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Volumn 115, Issue 15, 2018, Pages E3388-E3397

S-nitrosylation drives cell senescence and aging in mammals by controlling mitochondrial dynamics and mitophagy

(13)  Rizza, Salvatore a   Cardaci, Simone b   Montagna, Costanza a,c   Giacomo, Giuseppina Di d,l   De Zio, Daniela a   Bordi, Matteo d   Maiani, Emiliano a   Campello, Silvia d,e   Borreca, Antonella f   Puca, Annibale A g,h   Stamler, Jonathan S i,j   Cecconi, Francesco a,d,k   Filomeni, Giuseppe a,d  

f CNR   (Italy)

Author keywords

Aging; GSNOR; Mitochondria; Mitophagy; S nitrosylation

Indexed keywords

GLUTATHIONE REDUCTASE; NITROSOGLUTATHIONE REDUCTASE; UNCLASSIFIED DRUG; ALDEHYDE DEHYDROGENASE; FORMALDEHYDE DEHYDROGENASE, GLUTATHIONE-INDEPENDENT; NITRIC OXIDE; S NITROSOTHIOL;

EID: 85045103676     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1722452115     Document Type: Article
Times cited : (136)

References (71)
  • 1
    • 84856834347 scopus 로고    scopus 로고
    • Regulation by S-nitrosylation of protein post-translational modification
    • Hess DT, Stamler JS (2012) Regulation by S-nitrosylation of protein post-translational modification. J Biol Chem 287:4411-4418.
    • (2012) J Biol Chem , vol.287 , pp. 4411-4418
    • Hess, D.T.1    Stamler, J.S.2
  • 2
    • 0035929149 scopus 로고    scopus 로고
    • Nitrosylation. The prototypic redox-based signaling mechanism
    • Stamler JS, Lamas S, Fang FC (2001) Nitrosylation. The prototypic redox-based signaling mechanism. Cell 106:675-683.
    • (2001) Cell , vol.106 , pp. 675-683
    • Stamler, J.S.1    Lamas, S.2    Fang, F.C.3
  • 4
    • 84906086261 scopus 로고    scopus 로고
    • Nitrosothiol signaling and protein nitrosation in cell death
    • Iyer AKV, Rojanasakul Y, Azad N (2014) Nitrosothiol signaling and protein nitrosation in cell death. Nitric Oxide 42:9-18.
    • (2014) Nitric Oxide , vol.42 , pp. 9-18
    • Iyer, A.K.V.1    Rojanasakul, Y.2    Azad, N.3
  • 5
    • 80051781073 scopus 로고    scopus 로고
    • Redox modulation by S-nitrosylation contributes to protein misfolding, mitochondrial dynamics, and neuronal synaptic damage in neurodegenerative diseases
    • Nakamura T, Lipton SA (2011) Redox modulation by S-nitrosylation contributes to protein misfolding, mitochondrial dynamics, and neuronal synaptic damage in neurodegenerative diseases. Cell Death Differ 18:1478-1486.
    • (2011) Cell Death Differ , vol.18 , pp. 1478-1486
    • Nakamura, T.1    Lipton, S.A.2
  • 6
    • 84925725817 scopus 로고    scopus 로고
    • Aberrant protein S-nitrosylation contributes to the pathophysiology of neurodegenerative diseases
    • Nakamura T, et al. (2015) Aberrant protein S-nitrosylation contributes to the pathophysiology of neurodegenerative diseases. Neurobiol Dis 84:99-108.
    • (2015) Neurobiol Dis , vol.84 , pp. 99-108
    • Nakamura, T.1
  • 7
    • 85040632767 scopus 로고    scopus 로고
    • A multiplex enzymatic machinery for cellular protein S-nitrosylation
    • e6
    • Seth D, et al. (2018) A multiplex enzymatic machinery for cellular protein S-nitrosylation. Mol Cell 69:451-464.e6.
