메뉴 건너뛰기




Volumn 157, Issue 1, 2014, Pages 52-64

Differential scales of protein quality control

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; PROTEIN; PROTEOME; UBIQUITINATED PROTEIN;

EID: 84897129156     PISSN: 00928674     EISSN: 10974172     Source Type: Journal    
DOI: 10.1016/j.cell.2014.03.007     Document Type: Review
Times cited : (194)

References (137)
  • 2
    • 0242585476 scopus 로고    scopus 로고
    • Asymmetric inheritance of oxidatively damaged proteins during cytokinesis
    • H. Aguilaniu, L. Gustafsson, M. Rigoulet, and T. Nyström Asymmetric inheritance of oxidatively damaged proteins during cytokinesis Science 299 2003 1751 1753
    • (2003) Science , vol.299 , pp. 1751-1753
    • Aguilaniu, H.1    Gustafsson, L.2    Rigoulet, M.3    Nyström, T.4
  • 3
    • 0022455603 scopus 로고
    • Abnormal proteins serve as eukaryotic stress signals and trigger the activation of heat shock genes
    • J. Ananthan, A.L. Goldberg, and R. Voellmy Abnormal proteins serve as eukaryotic stress signals and trigger the activation of heat shock genes Science 232 1986 522 524
    • (1986) Science , vol.232 , pp. 522-524
    • Ananthan, J.1    Goldberg, A.L.2    Voellmy, R.3
  • 4
    • 4344568810 scopus 로고    scopus 로고
    • Protein crystallization and phase diagrams
    • N. Asherie Protein crystallization and phase diagrams Methods 34 2004 266 272
    • (2004) Methods , vol.34 , pp. 266-272
    • Asherie, N.1
  • 5
    • 84866782195 scopus 로고    scopus 로고
    • Eukaryotic initiation factor 2 phosphorylation and translational control in metabolism
    • T.D. Baird, and R.C. Wek Eukaryotic initiation factor 2 phosphorylation and translational control in metabolism Adv. Nutr. 3 2012 307 321
    • (2012) Adv. Nutr. , vol.3 , pp. 307-321
    • Baird, T.D.1    Wek, R.C.2
  • 8
    • 70349266064 scopus 로고    scopus 로고
    • Collapse of proteostasis represents an early molecular event in Caenorhabditis elegans aging
    • A. Ben-Zvi, E.A. Miller, and R.I. Morimoto Collapse of proteostasis represents an early molecular event in Caenorhabditis elegans aging Proc. Natl. Acad. Sci. USA 106 2009 14914 14919
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 14914-14919
    • Ben-Zvi, A.1    Miller, E.A.2    Morimoto, R.I.3
  • 9
    • 33748901113 scopus 로고    scopus 로고
    • Ubiquitin-like protein 5 positively regulates chaperone gene expression in the mitochondrial unfolded protein response
    • C. Benedetti, C.M. Haynes, Y. Yang, H.P. Harding, and D. Ron Ubiquitin-like protein 5 positively regulates chaperone gene expression in the mitochondrial unfolded protein response Genetics 174 2006 229 239
    • (2006) Genetics , vol.174 , pp. 229-239
    • Benedetti, C.1    Haynes, C.M.2    Yang, Y.3    Harding, H.P.4    Ron, D.5
  • 10
    • 77957169824 scopus 로고    scopus 로고
    • Role of a ribosome-associated E3 ubiquitin ligase in protein quality control
    • M.H. Bengtson, and C.A. Joazeiro Role of a ribosome-associated E3 ubiquitin ligase in protein quality control Nature 467 2010 470 473
    • (2010) Nature , vol.467 , pp. 470-473
    • Bengtson, M.H.1    Joazeiro, C.A.2
  • 14
    • 84856625798 scopus 로고    scopus 로고
    • High-resolution view of the yeast meiotic program revealed by ribosome profiling
    • G.A. Brar, M. Yassour, N. Friedman, A. Regev, N.T. Ingolia, and J.S. Weissman High-resolution view of the yeast meiotic program revealed by ribosome profiling Science 335 2012 552 557
    • (2012) Science , vol.335 , pp. 552-557
    • Brar, G.A.1    Yassour, M.2    Friedman, N.3    Regev, A.4    Ingolia, N.T.5    Weissman, J.S.6
  • 16
  • 21
    • 23944490117 scopus 로고    scopus 로고
    • Missense meanderings in sequence space: A biophysical view of protein evolution
    • M.A. DePristo, D.M. Weinreich, and D.L. Hartl Missense meanderings in sequence space: a biophysical view of protein evolution Nat. Rev. Genet. 6 2005 678 687
    • (2005) Nat. Rev. Genet. , vol.6 , pp. 678-687
    • Depristo, M.A.1    Weinreich, D.M.2    Hartl, D.L.3
  • 22
    • 70350136778 scopus 로고    scopus 로고
    • Polymorphisms in multiple genes contribute to the spontaneous mitochondrial genome instability of Saccharomyces cerevisiae S288C strains
    • L.N. Dimitrov, R.B. Brem, L. Kruglyak, and D.E. Gottschling Polymorphisms in multiple genes contribute to the spontaneous mitochondrial genome instability of Saccharomyces cerevisiae S288C strains Genetics 183 2009 365 383
    • (2009) Genetics , vol.183 , pp. 365-383
    • Dimitrov, L.N.1    Brem, R.B.2    Kruglyak, L.3    Gottschling, D.E.4
  • 23
    • 0021099528 scopus 로고
    • Identification and quantitation of levels of protein synthesis initiation factors in crude HeLa cell lysates by two-dimensional polyacrylamide gel electrophoresis
    • R. Duncan, and J.W. Hershey Identification and quantitation of levels of protein synthesis initiation factors in crude HeLa cell lysates by two-dimensional polyacrylamide gel electrophoresis J. Biol. Chem. 258 1983 7228 7235
    • (1983) J. Biol. Chem. , vol.258 , pp. 7228-7235
