, A. The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction. Physiol. Rev.2002, 82, 373–428
    • (2002) Physiol. Rev , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 198
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • Rubinsztein, D.C. The roles of intracellular protein-degradation pathways in neurodegeneration Nature 2006, 443, 780–786
    • (2006) Nature , vol.443 , pp. 780-786
    • Rubinsztein, D.C.1
  • 199
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • Mizushima, N.; Levine, B.; Cuervo, A.M.; Klionsky, D.J. Autophagy fights disease through cellular self-digestion. Nature 2008, 451, 1069–1075
    • (2008) Nature , vol.451 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 200
    • 34547227879 scopus 로고    scopus 로고
    • Kinetics and thermodynamics of amyloid formation from direct measurements of fluctuations in fibril mass
    • Knowles, T.P.J.; Shu, W.; Devlin, G.L.; Meehan, S.; Auer, S.; Dobson, C.M.; Welland, M.E Kinetics and thermodynamics of amyloid formation from direct measurements of fluctuations in fibril mass. Proc. Natl. Acad. Sci. USA2007, 104, 10016–10021
    • (2007) . Proc. Natl. Acad. Sci. Usa , vol.104 , pp. 10016-10021
    • Knowles, T.1    Shu, W.2    Devlin, G.L.3    Meehan, S.4    Auer, S.5    Dobson, C.M.6    Welland, M.E.7
  • 202
    • 84892646801 scopus 로고    scopus 로고
    • Unfolded protein response signaling and metabolic diseases
    • Lee, J.; Ozcan, U. Unfolded protein response signaling and metabolic diseases. J. Biol. Chem 2014, 289, 1203–1211
    • (2014) J. Biol. Chem , vol.289 , pp. 1203-1211
    • Lee, J.1    Ozcan, U.2
  • 203
    • 77951245032 scopus 로고    scopus 로고
    • Finding order within disorder: Elucidating the structure of proteins associated with neurodegenerative disease
    • Huang, A.; Stultz, C.M. Finding order within disorder: Elucidating the structure of proteins associated with neurodegenerative disease. Future Med. Chem.2009, 1, 467–482
    • (2009) Future Med. Chem , vol.1 , pp. 467-482
    • Huang, A.1    Stultz, C.M.2
  • 205
    • 84897094564 scopus 로고    scopus 로고
    • Disturbance of endoplasmic reticulum proteostasis in neurodegenerative diseases
    • Hetz, C.; Mollereau, B. Disturbance of endoplasmic reticulum proteostasis in neurodegenerative diseases. Nat. Rev. Neurosci. 2014, 15, 233–249
    • (2014) Nat. Rev. Neurosci , vol.15 , pp. 233-249
    • Hetz, C.1    Mollereau, B.2
  • 206
    • 0034568802 scopus 로고    scopus 로고
    • Intramembrane proteolysis by presenilins
    • Steiner, H.; Haass, C. Intramembrane proteolysis by presenilins. Nat. Rev. Mol. Cell Biol. 2000, 1, 217–224
    • (2000) Nat. Rev. Mol. Cell Biol , vol.1 , pp. 217-224
    • Steiner, H.1    Haass, C.2
  • 207
    • 79551603345 scopus 로고    scopus 로고
    • Bioenergetics of neurons inhibit the translocation response of Parkin following rapid mitochondrial depolarization
    • Van Laar, V.S.; Arnold, B.; Cassady, S.J.; Chu, C.T.; Burton, E.A.; Berman, S.B.; Bioenergetics of neurons inhibit the translocation response of Parkin following rapid mitochondrial depolarization. Hum. Mol. Genet. 2011, 20, 927–940
    • (2011) Hum. Mol. Genet , vol.20 , pp. 927-940
    • Van Laar, V.S.1    Arnold, B.2    Cassady, S.J.3    Chu, C.T.4    Burton, E.A.5    Berman, S.B.6
  • 208
    • 84875143788 scopus 로고    scopus 로고
    • Targeting endoplasmic reticulum stress in metabolic disease
    • Cao, S.S.; Kaufman, R.J. Targeting endoplasmic reticulum stress in metabolic disease. Expert Opin Ther. Targets 2012, 17, 437–448
    • (2012) Expert Opin Ther. Targets , vol.17 , pp. 437-448
    • Cao, S.S.1    Kaufman, R.J.2
  • 209
