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Volumn 13, Issue 2, 2016, Pages 164-173

Role of mitochondrial protein quality control in oxidative stress-induced neurodegenerative diseases

Author keywords

Alzheimer disease; Mitochondrial protein quality control (mtPQC); Oxidative stress; Parkinson disease

Indexed keywords

ADENOSINE TRIPHOSPHATE; CHAPERONE; FREE RADICAL; MITOCHONDRIAL PROTEIN; PROTEIN AGGREGATE; PROTEINASE; REACTIVE OXYGEN METABOLITE;

EID: 84959342156     PISSN: 15672050     EISSN: 18755828     Source Type: Journal    
DOI: 10.2174/1567205012666150921103213     Document Type: Article
Times cited : (26)

References (144)
  • 2
    • 0030982143 scopus 로고    scopus 로고
    • Degradation of oxidized proteins in mammalian cells
    • Grune T, Reinheckel T, Davies KJ. Degradation of oxidized proteins in mammalian cells. FASEB J 11(7): 526-34 (1997).
    • (1997) FASEB J , vol.11 , Issue.7 , pp. 526-534
    • Grune, T.1    Reinheckel, T.2    Davies, K.J.3
  • 3
    • 0038239701 scopus 로고    scopus 로고
    • Selective degradation of oxidatively modified protein substrates by the proteasome
    • Grune T, Merker K, Sandig G, Davies KJ. Selective degradation of oxidatively modified protein substrates by the proteasome. Biochem Biophys Res Commun 305(3): 709-18 (2003).
    • (2003) Biochem Biophys Res Commun , vol.305 , Issue.3 , pp. 709-718
    • Grune, T.1    Merker, K.2    Sandig, G.3    Davies, K.J.4
  • 4
    • 84871793725 scopus 로고    scopus 로고
    • Chaperone-protease networks in mitochondrial protein homeostasis
    • Voos W. Chaperone-protease networks in mitochondrial protein homeostasis. Biochim Biophys Acta 1833(2): 388-99 (2013).
    • (2013) Biochim Biophys Acta , vol.1833 , Issue.2 , pp. 388-399
    • Voos, W.1
  • 6
    • 71749108967 scopus 로고    scopus 로고
    • Mitochondrial protein homeostasis: The cooperative roles of chaperones and proteases
    • Voos W. Mitochondrial protein homeostasis: the cooperative roles of chaperones and proteases. Res Microbiol 160(9): 718-25 (2009).
    • (2009) Res Microbiol , vol.160 , Issue.9 , pp. 718-725
    • Voos, W.1
  • 7
    • 0035896360 scopus 로고    scopus 로고
    • Role of the ABC transporter Mdl1 in peptide export from mitochondria
    • Young L, Leonhard K, Tatsuta T, Trowsdale J, Langer T. Role of the ABC transporter Mdl1 in peptide export from mitochondria. Science 291(5511): 2135-8 (2001).
    • (2001) Science , vol.291 , Issue.5511 , pp. 2135-2138
    • Young, L.1    Leonhard, K.2    Tatsuta, T.3    Trowsdale, J.4    Langer, T.5
  • 8
    • 0027946910 scopus 로고
    • Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria
    • Wagner I, Arlt H, van Dyck L, Langer T, Neupert W. Molecular chaperones cooperate with PIM1 protease in the degradation of misfolded proteins in mitochondria. EMBO J 13(21): 5135-45 (1994).
    • (1994) EMBO J , vol.13 , Issue.21 , pp. 5135-5145
    • Wagner, I.1    Arlt, H.2    van Dyck, L.3    Langer, T.4    Neupert, W.5
  • 9
    • 0030936847 scopus 로고    scopus 로고
    • Protein quality control: Triage by chaperones and proteases
    • Gottesman S, Wickner S, Maurizi MR. Protein quality control: triage by chaperones and proteases. Genes Dev 11(7): 815-23 (1997).
    • (1997) Genes Dev , vol.11 , Issue.7 , pp. 815-823
    • Gottesman, S.1    Wickner, S.2    Maurizi, M.R.3
  • 10
    • 13944278132 scopus 로고    scopus 로고
    • Mitochondria, oxidants, and aging
    • Balaban RS, Nemoto S, Finkel T. Mitochondria, oxidants, and aging. Cell 120(4): 483-95 (2005).
    • (2005) Cell , vol.120 , Issue.4 , pp. 483-495
    • Balaban, R.S.1    Nemoto, S.2    Finkel, T.3
  • 11
    • 79955664111 scopus 로고    scopus 로고
    • Mitochondrial protein quality control during biogenesis and aging
    • Baker BM, Haynes CM. Mitochondrial protein quality control during biogenesis and aging. Trends Biochem Sci 36(5): 254-61 (2011).