    • Duncan, R.1    Hershey, J.W.2
  • 24
    • 78650944949 scopus 로고    scopus 로고
    • The cell-non-autonomous nature of electron transport chain-mediated longevity
    • J. Durieux, S. Wolff, and A. Dillin The cell-non-autonomous nature of electron transport chain-mediated longevity Cell 144 2011 79 91
    • (2011) Cell , vol.144 , pp. 79-91
    • Durieux, J.1    Wolff, S.2    Dillin, A.3
  • 25
    • 84883210213 scopus 로고    scopus 로고
    • Principles of cotranslational ubiquitination and quality control at the ribosome
    • S. Duttler, S. Pechmann, and J. Frydman Principles of cotranslational ubiquitination and quality control at the ribosome Mol. Cell 50 2013 379 393
    • (2013) Mol. Cell , vol.50 , pp. 379-393
    • Duttler, S.1    Pechmann, S.2    Frydman, J.3
  • 26
    • 84885095437 scopus 로고    scopus 로고
    • Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress
    • S. Escusa-Toret, W.I. Vonk, and J. Frydman Spatial sequestration of misfolded proteins by a dynamic chaperone pathway enhances cellular fitness during stress Nat. Cell Biol. 15 2013 1231 1243
    • (2013) Nat. Cell Biol. , vol.15 , pp. 1231-1243
    • Escusa-Toret, S.1    Vonk, W.I.2    Frydman, J.3
  • 27
    • 84883049362 scopus 로고    scopus 로고
    • Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis
    • A. Finka, and P. Goloubinoff Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis Cell Stress Chaperones 18 2013 591 605
    • (2013) Cell Stress Chaperones , vol.18 , pp. 591-605
    • Finka, A.1    Goloubinoff, P.2
  • 28
    • 27144524290 scopus 로고    scopus 로고
    • Active HSF1 significantly suppresses polyglutamine aggregate formation in cellular and mouse models
    • M. Fujimoto, E. Takaki, T. Hayashi, Y. Kitaura, Y. Tanaka, S. Inouye, and A. Nakai Active HSF1 significantly suppresses polyglutamine aggregate formation in cellular and mouse models J. Biol. Chem. 280 2005 34908 34916
    • (2005) J. Biol. Chem. , vol.280 , pp. 34908-34916
    • Fujimoto, M.1    Takaki, E.2    Hayashi, T.3    Kitaura, Y.4    Tanaka, Y.5    Inouye, S.6    Nakai, A.7
  • 29
    • 80053369081 scopus 로고    scopus 로고
    • Unfolded proteins are Ire1-activating ligands that directly induce the unfolded protein response
    • B.M. Gardner, and P. Walter Unfolded proteins are Ire1-activating ligands that directly induce the unfolded protein response Science 333 2011 1891 1894
    • (2011) Science , vol.333 , pp. 1891-1894
    • Gardner, B.M.1    Walter, P.2
  • 30
    • 17644396667 scopus 로고    scopus 로고
    • Degradation-mediated protein quality control in the nucleus
    • R.G. Gardner, Z.W. Nelson, and D.E. Gottschling Degradation-mediated protein quality control in the nucleus Cell 120 2005 803 815
    • (2005) Cell , vol.120 , pp. 803-815
    • Gardner, R.G.1    Nelson, Z.W.2    Gottschling, D.E.3
  • 31
    • 79954456859 scopus 로고    scopus 로고
    • Determinants of translation efficiency and accuracy
    • H. Gingold, and Y. Pilpel Determinants of translation efficiency and accuracy Mol. Syst. Biol. 7 2011 481
    • (2011) Mol. Syst. Biol. , vol.7 , pp. 481
    • Gingold, H.1    Pilpel, Y.2
  • 32
    • 84890423994 scopus 로고    scopus 로고
    • Co-translational mechanisms of protein maturation
    • F. Gloge, A.H. Becker, G.n. Kramer, and B. Bukau Co-translational mechanisms of protein maturation Curr. Opin. Struct. Biol. 24 2014 24 33
    • (2014) Curr. Opin. Struct. Biol. , vol.24 , pp. 24-33
    • Gloge, F.1    Becker, A.H.2    Bukau, B.3
  • 33
    • 0032503968 scopus 로고    scopus 로고
    • Hsp104, Hsp70, and Hsp40: A novel chaperone system that rescues previously aggregated proteins
    • J.R. Glover, and S. Lindquist Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins Cell 94 1998 73 82
    • (1998) Cell , vol.94 , pp. 73-82
    • Glover, J.R.1    Lindquist, S.2
  • 35
    • 34548419344 scopus 로고    scopus 로고
    • Thematic review series: Adipocyte Biology. Adipocyte stress: The endoplasmic reticulum and metabolic disease
    • M.F. Gregor, and G.S. Hotamisligil Thematic review series: Adipocyte Biology. Adipocyte stress: the endoplasmic reticulum and metabolic disease J. Lipid Res. 48 2007 1905 1914
    • (2007) J. Lipid Res. , vol.48 , pp. 1905-1914
    • Gregor, M.F.1    Hotamisligil, G.S.2
  • 36
    • 84874028131 scopus 로고    scopus 로고
    • Essential nontranslational functions of tRNA synthetases
    • M. Guo, and P. Schimmel Essential nontranslational functions of tRNA synthetases Nat. Chem. Biol. 9 2013 145 153
    • (2013) Nat. Chem. Biol. , vol.9 , pp. 145-153
    • Guo, M.1    Schimmel, P.2
  • 37
    • 44249122651 scopus 로고    scopus 로고
    • Lilliputians get into the limelight: Novel class of small peptide genes in morphogenesis
    • Y. Hashimoto, T. Kondo, and Y. Kageyama Lilliputians get into the limelight: novel class of small peptide genes in morphogenesis Dev. Growth Differ. 50 Suppl 1 2008 S269 S276
    • (2008) Dev. Growth Differ. , vol.50 , Issue.SUPPL. 1
    • Hashimoto, Y.1    Kondo, T.2    Kageyama, Y.3
  • 38
    • 34848861368 scopus 로고    scopus 로고