    • (2018) Mol Cell , vol.69 , pp. 451-464
    • Seth, D.1
  • 8
    • 0035932413 scopus 로고    scopus 로고
    • A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans
    • Liu L, et al. (2001) A metabolic enzyme for S-nitrosothiol conserved from bacteria to humans. Nature 410:490-494.
    • (2001) Nature , vol.410 , pp. 490-494
    • Liu, L.1
  • 9
    • 85019714803 scopus 로고    scopus 로고
    • Chronicles of a reductase: Biochemistry, genetics and physio-pathological role of GSNOR
    • Rizza S, Filomeni G (2017) Chronicles of a reductase: Biochemistry, genetics and physio-pathological role of GSNOR. Free Radic Biol Med 110:19-30.
    • (2017) Free Radic Biol Med , vol.110 , pp. 19-30
    • Rizza, S.1    Filomeni, G.2
  • 10
    • 84858216481 scopus 로고    scopus 로고
    • Dynamic denitrosylation via S-nitrosoglutathione reductase regulates cardiovascular function
    • Beigi F, et al. (2012) Dynamic denitrosylation via S-nitrosoglutathione reductase regulates cardiovascular function. Proc Natl Acad Sci USA 109:4314-4319.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 4314-4319
    • Beigi, F.1
  • 11
    • 33745840525 scopus 로고    scopus 로고
    • Nitric oxide synthase expression and nitric oxide toxicity in oligodendrocytes
    • Boullerne AI, Benjamins JA (2006) Nitric oxide synthase expression and nitric oxide toxicity in oligodendrocytes. Antioxid Redox Signal 8:967-980.
    • (2006) Antioxid Redox Signal , vol.8 , pp. 967-980
    • Boullerne, A.I.1    Benjamins, J.A.2
  • 12
    • 79953131110 scopus 로고    scopus 로고
    • Nitric oxide is the primary mediator of cytotoxicity induced by GSH depletion in neuronal cells
    • Aquilano K, Baldelli S, Cardaci S, Rotilio G, Ciriolo MR (2011) Nitric oxide is the primary mediator of cytotoxicity induced by GSH depletion in neuronal cells. J Cell Sci 124: 1043-1054.
    • (2011) J Cell Sci , vol.124 , pp. 1043-1054
    • Aquilano, K.1    Baldelli, S.2    Cardaci, S.3    Rotilio, G.4    Ciriolo, M.R.5
  • 13
    • 22144477159 scopus 로고    scopus 로고
    • S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding
    • Hara MR, et al. (2005) S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding. Nat Cell Biol 7:665-674.
    • (2005) Nat Cell Biol , vol.7 , pp. 665-674
    • Hara, M.R.1
  • 14
    • 84878443676 scopus 로고    scopus 로고
    • Aberrant protein S-nitrosylation in neurodegenerative diseases
    • Nakamura T, et al. (2013) Aberrant protein S-nitrosylation in neurodegenerative diseases. Neuron 78:596-614.
    • (2013) Neuron , vol.78 , pp. 596-614
    • Nakamura, T.1
  • 15
    • 78650663849 scopus 로고    scopus 로고
    • Lymphocyte development requires S-nitrosoglutathione reductase
    • Yang Z, et al. (2010) Lymphocyte development requires S-nitrosoglutathione reductase. J Immunol 185:6664-6669.
    • (2010) J Immunol , vol.185 , pp. 6664-6669
    • Yang, Z.1
  • 16
    • 10744230465 scopus 로고    scopus 로고
    • Essential roles of S-nitrosothiols in vascular homeostasis and en-dotoxic shock
    • Liu L, et al. (2004) Essential roles of S-nitrosothiols in vascular homeostasis and en-dotoxic shock. Cell 116:617-628.
    • (2004) Cell , vol.116 , pp. 617-628
    • Liu, L.1
  • 17
    • 79960030755 scopus 로고    scopus 로고
    • Targeted deletion of GSNOR in hepatocytes of mice causes nitrosative inactivation of O6-alkylguanine-DNA alkyltransferase and increased sensitivity to genotoxic diethylnitrosamine
    • Wei W, Yang Z, Tang CH, Liu L (2011) Targeted deletion of GSNOR in hepatocytes of mice causes nitrosative inactivation of O6-alkylguanine-DNA alkyltransferase and increased sensitivity to genotoxic diethylnitrosamine. Carcinogenesis 32:973-977.