    • (2011) Trends Biochem Sci , vol.36 , Issue.5 , pp. 254-261
    • Baker, B.M.1    Haynes, C.M.2
  • 12
    • 2442555970 scopus 로고    scopus 로고
    • The protein import machinery of mitochondria
    • Wiedemann N, Frazier AE, Pfanner N. The protein import machinery of mitochondria. J Biol Chem 279(15): 14473-6 (2004).
    • (2004) J Biol Chem , vol.279 , Issue.15 , pp. 14473-14476
    • Wiedemann, N.1    Frazier, A.E.2    Pfanner, N.3
  • 13
    • 84897390686 scopus 로고    scopus 로고
    • Mitochondrial protein quality control in health and disease
    • Baker MJ, Palmer CS, Stojanovski D. Mitochondrial protein quality control in health and disease. Br J Pharmacol 171(8): 1870-89.
    • Br J Pharmacol , vol.171 , Issue.8 , pp. 1870-1889
    • Baker, M.J.1    Palmer, C.S.2    Stojanovski, D.3
  • 14
    • 84875461582 scopus 로고    scopus 로고
    • Diversity in the origins of proteostasis networks--a driver for protein function in evolution
    • Powers ET, Balch WE. Diversity in the origins of proteostasis networks--a driver for protein function in evolution. Nat Rev Mol Cell Biol 14(4): 237-48 (2013).
    • (2013) Nat Rev Mol Cell Biol , vol.14 , Issue.4 , pp. 237-248
    • Powers, E.T.1    Balch, W.E.2
  • 15
    • 0023182502 scopus 로고
    • SSC1, a member of the 70-kDa heat shock protein multigene family of Saccharomyces cerevisiae, is essential for growth
    • Craig EA, Kramer J, Kosic-Smithers J. SSC1, a member of the 70-kDa heat shock protein multigene family of Saccharomyces cerevisiae, is essential for growth. Proc Natl Acad Sci USA 84(12): 4156-60 (1987).
    • (1987) Proc Natl Acad Sci USA , vol.84 , Issue.12 , pp. 4156-4160
    • Craig, E.A.1    Kramer, J.2    Kosic-Smithers, J.3
  • 16
    • 0033782977 scopus 로고    scopus 로고
    • The mitochondrial protein import motor
    • Strub A, Lim JH, Pfanner N, Voos W. The mitochondrial protein import motor. Biol Chem 381(9-10): 943-9 (2000).
    • (2000) Biol Chem , vol.381 , Issue.9-10 , pp. 943-949
    • Strub, A.1    Lim, J.H.2    Pfanner, N.3    Voos, W.4
  • 17
    • 84884589727 scopus 로고    scopus 로고
    • Hsp70 chaperone dynamics and molecular mechanism
    • Mayer MP. Hsp70 chaperone dynamics and molecular mechanism. Trends Biochem Sci 38(10): 507-14 (2013).
    • (2013) Trends Biochem Sci , vol.38 , Issue.10 , pp. 507-514
    • Mayer, M.P.1
  • 18
  • 19
    • 0031556950 scopus 로고    scopus 로고
    • Mge1 functions as a nucleotide release factor for Ssc1, a mitochondrial Hsp70 of Saccharomyces cerevisiae
    • Miao B, Davis JE, Craig EA. Mge1 functions as a nucleotide release factor for Ssc1, a mitochondrial Hsp70 of Saccharomyces cerevisiae. J Mol Biol 265(5): 541-52 (1997).
    • (1997) J Mol Biol , vol.265 , Issue.5 , pp. 541-552
    • Miao, B.1    Davis, J.E.2    Craig, E.A.3
  • 20
    • 14244268253 scopus 로고    scopus 로고
    • Effect of GRP75/mthsp70/PBP74/mortalin overexpression on intracellular ATP level, mitochondrial membrane potential and ROS accumulation following glucose deprivation in PC12 cells
    • Liu Y, Liu W, Song XD, Zuo J. Effect of GRP75/mthsp70/PBP74/mortalin overexpression on intracellular ATP level, mitochondrial membrane potential and ROS accumulation following glucose deprivation in PC12 cells. Mol Cell Biochem 268(1-2): 45-51 (2005).
