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Volumn 128, Issue 21, 2015, Pages 3861-3869

Surviving protein quality control catastrophes - From cells to organisms

Author keywords

Protein quality control; Proteostasis; Stress responses

Indexed keywords

CHAPERONE; PROTEASOME; PROTEIN;

EID: 84946031584     PISSN: 00219533     EISSN: 14779137     Source Type: Journal    
DOI: 10.1242/jcs.173047     Document Type: Note
Times cited : (49)

References (77)
  • 2
    • 84866905708 scopus 로고    scopus 로고
    • Discovery of 7-methyl-5-(1-{[3-(trifluoromethyl)phenyl]acetyl}-2, 3-dihydro-1H-indol-5-yl)-7Hpyrrolo[2, 3-d]pyrimidin-4-amine (GSK2606414), a potent and selective first-inclass inhibitor of protein kinase R (PKR)-like endoplasmic reticulum kinase (PERK)
    • Axten, J. M., Medina, J. R., Feng, Y., Shu, A., Romeril, S. P., Grant, S. W., Li, W. H. H., Heerding, D. A., Minthorn, E., Mencken, T. et al. (2012). Discovery of 7-methyl-5-(1-{[3-(trifluoromethyl)phenyl]acetyl}-2, 3-dihydro-1H-indol-5-yl)-7Hpyrrolo[2, 3-d]pyrimidin-4-amine (GSK2606414), a potent and selective first-inclass inhibitor of protein kinase R (PKR)-like endoplasmic reticulum kinase (PERK). J. Med. Chem. 55, 7193-7207.
    • (2012) J. Med. Chem , vol.55 , pp. 7193-7207
    • Axten, J.M.1    Medina, J.R.2    Feng, Y.3    Shu, A.4    Romeril, S.P.5    Grant, S.W.6    Li, W.H.H.7    Heerding, D.A.8    Minthorn, E.9    Mencken, T.10
  • 3
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • Balch, W. E., Morimoto, R. I., Dillin, A. and Kelly, J. W. (2008). Adapting proteostasis for disease intervention. Science 319, 916-919.
    • (2008) Science , vol.319 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 4
    • 84885428073 scopus 로고    scopus 로고
    • Reconstitution of the 26S proteasome reveals functional asymmetries in its AAA+ unfoldase
    • Beckwith, R., Estrin, E., Worden, E. J. and Martin, A. (2013). Reconstitution of the 26S proteasome reveals functional asymmetries in its AAA+ unfoldase. Nat. Struct. Mol. Biol. 20, 1164-1172.
    • (2013) Nat. Struct. Mol. Biol , vol.20 , pp. 1164-1172
    • Beckwith, R.1    Estrin, E.2    Worden, E.J.3    Martin, A.4
  • 5
    • 0033782015 scopus 로고    scopus 로고
    • Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response
    • Bertolotti, A., Zhang, Y., Hendershot, L. M., Harding, H. P. and Ron, D. (2000). Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response. Nat. Cell Biol. 2, 326-332.
    • (2000) Nat. Cell Biol , vol.2 , pp. 326-332
    • Bertolotti, A.1    Zhang, Y.2    Hendershot, L.M.3    Harding, H.P.4    Ron, D.5
  • 6
    • 33846978054 scopus 로고    scopus 로고
    • Impaired post-translational folding of familial ALS-linked Cu, Zn superoxide dismutase mutants
    • Bruns, C. K. and Kopito, R. R. (2007). Impaired post-translational folding of familial ALS-linked Cu, Zn superoxide dismutase mutants. EMBO J. 26, 855-866.
    • (2007) EMBO J , vol.26 , pp. 855-866
    • Bruns, C.K.1    Kopito, R.R.2
  • 7
    • 33646127577 scopus 로고    scopus 로고
    • Molecular chaperones and protein quality control
    • Bukau, B., Weissman, J. and Horwich, A. (2006). Molecular chaperones and protein quality control. Cell 125, 443-451.