    • (2011) Carcinogenesis , vol.32 , pp. 973-977
    • Wei, W.1    Yang, Z.2    Tang, C.H.3    Liu, L.4
  • 18
    • 77952963414 scopus 로고    scopus 로고
    • S-nitrosylation from GSNOR deficiency impairs DNA repair and promotes hepatocarcinogenesis
    • Wei W, et al. (2010) S-nitrosylation from GSNOR deficiency impairs DNA repair and promotes hepatocarcinogenesis. Sci Transl Med 2:19ra13.
    • (2010) Sci Transl Med , vol.2 , pp. 19ra13
    • Wei, W.1
  • 19
    • 84904007368 scopus 로고    scopus 로고
    • S-nitrosoglutathione reductase deficiency-induced S-nitrosylation results in neuromuscular dysfunction
    • Montagna C, et al. (2014) S-nitrosoglutathione reductase deficiency-induced S-nitrosylation results in neuromuscular dysfunction. Antioxid Redox Signal 21:570-587.
    • (2014) Antioxid Redox Signal , vol.21 , pp. 570-587
    • Montagna, C.1
  • 20
    • 84926297886 scopus 로고    scopus 로고
    • S-nitrosoglutathione reductase-dependent PPARγ denitrosylation participates in MSC-derived adipogenesis and osteogenesis
    • Cao Y, et al. (2015) S-nitrosoglutathione reductase-dependent PPARγ denitrosylation participates in MSC-derived adipogenesis and osteogenesis. J Clin Invest 125:1679-1691.
    • (2015) J Clin Invest , vol.125 , pp. 1679-1691
    • Cao, Y.1
  • 21
    • 85019217957 scopus 로고    scopus 로고
    • Brain aging and neurodegeneration: From a mitochondrial point of view
    • Grimm A, Eckert A (2017) Brain aging and neurodegeneration: From a mitochondrial point of view. J Neurochem 143:418-431.
    • (2017) J Neurochem , vol.143 , pp. 418-431
    • Grimm, A.1    Eckert, A.2
  • 22
    • 30044434360 scopus 로고    scopus 로고
    • The mitochondrial theory of aging and its relationship to reactive oxygen species damage and somatic mtDNA mutations
    • Loeb LA, Wallace DC, Martin GM (2005) The mitochondrial theory of aging and its relationship to reactive oxygen species damage and somatic mtDNA mutations. Proc Natl Acad Sci USA 102:18769-18770.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 18769-18770
    • Loeb, L.A.1    Wallace, D.C.2    Martin, G.M.3
  • 24
    • 84860481279 scopus 로고    scopus 로고
    • Regulation of mitochondrial processes by protein S-nitrosylation
    • Piantadosi CA (2012) Regulation of mitochondrial processes by protein S-nitrosylation. Biochim Biophys Acta 1820:712-721.
    • (2012) Biochim Biophys Acta , vol.1820 , pp. 712-721
    • Piantadosi, C.A.1
  • 25
    • 0032560572 scopus 로고    scopus 로고
    • Persistent inhibition of cell respiration by nitric oxide: Crucial role of S-nitrosylation of mitochondrial complex I and protective action of glutathione
    • Clementi E, Brown GC, Feelisch M, Moncada S (1998) Persistent inhibition of cell respiration by nitric oxide: Crucial role of S-nitrosylation of mitochondrial complex I and protective action of glutathione. Proc Natl Acad Sci USA 95:7631-7636.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 7631-7636
    • Clementi, E.1    Brown, G.C.2    Feelisch, M.3    Moncada, S.4
  • 26
    • 33744527052 scopus 로고    scopus 로고
    • Persistent S-nitrosation of complex I and other mitochondrial membrane proteins by S-nitrosothiols but not nitric oxide or perox-ynitrite: Implications for the interaction of nitric oxide with mitochondria
    • Dahm CC, Moore K, Murphy MP (2006) Persistent S-nitrosation of complex I and other mitochondrial membrane proteins by S-nitrosothiols but not nitric oxide or perox-ynitrite: Implications for the interaction of nitric oxide with mitochondria. J Biol Chem 281:10056-10065.