    • ClpP mediates activation of a mitochondrial unfolded protein response in C elegans
    • C.M. Haynes, K. Petrova, C. Benedetti, Y. Yang, and D. Ron ClpP mediates activation of a mitochondrial unfolded protein response in C elegans Dev. Cell 13 2007 467 480
    • (2007) Dev. Cell , vol.13 , pp. 467-480
    • Haynes, C.M.1    Petrova, K.2    Benedetti, C.3    Yang, Y.4    Ron, D.5
  • 39
    • 76849100919 scopus 로고    scopus 로고
    • The matrix peptide exporter HAF-1 signals a mitochondrial UPR by activating the transcription factor ZC376.7 in C elegans
    • C.M. Haynes, Y. Yang, S.P. Blais, T.A. Neubert, and D. Ron The matrix peptide exporter HAF-1 signals a mitochondrial UPR by activating the transcription factor ZC376.7 in C elegans Mol. Cell 37 2010 529 540
    • (2010) Mol. Cell , vol.37 , pp. 529-540
    • Haynes, C.M.1    Yang, Y.2    Blais, S.P.3    Neubert, T.A.4    Ron, D.5
  • 41
    • 0001089240 scopus 로고
    • Actin gene mutations in Drosophila; Heat shock activation in the indirect flight muscles
    • Y. Hiromi, and Y. Hotta Actin gene mutations in Drosophila; heat shock activation in the indirect flight muscles EMBO J. 4 1985 1681 1687
    • (1985) EMBO J. , vol.4 , pp. 1681-1687
    • Hiromi, Y.1    Hotta, Y.2
  • 42
    • 0022552545 scopus 로고
    • Germline transformation with Drosophila mutant actin genes induces constitutive expression of heat shock genes
    • Y. Hiromi, H. Okamoto, W.J. Gehring, and Y. Hotta Germline transformation with Drosophila mutant actin genes induces constitutive expression of heat shock genes Cell 44 1986 293 301
    • (1986) Cell , vol.44 , pp. 293-301
    • Hiromi, Y.1    Okamoto, H.2    Gehring, W.J.3    Hotta, Y.4
  • 43
    • 33745893809 scopus 로고    scopus 로고
    • Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response
    • J. Hollien, and J.S. Weissman Decay of endoplasmic reticulum-localized mRNAs during the unfolded protein response Science 313 2006 104 107
    • (2006) Science , vol.313 , pp. 104-107
    • Hollien, J.1    Weissman, J.S.2
  • 44
    • 77950343252 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and the inflammatory basis of metabolic disease
    • G.S. Hotamisligil Endoplasmic reticulum stress and the inflammatory basis of metabolic disease Cell 140 2010 900 917
    • (2010) Cell , vol.140 , pp. 900-917
    • Hotamisligil, G.S.1
  • 46
    • 0038701745 scopus 로고    scopus 로고
    • Regulation of aging and age-related disease by DAF-16 and heat-shock factor
    • A.L. Hsu, C.T. Murphy, and C. Kenyon Regulation of aging and age-related disease by DAF-16 and heat-shock factor Science 300 2003 1142 1145
    • (2003) Science , vol.300 , pp. 1142-1145
    • Hsu, A.L.1    Murphy, C.T.2    Kenyon, C.3
  • 47
    • 84871011474 scopus 로고    scopus 로고
    • An early age increase in vacuolar pH limits mitochondrial function and lifespan in yeast
    • A.L. Hughes, and D.E. Gottschling An early age increase in vacuolar pH limits mitochondrial function and lifespan in yeast Nature 492 2012 261 265
    • (2012) Nature , vol.492 , pp. 261-265
    • Hughes, A.L.1    Gottschling, D.E.2
  • 48
    • 84877801536 scopus 로고    scopus 로고
    • Quality control systems for aberrant mRNAs induced by aberrant translation elongation and termination
    • T. Inada Quality control systems for aberrant mRNAs induced by aberrant translation elongation and termination Biochim. Biophys. Acta 1829 2013 634 642
    • (2013) Biochim. Biophys. Acta , vol.1829 , pp. 634-642
    • Inada, T.1
  • 49
    • 81055155799 scopus 로고    scopus 로고
    • Ribosome profiling of mouse embryonic stem cells reveals the complexity and dynamics of mammalian proteomes
    • N.T. Ingolia, L.F. Lareau, and J.S. Weissman Ribosome profiling of mouse embryonic stem cells reveals the complexity and dynamics of mammalian proteomes Cell 147 2011 789 802
    • (2011) Cell , vol.147 , pp. 789-802
    • Ingolia, N.T.1    Lareau, L.F.2    Weissman, J.S.3
  • 50
    • 84875588179 scopus 로고    scopus 로고
    • BiP-bound and nonclustered mode of Ire1 evokes a weak but sustained unfolded protein response
    • Y. Ishiwata-Kimata, T. Promlek, K. Kohno, and Y. Kimata BiP-bound and nonclustered mode of Ire1 evokes a weak but sustained unfolded protein response Genes Cells 18 2013 288 301
    • (2013) Genes Cells , vol.18 , pp. 288-301
    • Ishiwata-Kimata, Y.1    Promlek, T.2    Kohno, K.3    Kimata, Y.4
  • 51
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • J.A. Johnston, C.L. Ward, and R.R. Kopito Aggresomes: a cellular response to misfolded proteins J. Cell Biol. 143 1998 1883 1898
    • (1998) J. Cell Biol. , vol.143 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 53
    • 50649116818 scopus 로고    scopus 로고
    • Misfolded proteins partition between two distinct quality control compartments
    • D. Kaganovich, R. Kopito, and J. Frydman Misfolded proteins partition between two distinct quality control compartments Nature 454 2008 1088 1095
    • (2008) Nature , vol.454 , pp. 1088-1095
    • Kaganovich, D.1    Kopito, R.2    Frydman, J.3