    • (2006) Cell , vol.125 , pp. 443-451
    • Bukau, B.1    Weissman, J.2    Horwich, A.3
  • 9
    • 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. and Ali, M. M. (2015). Noncanonical binding of BiP ATPase domain to Ire1 and Perk is dissociated by unfolded protein CH1 to initiate ER stress signaling. eLife 4, e03522.
    • (2015) eLife , vol.4
    • Carrara, M.1    Prischi, F.2    Nowak, P.R.3    Kopp, M.C.4    Ali, M.M.5
  • 10
    • 84865245211 scopus 로고    scopus 로고
    • Unfolded protein response
    • Cao, S. S. and Kaufman, R. J. (2012). Unfolded protein response. Curr. Biol. 22, R622-R626.
    • (2012) Curr. Biol , vol.22 , pp. R622-R626
    • Cao, S.S.1    Kaufman, R.J.2
  • 11
    • 57749098600 scopus 로고    scopus 로고
    • Amyloid formation by globular proteins under native conditions
    • Chiti, F. and Dobson, C. M. (2009). Amyloid formation by globular proteins under native conditions. Nat. Chem. Biol. 5, 15-22.
    • (2009) Nat. Chem. Biol , vol.5 , pp. 15-22
    • Chiti, F.1    Dobson, C.M.2
  • 13
    • 84878632676 scopus 로고    scopus 로고
    • Resetting translational homeostasis restores myelination in Charcot-Marie-Tooth disease type 1B mice
    • D'Antonio, M., Musner, N., Scapin, C., Ungaro, D., Del Carro, U., Ron, D., Feltri, M. L. and Wrabetz, L. (2013). Resetting translational homeostasis restores myelination in Charcot-Marie-Tooth disease type 1B mice. J. Exp. Med. 210, 821-838.
    • (2013) J. Exp. Med , vol.210 , pp. 821-838
    • D'Antonio, M.1    Musner, N.2    Scapin, C.3    Ungaro, D.4    Del Carro, U.5    Ron, D.6    Feltri, M.L.7    Wrabetz, L.8
  • 15
    • 76549115951 scopus 로고    scopus 로고
    • Evolution in health and medicine Sackler colloquium: Evolution of the human lifespan and diseases of aging: roles of infection, inflammation, and nutrition
    • Finch, C. E. (2010). Evolution in health and medicine Sackler colloquium: Evolution of the human lifespan and diseases of aging: roles of infection, inflammation, and nutrition. Proc. Natl. Acad. Sci. U.S.A. 107, 1718-1724.
    • (2010) Proc. Natl. Acad. Sci. U.S.A , vol.107 , pp. 1718-1724
    • Finch, C.E.1
  • 16
    • 80053369081 scopus 로고    scopus 로고
    • Unfolded proteins are Ire1-activating ligands that directly induce the unfolded protein response
    • Gardner, B. M. and Walter, P. (2011). Unfolded proteins are Ire1-activating ligands that directly induce the unfolded protein response. Science 333, 1891-1894.
    • (2011) Science , vol.333 , pp. 1891-1894
    • Gardner, B.M.1    Walter, P.2
  • 17
    • 84905492694 scopus 로고    scopus 로고
    • Allosteric inhibition of the IRE1a RNase preserves cell viability and function during endoplasmic reticulum stress
    • Ghosh, R., Wang, L., Wang, E. S., Perera, B. G. K., Igbaria, A., Morita, S., Prado, K., Thamsen, M., Caswell, D., Macias, H. et al. (2014). Allosteric inhibition of the IRE1a RNase preserves cell viability and function during endoplasmic reticulum stress. Cell 158, 534-548.
    • (2014) Cell , vol.158 , pp. 534-548
    • Ghosh, R.1    Wang, L.2    Wang, E.S.3    Perera, B.G.K.4    Igbaria, A.5    Morita, S.6    Prado, K.7    Thamsen, M.8    Caswell, D.9    Macias, H.10
  • 19
    • 0022257968 scopus 로고
    • Guanabenz Overdose
    • Hall, A. H. (1985). Guanabenz Overdose. Ann. Intern. Med. 102, 787-788.