    • (2006) J Biol Chem , vol.281 , pp. 10056-10065
    • Dahm, C.C.1    Moore, K.2    Murphy, M.P.3
  • 27
    • 84857397980 scopus 로고    scopus 로고
    • The nitric oxide pathway provides innate antiviral protection in conjunction with the type I interferon pathway in fibroblasts
    • Mehta DR, Ashkar AA, Mossman KL (2012) The nitric oxide pathway provides innate antiviral protection in conjunction with the type I interferon pathway in fibroblasts. PLoS One 7:e31688.
    • (2012) PLoS One , vol.7 , pp. e31688
    • Mehta, D.R.1    Ashkar, A.A.2    Mossman, K.L.3
  • 28
    • 0033526524 scopus 로고    scopus 로고
    • Neuronal expression of NOS-1 is required for host recovery from viral encephalitis
    • Komatsu T, Ireland DDC, Chen N, Reiss CS (1999) Neuronal expression of NOS-1 is required for host recovery from viral encephalitis. Virology 258:389-395.
    • (1999) Virology , vol.258 , pp. 389-395
    • Komatsu, T.1    Ireland, D.D.C.2    Chen, N.3    Reiss, C.S.4
  • 29
    • 82955207588 scopus 로고    scopus 로고
    • Mechanisms and functions of Tet protein-mediated 5-meth-ylcytosine oxidation
    • Wu H, Zhang Y (2011) Mechanisms and functions of Tet protein-mediated 5-meth-ylcytosine oxidation. Genes Dev 25:2436-2452.
    • (2011) Genes Dev , vol.25 , pp. 2436-2452
    • Wu, H.1    Zhang, Y.2
  • 30
    • 79955948324 scopus 로고    scopus 로고
    • Genome-wide regulation of 5hmC, 5mC, and gene expression by Tet1 hydroxylase in mouse embryonic stem cells
    • Xu Y, et al. (2011) Genome-wide regulation of 5hmC, 5mC, and gene expression by Tet1 hydroxylase in mouse embryonic stem cells. Mol Cell 42:451-464.
    • (2011) Mol Cell , vol.42 , pp. 451-464
    • Xu, Y.1
  • 31
    • 84866234079 scopus 로고    scopus 로고
    • Established principles and emerging concepts on the interplay between mitochondrial physiology and S-(De) nitrosylation: Implications in cancer and neurodegeneration
    • Di Giacomo G, Rizza S, Montagna C, Filomeni G (2012) Established principles and emerging concepts on the interplay between mitochondrial physiology and S-(De) nitrosylation: Implications in cancer and neurodegeneration. Int J Cell Biol 2012: 361872.
    • (2012) Int J Cell Biol , vol.2012 , pp. 361872
    • Di Giacomo, G.1    Rizza, S.2    Montagna, C.3    Filomeni, G.4
  • 32
    • 84978437143 scopus 로고    scopus 로고
    • S-nitrosylation of the mitochondrial chaperone TRAP1 sensitizes hepatocellular carcinoma cells to inhibitors of succinate dehydrogenase
    • Rizza S, et al. (2016) S-nitrosylation of the mitochondrial chaperone TRAP1 sensitizes hepatocellular carcinoma cells to inhibitors of succinate dehydrogenase. Cancer Res 76:4170-4182.
    • (2016) Cancer Res , vol.76 , pp. 4170-4182
    • Rizza, S.1
  • 33
    • 77955351652 scopus 로고    scopus 로고
    • New insights into the role of mitochondria in aging: Mitochondrial dynamics and more
    • Seo AY, et al. (2010) New insights into the role of mitochondria in aging: Mitochondrial dynamics and more. J Cell Sci 123:2533-2542.
