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Volumn 16, Issue 8, 2015, Pages 18224-18251

Mitochondria retrograde signaling and the UPRmt: Where are we in mammals?

Author keywords

Cell signaling; Gene expression; Mitochondria; Unfolded protein response

Indexed keywords

CALCIUM; MITOCHONDRIAL DNA; REACTIVE OXYGEN METABOLITE; TRANSCRIPTION FACTOR; MITOCHONDRIAL PROTEIN;

EID: 84938863498     PISSN: 16616596     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms160818224     Document Type: Review
Times cited : (114)

References (125)
  • 1
    • 0037250915 scopus 로고    scopus 로고
    • Regulation and co-ordination of nuclear gene expression during mitochondrial biogenesis
    • Goffart, S.; Wiesner, R.J. Regulation and co-ordination of nuclear gene expression during mitochondrial biogenesis. Exp. Physiol. 2003, 88, 33-40.
    • (2003) Exp. Physiol , vol.88 , pp. 33-40
    • Goffart, S.1    Wiesner, R.J.2
  • 2
    • 34250811284 scopus 로고    scopus 로고
    • Mitochondrial-nuclear communications
    • Ryan, M.T.; Hoogenraad, N.J. Mitochondrial-nuclear communications. Annu. Rev. Biochem. 2007, 76, 701-722.
    • (2007) Annu. Rev. Biochem , vol.76 , pp. 701-722
    • Ryan, M.T.1    Hoogenraad, N.J.2
  • 4
    • 84901441806 scopus 로고    scopus 로고
    • Shaping the dynamic mitochondrial network
    • Lackner, L.L. Shaping the dynamic mitochondrial network. BMC Biol. 2014, 12, 35.
    • (2014) BMC Biol , vol.12 , pp. 35
    • Lackner, L.L.1
  • 5
    • 84904967279 scopus 로고    scopus 로고
    • New functions of mitochondria associated membranes in cellular signaling
    • Van Vliet, A.R.; Verfaillie, T.; Agostinis, P. New functions of mitochondria associated membranes in cellular signaling. Biochim. Biophys. Acta 2014, 1843, 2253-2262.
    • (2014) Biochim. Biophys. Acta , vol.1843 , pp. 2253-2262
    • Van Vliet, A.R.1    Verfaillie, T.2    Agostinis, P.3
  • 7
    • 49749121841 scopus 로고    scopus 로고
    • A novel role for mitochondria in regulating epigenetic modification in the nucleus
    • Smiraglia, D.J.; Kulawiec, M.; Bistulfi, G.L.; Gupta, S.G.; Singh, K.K. A novel role for mitochondria in regulating epigenetic modification in the nucleus. Cancer Biol. Ther. 2008, 7, 1182-1190.
    • (2008) Cancer Biol. Ther , vol.7 , pp. 1182-1190
    • Smiraglia, D.J.1    Kulawiec, M.2    Bistulfi, G.L.3    Gupta, S.G.4    Singh, K.K.5
  • 8
    • 84895546187 scopus 로고    scopus 로고
    • Mitochondrial quality control and communications with the nucleus are important in maintaining mitochondrial function and cell health
    • Kotiadis, V.N.; Duchen, M.R.; Osellame, L.D. Mitochondrial quality control and communications with the nucleus are important in maintaining mitochondrial function and cell health. Biochim. Biophys. Acta 2014, 1840, 1254-1265.
    • (2014) Biochim. Biophys. Acta , vol.1840 , pp. 1254-1265
    • Kotiadis, V.N.1    Duchen, M.R.2    Osellame, L.D.3
  • 10
    • 84858791998 scopus 로고    scopus 로고
    • Mitochondrial quality control: A matter of life and death for neurons
    • Rugarli, E.I.; Langer, T. Mitochondrial quality control: A matter of life and death for neurons. EMBO J. 2012, 31, 1336-1349.
    • (2012) EMBO J , vol.31 , pp. 1336-1349
    • Rugarli, E.I.1    Langer, T.2
  • 11
    • 0033081478 scopus 로고    scopus 로고
    • Retrograde Ca2+ signaling in C2C12 skeletal myocytes in response to mitochondrial genetic and metabolic stress: A novel mode of inter-organelle crosstalk
    • Biswas, G.; Adebanjo, O.A.; Freedman, B.D.; Anandatheerthavarada, H.K.; Vijayasarathy, C.; Zaidi, M.; Kotlikoff, M.; Avadhani, N.G. Retrograde Ca2+ signaling in C2C12 skeletal myocytes in response to mitochondrial genetic and metabolic stress: A novel mode of inter-organelle crosstalk. EMBO J. 1999, 18, 522-533.
    • (1999) EMBO J , vol.18 , pp. 522-533
    • Biswas, G.1    Adebanjo, O.A.2    Freedman, B.D.3    Anandatheerthavarada, H.K.4    Vijayasarathy, C.5    Zaidi, M.6    Kotlikoff, M.7    Avadhani, N.G.8
  • 12
    • 0037038669 scopus 로고    scopus 로고
    • Mitochondrial stress-induced calcium signaling, phenotypic changes and invasive behavior in human lung carcinoma A549 cells
    • Amuthan, G.; Biswas, G.; Ananadatheerthavarada, H.K.; Vijayasarathy, C.; Shephard, H.M.; Avadhani, N.G. Mitochondrial stress-induced calcium signaling, phenotypic changes and invasive behavior in human lung carcinoma A549 cells. Oncogene 2002, 21, 7839-7849.
    • (2002) Oncogene , vol.21 , pp. 7839-7849
    • Amuthan, G.1    Biswas, G.2    Ananadatheerthavarada, H.K.3    Vijayasarathy, C.4    Shephard, H.M.5    Avadhani, N.G.6
  • 13
    • 0037080987 scopus 로고    scopus 로고
    • CREB activation induced by mitochondrial dysfunction is a new signaling pathway that impairs cell proliferation
    • Arnould, T.; Vankoningsloo, S.; Renard, P.; Houbion, A.; Ninane, N.; Demazy, C.; Remacle, J.; Raes, M. CREB activation induced by mitochondrial dysfunction is a new signaling pathway that impairs cell proliferation. EMBO J. 2002, 21, 53-63.
    • (2002) EMBO J , vol.21 , pp. 53-63
    • Arnould, T.1    Vankoningsloo, S.2    Renard, P.3    Houbion, A.4    Ninane, N.5    Demazy, C.6    Remacle, J.7    Raes, M.8
  • 14
    • 84879356734 scopus 로고    scopus 로고
    • Mitochondrial signaling: Forwards, backwards, and in between
    • Whelan, S.P.; Zuckerbraun, B.S. Mitochondrial signaling: Forwards, backwards, and in between. Oxid. Med. Cell. Longev. 2013, 2013, 351613.