    • (1985) Ann. Intern. Med , vol.102 , pp. 787-788
    • Hall, A.H.1
  • 21
    • 34249864120 scopus 로고    scopus 로고
    • A proteasome for all occasions
    • Hanna, J. and Finley, D. D. (2007). A proteasome for all occasions. FEBS Lett. 581, 2854-2861.
    • (2007) FEBS Lett , vol.581 , pp. 2854-2861
    • Hanna, J.1    Finley, D.D.2
  • 24
    • 60549114848 scopus 로고    scopus 로고
    • Ppp1r15 gene knockout reveals an essential role for translation initiation factor 2 alpha (eIF2alpha) dephosphorylation in mammalian development
    • Harding, H. P., Zhang, Y., Scheuner, D., Chen, J.-J., Kaufman, R. J. and Ron, D. (2009). Ppp1r15 gene knockout reveals an essential role for translation initiation factor 2 alpha (eIF2alpha) dephosphorylation in mammalian development. Proc. Natl. Acad. Sci. USA 106, 1832-1837.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 1832-1837
    • Harding, H.P.1    Zhang, Y.2    Scheuner, D.3    Chen, J.-J.4    Kaufman, R.J.5    Ron, D.6
  • 25
    • 84897094564 scopus 로고    scopus 로고
    • Disturbance of endoplasmic reticulum proteostasis in neurodegenerative diseases
    • Hetz, C. and Mollereau, B. (2014). Disturbance of endoplasmic reticulum proteostasis in neurodegenerative diseases. Nat. Rev. Neurosci. 15, 233-249.
    • (2014) Nat. Rev. Neurosci , vol.15 , pp. 233-249
    • Hetz, C.1    Mollereau, B.2
  • 26
    • 84883387793 scopus 로고    scopus 로고
    • Targeting the unfolded protein response in disease
    • Hetz, C., Chevet, E. and Harding, H. P. (2013). Targeting the unfolded protein response in disease. Nat. Rev. Drug Discov. 12, 703-719.
    • (2013) Nat. Rev. Drug Discov , vol.12 , pp. 703-719
    • Hetz, C.1    Chevet, E.2    Harding, H.P.3
  • 27
    • 84863889691 scopus 로고    scopus 로고
    • The mechanism of eukaryotic translation initiation: new insights and challenges
    • Hinnebusch, A. G. and Lorsch, J. R. (2012). The mechanism of eukaryotic translation initiation: new insights and challenges. Cold Spring Harb. Perspect. Biol. 4, a011544.
    • (2012) Cold Spring Harb. Perspect. Biol , vol.4
    • Hinnebusch, A.G.1    Lorsch, J.R.2
  • 28
    • 0020545855 scopus 로고
    • Guanabenz A review of its pharmacodynamic properties and therapeutic efficacy in hypertension
    • Holmes, B., Brogden, R. N., Heel, R. C., Speight, T. M. and Avery, G. S. (1983). Guanabenz A review of its pharmacodynamic properties and therapeutic efficacy in hypertension. Drugs 26, 212-229.
    • (1983) Drugs , vol.26 , pp. 212-229
    • Holmes, B.1    Brogden, R.N.2    Heel, R.C.3    Speight, T.M.4    Avery, G.S.5
  • 29
    • 0033562966 scopus 로고    scopus 로고
    • Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls
    • Kaufman, R. J. (1999). Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls. Genes Dev. 13, 1211-1233.