  • 55
    • 3042648746 scopus 로고    scopus 로고
    • Regulation of lifespan in Drosophila by modulation of genes in the TOR signaling pathway
    • P. Kapahi, B.M. Zid, T. Harper, D. Koslover, V. Sapin, and S. Benzer Regulation of lifespan in Drosophila by modulation of genes in the TOR signaling pathway Curr. Biol. 14 2004 885 890
    • (2004) Curr. Biol. , vol.14 , pp. 885-890
    • Kapahi, P.1    Zid, B.M.2    Harper, T.3    Koslover, D.4    Sapin, V.5    Benzer, S.6
  • 56
    • 84876816592 scopus 로고    scopus 로고
    • Quality control mechanisms during ribosome maturation
    • K. Karbstein Quality control mechanisms during ribosome maturation Trends Cell Biol. 23 2013 242 250
    • (2013) Trends Cell Biol. , vol.23 , pp. 242-250
    • Karbstein, K.1
  • 57
    • 0346020435 scopus 로고    scopus 로고
    • The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress
    • Y. Kawaguchi, J.J. Kovacs, A. McLaurin, J.M. Vance, A. Ito, and T.P. Yao The deacetylase HDAC6 regulates aggresome formation and cell viability in response to misfolded protein stress Cell 115 2003 727 738
    • (2003) Cell , vol.115 , pp. 727-738
    • Kawaguchi, Y.1    Kovacs, J.J.2    McLaurin, A.3    Vance, J.M.4    Ito, A.5    Yao, T.P.6
  • 60
    • 0032699491 scopus 로고    scopus 로고
    • Synonymous codon substitutions affect ribosome traffic and protein folding during in vitro translation
    • A.A. Komar, T. Lesnik, and C. Reiss Synonymous codon substitutions affect ribosome traffic and protein folding during in vitro translation FEBS Lett. 462 1999 387 391
    • (1999) FEBS Lett. , vol.462 , pp. 387-391
    • Komar, A.A.1    Lesnik, T.2    Reiss, C.3
  • 61
    • 35548973466 scopus 로고    scopus 로고
    • Functional specificity among ribosomal proteins regulates gene expression
    • S. Komili, N.G. Farny, F.P. Roth, and P.A. Silver Functional specificity among ribosomal proteins regulates gene expression Cell 131 2007 557 571
    • (2007) Cell , vol.131 , pp. 557-571
    • Komili, S.1    Farny, N.G.2    Roth, F.P.3    Silver, P.A.4
  • 63
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • R.R. Kopito Aggresomes, inclusion bodies and protein aggregation Trends Cell Biol. 10 2000 524 530
    • (2000) Trends Cell Biol. , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 65
    • 43049138051 scopus 로고    scopus 로고
    • Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease
    • C. Kraft, A. Deplazes, M. Sohrmann, and M. Peter Mature ribosomes are selectively degraded upon starvation by an autophagy pathway requiring the Ubp3p/Bre5p ubiquitin protease Nat. Cell Biol. 10 2008 602 610
    • (2008) Nat. Cell Biol. , vol.10 , pp. 602-610
    • Kraft, C.1    Deplazes, A.2    Sohrmann, M.3    Peter, M.4
  • 66
    • 78649338141 scopus 로고    scopus 로고
    • Autophagy and the integrated stress response
    • G. Kroemer, G. Mariño, and B. Levine Autophagy and the integrated stress response Mol. Cell 40 2010 280 293
    • (2010) Mol. Cell , vol.40 , pp. 280-293
    • Kroemer, G.1    Mariño, G.2    Levine, B.3
  • 67
    • 79953178205 scopus 로고    scopus 로고
    • The giant protein titin: A regulatory node that integrates myocyte signaling pathways
    • M. Krüger, and W.A. Linke The giant protein titin: a regulatory node that integrates myocyte signaling pathways J. Biol. Chem. 286 2011 9905 9912
    • (2011) J. Biol. Chem. , vol.286 , pp. 9905-9912
    • Krüger, M.1    Linke, W.A.2
  • 68
    • 78649472341 scopus 로고    scopus 로고
    • Receptor for activated C kinase 1 stimulates nascent polypeptide- dependent translation arrest
    • K. Kuroha, M. Akamatsu, L. Dimitrova, T. Ito, Y. Kato, K. Shirahige, and T. Inada Receptor for activated C kinase 1 stimulates nascent polypeptide-dependent translation arrest EMBO Rep. 11 2010 956 961
    • (2010) EMBO Rep. , vol.11 , pp. 956-961
    • Kuroha, K.1    Akamatsu, M.2    Dimitrova, L.3    Ito, T.4    Kato, Y.5    Shirahige, K.6    Inada, T.7
  • 69
    • 34247391127 scopus 로고    scopus 로고
    • Analysis of nucleolar protein dynamics reveals the nuclear degradation of ribosomal proteins
    • Y.W. Lam, A.I. Lamond, M. Mann, and J.S. Andersen Analysis of nucleolar protein dynamics reveals the nuclear degradation of ribosomal proteins Curr. Biol. 17 2007 749 760
    • (2007) Curr. Biol. , vol.17 , pp. 749-760
    • Lam, Y.W.1    Lamond, A.I.2    Mann, M.3    Andersen, J.S.4
  • 70
    • 84988044805 scopus 로고    scopus 로고
    • The energetics of genome complexity
    • N. Lane, and W. Martin The energetics of genome complexity Nature 467 2010 929 934
    • (2010) Nature , vol.467 , pp. 929-934
    • Lane, N.1    Martin, W.2
  • 72
    • 0034611628 scopus 로고    scopus 로고
    • Protein folding: Versatility of the cytosolic chaperonin TRiC/CCT
    • M.R. Leroux, and F.U. Hartl Protein folding: versatility of the cytosolic chaperonin TRiC/CCT Curr. Biol. 10 2000 R260 R264
    • (2000) Curr. Biol. , vol.10
    • Leroux, M.R.1    Hartl, F.U.2
  • 73
    • 84873467908 scopus 로고    scopus 로고
    • Cotranslational response to proteotoxic stress by elongation pausing of ribosomes