    • (2013) Oxid. Med. Cell. Longev , vol.2013
    • Whelan, S.P.1    Zuckerbraun, B.S.2
  • 15
    • 84929194905 scopus 로고    scopus 로고
    • The complex crosstalk between mitochondria and the nucleus: What goes in between?
    • Cagin, U.; Enriquez, J.A. The complex crosstalk between mitochondria and the nucleus: What goes in between? Int. J. Biochem. Cell Biol. 2015, 63, 10-15.
    • (2015) Int. J. Biochem. Cell Biol , vol.63 , pp. 10-15
    • Cagin, U.1    Enriquez, J.A.2
  • 16
    • 67651159365 scopus 로고    scopus 로고
    • Transcriptional control of mitochondrial biogenesis and function
    • Hock, M.B.; Kralli, A. Transcriptional control of mitochondrial biogenesis and function. Annu. Rev. Physiol. 2009, 71, 177-203.
    • (2009) Annu. Rev. Physiol , vol.71 , pp. 177-203
    • Hock, M.B.1    Kralli, A.2
  • 17
  • 18
    • 0023106633 scopus 로고
    • The mitochondrial genotype can influence nuclear gene expression in yeast
    • Parikh, V.S.; Morgan, M.M.; Scott, R.; Clements, L.S.; Butow, R.A. The mitochondrial genotype can influence nuclear gene expression in yeast. Science 1987, 235, 576-580.
    • (1987) Science , vol.235 , pp. 576-580
    • Parikh, V.S.1    Morgan, M.M.2    Scott, R.3    Clements, L.S.4    Butow, R.A.5
  • 19
    • 0024582668 scopus 로고
    • Interaction between the yeast mitochondrial and nuclear genomes influences the abundance of novel transcripts derived from the spacer region of the nuclear ribosomal DNA repeat
    • Parikh, V.S.; Conrad-Webb, H.; Docherty, R.; Butow, R.A. Interaction between the yeast mitochondrial and nuclear genomes influences the abundance of novel transcripts derived from the spacer region of the nuclear ribosomal DNA repeat. Mol. Cell. Biol. 1989, 9, 1897-1907.
    • (1989) Mol. Cell. Biol , vol.9 , pp. 1897-1907
    • Parikh, V.S.1    Conrad-Webb, H.2    Docherty, R.3    Butow, R.A.4
  • 20
    • 84871741160 scopus 로고    scopus 로고
    • The retrograde response: When mitochondrial quality control is not enough
    • Jazwinski, S.M. The retrograde response: When mitochondrial quality control is not enough. Biochim. Biophys. Acta 2013, 1833, 400-409.
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 400-409
    • Jazwinski, S.M.1
  • 21
    • 0027524176 scopus 로고
    • RTG1 and RTG2: Two yeast genes required for a novel path of communication from mitochondria to the nucleus
    • Liao, X.; Butow, R.A. RTG1 and RTG2: Two yeast genes required for a novel path of communication from mitochondria to the nucleus. Cell 1993, 72, 61-71.
    • (1993) Cell , vol.72 , pp. 61-71
    • Liao, X.1    Butow, R.A.2
  • 22
    • 0038612839 scopus 로고    scopus 로고
    • Mitochondria to nucleus stress signaling: A distinctive mechanism of NF-κB/Rel activation through calcineurin-mediated inactivation of IκBβ
    • Biswas, G.; Anandatheerthavarada, H.K.; Zaidi, M.; Avadhani, N.G. Mitochondria to nucleus stress signaling: A distinctive mechanism of NF-κB/Rel activation through calcineurin-mediated inactivation of IκBβ. J. Cell Biol. 2003, 161, 507-519.
    • (2003) J. Cell Biol , vol.161 , pp. 507-519
    • Biswas, G.1    Anandatheerthavarada, H.K.2    Zaidi, M.3    Avadhani, N.G.4
  • 24
    • 70350241253 scopus 로고    scopus 로고
    • Heterogeneous nuclear ribonucleoprotein A2 is a common transcriptional coactivator in the nuclear transcription response to mitochondrial respiratory stress
    • Guha, M.; Pan, H.; Fang, J.K.; Avadhani, N.G. Heterogeneous nuclear ribonucleoprotein A2 is a common transcriptional coactivator in the nuclear transcription response to mitochondrial respiratory stress. Mol. Biol. Cell 2009, 20, 4107-4119.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 4107-4119
    • Guha, M.1    Pan, H.2    Fang, J.K.3    Avadhani, N.G.4
  • 25
    • 69549135927 scopus 로고    scopus 로고
    • Hepatic CYP3A suppression by high concentrations of proteasomal inhibitors: A consequence of endoplasmic reticulum (ER) stress induction, activation of RNA-dependent protein kinase-like ER-bound eukaryotic initiation factor 2α (eIF2α)-kinase (PERK) and general control nonderepressible-2 eIF2α kinase (GCN2), and global translational shutoff
    • Acharya, P.; Engel, J.C.; Correia, M.A. Hepatic CYP3A suppression by high concentrations of proteasomal inhibitors: A consequence of endoplasmic reticulum (ER) stress induction, activation of RNA-dependent protein kinase-like ER-bound eukaryotic initiation factor 2α (eIF2α)-kinase (PERK) and general control nonderepressible-2 eIF2α kinase (GCN2), and global translational shutoff. Mol. Pharmacol. 2009, 76, 503-515.
    • (2009) Mol. Pharmacol , vol.76 , pp. 503-515
    • Acharya, P.1    Engel, J.C.2    Correia, M.A.3
  • 28
    • 77953806964 scopus 로고    scopus 로고
    • Role of calcineurin, hnRNPA2 and Akt in mitochondrial respiratory stress-mediated transcription activation of nuclear gene targets
    • Guha, M.; Tang, W.; Sondheimer, N.; Avadhani, N.G. Role of calcineurin, hnRNPA2 and Akt in mitochondrial respiratory stress-mediated transcription activation of nuclear gene targets. Biochim. Biophys. Acta 2010, 1797, 1055-1065.
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 1055-1065
    • Guha, M.1    Tang, W.2    Sondheimer, N.3    Avadhani, N.G.4
  • 29
    • 0032953192 scopus 로고    scopus 로고
    • Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain
    • Itoh, K.; Wakabayashi, N.; Katoh, Y.; Ishii, T.; Igarashi, K.; Engel, J.D.; Yamamoto, M. Keap1 represses nuclear activation of antioxidant responsive elements by Nrf2 through binding to the amino-terminal Neh2 domain. Genes Dev. 1999, 13, 76-86.
    • (1999) Genes Dev , vol.13 , pp. 76-86
    • Itoh, K.1    Wakabayashi, N.2    Katoh, Y.3    Ishii, T.4    Igarashi, K.5    Engel, J.D.6    Yamamoto, M.7
  • 30
    • 84888135529 scopus 로고    scopus 로고
    • Reduced mammalian target of rapamycin activity facilitates mitochondrial retrograde signaling and increases life span in normal human fibroblasts
    • Lerner, C.; Bitto, A.; Pulliam, D.; Nacarelli, T.; Konigsberg, M.; van Remmen, H.; Torres, C.; Sell, C. Reduced mammalian target of rapamycin activity facilitates mitochondrial retrograde signaling and increases life span in normal human fibroblasts. Aging Cell 2013, 12, 966-977.