    • (2005) Mol Cell Biochem , vol.268 , Issue.1-2 , pp. 45-51
    • Liu, Y.1    Liu, W.2    Song, X.D.3    Zuo, J.4
  • 21
    • 59149091608 scopus 로고    scopus 로고
    • Overexpression of mitochondrial Hsp70/Hsp75 in rat brain protects mitochondria, reduces oxidative stress, and protects from focal ischemia
    • Xu L, Voloboueva LA, Ouyang Y, Emery JF, Giffard RG. Overexpression of mitochondrial Hsp70/Hsp75 in rat brain protects mitochondria, reduces oxidative stress, and protects from focal ischemia. J Cereb Blood Flow Metab 29(2): 365-74 (2009).
    • (2009) J Cereb Blood Flow Metab , vol.29 , Issue.2 , pp. 365-374
    • Xu, L.1    Voloboueva, L.A.2    Ouyang, Y.3    Emery, J.F.4    Giffard, R.G.5
  • 22
    • 78651071860 scopus 로고    scopus 로고
    • Mortalin overexpression attenuates beta-amyloid-induced neurotoxicity in SH-SY5Y cells
    • Qu M, Zhou Z, Xu S, Chen C, Yu Z, Wang D. Mortalin overexpression attenuates beta-amyloid-induced neurotoxicity in SH-SY5Y cells. Brain Res 1368: 336-45 (2011).
    • (2011) Brain Res , vol.1368 , pp. 336-345
    • Qu, M.1    Zhou, Z.2    Xu, S.3    Chen, C.4    Yu, Z.5    Wang, D.6
  • 23
    • 84881237468 scopus 로고    scopus 로고
    • Over-expression of GRP75 inhibits liver injury induced by oxidative damage
    • E Q, Liu X, Liu Y, Liu W, Zuo J. Over-expression of GRP75 inhibits liver injury induced by oxidative damage. Acta Biochim Biophys Sin (Shanghai) 45(2): 129-34 (2013).
    • (2013) Acta Biochim Biophys Sin (Shanghai) , vol.45 , Issue.2 , pp. 129-134
    • Liu, X.1    Liu, Y.2    Liu, W.3    Zuo, J.4
  • 24
    • 38149030006 scopus 로고    scopus 로고
    • Mitochondria protection from hypoxia/reoxygenation injury with mitochondria heat shock protein 70 overexpression
    • Williamson CL, Dabkowski ER, Dillmann WH, Hollander JM. Mitochondria protection from hypoxia/reoxygenation injury with mitochondria heat shock protein 70 overexpression. Am J Physiol Heart Circ Physiol 294(1): H249-56 (2008).
    • (2008) Am J Physiol Heart Circ Physiol , vol.294 , Issue.1 , pp. H249-H256
    • Williamson, C.L.1    Dabkowski, E.R.2    Dillmann, W.H.3    Hollander, J.M.4
  • 25
    • 42549112997 scopus 로고    scopus 로고
    • Overexpression of mitochondrial Hsp70/Hsp75 protects astrocytes against ischemic injury in vitro
    • Voloboueva LA, Duan M, Ouyang Y, Emery JF, Stoy C, Giffard RG. Overexpression of mitochondrial Hsp70/Hsp75 protects astrocytes against ischemic injury in vitro. J Cereb Blood Flow Metab 28(5): 1009-16 (2008).
    • (2008) J Cereb Blood Flow Metab , vol.28 , Issue.5 , pp. 1009-1016
    • Voloboueva, L.A.1    Duan, M.2    Ouyang, Y.3    Emery, J.F.4    Stoy, C.5    Giffard, R.G.6
  • 26
    • 84894414901 scopus 로고    scopus 로고
    • Mortalin and DJ-1 coordinately regulate hematopoietic stem cell function through the control of oxidative stress
    • Tai-Nagara I, Matsuoka S, Ariga H, Suda T. Mortalin and DJ-1 coordinately regulate hematopoietic stem cell function through the control of oxidative stress. Blood 123(1): 41-50 (2014).
    • (2014) Blood , vol.123 , Issue.1 , pp. 41-50
    • Tai-Nagara, I.1    Matsuoka, S.2    Ariga, H.3    Suda, T.4
  • 27
    • 84875127081 scopus 로고    scopus 로고
    • Mge1, a nucleotide exchange factor of Hsp70, acts as an oxidative sensor to regulate mitochondrial Hsp70 function
    • Marada A, Allu PK, Murari A, PullaReddy B, Tammineni P, Thiriveedi VR, et al. Mge1, a nucleotide exchange factor of Hsp70, acts as an oxidative sensor to regulate mitochondrial Hsp70 function. Mol Biol Cell 24(6): 692-703 (2013).