    • (1999) Genes Dev , vol.13 , pp. 1211-1233
    • Kaufman, R.J.1
  • 30
    • 0032432673 scopus 로고    scopus 로고
    • Endocrinopathies in the family of endoplasmic reticulum (ER) storage diseases: disorders of protein trafficking and the role of ER molecular chaperones*
    • Kim, P. S. and Arvan, P. (1998). Endocrinopathies in the family of endoplasmic reticulum (ER) storage diseases: disorders of protein trafficking and the role of ER molecular chaperones*. Endocr. Rev. 19, 173-202.
    • (1998) Endocr. Rev , vol.19 , pp. 173-202
    • Kim, P.S.1    Arvan, P.2
  • 32
    • 8444250981 scopus 로고    scopus 로고
    • A role for BiP as an adjustor for the endoplasmic reticulum stress-sensing protein Ire1
    • Kimata, Y., Oikawa, D., Shimizu, Y., Ishiwata-Kimata, Y. and Kohno, K. (2004). A role for BiP as an adjustor for the endoplasmic reticulum stress-sensing protein Ire1. J. Cell Biol. 167, 445-456.
    • (2004) J. Cell Biol , vol.167 , pp. 445-456
    • Kimata, Y.1    Oikawa, D.2    Shimizu, Y.3    Ishiwata-Kimata, Y.4    Kohno, K.5
  • 33
    • 35348967427 scopus 로고    scopus 로고
    • Two regulatory steps of ER-stress sensor Ire1 involving its cluster formation and interaction with unfolded proteins
    • Kimata, Y., Ishiwata-Kimata, Y., Ito, T., Hirata, A., Suzuki, T., Oikawa, D., Takeuchi, M. and Kohno, K. (2007). Two regulatory steps of ER-stress sensor Ire1 involving its cluster formation and interaction with unfolded proteins. J. Cell Biol. 179, 75-86.
    • (2007) J. Cell Biol , vol.179 , pp. 75-86
    • Kimata, Y.1    Ishiwata-Kimata, Y.2    Ito, T.3    Hirata, A.4    Suzuki, T.5    Oikawa, D.6    Takeuchi, M.7    Kohno, K.8
  • 34
    • 0041703031 scopus 로고    scopus 로고
    • The function of GADD34 is a recovery from a shutoff of protein synthesis induced by ER stress: elucidation by GADD34-deficient mice
    • Kojima, E., Takeuchi, A., Haneda, M., Yagi, A., Hasegawa, T., Yamaki, K., Takeda, K., Akira, S., Shimokata, K. and Isobe, K. (2003). The function of GADD34 is a recovery from a shutoff of protein synthesis induced by ER stress: elucidation by GADD34-deficient mice. FASEB J. 17, 1573-1575.
    • (2003) FASEB J , vol.17 , pp. 1573-1575
    • Kojima, E.1    Takeuchi, A.2    Haneda, M.3    Yagi, A.4    Hasegawa, T.5    Yamaki, K.6    Takeda, K.7    Akira, S.8    Shimokata, K.9    Isobe, K.10
  • 35
    • 77950487987 scopus 로고    scopus 로고
    • Mechanisms of cross-talk between the ubiquitin-proteasome and autophagy-lysosome systems
    • Korolchuk, V. I., Menzies, F. M. and Rubinsztein, D. C. (2009). Mechanisms of cross-talk between the ubiquitin-proteasome and autophagy-lysosome systems. FEBS Lett. 584, 1393-1398.
    • (2009) FEBS Lett , vol.584 , pp. 1393-1398
    • Korolchuk, V.I.1    Menzies, F.M.2    Rubinsztein, D.C.3
  • 38
    • 0034637605 scopus 로고    scopus 로고
    • Ligand-independent dimerization activates the stress response kinases IRE1 and PERK in the lumen of the endoplasmic reticulum
    • Liu, C. Y., Schroder, M. and Kaufman, R. J. (2000). Ligand-independent dimerization activates the stress response kinases IRE1 and PERK in the lumen of the endoplasmic reticulum. J. Biol. Chem. 275, 24881-24885.