    • (2013) Aging Cell , vol.12 , pp. 966-977
    • Lerner, C.1    Bitto, A.2    Pulliam, D.3    Nacarelli, T.4    Konigsberg, M.5    van Remmen, H.6    Torres, C.7    Sell, C.8
  • 31
    • 33644852502 scopus 로고    scopus 로고
    • Mitochondrial transcription factor a induction by redox activation of nuclear respiratory factor 1
    • Piantadosi, C.A.; Suliman, H.B. Mitochondrial transcription factor a induction by redox activation of nuclear respiratory factor 1. J. Biol. Chem. 2006, 281, 324-333.
    • (2006) J. Biol. Chem , vol.281 , pp. 324-333
    • Piantadosi, C.A.1    Suliman, H.B.2
  • 32
    • 77954542997 scopus 로고    scopus 로고
    • Mitochondrial pyrimidine nucleotide carrier (PNC1) regulates mitochondrial biogenesis and the invasive phenotype of cancer cells
    • Favre, C.; Zhdanov, A.; Leahy, M.; Papkovsky, D.; O'Connor, R. Mitochondrial pyrimidine nucleotide carrier (PNC1) regulates mitochondrial biogenesis and the invasive phenotype of cancer cells. Oncogene 2010, 29, 3964-3976.
    • (2010) Oncogene , vol.29 , pp. 3964-3976
    • Favre, C.1    Zhdanov, A.2    Leahy, M.3    Papkovsky, D.4    O'Connor, R.5
  • 33
    • 27744601111 scopus 로고    scopus 로고
    • Reactive oxygen species mediates homocysteine-induced mitochondrial biogenesis in human endothelial cells: Modulation by antioxidants
    • Perez-de-Arce, K.; Foncea, R.; Leighton, F. Reactive oxygen species mediates homocysteine-induced mitochondrial biogenesis in human endothelial cells: Modulation by antioxidants. Biochem. Biophys. Res. Commun. 2005, 338, 1103-1109.
    • (2005) Biochem. Biophys. Res. Commun , vol.338 , pp. 1103-1109
    • Perez-de-Arce, K.1    Foncea, R.2    Leighton, F.3
  • 34
    • 25444449225 scopus 로고    scopus 로고
    • Protein kinase D mediates mitochondrion-to-nucleus signaling and detoxification from mitochondrial reactive oxygen species
    • Storz, P.; Doppler, H.; Toker, A. Protein kinase D mediates mitochondrion-to-nucleus signaling and detoxification from mitochondrial reactive oxygen species. Mol. Cell. Biol. 2005, 25, 8520-8530.
    • (2005) Mol. Cell. Biol , vol.25 , pp. 8520-8530
    • Storz, P.1    Doppler, H.2    Toker, A.3
  • 37
  • 38
    • 26244465857 scopus 로고    scopus 로고
    • Mitochondrial biogenesis in mtDNA-depleted cells involves a Ca2+-dependent pathway and a reduced mitochondrial protein import
    • Mercy, L.; Pauw, A.; Payen, L.; Tejerina, S.; Houbion, A.; Demazy, C.; Raes, M.; Renard, P.; Arnould, T. Mitochondrial biogenesis in mtDNA-depleted cells involves a Ca2+-dependent pathway and a reduced mitochondrial protein import. FEBS J. 2005, 272, 5031-5055.
    • (2005) FEBS J , vol.272 , pp. 5031-5055
    • Mercy, L.1    Pauw, A.2    Payen, L.3    Tejerina, S.4    Houbion, A.5    Demazy, C.6    Raes, M.7    Renard, P.8    Arnould, T.9
  • 40
    • 10944247187 scopus 로고    scopus 로고
    • The AMP-activated protein kinase pathway-New players upstream and downstream
    • Hardie, D.G. The AMP-activated protein kinase pathway-New players upstream and downstream. J. Cell Sci. 2004, 117, 5479-5487.
    • (2004) J. Cell Sci , vol.117 , pp. 5479-5487
    • Hardie, D.G.1
  • 41
    • 0037025356 scopus 로고    scopus 로고
    • AMP-activated protein kinase suppresses protein synthesis in rat skeletal muscle through down-regulated mammalian target of rapamycin (mTOR) signaling
    • Bolster, D.R.; Crozier, S.J.; Kimball, S.R.; Jefferson, L.S. AMP-activated protein kinase suppresses protein synthesis in rat skeletal muscle through down-regulated mammalian target of rapamycin (mTOR) signaling. J. Biol. Chem. 2002, 277, 23977-23980.
    • (2002) J. Biol. Chem , vol.277 , pp. 23977-23980
    • Bolster, D.R.1    Crozier, S.J.2    Kimball, S.R.3    Jefferson, L.S.4
  • 42
    • 34547545892 scopus 로고    scopus 로고
    • AMP-activated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1α
    • Jager, S.; Handschin, C.; St-Pierre, J.; Spiegelman, B.M. AMP-activated protein kinase (AMPK) action in skeletal muscle via direct phosphorylation of PGC-1α. Proc. Natl. Acad. Sci. USA 2007, 104, 12017-12022.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 12017-12022
    • Jager, S.1    Handschin, C.2    St-Pierre, J.3    Spiegelman, B.M.4
  • 43
    • 0036364274 scopus 로고    scopus 로고
    • Control of p70 ribosomal protein S6 kinase and acetyl-CoA carboxylase by AMP-activated protein kinase and protein phosphatases in isolated hepatocytes
    • Krause, U.; Bertrand, L.; Hue, L. Control of p70 ribosomal protein S6 kinase and acetyl-CoA carboxylase by AMP-activated protein kinase and protein phosphatases in isolated hepatocytes. Eur. J. Biochem. 2002, 269, 3751-3759.
    • (2002) Eur. J. Biochem , vol.269 , pp. 3751-3759
    • Krause, U.1    Bertrand, L.2    Hue, L.3
  • 44
    • 0345167800 scopus 로고    scopus 로고
    • TSC2 mediates cellular energy response to control cell growth and survival
    • Inoki, K.; Zhu, T.; Guan, K.L. TSC2 mediates cellular energy response to control cell growth and survival. Cell 2003, 115, 577-590.
    • (2003) Cell , vol.115 , pp. 577-590
    • Inoki, K.1    Zhu, T.2    Guan, K.L.3
  • 46
    • 77953631698 scopus 로고    scopus 로고
    • The secret life of NAD+: An old metabolite controlling new metabolic signaling pathways
    • Houtkooper, R.H.; Canto, C.; Wanders, R.J.; Auwerx, J. The secret life of NAD+: An old metabolite controlling new metabolic signaling pathways. Endocr. Rev. 2010, 31, 194-223.