    • 77950343252 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and the inflammatory basis of metabolic disease
    • Hotamisligil, G.S. Endoplasmic reticulum stress and the inflammatory basis of metabolic disease Cell 2010, 140, 900–917
    • (2010) Cell , vol.140 , pp. 900-917
    • Hotamisligil, G.S.1
  • 210
    • 84873527000 scopus 로고    scopus 로고
    • Aggregation of islet amyloid polypeptide: From physical chemistry to cell biology
    • Cao, P.; Abedini, A.; Raleigh, D.P. Aggregation of islet amyloid polypeptide: From physical chemistry to cell biology. Curr. Opin. Struct. Biol. 2013, 23, 82–89
    • (2013) Curr. Opin. Struct. Biol , vol.23 , pp. 82-89
    • Cao, P.1    Abedini, A.2    Raleigh, D.P.3
  • 211
    • 84912064413 scopus 로고    scopus 로고
    • Human IAPP amyloidogenic properties and pancreatic β-cell death
    • Fernández, M.S. Human IAPP amyloidogenic properties and pancreatic β-cell death. Cell Calcium 2014, 56, 416–427
    • (2014) Cell Calcium , vol.56 , pp. 416-427
    • Fernández, M.S.1
  • 212
    • 34548462199 scopus 로고    scopus 로고
    • Impairment of the ubiquitin-proteasome pathway is a downstream endoplasmic reticulum stress response induced by extracellular human islet amyloid polypeptide and contributes to pancreatic β-cell apoptosis
    • Casas, S.; Gomis, R.; Gribble, F.M.; Altirriba, J.; Knuutila, S.; Novials, A. Impairment of the ubiquitin-proteasome pathway is a downstream endoplasmic reticulum stress response induced by extracellular human islet amyloid polypeptide and contributes to pancreatic β-cell apoptosis Diabetes 2007, 56, 2284–2294
    • (2007) Diabetes , vol.56 , pp. 2284-2294
    • Casas, S.1    Gomis, R.2    Gribble, F.M.3    Altirriba, J.4    Knuutila, S.5    Novials, A.6
  • 213
    • 78751490442 scopus 로고    scopus 로고
    • β-cell dysfunctional ERAD/ubiquitin/proteasome system in type 2 diabetes mediated by islet amyloid polypeptide-induced UCH-L1 deficiency
    • Costes, S.; Huang, C.J.; Gurlo, T.; Daval, M.; Matveyenko, A.V.; Rizza, R.A.; Butler, A.E.; Butler, P.C. β-cell dysfunctional ERAD/ubiquitin/proteasome system in type 2 diabetes mediated by islet amyloid polypeptide-induced UCH-L1 deficiency. Diabetes 2011, 60, 227–238
    • (2011) Diabetes , vol.60 , pp. 227-238
    • Costes, S.1    Huang, C.J.2    Gurlo, T.3    Daval, M.4    Matveyenko, A.V.5    Rizza, R.A.6    Butler, A.E.7    Butler, P.C.8
  • 215
    • 1342286820 scopus 로고    scopus 로고
    • Mono-unsaturated fatty acids protect against β-cell apoptosis induced by saturated fatty acids, serum withdrawal or cytokine exposure
    • Welters, H.J.; Tadayyon, M.; Scarpello, J.H.; Smith, S.A.; Morgan, N.G. Mono-unsaturated fatty acids protect against β-cell apoptosis induced by saturated fatty acids, serum withdrawal or cytokine exposure. FEBS Lett. 2004, 560, 103–108
    • (2004) FEBS Lett , vol.560 , pp. 103-108
    • Welters, H.J.1    Tadayyon, M.2    Scarpello, J.H.3    Smith, S.A.4    Morgan, N.G.5
  • 217
    • 77958003056 scopus 로고    scopus 로고
    • The role of endoplasmic reticulum stress in the progression of atherosclerosis
    • Tabas, I. The role of endoplasmic reticulum stress in the progression of atherosclerosis. Circ. Res 2010, 107, 839–850
    • (2010) Circ. Res , vol.107 , pp. 839-850
    • Tabas, I.1
  • 218
    • 0036853914 scopus 로고    scopus 로고
    • Orchestrating the unfolded protein response in health and disease
    • Kaufman, R.J. Orchestrating the unfolded protein response in health and disease. J. Clin. Investig2002, 110, 1389–1398
    • (2002) J. Clin. Investig , vol.110 , pp. 1389-1398
    • Kaufman, R.J.1
  • 219
    • 68049110633 scopus 로고    scopus 로고