    • (2000) J. Biol. Chem , vol.275 , pp. 24881-24885
    • Liu, C.Y.1    Schroder, M.2    Kaufman, R.J.3
  • 39
    • 84921403151 scopus 로고    scopus 로고
    • Druggable sensors of the unfolded protein response
    • Maly, D. J. and Papa, F. R. (2014). Druggable sensors of the unfolded protein response. Nat. Chem. Biol. 10, 892-901.
    • (2014) Nat. Chem. Biol , vol.10 , pp. 892-901
    • Maly, D.J.1    Papa, F.R.2
  • 41
    • 0034716887 scopus 로고    scopus 로고
    • Tripartite management of unfolded proteins in the endoplasmic reticulum
    • Mori, K. (2000). Tripartite management of unfolded proteins in the endoplasmic reticulum. Cell 101, 451-454.
    • (2000) Cell , vol.101 , pp. 451-454
    • Mori, K.1
  • 42
    • 84866488172 scopus 로고    scopus 로고
    • The heat shock response: systems biology of proteotoxic stress in aging and disease
    • Morimoto, R. I. (2011). The heat shock response: systems biology of proteotoxic stress in aging and disease. Cold Spring Harb. Symp. Quant. Biol. 76, 91-99.
    • (2011) Cold Spring Harb. Symp. Quant. Biol , vol.76 , pp. 91-99
    • Morimoto, R.I.1
  • 43
    • 84901047429 scopus 로고    scopus 로고
    • Proteostasis and the aging proteome in health and disease
    • Morimoto, R. I. and Cuervo, A. M. (2014). Proteostasis and the aging proteome in health and disease. J. Gerontol. A Biol. Sci. Med. Sci. 69 Suppl 1, S33-S38.
    • (2014) J. Gerontol. A Biol. Sci. Med. Sci , vol.69 , pp. S33-S38
    • Morimoto, R.I.1    Cuervo, A.M.2
  • 45
    • 67649467294 scopus 로고    scopus 로고
    • Dynamics and diversity in autophagy mechanisms: lessons from yeast
    • Nakatogawa, H., Suzuki, K., Kamada, Y. and Ohsumi, Y. (2009). Dynamics and diversity in autophagy mechanisms: lessons from yeast. Nat. Rev. Mol. Cell Biol. 10, 458-467.
    • (2009) Nat. Rev. Mol. Cell Biol , vol.10 , pp. 458-467
    • Nakatogawa, H.1    Suzuki, K.2    Kamada, Y.3    Ohsumi, Y.4
  • 46
    • 84855457952 scopus 로고    scopus 로고
    • Hsp90 molecular chaperone inhibitors: are we there yet?
    • Neckers, L. and Workman, P. (2012). Hsp90 molecular chaperone inhibitors: are we there yet? Clinical Cancer Research 18, 64-76.
    • (2012) Clinical Cancer Research , vol.18 , pp. 64-76
    • Neckers, L.1    Workman, P.2
  • 48
    • 0035947778 scopus 로고    scopus 로고
    • Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2alpha
    • Novoa, I., Zeng, H., Harding, H. P. and Ron, D. (2001). Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2alpha. J. Cell Biol. 153, 1011-1022.
    • (2001) J. Cell Biol , vol.153 , pp. 1011-1022
    • Novoa, I.1    Zeng, H.2    Harding, H.P.3    Ron, D.4
  • 49
    • 67651045789 scopus 로고    scopus 로고
    • Activation of mammalian IRE1a upon ER stress depends on dissociation of BiP rather than on direct interaction with unfolded proteins
    • Oikawa, D., Kimata, Y., Kohno, K. and Iwawaki, T. (2009). Activation of mammalian IRE1a upon ER stress depends on dissociation of BiP rather than on direct interaction with unfolded proteins. Exp. Cell Res. 315, 2496-2504.