    • (2010) Endocr. Rev , vol.31 , pp. 194-223
    • Houtkooper, R.H.1    Canto, C.2    Wanders, R.J.3    Auwerx, J.4
  • 47
    • 80052968080 scopus 로고    scopus 로고
    • Regulation of FoxO transcription factors by acetylation and protein-protein interactions
    • Daitoku, H.; Sakamaki, J.; Fukamizu, A. Regulation of FoxO transcription factors by acetylation and protein-protein interactions. Biochim. Biophys. Acta 2011, 1813, 1954-1960.
    • (2011) Biochim. Biophys. Acta , vol.1813 , pp. 1954-1960
    • Daitoku, H.1    Sakamaki, J.2    Fukamizu, A.3
  • 48
    • 73449116731 scopus 로고    scopus 로고
    • Mitochondrial acetylcarnitine provides acetyl groups for nuclear histone acetylation
    • Madiraju, P.; Pande, S.V.; Prentki, M.; Madiraju, S.R. Mitochondrial acetylcarnitine provides acetyl groups for nuclear histone acetylation. Epigenetics 2009, 4, 399-403.
    • (2009) Epigenetics , vol.4 , pp. 399-403
    • Madiraju, P.1    Pande, S.V.2    Prentki, M.3    Madiraju, S.R.4
  • 49
    • 56049090769 scopus 로고    scopus 로고
    • Acetylation of non-histone proteins modulates cellular signalling at multiple levels
    • Spange, S.; Wagner, T.; Heinzel, T.; Kramer, O.H. Acetylation of non-histone proteins modulates cellular signalling at multiple levels. Int. J. Biochem. Cell Biol. 2009, 41, 185-198.
    • (2009) Int. J. Biochem. Cell Biol , vol.41 , pp. 185-198
    • Spange, S.1    Wagner, T.2    Heinzel, T.3    Kramer, O.H.4
  • 50
    • 70450231612 scopus 로고    scopus 로고
    • Energetics, epigenetics, mitochondrial genetics
    • Wallace, D.C.; Fan, W. Energetics, epigenetics, mitochondrial genetics. Mitochondrion 2010, 10, 12-31.
    • (2010) Mitochondrion , vol.10 , pp. 12-31
    • Wallace, D.C.1    Fan, W.2
  • 51
    • 84900295547 scopus 로고    scopus 로고
    • Mitohormesis
    • Yun, J.; Finkel, T. Mitohormesis. Cell Metab. 2014, 19, 757-766.
    • (2014) Cell Metab , vol.19 , pp. 757-766
    • Yun, J.1    Finkel, T.2
  • 52
    • 84858376953 scopus 로고    scopus 로고
    • Mitochondria: In sickness and in health
    • Nunnari, J.; Suomalainen, A. Mitochondria: In sickness and in health. Cell 2012, 148, 1145-1159.
    • (2012) Cell , vol.148 , pp. 1145-1159
    • Nunnari, J.1    Suomalainen, A.2
  • 53
    • 84907211065 scopus 로고    scopus 로고
    • FGF21 expression and release in muscle cells: Involvement of MyoD and regulation by mitochondria-driven signalling
    • Ribas, F.; Villarroya, J.; Hondares, E.; Giralt, M.; Villarroya, F. FGF21 expression and release in muscle cells: Involvement of MyoD and regulation by mitochondria-driven signalling. Biochem. J. 2014, 463, 191-199.
    • (2014) Biochem. J , vol.463 , pp. 191-199
    • Ribas, F.1    Villarroya, J.2    Hondares, E.3    Giralt, M.4    Villarroya, F.5
  • 54
    • 84928895286 scopus 로고    scopus 로고
    • Skeletal muscle increase FGF21 expression in mitochondrial disorder to compensate for the energy metabolic insufficiency by activating mTOR-YY1-PGC1α pathway
    • Ji, K.; Zheng, J.; Lv, J.; Xu, J.; Ji, X.; Luo, Y.B.; Li, W.; Zhao, Y.; Yan, C. Skeletal muscle increase FGF21 expression in mitochondrial disorder to compensate for the energy metabolic insufficiency by activating mTOR-YY1-PGC1α pathway. Free Radic. Biol. Med. 2015, 84, 161-170.
    • (2015) Free Radic. Biol. Med , vol.84 , pp. 161-170
    • Ji, K.1    Zheng, J.2    Lv, J.3    Xu, J.4    Ji, X.5    Luo, Y.B.6    Li, W.7    Zhao, Y.8    Yan, C.9
  • 55
    • 78650944949 scopus 로고    scopus 로고
    • The cell-non-autonomous nature of electron transport chain-mediated longevity
    • Durieux, J.; Wolff, S.; Dillin, A. The cell-non-autonomous nature of electron transport chain-mediated longevity. Cell 2011, 144, 79-91.
    • (2011) Cell , vol.144 , pp. 79-91
    • Durieux, J.1    Wolff, S.2    Dillin, A.3
  • 56
    • 84941747116 scopus 로고    scopus 로고
    • UPRmt-mediated cytoprotection and organismal aging
    • Schulz, A.M.; Haynes, C.M. UPRmt-mediated cytoprotection and organismal aging. Biochim. Biophys. Acta 2015, doi:10.1016/j.bbabio.2015.03.008.
    • (2015) Biochim. Biophys. Acta
    • Schulz, A.M.1    Haynes, C.M.2
  • 57
    • 80054026314 scopus 로고    scopus 로고
    • A review of the mammalian unfolded protein response
    • Chakrabarti, A.; Chen, A.W.; Varner, J.D. A review of the mammalian unfolded protein response. Biotechnol. Bioeng. 2011, 108, 2777-2793.
    • (2011) Biotechnol. Bioeng , vol.108 , pp. 2777-2793
    • Chakrabarti, A.1    Chen, A.W.2    Varner, J.D.3
  • 58
    • 84878225746 scopus 로고    scopus 로고
    • Functional and morphological impact of ER stress on mitochondria
    • Vannuvel, K.; Renard, P.; Raes, M.; Arnould, T. Functional and morphological impact of ER stress on mitochondria. J. Cell. Physiol. 2013, 228, 1802-1818.
    • (2013) J. Cell. Physiol , vol.228 , pp. 1802-1818
    • Vannuvel, K.1    Renard, P.2    Raes, M.3    Arnould, T.4
  • 59
    • 84923195554 scopus 로고    scopus 로고
    • UPR, autophagy, and mitochondria crosstalk underlies the ER stress response
    • Senft, D.; Ronai, Z.A. UPR, autophagy, and mitochondria crosstalk underlies the ER stress response. Trends Biochem. Sci. 2015, 40, 141-148.
    • (2015) Trends Biochem. Sci , vol.40 , pp. 141-148
    • Senft, D.1    Ronai, Z.A.2
  • 61
    • 84901838039 scopus 로고    scopus 로고
    • The mitochondrial unfolded protein response and increased longevity: Cause, consequence, or correlation?