    • B. Liu, Y. Han, and S.B. Qian Cotranslational response to proteotoxic stress by elongation pausing of ribosomes Mol. Cell 49 2013 453 463
    • (2013) Mol. Cell , vol.49 , pp. 453-463
    • Liu, B.1    Han, Y.2    Qian, S.B.3
  • 74
    • 77955455232 scopus 로고    scopus 로고
    • Proteomic identification of carbonylated proteins and their oxidation sites
    • A.G. Madian, and F.E. Regnier Proteomic identification of carbonylated proteins and their oxidation sites J. Proteome Res. 9 2010 3766 3780
    • (2010) J. Proteome Res. , vol.9 , pp. 3766-3780
    • Madian, A.G.1    Regnier, F.E.2
  • 75
    • 84882781969 scopus 로고    scopus 로고
    • Genetics. Mysterious ribosomopathies
    • K.L. McCann, and S.J. Baserga Genetics. Mysterious ribosomopathies Science 341 2013 849 850
    • (2013) Science , vol.341 , pp. 849-850
    • McCann, K.L.1    Baserga, S.J.2
  • 77
    • 75549087930 scopus 로고    scopus 로고
    • BioNumbers - The database of key numbers in molecular and cell biology
    • R. Milo, P. Jorgensen, U. Moran, G. Weber, and M. Springer BioNumbers - the database of key numbers in molecular and cell biology Nucleic Acids Res. 38 Database issue 2010 D750 D753
    • (2010) Nucleic Acids Res. , vol.38 , Issue.DATABASE ISSUE
    • Milo, R.1    Jorgensen, P.2    Moran, U.3    Weber, G.4    Springer, M.5
  • 78
    • 34247103448 scopus 로고    scopus 로고
    • The tmRNA system for translational surveillance and ribosome rescue
    • S.D. Moore, and R.T. Sauer The tmRNA system for translational surveillance and ribosome rescue Annu. Rev. Biochem. 76 2007 101 124
    • (2007) Annu. Rev. Biochem. , vol.76 , pp. 101-124
    • Moore, S.D.1    Sauer, R.T.2
  • 79
    • 44849094781 scopus 로고    scopus 로고
    • Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging
    • R.I. Morimoto Proteotoxic stress and inducible chaperone networks in neurodegenerative disease and aging Genes Dev. 22 2008 1427 1438
    • (2008) Genes Dev. , vol.22 , pp. 1427-1438
    • Morimoto, R.I.1
  • 80
    • 67349217063 scopus 로고    scopus 로고
    • ER and aging-Protein folding and the ER stress response
    • N. Naidoo ER and aging-Protein folding and the ER stress response Ageing Res. Rev. 8 2009 150 159
    • (2009) Ageing Res. Rev. , vol.8 , pp. 150-159
    • Naidoo, N.1
  • 81
    • 84864744900 scopus 로고    scopus 로고
    • Mitochondrial import efficiency of ATFS-1 regulates mitochondrial UPR activation
    • A.M. Nargund, M.W. Pellegrino, C.J. Fiorese, B.M. Baker, and C.M. Haynes Mitochondrial import efficiency of ATFS-1 regulates mitochondrial UPR activation Science 337 2012 587 590
    • (2012) Science , vol.337 , pp. 587-590
    • Nargund, A.M.1    Pellegrino, M.W.2    Fiorese, C.J.3    Baker, B.M.4    Haynes, C.M.5
  • 82
    • 0030844281 scopus 로고    scopus 로고
    • Recombination of protein domains facilitated by co-translational folding in eukaryotes
    • W.J. Netzer, and F.U. Hartl Recombination of protein domains facilitated by co-translational folding in eukaryotes Nature 388 1997 343 349
    • (1997) Nature , vol.388 , pp. 343-349
    • Netzer, W.J.1    Hartl, F.U.2
  • 83
    • 84863967724 scopus 로고    scopus 로고
    • Evolution of protein synthesis from an RNA world
    • H.F. Noller Evolution of protein synthesis from an RNA world Cold Spring Harb. Perspect. Biol. 4 2012 a003681
    • (2012) Cold Spring Harb. Perspect. Biol. , vol.4 , pp. 003681
    • Noller, H.F.1
  • 84
    • 84891871414 scopus 로고    scopus 로고
    • Kinetic modelling indicates that fast-translating codons can coordinate cotranslational protein folding by avoiding misfolded intermediates
    • E.P. O'Brien, M. Vendruscolo, and C.M. Dobson Kinetic modelling indicates that fast-translating codons can coordinate cotranslational protein folding by avoiding misfolded intermediates Nat. Commun. 5 2014 2988
    • (2014) Nat. Commun. , vol.5 , pp. 2988
    • O'Brien, E.P.1    Vendruscolo, M.2    Dobson, C.M.3
  • 85
    • 84870868447 scopus 로고    scopus 로고
    • Direct association of unfolded proteins with mammalian ER stress sensor, IRE1β
    • D. Oikawa, A. Kitamura, M. Kinjo, and T. Iwawaki Direct association of unfolded proteins with mammalian ER stress sensor, IRE1β PLoS ONE 7 2012 e51290
    • (2012) PLoS ONE , vol.7 , pp. 51290
    • Oikawa, D.1    Kitamura, A.2    Kinjo, M.3    Iwawaki, T.4
  • 87
    • 84886786722 scopus 로고    scopus 로고
    • Muscle mitohormesis promotes longevity via systemic repression of insulin signaling
    • E. Owusu-Ansah, W. Song, and N. Perrimon Muscle mitohormesis promotes longevity via systemic repression of insulin signaling Cell 155 2013 699 712
    • (2013) Cell , vol.155 , pp. 699-712
    • Owusu-Ansah, E.1    Song, W.2    Perrimon, N.3
  • 88
    • 0021154216 scopus 로고
    • A Drosophila RNA polymerase II transcription factor binds to the regulatory site of an hsp 70 gene
    • C.S. Parker, and J. Topol A Drosophila RNA polymerase II transcription factor binds to the regulatory site of an hsp 70 gene Cell 37 1984 273 283