    • (2009) Exp. Cell Res , vol.315 , pp. 2496-2504
    • Oikawa, D.1    Kimata, Y.2    Kohno, K.3    Iwawaki, T.4
  • 50
    • 0034694896 scopus 로고    scopus 로고
    • Dissociation of Kar2p/BiP from an ER sensory molecule, Ire1p, triggers the unfolded protein response in yeast
    • Okamura, K., Kimata, Y., Higashio, H., Tsuru, A. and Kohno, K. (2000). Dissociation of Kar2p/BiP from an ER sensory molecule, Ire1p, triggers the unfolded protein response in yeast. Biochem. Biophys. Res. Commun. 279, 445-450.
    • (2000) Biochem. Biophys. Res. Commun , vol.279 , pp. 445-450
    • Okamura, K.1    Kimata, Y.2    Higashio, H.3    Tsuru, A.4    Kohno, K.5
  • 51
    • 24744441497 scopus 로고    scopus 로고
    • Autophagy is required for maintenance of amino acid levels and protein synthesis under nitrogen starvation
    • Onodera, J. and Ohsumi, Y. (2005). Autophagy is required for maintenance of amino acid levels and protein synthesis under nitrogen starvation. J. Biol. Chem. 280, 31582-31586.
    • (2005) J. Biol. Chem , vol.280 , pp. 31582-31586
    • Onodera, J.1    Ohsumi, Y.2
  • 53
    • 38749104284 scopus 로고    scopus 로고
    • Ablation of the UPR-mediator CHOP restores motor function and reduces demyelination in Charcot-Marie-Tooth 1B mice
    • Pennuto, M., Tinelli, E., Malaguti, M., Del Carro, U., D'Antonio, M., Ron, D., Quattrini, A., Feltri, M. L. and Wrabetz, L. (2008). Ablation of the UPR-mediator CHOP restores motor function and reduces demyelination in Charcot-Marie-Tooth 1B mice. Neuron 57, 393-405.
    • (2008) Neuron , vol.57 , pp. 393-405
    • Pennuto, M.1    Tinelli, E.2    Malaguti, M.3    Del Carro, U.4    D'Antonio, M.5    Ron, D.6    Quattrini, A.7    Feltri, M.L.8    Wrabetz, L.9
  • 54
    • 77955023666 scopus 로고    scopus 로고
    • BiP binding to the ER-stress sensor Ire1 tunes the homeostatic behavior of the unfolded protein response
    • Pincus, D., Chevalier, M. W., Aragón, T., van Anken, E., Vidal, S. E., El-Samad, H. and Walter, P. (2010). BiP binding to the ER-stress sensor Ire1 tunes the homeostatic behavior of the unfolded protein response. PLoS Biol. 8, e1000415.
    • (2010) PLoS Biol , vol.8
    • Pincus, D.1    Chevalier, M.W.2    Aragón, T.3    van Anken, E.4    Vidal, S.E.5    El-Samad, H.6    Walter, P.7
  • 55
    • 77950366349 scopus 로고    scopus 로고
    • Transcription Factor Nrf1 Mediates the Proteasome Recovery Pathway after Proteasome Inhibition in Mammalian Cells
    • Radhakrishnan, S. K., Lee, C. S., Young, P., Beskow, A., Chan, J. Y. and Deshaies, R. J. (2010). Transcription Factor Nrf1 Mediates the Proteasome Recovery Pathway after Proteasome Inhibition in Mammalian Cells. Molecular Cell 38, 17-28.
    • (2010) Molecular Cell , vol.38 , pp. 17-28
    • Radhakrishnan, S.K.1    Lee, C.S.2    Young, P.3    Beskow, A.4    Chan, J.Y.5    Deshaies, R.J.6
  • 56
    • 78649346692 scopus 로고    scopus 로고
    • The heat shock response: life on the verge of death
    • Richter, K., Haslbeck, M. and Buchner, J. (2010). The heat shock response: life on the verge of death. Mol. Cell 40, 253-266.