    • IRE1α kinase activation modes control alternate endoribonuclease outputs to determine divergent cell fates
    • Han, D.; Lerner, A.G.; Vande, W.L.; Upton, J.P.; Xu, W.; Hagen, A.; Backes, B.J.; Oakes, S.A.; Papa, F.R. IRE1α kinase activation modes control alternate endoribonuclease outputs to determine divergent cell fates. Cell 2009, 138, 562–575
    • (2009) Cell , vol.138 , pp. 562-575
    • Han, D.1    Lerner, A.G.2    Vande, W.L.3    Upton, J.P.4    Xu, W.5    Hagen, A.6    Backes, B.J.7    Oakes, S.A.8    Papa, F.R.9
  • 220
    • 77954225337 scopus 로고    scopus 로고
    • Small molecule inhibitor of endoplasmic reticulum oxidation 1 (ERO1) with selectively reversible thiol reactivity
    • Blais, J.D.; Chin, K.T.; Zito, E.; Zhang, Y.; Heldman, N.; Harding, H.P.; Fass, D.; Thorpe, C.; Ron, D.A. Small molecule inhibitor of endoplasmic reticulum oxidation 1 (ERO1) with selectively reversible thiol reactivity. J. Biol. Chem. 2010, 285, 20993–21003
    • (2010) J. Biol. Chem , vol.285 , pp. 20993-21003
    • Blais, J.D.1    Chin, K.T.2    Zito, E.3    Zhang, Y.4    Heldman, N.5    Harding, H.P.6    Fass, D.7    Thorpe, C.8    Ron, D.A.9
  • 221
    • 10344222124 scopus 로고    scopus 로고
    • The role of the unfolded protein response in tumour development: Friend or foe?
    • Ma, Y.; Hendershot, L.M. The role of the unfolded protein response in tumour development: Friend or foe? Nat. Rev. Cancer 2004, 4, 966–977.
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 966-977
    • Ma, Y.1    Hendershot, L.M.2
  • 222
    • 36348943088 scopus 로고    scopus 로고
    • Integrated endoplasmic reticulum stress responses in cancer
    • Moenner, M.; Pluquet, O.; Bouchecareilh, M.; Chevet, E. Integrated endoplasmic reticulum stress responses in cancer. Cancer Res. 2007, 67, 10631–10634
    • (2007) Cancer Res , vol.67 , pp. 10631-10634
    • Moenner, M.1    Pluquet, O.2    Bouchecareilh, M.3    Chevet, E.4
  • 225
    • 75149165640 scopus 로고    scopus 로고
    • Imaging the unfolded protein response in primary tumors reveals microenvironments with metabolic variations that predict tumor growth
    • Spiotto, M.T.; Banh, A.; Papandreou, I.; Cao, H.; Galvez, M.G.; Gurtner, G.C.; Denko, N.C.; Le, Q.T.; Koong, A.C. Imaging the unfolded protein response in primary tumors reveals microenvironments with metabolic variations that predict tumor growth. Cancer Res. 2010, 70, 78–88
    • (2010) Cancer Res , vol.70 , pp. 78-88
    • Spiotto, M.T.1    Banh, A.2    Papandreou, I.3    Cao, H.4    Galvez, M.G.5    Gurtner, G.C.6    Denko, N.C.7    Le, Q.T.8    Koong, A.C.9
  • 226
    • 34248571826 scopus 로고    scopus 로고
    • GRP78 induction in cancer: Therapeutic and prognostic implications
    • Lee, A.S. GRP78 induction in cancer: Therapeutic and prognostic implications. Cancer Res 2007, 67, 3496–3499
    • (2007) Cancer Res , vol.67 , pp. 3496-3499
    • Lee, A.S.1
  • 227
    • 35448967382 scopus 로고    scopus 로고
    • The unfolded protein response regulator GRP78/BiP as a novel target for increasing chemosensitivity in malignant gliomas
    • Pyrko, P.; Schonthal, A.H.; Hofman, F.M.; Chen, T.C.; Lee, A.S. The unfolded protein response regulator GRP78/BiP as a novel target for increasing chemosensitivity in malignant gliomas Cancer Res. 2007, 67, 9809–9816
    • (2007) Cancer Res , vol.67 , pp. 9809-9816
    • Pyrko, P.1    Schonthal, A.H.2    Hofman, F.M.3    Chen, T.C.4    Lee, A.S.5
  • 228
    • 79951590699 scopus 로고    scopus 로고
    • GRP78/BiP modulation of GRP78/BiP in altering sensitivity to chemotherapy
    • Chen, T.C. GRP78/BiP modulation of GRP78/BiP in altering sensitivity to chemotherapy Methods Enzymol. 2011, 491, 25–36