    • Bennett, C.F.; Kaeberlein, M. The mitochondrial unfolded protein response and increased longevity: Cause, consequence, or correlation? Exp. Gerontol. 2014, 56, 142-146.
    • (2014) Exp. Gerontol , vol.56 , pp. 142-146
    • Bennett, C.F.1    Kaeberlein, M.2
  • 62
    • 84905820762 scopus 로고    scopus 로고
    • Mitochondrial proteostasis in the control of aging and longevity
    • Jensen, M.B.; Jasper, H. Mitochondrial proteostasis in the control of aging and longevity. Cell Metab. 2014, 20, 214-225.
    • (2014) Cell Metab , vol.20 , pp. 214-225
    • Jensen, M.B.1    Jasper, H.2
  • 63
    • 84896499806 scopus 로고    scopus 로고
    • The mitochondrial unfolded protein response, a conserved stress response pathway with implications in health and disease
    • Jovaisaite, V.; Mouchiroud, L.; Auwerx, J. The mitochondrial unfolded protein response, a conserved stress response pathway with implications in health and disease. J. Exp. Biol. 2014, 217, 137-143.
    • (2014) J. Exp. Biol , vol.217 , pp. 137-143
    • Jovaisaite, V.1    Mouchiroud, L.2    Auwerx, J.3
  • 64
    • 84919775416 scopus 로고    scopus 로고
    • The mitochondrial unfolded protein response-synchronizing genomes
    • Jovaisaite, V.; Auwerx, J. The mitochondrial unfolded protein response-synchronizing genomes. Curr. Opin. Cell Biol. 2015, 33, 74-81.
    • (2015) Curr. Opin. Cell Biol , vol.33 , pp. 74-81
    • Jovaisaite, V.1    Auwerx, J.2
  • 65
    • 4944234936 scopus 로고    scopus 로고
    • Compartment-specific perturbation of protein handling activates genes encoding mitochondrial chaperones
    • Yoneda, T.; Benedetti, C.; Urano, F.; Clark, S.G.; Harding, H.P.; Ron, D. Compartment-specific perturbation of protein handling activates genes encoding mitochondrial chaperones. J. Cell Sci. 2004, 117, 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
  • 66
    • 0033060854 scopus 로고    scopus 로고
    • The mitochondrial genome: Structure, transcription, translation and replication
    • Taanman, J.W. The mitochondrial genome: Structure, transcription, translation and replication. Biochim. Biophys. Acta 1999, 1410, 103-123.
    • (1999) Biochim. Biophys. Acta , vol.1410 , pp. 103-123
    • Taanman, J.W.1
  • 68
    • 34848861368 scopus 로고    scopus 로고
    • ClpP mediates activation of a mitochondrial unfolded protein response in C. elegans
    • Haynes, C.M.; Petrova, K.; Benedetti, C.; Yang, Y.; Ron, D. ClpP mediates activation of a mitochondrial unfolded protein response in C. elegans. Dev. Cell 2007, 13, 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
  • 69
    • 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
    • Haynes, C.M.; Yang, Y.; Blais, S.P.; Neubert, T.A.; Ron, D. The matrix peptide exporter HAF-1 signals a mitochondrial UPR by activating the transcription factor ZC376.7 in C. Elegans. Mol. Cell 2010, 37, 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
  • 70
    • 84864744900 scopus 로고    scopus 로고
    • Mitochondrial import efficiency of ATFS-1 regulates mitochondrial UPR activation
    • Nargund, A.M.; Pellegrino, M.W.; Fiorese, C.J.; Baker, B.M.; Haynes, C.M. Mitochondrial import efficiency of ATFS-1 regulates mitochondrial UPR activation. Science 2012, 337, 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
  • 71
    • 84896716062 scopus 로고    scopus 로고
    • The protein import machinery of mitochondria-A regulatory hub in metabolism, stress, and disease
    • Harbauer, A.B.; Zahedi, R.P.; Sickmann, A.; Pfanner, N.; Meisinger, C. The protein import machinery of mitochondria-A regulatory hub in metabolism, stress, and disease. Cell Metab. 2014, 19, 357-372.
    • (2014) Cell Metab , vol.19 , pp. 357-372
    • Harbauer, A.B.1    Zahedi, R.P.2    Sickmann, A.3    Pfanner, N.4    Meisinger, C.5
  • 72
    • 84926180334 scopus 로고    scopus 로고
    • Mitochondrial and nuclear accumulation of the transcription factor ATFS-1 promotes OXPHOS recovery during the UPRmt
    • Nargund, A.M.; Fiorese, C.J.; Pellegrino, M.W.; Deng, P.; Haynes, C.M. Mitochondrial and nuclear accumulation of the transcription factor ATFS-1 promotes OXPHOS recovery during the UPRmt. Mol. Cell 2015, 58, 123-133.
    • (2015) Mol. Cell , vol.58 , pp. 123-133
    • Nargund, A.M.1    Fiorese, C.J.2    Pellegrino, M.W.3    Deng, P.4    Haynes, C.M.5
  • 73
    • 0025258481 scopus 로고
    • The mitochondrial chaperonin HSP60 is required for its own assembly
    • Cheng, M.Y.; Hartl, F.U.; Horwich, A.L. The mitochondrial chaperonin HSP60 is required for its own assembly. Nature 1990, 348, 455-458.
    • (1990) Nature , vol.348 , pp. 455-458
    • Cheng, M.Y.1    Hartl, F.U.2    Horwich, A.L.3
  • 74
    • 84889652177 scopus 로고    scopus 로고
    • Stress-regulated translational attenuation adapts mitochondrial protein import through Tim17A degradation
    • Rainbolt, T.K.; Atanassova, N.; Genereux, J.C.; Wiseman, R.L. Stress-regulated translational attenuation adapts mitochondrial protein import through Tim17A degradation. Cell Metab. 2013, 18, 908-919.
    • (2013) Cell Metab , vol.18 , pp. 908-919
    • Rainbolt, T.K.1    Atanassova, N.2    Genereux, J.C.3    Wiseman, R.L.4
  • 75
    • 84864065342 scopus 로고    scopus 로고
    • Protective coupling of mitochondrial function and protein synthesis via the eIF2α kinase GCN-2
    • Baker, B.M.; Nargund, A.M.; Sun, T.; Haynes, C.M. Protective coupling of mitochondrial function and protein synthesis via the eIF2α kinase GCN-2. PLoS Genet. 2012, 8, e1002760.
    • (2012) PLoS Genet , vol.8
    • Baker, B.M.1    Nargund, A.M.2    Sun, T.3    Haynes, C.M.4
  • 76
    • 84895835925 scopus 로고    scopus 로고
    • Forever young: SIRT3 a shield against mitochondrial meltdown, aging, and neurodegeneration
    • Kincaid, B.; Bossy-Wetzel, E. Forever young: SIRT3 a shield against mitochondrial meltdown, aging, and neurodegeneration. Front. Aging Neurosci. 2013, 5, 48.