    • (2010) Mol. Cell , vol.40 , pp. 253-266
    • Richter, K.1    Haslbeck, M.2    Buchner, J.3
  • 59
    • 60149091189 scopus 로고    scopus 로고
    • Regulation of translation initiation in eukaryotes: mechanisms and biological targets
    • Sonenberg, N. and Hinnebusch, A. G. (2009). Regulation of translation initiation in eukaryotes: mechanisms and biological targets. Cell 136, 731-745.
    • (2009) Cell , vol.136 , pp. 731-745
    • Sonenberg, N.1    Hinnebusch, A.G.2
  • 60
    • 0037264120 scopus 로고    scopus 로고
    • Unfolding the role of protein misfolding in neurodegenerative diseases
    • Soto, C. (2003). Unfolding the role of protein misfolding in neurodegenerative diseases. Nat. Rev. Neurosci. 4, 49-60.
    • (2003) Nat. Rev. Neurosci , vol.4 , pp. 49-60
    • Soto, C.1
  • 61
    • 84868148725 scopus 로고    scopus 로고
    • Failure of amino acid homeostasis causes cell death following proteasome inhibition
    • Suraweera, A., Münch, C., Hanssum, A. and Bertolotti, A. (2012). Failure of amino acid homeostasis causes cell death following proteasome inhibition. Mol. Cell 48, 242-253.
    • (2012) Mol. Cell , vol.48 , pp. 242-253
    • Suraweera, A.1    Münch, C.2    Hanssum, A.3    Bertolotti, A.4
  • 62
    • 84890146490 scopus 로고    scopus 로고
    • Proteostasis and neurodegeneration: The roles of proteasomal degradation and autophagy
    • Tanaka, K. and Matsuda, N. (2014). Proteostasis and neurodegeneration: The roles of proteasomal degradation and autophagy. Biochimica et Biophysica Acta-Molecular Cell Research 1843, 197-204.
    • (2014) Biochimica et Biophysica Acta-Molecular Cell Research , vol.1843 , pp. 197-204
    • Tanaka, K.1    Matsuda, N.2
  • 63
    • 33847324367 scopus 로고    scopus 로고
    • Lobe IB of the ATPase domain of Kar2p/BiP interacts with Ire1p to negatively regulate the unfolded protein Response in Saccharomyces cerevisiae
    • Todd-Corlett, A., Jones, E., Seghers, C. and Gething, M.-J. (2007). Lobe IB of the ATPase domain of Kar2p/BiP interacts with Ire1p to negatively regulate the unfolded protein Response in Saccharomyces cerevisiae. J. Mol. Biol. 367, 770-787.
    • (2007) J. Mol. Biol , vol.367 , pp. 770-787
    • Todd-Corlett, A.1    Jones, E.2    Seghers, C.3    Gething, M.-J.4
  • 64
    • 84878942836 scopus 로고    scopus 로고
    • Molecular architecture and assembly of the eukaryotic proteasome
    • Tomko, R. J. and Hochstrasser, M. (2013). Molecular architecture and assembly of the eukaryotic proteasome. Annu. Rev. Biochem. 82, 415-445.
    • (2013) Annu. Rev. Biochem , vol.82 , pp. 415-445
    • Tomko, R.J.1    Hochstrasser, M.2
  • 67
    • 84872778575 scopus 로고    scopus 로고
    • Exploiting the selectivity of protein phosphatase 1 for pharmacological intervention
    • Tsaytler, P. and Bertolotti, A. (2012). Exploiting the selectivity of protein phosphatase 1 for pharmacological intervention. FEBS J. 280, 766-770.
    • (2012) FEBS J , vol.280 , pp. 766-770
    • Tsaytler, P.1    Bertolotti, A.2
  • 68
    • 79953288480 scopus 로고    scopus 로고
    • Selective inhibition of a regulatory subunit of protein phosphatase 1 restores proteostasis
    • Tsaytler, P., Harding, H. P., Ron, D. and Bertolotti, A. (2011). Selective inhibition of a regulatory subunit of protein phosphatase 1 restores proteostasis. Science 332, 91-94.