    • (2010) J Cell Sci , vol.123 , pp. 2533-2542
    • Seo, A.Y.1
  • 34
    • 33745274726 scopus 로고    scopus 로고
    • Mitochondria: Dynamic organelles in disease, aging, and development
    • Chan DC (2006) Mitochondria: Dynamic organelles in disease, aging, and development. Cell 125:1241-1252.
    • (2006) Cell , vol.125 , pp. 1241-1252
    • Chan, D.C.1
  • 35
    • 84869030015 scopus 로고    scopus 로고
    • Fusion and fission: Interlinked processes critical for mitochondrial health
    • Chan DC (2012) Fusion and fission: Interlinked processes critical for mitochondrial health. Annu Rev Genet 46:265-287.
    • (2012) Annu Rev Genet , vol.46 , pp. 265-287
    • Chan, D.C.1
  • 36
    • 84923685347 scopus 로고    scopus 로고
    • Mitochondria: From cell death executioners to regulators of cell differentiation
    • Kasahara A, Scorrano L (2014) Mitochondria: From cell death executioners to regulators of cell differentiation. Trends Cell Biol 24:761-770.
    • (2014) Trends Cell Biol , vol.24 , pp. 761-770
    • Kasahara, A.1    Scorrano, L.2
  • 37
    • 64249133725 scopus 로고    scopus 로고
    • S-nitrosylation of Drp1 mediates beta-amyloid-related mitochondrial fission and neuronal injury
    • Cho D-HH, et al. (2009) S-nitrosylation of Drp1 mediates beta-amyloid-related mitochondrial fission and neuronal injury. Science 324:102-105.
    • (2009) Science , vol.324 , pp. 102-105
    • Cho, D.-H.H.1
  • 39
    • 85016487669 scopus 로고    scopus 로고
    • The putative Drp1 inhibitor mdivi-1 is a reversible mitochondrial complex I inhibitor that modulates reactive oxygen species
    • e6
    • Bordt EA, et al. (2017) The putative Drp1 inhibitor mdivi-1 is a reversible mitochondrial complex I inhibitor that modulates reactive oxygen species. Dev Cell 40:583-594. e6.
    • (2017) Dev Cell , vol.40 , pp. 583-594
    • Bordt, E.A.1
  • 40
    • 79959886743 scopus 로고    scopus 로고
    • Complex inhibitory effects of nitric oxide on autophagy
    • Sarkar S, et al. (2011) Complex inhibitory effects of nitric oxide on autophagy. Mol Cell 43:19-32.
    • (2011) Mol Cell , vol.43 , pp. 19-32
    • Sarkar, S.1
  • 41
    • 84894273991 scopus 로고    scopus 로고
    • Inducible nitric oxide synthase drives mTOR pathway activation and proliferation of human melanoma by reversible nitrosylation of TSC2
    • Lopez-Rivera E, et al. (2014) Inducible nitric oxide synthase drives mTOR pathway activation and proliferation of human melanoma by reversible nitrosylation of TSC2. Cancer Res 74:1067-1078.
    • (2014) Cancer Res , vol.74 , pp. 1067-1078
    • Lopez-Rivera, E.1
  • 42
    • 77649265091 scopus 로고    scopus 로고
    • The selective autophagy substrate p62 activates the stress responsive transcription factor Nrf2 through inactivation of Keap1
    • Komatsu M, et al. (2010) The selective autophagy substrate p62 activates the stress responsive transcription factor Nrf2 through inactivation of Keap1. Nat Cell Biol 12: 213-223.
    • (2010) Nat Cell Biol , vol.12 , pp. 213-223
    • Komatsu, M.1
  • 44
    • 84939804206 scopus 로고    scopus 로고
    • The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy
    • Lazarou M, et al. (2015) The ubiquitin kinase PINK1 recruits autophagy receptors to induce mitophagy. Nature 524:309-314.
    • (2015) Nature , vol.524 , pp. 309-314
    • Lazarou, M.1
  • 45
    • 2542534741 scopus 로고    scopus 로고
    • S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function
    • Chung KKK, et al. (2004) S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function. Science 304:1328-1331.