    • (2013) Mol Biol Cell , vol.24 , Issue.6 , pp. 692-703
    • Marada, A.1    Allu, P.K.2    Murari, A.3    Pullareddy, B.4    Tammineni, P.5    Thiriveedi, V.R.6
  • 28
    • 0024972083 scopus 로고
    • Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria
    • Cheng MY, Hartl FU, Martin J, Pollock RA, Kalousek F, Neupert W, et al. Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria. Nature 337(6208): 620-5 (1989).
    • (1989) Nature , vol.337 , Issue.6208 , pp. 620-625
    • Cheng, M.Y.1    Hartl, F.U.2    Martin, J.3    Pollock, R.A.4    Kalousek, F.5    Neupert, W.6
  • 29
  • 30
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl FU, Bracher A, Hayer-Hartl M. Molecular chaperones in protein folding and proteostasis. Nature 475(7356): 324-32 (2011).
    • (2011) Nature , vol.475 , Issue.7356 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 31
    • 79952328398 scopus 로고    scopus 로고
    • Mitochondrial enzymes are protected from stress-induced aggregation by mitochondrial chaperones and the Pim1/LON protease
    • Bender T, Lewrenz I, Franken S, Baitzel C, Voos W. Mitochondrial enzymes are protected from stress-induced aggregation by mitochondrial chaperones and the Pim1/LON protease. Mol Biol Cell 22(5): 541-54 (2011).
    • (2011) Mol Biol Cell , vol.22 , Issue.5 , pp. 541-554
    • Bender, T.1    Lewrenz, I.2    Franken, S.3    Baitzel, C.4    Voos, W.5
  • 32
    • 0036809967 scopus 로고    scopus 로고
    • Structure and function of the GroE chaperone
    • Walter S. Structure and function of the GroE chaperone. Cell Mol Life Sci 59(10): 1589-97 (2002).
    • (2002) Cell Mol Life Sci , vol.59 , Issue.10 , pp. 1589-1597
    • Walter, S.1
  • 33
    • 0024972079 scopus 로고
    • Characterization of the yeast HSP60 gene coding for a mitochondrial assembly factor
    • Reading DS, Hallberg RL, Myers AM. Characterization of the yeast HSP60 gene coding for a mitochondrial assembly factor. Nature 337(6208): 655-9 (1989).
    • (1989) Nature , vol.337 , Issue.6208 , pp. 655-659
    • Reading, D.S.1    Hallberg, R.L.2    Myers, A.M.3
  • 34
    • 46149118689 scopus 로고    scopus 로고
    • The Hsp60-(P.V98I) mutation associated with hereditary spastic paraplegia SPG13 compromises chaperonin function both in vitro and in vivo
    • Bross P, Naundrup S, Hansen J, Nielsen MN, Christensen JH, Kruhoffer M, et al. The Hsp60-(p.V98I) mutation associated with hereditary spastic paraplegia SPG13 compromises chaperonin function both in vitro and in vivo. J Biol Chem 283(23): 15694-700 (2008).
    • (2008) J Biol Chem , vol.283 , Issue.23 , pp. 15694-15700
    • Bross, P.1    Naundrup, S.2    Hansen, J.3    Nielsen, M.N.4    Christensen, J.H.5    Kruhoffer, M.6
  • 35
    • 78549293327 scopus 로고    scopus 로고
    • Heat shock protein 60 regulation of the mitochondrial permeability transition pore in tumor cells
    • Ghosh JC, Siegelin MD, Dohi T, Altieri DC. Heat shock protein 60 regulation of the mitochondrial permeability transition pore in tumor cells. Cancer Res 70(22): 8988-93 (2010).
    • (2010) Cancer Res , vol.70 , Issue.22 , pp. 8988-8993
    • Ghosh, J.C.1    Siegelin, M.D.2    Dohi, T.3    Altieri, D.C.4
  • 36
    • 0036138947 scopus 로고    scopus 로고
    • A subset of newly synthesized polypeptides in mitochondria from human endothelial cells exposed to hydroperoxide stress
    • Mitsumoto A, Takeuchi A, Okawa K, Nakagawa Y. A subset of newly synthesized polypeptides in mitochondria from human endothelial cells exposed to hydroperoxide stress. Free Radic Biol Med 32(1): 22-37 (2002).
    • (2002) Free Radic Biol Med , vol.32 , Issue.1 , pp. 22-37
    • Mitsumoto, A.1    Takeuchi, A.2    Okawa, K.3    Nakagawa, Y.4
  • 37
    • 84883609143 scopus 로고    scopus 로고
    • Hsp60 chaperonin acts as barrier to pharmacologically induced oxidative stress mediated apoptosis in tumor cells with differential stress response
    • Sarangi U, Singh MK, Abhijnya KV, Reddy LP, Prasad BS, Pitke VV, et al. Hsp60 chaperonin acts as barrier to pharmacologically induced oxidative stress mediated apoptosis in tumor cells with differential stress response. Drug Target Insights 7: 35-51 (2013).