    • (2011) Science , vol.332 , pp. 91-94
    • Tsaytler, P.1    Harding, H.P.2    Ron, D.3    Bertolotti, A.4
  • 69
    • 29344464782 scopus 로고    scopus 로고
    • Protein synthesis upon acute nutrient restriction relies on proteasome function
    • Vabulas, R. M. and Hartl, F. U. (2005). Protein synthesis upon acute nutrient restriction relies on proteasome function. Science 310, 1960-1963.
    • (2005) Science , vol.310 , pp. 1960-1963
    • Vabulas, R.M.1    Hartl, F.U.2
  • 70
    • 22244479388 scopus 로고    scopus 로고
    • Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis
    • Valentine, J. S., Doucette, P. A. and Zittin Potter, S. (2005). Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis. Annu. Rev. Biochem. 74, 563-593.
    • (2005) Annu. Rev. Biochem , vol.74 , pp. 563-593
    • Valentine, J.S.1    Doucette, P.A.2    Zittin Potter, S.3
  • 71
    • 84922606978 scopus 로고    scopus 로고
    • The role of protein clearance mechanisms in organismal ageing and age-related diseases
    • Vilchez, D., Saez, I. and Dillin, A. (2014). The role of protein clearance mechanisms in organismal ageing and age-related diseases. Nat. Commun. 5, 5659.
    • (2014) Nat. Commun , vol.5 , pp. 5659
    • Vilchez, D.1    Saez, I.2    Dillin, A.3
  • 72
    • 79551584057 scopus 로고    scopus 로고
    • The unfolded protein response in familial amyotrophic lateral sclerosis
    • Wang, L., Popko, B. and Roos, R. P. (2011). The unfolded protein response in familial amyotrophic lateral sclerosis. Hum. Mol. Genet. 20, 1008-1015.
    • (2011) Hum. Mol. Genet , vol.20 , pp. 1008-1015
    • Wang, L.1    Popko, B.2    Roos, R.P.3
  • 73
    • 84898817967 scopus 로고    scopus 로고
    • An enhanced integrated stress response ameliorates mutant SOD1-induced ALS
    • Wang, L., Popko, B. and Roos, R. P. (2014). An enhanced integrated stress response ameliorates mutant SOD1-induced ALS. Hum. Mol. Genet. 23, 2629-2638.
    • (2014) Hum. Mol. Genet , vol.23 , pp. 2629-2638
    • Wang, L.1    Popko, B.2    Roos, R.P.3
  • 74
    • 76749152448 scopus 로고    scopus 로고
    • SnapShot: the unfolded protein response
    • Wiseman, R. L., Haynes, C. M. and Ron, D. (2010). SnapShot: the unfolded protein response. Cell 140, 590-590.e2.
    • (2010) Cell , vol.140 , pp. 590-590
    • Wiseman, R.L.1    Haynes, C.M.2    Ron, D.3
  • 76
    • 0035853037 scopus 로고    scopus 로고
    • RPN4 is a ligand, substrate, and transcriptional regulator of the 26S proteasome: a negative feedback circuit
    • Xie, Y. and Varshavsky, A. (2001). RPN4 is a ligand, substrate, and transcriptional regulator of the 26S proteasome: a negative feedback circuit. Proc. Natl. Acad. Sci. USA 98, 3056-3061.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 3056-3061
    • Xie, Y.1    Varshavsky, A.2
  • 77
    • 78650510609 scopus 로고    scopus 로고
    • mTOR: from growth signal integration to cancer, diabetes and ageing
    • Zoncu, R., Efeyan, A. and Sabatini, D. M. (2011). mTOR: from growth signal integration to cancer, diabetes and ageing. Nat. Rev. Mol. Cell Biol. 12, 21-35.
    • (2011) Nat. Rev. Mol. Cell Biol , vol.12 , pp. 21-35
    • Zoncu, R.1    Efeyan, A.2    Sabatini, D.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.