    • (2004) Science , vol.304 , pp. 1328-1331
    • Chung, K.K.K.1
  • 46
    • 3242733689 scopus 로고    scopus 로고
    • Nitrosative stress linked to sporadic Parkinson's disease: S-nitrosylation of parkin regulates its E3 ubiquitin ligase activity
    • Yao D, et al. (2004) Nitrosative stress linked to sporadic Parkinson's disease: S-nitrosylation of parkin regulates its E3 ubiquitin ligase activity. Proc Natl Acad Sci USA 101:10810-10814.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 10810-10814
    • Yao, D.1
  • 47
    • 84910624272 scopus 로고    scopus 로고
    • Inflammatory stimuli induce inhibitory S-nitrosylation of the deacetylase SIRT1 to increase acetylation and activation of p53 and p65
    • Shinozaki S, et al. (2014) Inflammatory stimuli induce inhibitory S-nitrosylation of the deacetylase SIRT1 to increase acetylation and activation of p53 and p65. Sci Signal 7: ra106.
    • (2014) Sci Signal , vol.7 , pp. ra106
    • Shinozaki, S.1
  • 48
    • 17944375119 scopus 로고    scopus 로고
    • A genome-wide scan for linkage to human exceptional longevity identifies a locus on chromosome 4
    • Puca AA, et al. (2001) A genome-wide scan for linkage to human exceptional longevity identifies a locus on chromosome 4. Proc Natl Acad Sci USA 98:10505-10508.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 10505-10508
    • Puca, A.A.1
  • 49
    • 84991510905 scopus 로고    scopus 로고
    • Analysis of the machinery and intermediates of the 5hmC-mediated DNA demethylation pathway in aging on samples from the MARK-AGE study
    • Valentini E, et al. (2016) Analysis of the machinery and intermediates of the 5hmC-mediated DNA demethylation pathway in aging on samples from the MARK-AGE study. Aging (Albany NY) 8:1896-1922.
    • (2016) Aging (Albany NY) , vol.8 , pp. 1896-1922
    • Valentini, E.1
  • 50
    • 84964694062 scopus 로고    scopus 로고
    • Age-dependent decrease of DNA hydroxymethylation in human T cells
    • Truong TP, et al. (2015) Age-dependent decrease of DNA hydroxymethylation in human T cells. J Clin Exp Hematop 55:1-6.
    • (2015) J Clin Exp Hematop , vol.55 , pp. 1-6
    • Truong, T.P.1
  • 51
    • 84921989642 scopus 로고    scopus 로고
    • Connections between TET proteins and aberrant DNA modification in cancer
    • Huang Y, Rao A (2014) Connections between TET proteins and aberrant DNA modification in cancer. Trends Genet 30:464-474.
    • (2014) Trends Genet , vol.30 , pp. 464-474
    • Huang, Y.1    Rao, A.2
  • 52
    • 84906217278 scopus 로고    scopus 로고
    • Distinct and overlapping control of 5-methylcytosine and 5-hydroxymethylcytosine by the TET proteins in human cancer cells
    • Putiri EL, et al. (2014) Distinct and overlapping control of 5-methylcytosine and 5-hydroxymethylcytosine by the TET proteins in human cancer cells. Genome Biol 15: R81.
    • (2014) Genome Biol , vol.15 , pp. R81
    • Putiri, E.L.1
  • 53
    • 84871563384 scopus 로고    scopus 로고
    • MeCP2 binds to 5hmC enriched within active genes and accessible chromatin in the nervous system
    • Mellén M, Ayata P, Dewell S, Kriaucionis S, Heintz N (2012) MeCP2 binds to 5hmC enriched within active genes and accessible chromatin in the nervous system. Cell 151: 1417-1430.