    • (2013) Drug Target Insights , vol.7 , pp. 35-51
    • Sarangi, U.1    Singh, M.K.2    Abhijnya, K.V.3    Reddy, L.P.4    Prasad, B.S.5    Pitke, V.V.6
  • 38
    • 26244467311 scopus 로고    scopus 로고
    • The Golgi Ca2+-ATPase KlPmr1p function is required for oxidative stress response by controlling the expression of the heatshock element HSP60 in Kluyveromyces lactis
    • Uccelletti D, Farina F, Pinton P, Goffrini P, Mancini P, Talora C, et al. The Golgi Ca2+-ATPase KlPmr1p function is required for oxidative stress response by controlling the expression of the heatshock element HSP60 in Kluyveromyces lactis. Mol Biol Cell 16(10): 4636-47 (2005).
    • (2005) Mol Biol Cell , vol.16 , Issue.10 , pp. 4636-4647
    • Uccelletti, D.1    Farina, F.2    Pinton, P.3    Goffrini, P.4    Mancini, P.5    Talora, C.6
  • 39
    • 0037113995 scopus 로고    scopus 로고
    • Mitochondrial Hsp60, resistance to oxidative stress, and the labile iron pool are closely connected in Saccharomyces cerevisiae
    • Cabiscol E, Belli G, Tamarit J, Echave P, Herrero E, Ros J. Mitochondrial Hsp60, resistance to oxidative stress, and the labile iron pool are closely connected in Saccharomyces cerevisiae. J Biol Chem 277(46): 44531-8 (2002).
    • (2002) J Biol Chem , vol.277 , Issue.46 , pp. 44531-44538
    • Cabiscol, E.1    Belli, G.2    Tamarit, J.3    Echave, P.4    Herrero, E.5    Ros, J.6
  • 40
    • 84912102339 scopus 로고    scopus 로고
    • Natural thermal adaptation increases heat shock protein levels and decreases oxidative stress
    • Oksala NK, Ekmekci FG, Ozsoy E, Kirankaya S, Kokkola T, Emecen G, et al. Natural thermal adaptation increases heat shock protein levels and decreases oxidative stress. Redox Biol 3: 25-8 (2014).
    • (2014) Redox Biol , vol.3 , pp. 25-28
    • Oksala, N.K.1    Ekmekci, F.G.2    Ozsoy, E.3    Kirankaya, S.4    Kokkola, T.5    Emecen, G.6
  • 41
    • 18344390036 scopus 로고    scopus 로고
    • Identification by redox proteomics of glutathionylated proteins in oxidatively stressed human T lymphocytes
    • Fratelli M, Demol H, Puype M, Casagrande S, Eberini I, Salmona M, et al. Identification by redox proteomics of glutathionylated proteins in oxidatively stressed human T lymphocytes. Proc Natl Acad Sci U S A 99(6): 3505-10 (2002).
    • (2002) Proc Natl Acad Sci U S A , vol.99 , Issue.6 , pp. 3505-3510
    • Fratelli, M.1    Demol, H.2    Puype, M.3    Casagrande, S.4    Eberini, I.5    Salmona, M.6
  • 42
    • 0034633963 scopus 로고    scopus 로고
    • Immunoelectron microscopy provides evidence that tumor necrosis factor receptor-associated protein 1 (TRAP-1) is a mitochondrial protein which also localizes at specific extramitochondrial sites
    • Cechetto JD, Gupta RS. Immunoelectron microscopy provides evidence that tumor necrosis factor receptor-associated protein 1 (TRAP-1) is a mitochondrial protein which also localizes at specific extramitochondrial sites. Exp Cell Res 260(1): 30-9 (2000).
    • (2000) Exp Cell Res , vol.260 , Issue.1 , pp. 30-39
    • Cechetto, J.D.1    Gupta, R.S.2
  • 43
    • 0034603178 scopus 로고    scopus 로고
    • The hsp90-related protein TRAP1 is a mitochondrial protein with distinct functional properties
    • Felts SJ, Owen BA, Nguyen P, Trepel J, Donner DB, Toft DO. The hsp90-related protein TRAP1 is a mitochondrial protein with distinct functional properties. J Biol Chem 275(5): 3305-12 (2000).