    • (2013) Front. Aging Neurosci , vol.5 , pp. 48
    • Kincaid, B.1    Bossy-Wetzel, E.2
  • 77
    • 37849038317 scopus 로고    scopus 로고
    • The chop gene contains an element for the positive regulation of the mitochondrial unfolded protein response
    • Horibe, T.; Hoogenraad, N.J. The chop gene contains an element for the positive regulation of the mitochondrial unfolded protein response. PLoS ONE 2007, 2, e835.
    • (2007) PLoS ONE , vol.2
    • Horibe, T.1    Hoogenraad, N.J.2
  • 78
    • 79955549674 scopus 로고    scopus 로고
    • Estrogen receptor mediates a distinct mitochondrial unfolded protein response
    • Papa, L.; Germain, D. Estrogen receptor mediates a distinct mitochondrial unfolded protein response. J. Cell Sci. 2011, 124, 1396-1402.
    • (2011) J. Cell Sci , vol.124 , pp. 1396-1402
    • Papa, L.1    Germain, D.2
  • 80
    • 37849048003 scopus 로고    scopus 로고
    • Discovery of genes activated by the mitochondrial unfolded protein response (mtUPR) and cognate promoter elements
    • Aldridge, J.E.; Horibe, T.; Hoogenraad, N.J. Discovery of genes activated by the mitochondrial unfolded protein response (mtUPR) and cognate promoter elements. PLoS ONE 2007, 2, e874.
    • (2007) PLoS ONE , vol.2
    • Aldridge, J.E.1    Horibe, T.2    Hoogenraad, N.J.3
  • 81
    • 70249121045 scopus 로고    scopus 로고
    • The logic of chromatin architecture and remodelling at promoters
    • Cairns, B.R. The logic of chromatin architecture and remodelling at promoters. Nature 2009, 461, 193-198.
    • (2009) Nature , vol.461 , pp. 193-198
    • Cairns, B.R.1
  • 82
    • 84864985287 scopus 로고    scopus 로고
    • Induction of dsRNA-activated protein kinase links mitochondrial unfolded protein response to the pathogenesis of intestinal inflammation
    • Rath, E.; Berger, E.; Messlik, A.; Nunes, T.; Liu, B.; Kim, S.C.; Hoogenraad, N.; Sans, M.; Sartor, R.B.; Haller, D. Induction of dsRNA-activated protein kinase links mitochondrial unfolded protein response to the pathogenesis of intestinal inflammation. Gut 2012, 61, 1269-1278.
    • (2012) Gut , vol.61 , pp. 1269-1278
    • Rath, E.1    Berger, E.2    Messlik, A.3    Nunes, T.4    Liu, B.5    Kim, S.C.6    Hoogenraad, N.7    Sans, M.8    Sartor, R.B.9    Haller, D.10
  • 83
    • 84887020906 scopus 로고    scopus 로고
    • Dual control of mitochondrial biogenesis by sirtuin 1 and sirtuin 3
    • Brenmoehl, J.; Hoeflich, A. Dual control of mitochondrial biogenesis by sirtuin 1 and sirtuin 3. Mitochondrion 2013, 13, 755-761.
    • (2013) Mitochondrion , vol.13 , pp. 755-761
    • Brenmoehl, J.1    Hoeflich, A.2
  • 84
    • 84892989225 scopus 로고    scopus 로고
    • SirT3 regulates the mitochondrial unfolded protein response
    • Papa, L.; Germain, D. SirT3 regulates the mitochondrial unfolded protein response. Mol. Cell. Biol. 2014, 34, 699-710.
    • (2014) Mol. Cell. Biol , vol.34 , pp. 699-710
    • Papa, L.1    Germain, D.2
  • 86
    • 84922635413 scopus 로고    scopus 로고
    • Inhibition of mitochondrial genome expression triggers the activation of chop-10 by a cell signaling dependent on the integrated stress response but not the mitochondrial unfolded protein response
    • Michel, S.; Canonne, M.; Arnould, T.; Renard, P. Inhibition of mitochondrial genome expression triggers the activation of chop-10 by a cell signaling dependent on the integrated stress response but not the mitochondrial unfolded protein response. Mitochondrion 2015, 21, 58-68.
    • (2015) Mitochondrion , vol.21 , pp. 58-68
    • Michel, S.1    Canonne, M.2    Arnould, T.3    Renard, P.4
  • 87
    • 33748154507 scopus 로고    scopus 로고
    • Mitochondrial disease activates transcripts of the unfolded protein response and cell cycle and inhibits vesicular secretion and oligodendrocyte-specific transcripts
    • Cortopassi, G.; Danielson, S.; Alemi, M.; Zhan, S.S.; Tong, W.; Carelli, V.; Martinuzzi, A.; Marzuki, S.; Majamaa, K.; Wong, A. Mitochondrial disease activates transcripts of the unfolded protein response and cell cycle and inhibits vesicular secretion and oligodendrocyte-specific transcripts. Mitochondrion 2006, 6, 161-175.
    • (2006) Mitochondrion , vol.6 , pp. 161-175
    • Cortopassi, G.1    Danielson, S.2    Alemi, M.3    Zhan, S.S.4    Tong, W.5    Carelli, V.6    Martinuzzi, A.7    Marzuki, S.8    Majamaa, K.9    Wong, A.10
  • 88
    • 33847653346 scopus 로고    scopus 로고
    • CHOP (C/EBP homologous protein) and ASNS (asparagine synthetase) induction in cybrid cells harboring MELAS and NARP mitochondrial DNA mutations
    • Fujita, Y.; Ito, M.; Nozawa, Y.; Yoneda, M.; Oshida, Y.; Tanaka, M. CHOP (C/EBP homologous protein) and ASNS (asparagine synthetase) induction in cybrid cells harboring MELAS and NARP mitochondrial DNA mutations. Mitochondrion 2007, 7, 80-88.
    • (2007) Mitochondrion , vol.7 , pp. 80-88
    • Fujita, Y.1    Ito, M.2    Nozawa, Y.3    Yoneda, M.4    Oshida, Y.5    Tanaka, M.6
  • 89
    • 67651183896 scopus 로고    scopus 로고
    • Gene expression profiling identifies a role for CHOP during inhibition of the mitochondrial respiratory chain
    • Ishikawa, F.; Akimoto, T.; Yamamoto, H.; Araki, Y.; Yoshie, T.; Mori, K.; Hayashi, H.; Nose, K.; Shibanuma, M. Gene expression profiling identifies a role for CHOP during inhibition of the mitochondrial respiratory chain. J. Biochem. 2009, 146, 123-132.