    • (2011) Methods Enzymol , vol.491 , pp. 25-36
    • Chen, T.C.1
  • 229
    • 79951857650 scopus 로고    scopus 로고
    • Unfolded protein response in cancer: The physician’s perspective
    • Li, X.; Zhang, K.; Li, Z. Unfolded protein response in cancer: The physician’s perspective J. Hematol. Oncol. 2011, 4, 8
    • (2011) J. Hematol. Oncol , vol.4
    • Li, X.1    Zhang, K.2    Li, Z.3
  • 231
    • 66249092010 scopus 로고    scopus 로고
    • Chemical genomics identifies the unfolded protein response as a target for selective cancer cell killing during glucose deprivation
    • Saito, S.; Furuno, A.; Sakurai, J.; Sakamoto, A.; Park, H.R.; Shin-Ya, K.; Tsuruo, T.; Tomida, A Chemical genomics identifies the unfolded protein response as a target for selective cancer cell killing during glucose deprivation. Cancer Res. 2009, 69, 4225–4234
    • (2009) Cancer Res , vol.69 , pp. 4225-4234
    • Saito, S.1    Furuno, A.2    Sakurai, J.3    Sakamoto, A.4    Park, H.R.5    Shin-Ya, K.6    Tsuruo, T.7    Tomida, A.8
  • 234
  • 235
    • 0027983669 scopus 로고
    • Crystal structure of a p53 tumor suppressor-DNA complex: Understanding tumorigenic mutations
    • Cho, Y.; Gorina, S.; Jeffrey, P.D.; Pavletich, N.P. Crystal structure of a p53 tumor suppressor-DNA complex: Understanding tumorigenic mutations. Science 1994, 265, 346–355
    • (1994) Science , vol.265 , pp. 346-355
    • Cho, Y.1    Gorina, S.2    Jeffrey, P.D.3    Pavletich, N.P.4
  • 236
    • 34547689085 scopus 로고    scopus 로고
    • Loss-of-function genetic diseases and the concept of pharmaceutical targets
    • Segalat, L. Loss-of-function genetic diseases and the concept of pharmaceutical targets Orphanet. J. Rare Dis. 2007, 2, 30–36
    • (2007) Orphanet. J. Rare Dis , vol.2 , pp. 30-36
    • Segalat, L.1
  • 237
  • 239
    • 0035253217 scopus 로고    scopus 로고
    • Macromolecular crowding: An important but neglected aspect of the intracellular environment
    • Ellis, R.J. Macromolecular crowding: An important but neglected aspect of the intracellular environment. Curr. Opin. Struct. Biol. 2001, 11, 114–119
    • (2001) Curr. Opin. Struct. Biol , vol.11 , pp. 114-119
    • Ellis, R.J.1
  • 242
    • 0037117499 scopus 로고    scopus 로고
    • Aggregation of proteins with expanded glutamine and alanine repeats of the glutamine-rich and asparagine rich domains of Sup35 and of the amyloid β-peptide of amyloid plaques
    • Perutz, M.F.; Pope, B.J.; Owen, D.; Wanker, E.E.; Scherzinger, E. Aggregation of proteins with expanded glutamine and alanine repeats of the glutamine-rich and asparagine rich domains of Sup35 and of the amyloid β-peptide of amyloid plaques. Proc. Natl. Acad. Sci. USA 2002, 99, 5596–5600
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 5596-5600
    • Perutz, M.F.1    Pope, B.J.2    Owen, D.3    Wanker, E.E.4    Scherzinger, E.5
  • 245
    • 28244502156 scopus 로고    scopus 로고
    • Native state kinetic stabilization as a strategy to ameliorate protein misfolding diseases: A focus on the transthyretin amyloidoses
    • Johnson, S.M.; Wiseman, R.L.; Sekijima, Y.; Green, N.S.; Adamski-Werner, S.L.; Kelly, J.W Native state kinetic stabilization as a strategy to ameliorate protein misfolding diseases: A focus on the transthyretin amyloidoses. Acc. Chem. Res.2005, 38, 911–921
    • (2005) Acc. Chem. Res , vol.38 , pp. 911-921
    • Johnson, S.M.1    Wiseman, R.L.2    Sekijima, Y.3    Green, N.S.4    Adamski-Werner, S.L.5    Kelly, J.W.6
  • 246
    • 0033616682 scopus 로고    scopus 로고
    • Evolution of amyloid: What normal protein folding may tell us about fibrillogenesis and disease?