    • (2000) J Biol Chem , vol.275 , Issue.5 , pp. 3305-3312
    • Felts, S.J.1    Owen, B.A.2    Nguyen, P.3    Trepel, J.4    Donner, D.B.5    Toft, D.O.6
  • 44
    • 33746364784 scopus 로고    scopus 로고
    • Structure and mechanism of the Hsp90 molecular chaperone machinery
    • Pearl LH, Prodromou C. Structure and mechanism of the Hsp90 molecular chaperone machinery. Annu Rev Biochem 75: 271-94 (2006).
    • (2006) Annu Rev Biochem , vol.75 , pp. 271-294
    • Pearl, L.H.1    Prodromou, C.2
  • 45
    • 67349088746 scopus 로고    scopus 로고
    • TRAP1, a novel mitochondrial chaperone responsible for multi-drug resistance and protection from apoptotis in human colorectal carcinoma cells
    • Costantino E, Maddalena F, Calise S, Piscazzi A, Tirino V, Fersini A, et al. TRAP1, a novel mitochondrial chaperone responsible for multi-drug resistance and protection from apoptotis in human colorectal carcinoma cells. Cancer Lett 279(1): 39-46 (2009).
    • (2009) Cancer Lett , vol.279 , Issue.1 , pp. 39-46
    • Costantino, E.1    Maddalena, F.2    Calise, S.3    Piscazzi, A.4    Tirino, V.5    Fersini, A.6
  • 46
    • 35348887850 scopus 로고    scopus 로고
    • Regulation of tumor cell mitochondrial homeostasis by an organelle-specific Hsp90 chaperone network
    • Kang BH, Plescia J, Dohi T, Rosa J, Doxsey SJ, Altieri DC. Regulation of tumor cell mitochondrial homeostasis by an organelle-specific Hsp90 chaperone network. Cell 131(2): 257-70 (2007).
    • (2007) Cell , vol.131 , Issue.2 , pp. 257-270
    • Kang, B.H.1    Plescia, J.2    Dohi, T.3    Rosa, J.4    Doxsey, S.J.5    Altieri, D.C.6
  • 47
    • 84878813471 scopus 로고    scopus 로고
    • The mitochondrial chaperone TRAP1 promotes neoplastic growth by inhibiting succinate dehydrogenase
    • Sciacovelli M, Guzzo G, Morello V, Frezza C, Zheng L, Nannini N, et al. The mitochondrial chaperone TRAP1 promotes neoplastic growth by inhibiting succinate dehydrogenase. Cell Metab 17(6): 988-99 (2013).
    • (2013) Cell Metab , vol.17 , Issue.6 , pp. 988-999
    • Sciacovelli, M.1    Guzzo, G.2    Morello, V.3    Frezza, C.4    Zheng, L.5    Nannini, N.6
  • 48
    • 33846426804 scopus 로고    scopus 로고
    • Iron chelation study in a normal human hepatocyte cell line suggests that tumor necrosis factor receptor-associated protein 1 (TRAP1) regulates production of reactive oxygen species
    • Im CN, Lee JS, Zheng Y, Seo JS. Iron chelation study in a normal human hepatocyte cell line suggests that tumor necrosis factor receptor-associated protein 1 (TRAP1) regulates production of reactive oxygen species. J Cell Biochem 100(2): 474-86 (2007).
    • (2007) J Cell Biochem , vol.100 , Issue.2 , pp. 474-486
    • Im, C.N.1    Lee, J.S.2    Zheng, Y.3    Seo, J.S.4
  • 49
    • 5644259582 scopus 로고    scopus 로고
    • Involvement of tumor necrosis factor receptor-associated protein 1 (TRAP1) in apoptosis induced by beta-hydroxyisovalerylshikonin
    • Masuda Y, Shima G, Aiuchi T, Horie M, Hori K, Nakajo S, et al. Involvement of tumor necrosis factor receptor-associated protein 1 (TRAP1) in apoptosis induced by beta-hydroxyisovalerylshikonin. J Biol Chem 279(41): 42503-15 (2004).
    • (2004) J Biol Chem , vol.279 , Issue.41 , pp. 42503-42515
    • Masuda, Y.1    Shima, G.2    Aiuchi, T.3    Horie, M.4    Hori, K.5    Nakajo, S.6
  • 50
    • 34547138950 scopus 로고    scopus 로고
    • Heat shock protein 75 (TRAP1) antagonizes reactive oxygen species generation and protects cells from granzyme M-mediated apoptosis
    • Hua G, Zhang Q, Fan Z. Heat shock protein 75 (TRAP1) antagonizes reactive oxygen species generation and protects cells from granzyme M-mediated apoptosis. J Biol Chem 282(28): 20553-60 (2007).