    • (2009) J. Biochem , vol.146 , pp. 123-132
    • Ishikawa, F.1    Akimoto, T.2    Yamamoto, H.3    Araki, Y.4    Yoshie, T.5    Mori, K.6    Hayashi, H.7    Nose, K.8    Shibanuma, M.9
  • 92
    • 32544446451 scopus 로고    scopus 로고
    • Coping with stress: EIF2 kinases and translational control
    • Wek, R.C.; Jiang, H.Y.; Anthony, T.G. Coping with stress: eIF2 kinases and translational control. Biochem. Soc. Trans. 2006, 34, 7-11.
    • (2006) Biochem. Soc. Trans , vol.34 , pp. 7-11
    • Wek, R.C.1    Jiang, H.Y.2    Anthony, T.G.3
  • 94
    • 84866782195 scopus 로고    scopus 로고
    • Eukaryotic initiation factor 2 phosphorylation and translational control in metabolism
    • Baird, T.D.; Wek, R.C. Eukaryotic initiation factor 2 phosphorylation and translational control in metabolism. Adv. Nutr. 2012, 3, 307-321.
    • (2012) Adv. Nutr , vol.3 , pp. 307-321
    • Baird, T.D.1    Wek, R.C.2
  • 95
    • 3142545254 scopus 로고    scopus 로고
    • Herp stabilizes neuronal Ca2+ homeostasis and mitochondrial function during endoplasmic reticulum stress
    • Chan, S.L.; Fu, W.; Zhang, P.; Cheng, A.; Lee, J.; Kokame, K.; Mattson, M.P. Herp stabilizes neuronal Ca2+ homeostasis and mitochondrial function during endoplasmic reticulum stress. J. Biol. Chem. 2004, 279, 28733-28743.
    • (2004) J. Biol. Chem , vol.279 , pp. 28733-28743
    • Chan, S.L.1    Fu, W.2    Zhang, P.3    Cheng, A.4    Lee, J.5    Kokame, K.6    Mattson, M.P.7
  • 96
    • 84864025989 scopus 로고    scopus 로고
    • The mammalian tribbles homolog TRIB3, glucose homeostasis, and cardiovascular diseases
    • Prudente, S.; Sesti, G.; Pandolfi, A.; Andreozzi, F.; Consoli, A.; Trischitta, V. The mammalian tribbles homolog TRIB3, glucose homeostasis, and cardiovascular diseases. Endocr. Rev. 2012, 33, 526-546.
    • (2012) Endocr. Rev , vol.33 , pp. 526-546
    • Prudente, S.1    Sesti, G.2    Pandolfi, A.3    Andreozzi, F.4    Consoli, A.5    Trischitta, V.6
  • 97
    • 23844554840 scopus 로고    scopus 로고
    • Structural basis for autoinhibition and mutational activation of eukaryotic initiation factor 2α protein kinase GCN2
    • Padyana, A.K.; Qiu, H.; Roll-Mecak, A.; Hinnebusch, A.G.; Burley, S.K. Structural basis for autoinhibition and mutational activation of eukaryotic initiation factor 2α protein kinase GCN2. J. Biol. Chem. 2005, 280, 29289-29299.
    • (2005) J. Biol. Chem , vol.280 , pp. 29289-29299
    • Padyana, A.K.1    Qiu, H.2    Roll-Mecak, A.3    Hinnebusch, A.G.4    Burley, S.K.5
  • 98
    • 12844259491 scopus 로고    scopus 로고
    • GCN2 phosphorylation of eIF2α activates NF-κB in response to UV irradiation
    • Jiang, H.Y.; Wek, R.C. GCN2 phosphorylation of eIF2α activates NF-κB in response to UV irradiation. Biochem. J. 2005, 385, 371-380.
    • (2005) Biochem. J , vol.385 , pp. 371-380
    • Jiang, H.Y.1    Wek, R.C.2
  • 99
    • 17144389838 scopus 로고    scopus 로고
    • Phosphorylation of the α-subunit of the eukaryotic initiation factor-2 (eIF2α) reduces protein synthesis and enhances apoptosis in response to proteasome inhibition
    • Jiang, H.Y.; Wek, R.C. Phosphorylation of the α-subunit of the eukaryotic initiation factor-2 (eIF2α) reduces protein synthesis and enhances apoptosis in response to proteasome inhibition. J. Biol. Chem. 2005, 280, 14189-14202.
    • (2005) J. Biol. Chem , vol.280 , pp. 14189-14202
    • Jiang, H.Y.1    Wek, R.C.2
  • 100
    • 0026546365 scopus 로고
    • CHOP, a novel developmentally regulated nuclear protein that dimerizes with transcription factors C/EBP and LAP and functions as a dominant-negative inhibitor of gene transcription
    • Ron, D.; Habener, J.F. CHOP, a novel developmentally regulated nuclear protein that dimerizes with transcription factors C/EBP and LAP and functions as a dominant-negative inhibitor of gene transcription. Genes Dev. 1992, 6, 439-453.
    • (1992) Genes Dev , vol.6 , pp. 439-453
    • Ron, D.1    Habener, J.F.2
  • 101
    • 17144417669 scopus 로고    scopus 로고
    • TRB3, a novel ER stress-inducible gene, is induced via ATF4-CHOP pathway and is involved in cell death
    • Ohoka, N.; Yoshii, S.; Hattori, T.; Onozaki, K.; Hayashi, H. TRB3, a novel ER stress-inducible gene, is induced via ATF4-CHOP pathway and is involved in cell death. EMBO J. 2005, 24, 1243-1255.
    • (2005) EMBO J , vol.24 , pp. 1243-1255
    • Ohoka, N.1    Yoshii, S.2    Hattori, T.3    Onozaki, K.4    Hayashi, H.5
  • 102
    • 58049203872 scopus 로고    scopus 로고
    • C/EBP homology protein (CHOP) interacts with activating transcription factor 4 (ATF4) and negatively regulates the stress-dependent induction of the asparagine synthetase gene
    • Su, N.; Kilberg, M.S. C/EBP homology protein (CHOP) interacts with activating transcription factor 4 (ATF4) and negatively regulates the stress-dependent induction of the asparagine synthetase gene. J. Biol. Chem. 2008, 283, 35106-35117.
    • (2008) J. Biol. Chem , vol.283 , pp. 35106-35117
    • Su, N.1    Kilberg, M.S.2
  • 105
    • 84887486172 scopus 로고    scopus 로고
    • The accumulation of misfolded proteins in the mitochondrial matrix is sensed by PINK1 to induce PARK2/Parkin-mediated mitophagy of polarized mitochondria
    • Jin, S.M.; Youle, R.J. The accumulation of misfolded proteins in the mitochondrial matrix is sensed by PINK1 to induce PARK2/Parkin-mediated mitophagy of polarized mitochondria. Autophagy 2013, 9, 1750-1757
    • (2013) Autophagy , vol.9 , pp. 1750-1757
    • Jin, S.M.1    Youle, R.J.2
  • 106
    • 78649685455 scopus 로고    scopus 로고
    • Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL
    • Jin, S.M.; Lazarou, M.; Wang, C.; Kane, L.A.; Narendra, D.P.; Youle, R.J. Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL. J. Cell Biol. 2010, 191, 933-942.