    • (2012) Cell , vol.151 , pp. 1417-1430
    • Mellén, M.1    Ayata, P.2    Dewell, S.3    Kriaucionis, S.4    Heintz, N.5
  • 54
    • 84877336241 scopus 로고    scopus 로고
    • Decrease of 5-hydroxymethylcytosine is associated with progression of hepatocellular carcinoma through downregulation of TET1
    • Liu C, et al. (2013) Decrease of 5-hydroxymethylcytosine is associated with progression of hepatocellular carcinoma through downregulation of TET1. PLoS One 8:e62828.
    • (2013) PLoS One , vol.8 , pp. e62828
    • Liu, C.1
  • 55
    • 84964614586 scopus 로고    scopus 로고
    • Fumarate and succinate regulate expression of hypoxia-inducible genes via TET enzymes
    • Laukka T, et al. (2016) Fumarate and succinate regulate expression of hypoxia-inducible genes via TET enzymes. J Biol Chem 291:4256-4265.
    • (2016) J Biol Chem , vol.291 , pp. 4256-4265
    • Laukka, T.1
  • 56
    • 84862632865 scopus 로고    scopus 로고
    • Inhibition of α-KG-dependent histone and DNA demethylases by fumarate and succinate that are accumulated in mutations of FH and SDH tumor suppressors
    • Xiao M, et al. (2012) Inhibition of α-KG-dependent histone and DNA demethylases by fumarate and succinate that are accumulated in mutations of FH and SDH tumor suppressors. Genes Dev 26:1326-1338.
    • (2012) Genes Dev , vol.26 , pp. 1326-1338
    • Xiao, M.1
  • 57
    • 84923197588 scopus 로고    scopus 로고
    • Fumarate induces redox-dependent senescence by modifying glutathione metabolism
    • Zheng L, et al. (2015) Fumarate induces redox-dependent senescence by modifying glutathione metabolism. Nat Commun 6:6001.
    • (2015) Nat Commun , vol.6 , pp. 6001
    • Zheng, L.1
  • 58
    • 67650732998 scopus 로고    scopus 로고
    • Impaired balance of mitochondrial fission and fusion in Alzheimer's disease
    • Wang X, et al. (2009) Impaired balance of mitochondrial fission and fusion in Alzheimer's disease. J Neurosci 29:9090-9103.
    • (2009) J Neurosci , vol.29 , pp. 9090-9103
    • Wang, X.1
  • 59
    • 24744466753 scopus 로고    scopus 로고
    • Of mice and men. When it comes to studying ageing and the means to slow it down, mice are not just small humans
    • Demetrius L (2005) Of mice and men. When it comes to studying ageing and the means to slow it down, mice are not just small humans. EMBO Rep 6(Suppl 1):S39-S44.
    • (2005) EMBO Rep , vol.6 , pp. S39-S44
    • Demetrius, L.1
  • 60
    • 58149314211 scopus 로고    scopus 로고
    • Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
    • Narendra D, Tanaka A, Suen D-F, Youle RJ (2008) Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. J Cell Biol 183:795-803.
    • (2008) J Cell Biol , vol.183 , pp. 795-803
    • Narendra, D.1    Tanaka, A.2    Suen, D.-F.3    Youle, R.J.4
  • 61
    • 84921369563 scopus 로고    scopus 로고
    • The roles of PINK1, parkin, and mitochondrial fidelity in Parkinson's disease
    • Pickrell AM, Youle RJ (2015) The roles of PINK1, parkin, and mitochondrial fidelity in Parkinson's disease. Neuron 85:257-273.
    • (2015) Neuron , vol.85 , pp. 257-273
    • Pickrell, A.M.1    Youle, R.J.2
  • 62
    • 84880338625 scopus 로고    scopus 로고
    • S-nitrosylation regulates mitochondrial quality control via activation of parkin
    • Ozawa K, et al. (2013) S-nitrosylation regulates mitochondrial quality control via activation of parkin. Sci Rep 3:2202.
    • (2013) Sci Rep , vol.3 , pp. 2202
    • Ozawa, K.1
  • 63
    • 85034844982 scopus 로고    scopus 로고
    • S-nitrosylation of PINK1 attenuates PINK1/parkin-dependent mitophagy in hiPSC-based Parkinson's disease models
    • Oh CK, et al. (2017) S-nitrosylation of PINK1 attenuates PINK1/parkin-dependent mitophagy in hiPSC-based Parkinson's disease models. Cell Rep 21:2171-2182.