    • (2007) J Biol Chem , vol.282 , Issue.28 , pp. 20553-20560
    • Hua, G.1    Zhang, Q.2    Fan, Z.3
  • 51
    • 36248980938 scopus 로고    scopus 로고
    • Tumor necrosis factor-associated protein 1 (TRAP-1) protects cells from oxidative stress and apoptosis
    • Montesano Gesualdi N, Chirico G, Pirozzi G, Costantino E, Landriscina M, Esposito F. Tumor necrosis factor-associated protein 1 (TRAP-1) protects cells from oxidative stress and apoptosis. Stress 10(4): 342-50 (2007).
    • (2007) Stress , vol.10 , Issue.4 , pp. 342-350
    • Montesano Gesualdi, N.1    Chirico, G.2    Pirozzi, G.3    Costantino, E.4    Landriscina, M.5    Esposito, F.6
  • 52
    • 84949154445 scopus 로고    scopus 로고
    • Mitochondrial chaperone TRAP1 activates the mitochondrial UPR and extends healthspan in Drosophila
    • Baqri RM, Pietron AV, Gokhale RH, Turner BA, Kaguni LS, Shingleton AW, et al. Mitochondrial chaperone TRAP1 activates the mitochondrial UPR and extends healthspan in Drosophila. Mech Ageing Dev 141-142C: 35-45 (2014).
    • (2014) Mech Ageing Dev , vol.141 142C , pp. 35-45
    • Baqri, R.M.1    Pietron, A.V.2    Gokhale, R.H.3    Turner, B.A.4    Kaguni, L.S.5    Shingleton, A.W.6
  • 53
    • 0028362456 scopus 로고
    • Requirement for the yeast gene LON in intramitochondrial proteolysis and maintenance of respiration
    • Suzuki CK, Suda K, Wang N, Schatz G. Requirement for the yeast gene LON in intramitochondrial proteolysis and maintenance of respiration. Science 264(5161): 891 (1994).
    • (1994) Science , vol.264 , Issue.5161 , pp. 891
    • Suzuki, C.K.1    Suda, K.2    Wang, N.3    Schatz, G.4
  • 54
    • 84872271398 scopus 로고    scopus 로고
    • Phosphorylation of human TFAM in mitochondria impairs DNA binding and promotes degradation by the AAA+ Lon protease
    • Lu B, Lee J, Nie X, Li M, Morozov YI, Venkatesh S, et al. Phosphorylation of human TFAM in mitochondria impairs DNA binding and promotes degradation by the AAA+ Lon protease. Mol Cell 49(1): 121-32 (2013).
    • (2013) Mol Cell , vol.49 , Issue.1 , pp. 121-132
    • Lu, B.1    Lee, J.2    Nie, X.3    Li, M.4    Morozov, Y.I.5    Venkatesh, S.6
  • 55
    • 84855225838 scopus 로고    scopus 로고
    • Multitasking in the mitochondrion by the ATP-dependent Lon protease
    • Venkatesh S, Lee J, Singh K, Lee I, Suzuki CK. Multitasking in the mitochondrion by the ATP-dependent Lon protease. Biochim Biophys Acta 1823(1): 56-66 (2012).
    • (2012) Biochim Biophys Acta , vol.1823 , Issue.1 , pp. 56-66
    • Venkatesh, S.1    Lee, J.2    Singh, K.3    Lee, I.4    Suzuki, C.K.5
  • 56
    • 77958477536 scopus 로고    scopus 로고
    • Crystal structure of Lon protease: Molecular architecture of gated entry to a sequestered degradation chamber
    • Cha SS, An YJ, Lee CR, Lee HS, Kim YG, Kim SJ, et al. Crystal structure of Lon protease: molecular architecture of gated entry to a sequestered degradation chamber. EMBO J 29(20): 3520-30 (2010).
    • (2010) EMBO J , vol.29 , Issue.20 , pp. 3520-3530
    • Cha, S.S.1    An, Y.J.2    Lee, C.R.3    Lee, H.S.4    Kim, Y.G.5    Kim, S.J.6
  • 57
    • 15744384860 scopus 로고    scopus 로고
    • Downregulation of the human Lon protease impairs mitochondrial structure and function and causes cell death
    • Bota DA, Ngo JK, Davies KJ. Downregulation of the human Lon protease impairs mitochondrial structure and function and causes cell death. Free Radic Biol Med 38(5): 665-77 (2005).
    • (2005) Free Radic Biol Med , vol.38 , Issue.5 , pp. 665-677
    • Bota, D.A.1    Ngo, J.K.2    Davies, K.J.3
  • 58
    • 0036713692 scopus 로고    scopus 로고
    • Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism
    • Bota DA, Davies KJ. Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism. Nat Cell Biol 4(9): 674-80 (2002).