    • (1984) Cell , vol.37 , pp. 273-283
    • Parker, C.S.1    Topol, J.2
  • 91
    • 84867623952 scopus 로고    scopus 로고
    • Post-translational modification: Nature's escape from genetic imprisonment and the basis for dynamic information encoding
    • S. Prabakaran, G. Lippens, H. Steen, and J. Gunawardena Post-translational modification: nature's escape from genetic imprisonment and the basis for dynamic information encoding Wiley Interdiscip. Rev. Syst. Biol. Med. 4 2012 565 583
    • (2012) Wiley Interdiscip. Rev. Syst. Biol. Med. , vol.4 , pp. 565-583
    • Prabakaran, S.1    Lippens, G.2    Steen, H.3    Gunawardena, J.4
  • 92
    • 80052137410 scopus 로고    scopus 로고
    • Neuronal circuitry regulates the response of Caenorhabditis elegans to misfolded proteins
    • V. Prahlad, and R.I. Morimoto Neuronal circuitry regulates the response of Caenorhabditis elegans to misfolded proteins Proc. Natl. Acad. Sci. USA 108 2011 14204 14209
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 14204-14209
    • Prahlad, V.1    Morimoto, R.I.2
  • 93
    • 34250561475 scopus 로고
    • A new puffing pattern induced by temperature shock and DNP in Drosophila
    • F. Ritossa A new puffing pattern induced by temperature shock and DNP in Drosophila Experientia 18 1962 571 573
    • (1962) Experientia , vol.18 , pp. 571-573
    • Ritossa, F.1
  • 94
    • 84897428027 scopus 로고    scopus 로고
    • Re-examining class-I presentation and the DRiP hypothesis
    • 10.1016/j.it.2014.01.002 Published online February 21, 2014
    • K.L. Rock, D.J. Farfán-Arribas, J.D. Colbert, and A.L. Goldberg Re-examining class-I presentation and the DRiP hypothesis Trends Immunol. 2014 10.1016/j.it.2014.01.002 Published online February 21, 2014
    • (2014) Trends Immunol.
    • Rock, K.L.1    Farfán-Arribas, D.J.2    Colbert, J.D.3    Goldberg, A.L.4
  • 95
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • D. Ron, and P. Walter Signal integration in the endoplasmic reticulum unfolded protein response Nat. Rev. Mol. Cell Biol. 8 2007 519 529
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 98
    • 0030961006 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1alpha (HIF-1alpha) protein is rapidly degraded by the ubiquitin-proteasome system under normoxic conditions. Its stabilization by hypoxia depends on redox-induced changes
    • S. Salceda, and J. Caro Hypoxia-inducible factor 1alpha (HIF-1alpha) protein is rapidly degraded by the ubiquitin-proteasome system under normoxic conditions. Its stabilization by hypoxia depends on redox-induced changes J. Biol. Chem. 272 1997 22642 22647
    • (1997) J. Biol. Chem. , vol.272 , pp. 22642-22647
    • Salceda, S.1    Caro, J.2
  • 99
    • 77952552782 scopus 로고    scopus 로고
    • ER stress and hormetic regulation of the aging process
    • A. Salminen, and K. Kaarniranta ER stress and hormetic regulation of the aging process Ageing Res. Rev. 9 2010 211 217
    • (2010) Ageing Res. Rev. , vol.9 , pp. 211-217
    • Salminen, A.1    Kaarniranta, K.2
  • 100
    • 0034643336 scopus 로고    scopus 로고
    • Rapid degradation of a large fraction of newly synthesized proteins by proteasomes
    • U. Schubert, L.C. Antón, J. Gibbs, C.C. Norbury, J.W. Yewdell, and J.R. Bennink Rapid degradation of a large fraction of newly synthesized proteins by proteasomes Nature 404 2000 770 774
    • (2000) Nature , vol.404 , pp. 770-774
    • Schubert, U.1    Antón, L.C.2    Gibbs, J.3    Norbury, C.C.4    Yewdell, J.W.5    Bennink, J.R.6
  • 102
    • 33745606008 scopus 로고    scopus 로고
    • Genetic interactions due to constitutive and inducible gene regulation mediated by the unfolded protein response in C elegans
    • X. Shen, R.E. Ellis, K. Sakaki, and R.J. Kaufman Genetic interactions due to constitutive and inducible gene regulation mediated by the unfolded protein response in C elegans PLoS Genet. 1 2005 e37
    • (2005) PLoS Genet. , vol.1 , pp. 37
    • Shen, X.1    Ellis, R.E.2    Sakaki, K.3    Kaufman, R.J.4
  • 103
    • 84861841297 scopus 로고    scopus 로고
    • Translation drives mRNA quality control
    • C.J. Shoemaker, and R. Green Translation drives mRNA quality control Nat. Struct. Mol. Biol. 19 2012 594 601
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 594-601
    • Shoemaker, C.J.1    Green, R.2
  • 104
    • 77957935294 scopus 로고    scopus 로고
    • Dom34:Hbs1 promotes subunit dissociation and peptidyl-tRNA drop-off to initiate no-go decay
    • C.J. Shoemaker, D.E. Eyler, and R. Green Dom34:Hbs1 promotes subunit dissociation and peptidyl-tRNA drop-off to initiate no-go decay Science 330 2010 369 372
    • (2010) Science , vol.330 , pp. 369-372
    • Shoemaker, C.J.1    Eyler, D.E.2    Green, R.3
  • 105
    • 77649272553 scopus 로고    scopus 로고
    • Slowing bacterial translation speed enhances eukaryotic protein folding efficiency
    • E. Siller, D.C. DeZwaan, J.F. Anderson, B.C. Freeman, and J.M. Barral Slowing bacterial translation speed enhances eukaryotic protein folding efficiency J. Mol. Biol. 396 2010 1310 1318