    • Lansbury, P. Evolution of amyloid: What normal protein folding may tell us about fibrillogenesis and disease? Proc. Natl. Acad. Sci. USA 1999, 96, 3342–3344
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3342-3344
    • Lansbury, P.1
  • 247
    • 84883387793 scopus 로고    scopus 로고
    • Targeting the unfolded protein response in disease
    • Hetz, C.; Chevet, E.; Harding, H.P. Targeting the unfolded protein response in disease. Nat. Rev Drug Discov. 2013, 12, 703–719
    • (2013) Nat. Rev Drug Discov , vol.12 , pp. 703-719
    • Hetz, C.1    Chevet, E.2    Harding, H.P.3
  • 248
    • 84856551514 scopus 로고    scopus 로고
    • InterfERing with endoplasmic reticulum stress
    • Kraskiewicz, H.; FitzGerald, U. InterfERing with endoplasmic reticulum stress. Trends Pharmacol. Sci2012, 33, 53–63
    • (2012) Trends Pharmacol. Sci , vol.33 , pp. 53-63
    • Kraskiewicz, H.1    Fitzgerald, U.2
  • 249
    • 84863903065 scopus 로고    scopus 로고
    • Chemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases: Progress and prognosis
    • Lindquist, S.L.; Kelly, J.W. Chemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases: Progress and prognosis. Cold Spring Harb. Perspect. Biol. 2011, 3, a004507
    • (2011) Cold Spring Harb. Perspect. Biol , vol.3
    • Lindquist, S.L.1    Kelly, J.W.2
  • 251
    • 57849115277 scopus 로고    scopus 로고
    • Ozcan, U Endoplasmic reticulum stress plays a central role in development of leptin resistance
    • Ozcan, L.; Ergin, A.S.; Lu, A.; Chung, J.; Sarkar, S.; Nie, D.; Myers, M.G.,; Ozcan, U Endoplasmic reticulum stress plays a central role in development of leptin resistance. Cell Metab 2009, 9, 35–51
    • (2009) Cell Metab , vol.9 , pp. 35-51
    • Ozcan, L.1    Ergin, A.S.2    Lu, A.3    Chung, J.4    Sarkar, S.5    Nie, D.6    Myers, M.G.7
  • 252
    • 79952410092 scopus 로고    scopus 로고
    • Sodium phenylbutyrate, a drug with known capacity to reduce endoplasmic reticulum stress, partially alleviates lipid-induced insulin resistance and β-cell dysfunction in humans
    • Xiao, C.; Giacca, A.; Lewis, G.F. Sodium phenylbutyrate, a drug with known capacity to reduce endoplasmic reticulum stress, partially alleviates lipid-induced insulin resistance and β-cell dysfunction in humans. Diabetes 2011, 60, 918–924.
    • (2011) Diabetes , vol.60 , pp. 918-924
    • Xiao, C.1    Giacca, A.2    Lewis, G.F.3
  • 255
    • 77950887221 scopus 로고    scopus 로고
    • Flavonol activation defines an unanticipated ligand-binding site in the kinase-RNase domain of IRE1
    • Wiseman, R.L.; Zhang, Y.; Lee, K.P.; Harding, H.P.; Haynes, C.M.; Price, J.; Sicheri, F.; Ron, D. Flavonol activation defines an unanticipated ligand-binding site in the kinase-RNase domain of IRE1. Mol. Cell2010, 38, 291–304
    • (2010) Mol. Cell , vol.38 , pp. 291-304
    • Wiseman, R.L.1    Zhang, Y.2    Lee, K.P.3    Harding, H.P.4    Haynes, C.M.5    Price, J.6    Sicheri, F.7    Ron, D.8
  • 256
    • 0033601370 scopus 로고    scopus 로고
    • Pharmacological rescue of mutant p53 conformation and function
    • Foster, B.A.; Coffey, H.A.; Morin, M.J.; Rastinejad, F. Pharmacological rescue of mutant p53 conformation and function. Science1999, 286, 2507–2510
    • (1999) Science , vol.286 , pp. 2507-2510
    • Foster, B.A.1    Coffey, H.A.2    Morin, M.J.3    Rastinejad, F.4


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