    • (2010) J. Cell Biol , vol.191 , pp. 933-942
    • Jin, S.M.1    Lazarou, M.2    Wang, C.3    Kane, L.A.4    Narendra, D.P.5    Youle, R.J.6
  • 108
    • 33845918450 scopus 로고    scopus 로고
    • β-Amyloid precursor protein is a direct cleavage target of HtrA2 serine protease. Implications for the physiological function of HtrA2 in the mitochondria
    • Park, H.J.; Kim, S.S.; Seong, Y.M.; Kim, K.H.; Goo, H.G.; Yoon, E.J.; Min, D.S.; Kang, S.; Rhim, H. β-Amyloid precursor protein is a direct cleavage target of HtrA2 serine protease. Implications for the physiological function of HtrA2 in the mitochondria. J. Biol. Chem. 2006, 281, 34277-34287.
    • (2006) J. Biol. Chem , vol.281 , pp. 34277-34287
    • Park, H.J.1    Kim, S.S.2    Seong, Y.M.3    Kim, K.H.4    Goo, H.G.5    Yoon, E.J.6    Min, D.S.7    Kang, S.8    Rhim, H.9
  • 109
    • 67849129079 scopus 로고    scopus 로고
    • A new function of human HtrA2 as an amyloid-β oligomerization inhibitor
    • Kooistra, J.; Milojevic, J.; Melacini, G.; Ortega, J. A new function of human HtrA2 as an amyloid-β oligomerization inhibitor. J. Alzheimer's Dis. 2009, 17, 281-294.
    • (2009) J. Alzheimer's Dis , vol.17 , pp. 281-294
    • Kooistra, J.1    Milojevic, J.2    Melacini, G.3    Ortega, J.4
  • 110
    • 44049099669 scopus 로고    scopus 로고
    • Mitochondrial import and accumulation of α-synuclein impair complex I in human dopaminergic neuronal cultures and Parkinson disease brain
    • Devi, L.; Raghavendran, V.; Prabhu, B.M.; Avadhani, N.G.; Anandatheerthavarada, H.K. Mitochondrial import and accumulation of α-synuclein impair complex I in human dopaminergic neuronal cultures and Parkinson disease brain. J. Biol. Chem. 2008, 283, 9089-9100.
    • (2008) J. Biol. Chem , vol.283 , pp. 9089-9100
    • Devi, L.1    Raghavendran, V.2    Prabhu, B.M.3    Avadhani, N.G.4    Anandatheerthavarada, H.K.5
  • 111
    • 44649150145 scopus 로고    scopus 로고
    • Mitochondrial localization of α-synuclein protein in α-synuclein overexpressing cells
    • Shavali, S.; Brown-Borg, H.M.; Ebadi, M.; Porter, J. Mitochondrial localization of α-synuclein protein in α-synuclein overexpressing cells. Neurosci. Lett. 2008, 439, 125-128.
    • (2008) Neurosci. Lett , vol.439 , pp. 125-128
    • Shavali, S.1    Brown-Borg, H.M.2    Ebadi, M.3    Porter, J.4
  • 113
    • 84926334923 scopus 로고    scopus 로고
    • Mitophagy and the mitochondrial unfolded protein response in neurodegeneration and bacterial infection
    • Pellegrino, M.W.; Haynes, C.M. Mitophagy and the mitochondrial unfolded protein response in neurodegeneration and bacterial infection. BMC Biol. 2015, 13, 22.
    • (2015) BMC Biol , vol.13 , pp. 22
    • Pellegrino, M.W.1    Haynes, C.M.2
  • 114
    • 84905815492 scopus 로고    scopus 로고
    • Mitochondrial stress signaling in longevity: A new role for mitochondrial function in aging
    • Hill, S.; van Remmen, H. Mitochondrial stress signaling in longevity: A new role for mitochondrial function in aging. Redox Biol. 2014, 2, 936-944.
    • (2014) Redox Biol , vol.2 , pp. 936-944
    • Hill, S.1    van Remmen, H.2
  • 115
    • 84925265469 scopus 로고    scopus 로고
    • Stem cell aging. A mitochondrial UPR-mediated metabolic checkpoint regulates hematopoietic stem cell aging
    • Mohrin, M.; Shin, J.; Liu, Y.; Brown, K.; Luo, H.; Xi, Y.; Haynes, C.M.; Chen, D. Stem cell aging. A mitochondrial UPR-mediated metabolic checkpoint regulates hematopoietic stem cell aging. Science 2015, 347, 1374-1377.
    • (2015) Science , vol.347 , pp. 1374-1377
    • Mohrin, M.1    Shin, J.2    Liu, Y.3    Brown, K.4    Luo, H.5    Xi, Y.6    Haynes, C.M.7    Chen, D.8
  • 117
    • 84921774753 scopus 로고    scopus 로고
    • Mitochondrial UPR-regulated innate immunity provides resistance to pathogen infection
    • Pellegrino, M.W.; Nargund, A.M.; Kirienko, N.V.; Gillis, R.; Fiorese, C.J.; Haynes, C.M. Mitochondrial UPR-regulated innate immunity provides resistance to pathogen infection. Nature 2014, 516, 414-417.
    • (2014) Nature , vol.516 , pp. 414-417
    • Pellegrino, M.W.1    Nargund, A.M.2    Kirienko, N.V.3    Gillis, R.4    Fiorese, C.J.5    Haynes, C.M.6
  • 118
    • 84866254933 scopus 로고    scopus 로고
    • Unfolded protein responses in the intestinal epithelium: Sensors for the microbial and metabolic environment
    • Rath, E.; Haller, D. Unfolded protein responses in the intestinal epithelium: Sensors for the microbial and metabolic environment. J. Clin. Gastroenterol. 2012, 46, S3-S5.
    • (2012) J. Clin. Gastroenterol , vol.46 , pp. S3-S5
    • Rath, E.1    Haller, D.2
  • 119
    • 84865000368 scopus 로고    scopus 로고
    • PKR protects colonic epithelium against colitis through the unfolded protein response and prosurvival signaling
    • Cao, S.S.; Song, B.; Kaufman, R.J. PKR protects colonic epithelium against colitis through the unfolded protein response and prosurvival signaling. Inflamm. Bowel Dis. 2012, 18, 1735-1742.
    • (2012) Inflamm. Bowel Dis , vol.18 , pp. 1735-1742
    • Cao, S.S.1    Song, B.2    Kaufman, R.J.3
  • 121
    • 84914178820 scopus 로고    scopus 로고
    • Post-transcriptional RNA regulons affecting cell cycle and proliferation
    • Blackinton, J.G.; Keene, J.D. Post-transcriptional RNA regulons affecting cell cycle and proliferation. Semin. Cell Dev. Biol. 2014, 34, 44-54.
    • (2014) Semin. Cell Dev. Biol , vol.34 , pp. 44-54
    • Blackinton, J.G.1    Keene, J.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.