    • (2017) Cell Rep , vol.21 , pp. 2171-2182
    • Oh, C.K.1
  • 64
    • 0037117548 scopus 로고    scopus 로고
    • Stimulation of retinoic acid production and growth by ubiquitously expressed alcohol dehydrogenase Adh3
    • Molotkov A, et al. (2002) Stimulation of retinoic acid production and growth by ubiquitously expressed alcohol dehydrogenase Adh3. Proc Natl Acad Sci USA 99: 5337-5342.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 5337-5342
    • Molotkov, A.1
  • 65
    • 84896845042 scopus 로고    scopus 로고
    • S-nitrosation and ubiquitin-proteasome system interplay in neuromuscular disorders
    • Rizza S, Montagna C, Di Giacomo G, Cirotti C, Filomeni G (2014) S-nitrosation and ubiquitin-proteasome system interplay in neuromuscular disorders. Int J Cell Biol 2014:428764.
    • (2014) Int J Cell Biol , vol.2014 , pp. 428764
    • Rizza, S.1    Montagna, C.2    Di Giacomo, G.3    Cirotti, C.4    Filomeni, G.5
  • 66
    • 61949338001 scopus 로고    scopus 로고
    • Hypernitrosylated ryanodine receptor calcium release channels are leaky in dystrophic muscle
    • Bellinger AM, et al. (2009) Hypernitrosylated ryanodine receptor calcium release channels are leaky in dystrophic muscle. Nat Med 15:325-330.
    • (2009) Nat Med , vol.15 , pp. 325-330
    • Bellinger, A.M.1
  • 67
    • 77951667450 scopus 로고    scopus 로고
    • Derivation of primary mouse embryonic fibroblast (PMEF) cultures
    • eds Ward A, Tosh D (Humana Press, Totowa, NJ)
    • Garfield AS (2010) Derivation of primary mouse embryonic fibroblast (PMEF) cultures. Mouse Cell Culture: Methods and Protocols, eds Ward A, Tosh D (Humana Press, Totowa, NJ), pp 19-27.
    • (2010) Mouse Cell Culture: Methods and Protocols , pp. 19-27
    • Garfield, A.S.1
  • 68
    • 84862520770 scopus 로고    scopus 로고
    • Fiji: An open-source platform for biological-image analysis
    • Schindelin J, et al. (2012) Fiji: An open-source platform for biological-image analysis. Nat Methods 9:676-682.
    • (2012) Nat Methods , vol.9 , pp. 676-682
    • Schindelin, J.1
  • 69
    • 33748028841 scopus 로고    scopus 로고
    • Nitric oxide-induced mitochondrial fission is regulated by dynamin-related GTPases in neurons
    • Barsoum MJ, et al. (2006) Nitric oxide-induced mitochondrial fission is regulated by dynamin-related GTPases in neurons. EMBO J 25:3900-3911.
    • (2006) EMBO J , vol.25 , pp. 3900-3911
    • Barsoum, M.J.1
  • 70
    • 85006747576 scopus 로고    scopus 로고
    • Methods to assess mitochondrial morphology in mammalian cells mounting autophagic or mitophagic responses
    • Marchi S, Bonora M, Patergnani S, Giorgi C, Pinton P (2017) Methods to assess mitochondrial morphology in mammalian cells mounting autophagic or mitophagic responses. Methods Enzymol 588:171-186.
    • (2017) Methods Enzymol , vol.588 , pp. 171-186
    • Marchi, S.1    Bonora, M.2    Patergnani, S.3    Giorgi, C.4    Pinton, P.5
  • 71
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera-A visualization system for exploratory research and analysis
    • Pettersen EF, et al. (2004) UCSF Chimera-A visualization system for exploratory research and analysis. J Comput Chem 25:1605-1612.
    • (2004) J Comput Chem , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1


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