    • (2010) J. Mol. Biol. , vol.396 , pp. 1310-1318
    • Siller, E.1    Dezwaan, D.C.2    Anderson, J.F.3    Freeman, B.C.4    Barral, J.M.5
  • 106
    • 0028426938 scopus 로고
    • Kinetic partitioning during protein folding yields multiple native states
    • J.F. Sinclair, M.M. Ziegler, and T.O. Baldwin Kinetic partitioning during protein folding yields multiple native states Nat. Struct. Biol. 1 1994 320 326
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 320-326
    • Sinclair, J.F.1    Ziegler, M.M.2    Baldwin, T.O.3
  • 107
    • 84883549935 scopus 로고    scopus 로고
    • Transimulation - Protein biosynthesis web service
    • M. Siwiak, and P. Zielenkiewicz Transimulation - protein biosynthesis web service PLoS ONE 8 2013 e73943
    • (2013) PLoS ONE , vol.8 , pp. 73943
    • Siwiak, M.1    Zielenkiewicz, P.2
  • 108
    • 33645156037 scopus 로고    scopus 로고
    • Endoplasmic reticulum biogenesis proliferation and differentiation
    • C. Mullins, Kluwer Academic/Plenum Publishers New York
    • E.L. Snapp Endoplasmic reticulum biogenesis proliferation and differentiation C. Mullins, The Biogenesis of Cellular Organelles 2005 Kluwer Academic/Plenum Publishers New York 63 95
    • (2005) The Biogenesis of Cellular Organelles , pp. 63-95
    • Snapp, E.L.1
  • 109
    • 0030013835 scopus 로고    scopus 로고
    • Identification of endoplasmic reticulum in the primitive eukaryote Giardia lamblia using cryoelectron microscopy and antibody to Bip
    • B.J. Soltys, M. Falah, and R.S. Gupta Identification of endoplasmic reticulum in the primitive eukaryote Giardia lamblia using cryoelectron microscopy and antibody to Bip J. Cell Sci. 109 1996 1909 1917
    • (1996) J. Cell Sci. , vol.109 , pp. 1909-1917
    • Soltys, B.J.1    Falah, M.2    Gupta, R.S.3
  • 110
    • 84892865694 scopus 로고    scopus 로고
    • Sorting out the trash: The spatial nature of eukaryotic protein quality control
    • E.M. Sontag, W.I. Vonk, and J. Frydman Sorting out the trash: the spatial nature of eukaryotic protein quality control Curr. Opin. Cell Biol. 26C 2014 139 146
    • (2014) Curr. Opin. Cell Biol. , vol.26 C , pp. 139-146
    • Sontag, E.M.1    Vonk, W.I.2    Frydman, J.3
  • 111
    • 81355149538 scopus 로고    scopus 로고
    • Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae
    • S. Specht, S.B. Miller, A. Mogk, and B. Bukau Hsp42 is required for sequestration of protein aggregates into deposition sites in Saccharomyces cerevisiae J. Cell Biol. 195 2011 617 629
    • (2011) J. Cell Biol. , vol.195 , pp. 617-629
    • Specht, S.1    Miller, S.B.2    Mogk, A.3    Bukau, B.4
  • 112
    • 84865098071 scopus 로고    scopus 로고
    • Silent substitutions predictably alter translation elongation rates and protein folding efficiencies
    • P.S. Spencer, E. Siller, J.F. Anderson, and J.M. Barral Silent substitutions predictably alter translation elongation rates and protein folding efficiencies J. Mol. Biol. 422 2012 328 335
    • (2012) J. Mol. Biol. , vol.422 , pp. 328-335
    • Spencer, P.S.1    Siller, E.2    Anderson, J.F.3    Barral, J.M.4
  • 113
    • 13944272143 scopus 로고    scopus 로고
    • Aging and death in an organism that reproduces by morphologically symmetric division
    • E.J. Stewart, R. Madden, G. Paul, and F. Taddei Aging and death in an organism that reproduces by morphologically symmetric division PLoS Biol. 3 2005 e45
    • (2005) PLoS Biol. , vol.3 , pp. 45
    • Stewart, E.J.1    Madden, R.2    Paul, G.3    Taddei, F.4
  • 114
    • 33847199335 scopus 로고    scopus 로고
    • EIF4E function in somatic cells modulates ageing in Caenorhabditis elegans
    • P. Syntichaki, K. Troulinaki, and N. Tavernarakis eIF4E function in somatic cells modulates ageing in Caenorhabditis elegans Nature 445 2007 922 926
    • (2007) Nature , vol.445 , pp. 922-926
    • Syntichaki, P.1    Troulinaki, K.2    Tavernarakis, N.3
  • 117
    • 84879343155 scopus 로고    scopus 로고
    • XBP-1 is a cell-nonautonomous regulator of stress resistance and longevity
    • R.C. Taylor, and A. Dillin XBP-1 is a cell-nonautonomous regulator of stress resistance and longevity Cell 153 2013 1435 1447
    • (2013) Cell , vol.153 , pp. 1435-1447
    • Taylor, R.C.1    Dillin, A.2
  • 118
    • 84883415285 scopus 로고    scopus 로고
    • Identification of long-lived proteins reveals exceptional stability of essential cellular structures
    • B.H. Toyama, J.N. Savas, S.K. Park, M.S. Harris, N.T. Ingolia, J.R. Yates III, and M.W. Hetzer Identification of long-lived proteins reveals exceptional stability of essential cellular structures Cell 154 2013 971 982
    • (2013) Cell , vol.154 , pp. 971-982
    • Toyama, B.H.1    Savas, J.N.2    Park, S.K.3    Harris, M.S.4    Ingolia, N.T.5    Yates III, J.R.6    Hetzer, M.W.7
  • 119
    • 84878873702 scopus 로고    scopus 로고
    • Regulation of organismal proteostasis by transcellular chaperone signaling
    • P. van Oosten-Hawle, R.S. Porter, and R.I. Morimoto Regulation of organismal proteostasis by transcellular chaperone signaling Cell 153 2013 1366 1378
    • (2013) Cell , vol.153 , pp. 1366-1378
    • Van Oosten-Hawle, P.1    Porter, R.S.2    Morimoto, R.I.3
  • 120
    • 84861881296 scopus 로고    scopus 로고
    • The ubiquitin system, an immense realm
    • A. Varshavsky The ubiquitin system, an immense realm Annu. Rev. Biochem. 81 2012 167 176
    • (2012) Annu. Rev. Biochem. , vol.81 , pp. 167-176
    • Varshavsky, A.1
  • 121
    • 67549136242 scopus 로고    scopus 로고
    • Mitochondrial dysfunction leads to nuclear genome instability via an iron-sulfur cluster defect
    • J.R. Veatch, M.A. McMurray, Z.W. Nelson, and D.E. Gottschling Mitochondrial dysfunction leads to nuclear genome instability via an iron-sulfur cluster defect Cell 137 2009 1247 1258
    • (2009) Cell , vol.137 , pp. 1247-1258
    • Veatch, J.R.1    McMurray, M.A.2    Nelson, Z.W.3    Gottschling, D.E.4
  • 122
    • 84879034688 scopus 로고    scopus 로고
    • Cdc48/p97 promotes degradation of aberrant nascent polypeptides bound to the ribosome
    • R. Verma, R.S. Oania, N.J. Kolawa, and R.J. Deshaies Cdc48/p97 promotes degradation of aberrant nascent polypeptides bound to the ribosome eLife 2 2013 e00308
    • (2013) ELife , vol.2 , pp. 00308
    • Verma, R.1    Oania, R.S.2    Kolawa, N.J.3    Deshaies, R.J.4
  • 127
    • 84883229070 scopus 로고    scopus 로고
    • A cotranslational ubiquitination pathway for quality control of misfolded proteins
    • F. Wang, L.A. Durfee, and J.M. Huibregtse A cotranslational ubiquitination pathway for quality control of misfolded proteins Mol. Cell 50 2013 368 378
    • (2013) Mol. Cell , vol.50 , pp. 368-378
    • Wang, F.1    Durfee, L.A.2    Huibregtse, J.M.3
  • 128
    • 25844466597 scopus 로고    scopus 로고
    • Heat shock response modulators as therapeutic tools for diseases of protein conformation
    • S.D. Westerheide, and R.I. Morimoto Heat shock response modulators as therapeutic tools for diseases of protein conformation J. Biol. Chem. 280 2005 33097 33100
    • (2005) J. Biol. Chem. , vol.280 , pp. 33097-33100
    • Westerheide, S.D.1    Morimoto, R.I.2
  • 129
    • 34250377197 scopus 로고    scopus 로고
    • The weird and wonderful world of bacterial ribosome regulation
    • D.N. Wilson, and K.H. Nierhaus The weird and wonderful world of bacterial ribosome regulation Crit. Rev. Biochem. Mol. Biol. 42 2007 187 219
    • (2007) Crit. Rev. Biochem. Mol. Biol. , vol.42 , pp. 187-219
    • Wilson, D.N.1    Nierhaus, K.H.2
  • 130
    • 0021272985 scopus 로고
    • Activating protein factor binds in vitro to upstream control sequences in heat shock gene chromatin
    • C. Wu Activating protein factor binds in vitro to upstream control sequences in heat shock gene chromatin Nature 311 1984 81 84
    • (1984) Nature , vol.311 , pp. 81-84
    • Wu, C.1
  • 131
    • 0031932170 scopus 로고    scopus 로고
    • Favorable domain size in proteins
    • D. Xu, and R. Nussinov Favorable domain size in proteins Fold. Des. 3 1998 11 17
    • (1998) Fold. Des. , vol.3 , pp. 11-17
    • Xu, D.1    Nussinov, R.2
  • 132
    • 4944234936 scopus 로고    scopus 로고
    • Compartment-specific perturbation of protein handling activates genes encoding mitochondrial chaperones
    • T. Yoneda, C. Benedetti, F. Urano, S.G. Clark, H.P. Harding, and D. Ron Compartment-specific perturbation of protein handling activates genes encoding mitochondrial chaperones J. Cell Sci. 117 2004 4055 4066
    • (2004) J. Cell Sci. , vol.117 , pp. 4055-4066
    • Yoneda, T.1    Benedetti, C.2    Urano, F.3    Clark, S.G.4    Harding, H.P.5    Ron, D.6
  • 133
    • 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
    • H. Yoshida, T. Matsui, A. Yamamoto, T. Okada, and K. Mori XBP1 mRNA is induced by ATF6 and spliced by IRE1 in response to ER stress to produce a highly active transcription factor Cell 107 2001 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
    • 60149099539 scopus 로고    scopus 로고
    • Fidelity at the molecular level: Lessons from protein synthesis
    • H.S. Zaher, and R. Green Fidelity at the molecular level: lessons from protein synthesis Cell 136 2009 746 762
    • (2009) Cell , vol.136 , pp. 746-762
    • Zaher, H.S.1    Green, R.2
  • 136
    • 84874683740 scopus 로고    scopus 로고
    • Non-optimal codon usage affects expression, structure and function of clock protein FRQ
    • M. Zhou, J. Guo, J. Cha, M. Chae, S. Chen, J.M. Barral, M.S. Sachs, and Y. Liu Non-optimal codon usage affects expression, structure and function of clock protein FRQ Nature 495 2013 111 115
    • (2013) Nature , vol.495 , pp. 111-115
    • Zhou, M.1    Guo, J.2    Cha, J.3    Chae, M.4    Chen, S.5    Barral, J.M.6    Sachs, M.S.7    Liu, Y.8
  • 137
    • 0032555685 scopus 로고    scopus 로고
    • Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1
    • J. Zou, Y. Guo, T. Guettouche, D.F. Smith, and R. Voellmy Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1 Cell 94 1998 471 480
    • (1998) Cell , vol.94 , pp. 471-480
    • Zou, J.1    Guo, Y.2    Guettouche, T.3    Smith, D.F.4    Voellmy, R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.