    • (2002) Nat Cell Biol , vol.4 , Issue.9 , pp. 674-680
    • Bota, D.A.1    Davies, K.J.2
  • 59
    • 0028260177 scopus 로고
    • Purification and characterization of a substrate protein for mitochondrial ATP-dependent protease in bovine adrenal cortex
    • Watabe S, Kohno H, Kouyama H, Hiroi T, Yago N, Nakazawa T. Purification and characterization of a substrate protein for mitochondrial ATP-dependent protease in bovine adrenal cortex. J Biochem 115(4): 648-54 (1994).
    • (1994) J Biochem , vol.115 , Issue.4 , pp. 648-654
    • Watabe, S.1    Kohno, H.2    Kouyama, H.3    Hiroi, T.4    Yago, N.5    Nakazawa, T.6
  • 60
    • 0027367968 scopus 로고
    • A human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease
    • Wang N, Gottesman S, Willingham MC, Gottesman MM, Maurizi MR. A human mitochondrial ATP-dependent protease that is highly homologous to bacterial Lon protease. Proc Natl Acad Sci U S A 90(23): 11247-51 (1993).
    • (1993) Proc Natl Acad Sci U S A , vol.90 , Issue.23 , pp. 11247-11251
    • Wang, N.1    Gottesman, S.2    Willingham, M.C.3    Gottesman, M.M.4    Maurizi, M.R.5
  • 61
    • 0028219787 scopus 로고
    • Cloning and sequence analysis of cDNA for a human homolog of eubacterial ATP-dependent Lon proteases
    • Amerik A, Petukhova GV, Grigorenko VG, Lykov IP, Yarovoi SV, Lipkin VM, et al. Cloning and sequence analysis of cDNA for a human homolog of eubacterial ATP-dependent Lon proteases. FEBS Lett 340(1-2): 25-8 (1994).
    • (1994) FEBS Lett , vol.340 , Issue.1-2 , pp. 25-28
    • Amerik, A.1    Petukhova, G.V.2    Grigorenko, V.G.3    Lykov, I.P.4    Yarovoi, S.V.5    Lipkin, V.M.6
  • 62
    • 0033036242 scopus 로고    scopus 로고
    • Enhanced mitochondrial biogenesis is associated with increased expression of the mitochondrial ATP-dependent Lon protease
    • Luciakova K, Sokolikova B, Chloupkova M, Nelson BD. Enhanced mitochondrial biogenesis is associated with increased expression of the mitochondrial ATP-dependent Lon protease. FEBS Lett 444(2-3): 186-8 (1999).
    • (1999) FEBS Lett , vol.444 , Issue.2-3 , pp. 186-188
    • Luciakova, K.1    Sokolikova, B.2    Chloupkova, M.3    Nelson, B.D.4
  • 63
    • 18444390287 scopus 로고    scopus 로고
    • Transmission of cell stress from endoplasmic reticulum to mitochondria: Enhanced expression of Lon protease
    • Hori O, Ichinoda F, Tamatani T, Yamaguchi A, Sato N, Ozawa K, et al. Transmission of cell stress from endoplasmic reticulum to mitochondria: enhanced expression of Lon protease. J Cell Biol 157(7): 1151-60 (2002).
    • (2002) J Cell Biol , vol.157 , Issue.7 , pp. 1151-1160
    • Hori, O.1    Ichinoda, F.2    Tamatani, T.3    Yamaguchi, A.4    Sato, N.5    Ozawa, K.6
  • 64
    • 77950676470 scopus 로고    scopus 로고
    • The role of protein quality control in mitochondrial protein homeostasis under oxidative stress
    • Bender T, Leidhold C, Ruppert T, Franken S, Voos W. The role of protein quality control in mitochondrial protein homeostasis under oxidative stress. Proteomics 10(7): 1426-43 (2010).
    • (2010) Proteomics , vol.10 , Issue.7 , pp. 1426-1443
    • Bender, T.1    Leidhold, C.2    Ruppert, T.3    Franken, S.4    Voos, W.5
  • 65
    • 0037021453 scopus 로고    scopus 로고
    • Modulation of Lon protease activity and aconitase turnover during aging and oxidative stress
    • Bota DA, Van Remmen H, Davies KJ. Modulation of Lon protease activity and aconitase turnover during aging and oxidative stress. FEBS Lett 532(1-2): 103-6 (2002).
    • (2002) FEBS Lett , vol.532 , Issue.1-2 , pp. 103-106
    • Bota, D.A.1    Van Remmen, H.2    Davies, K.J.3
  • 66
    • 63049095076 scopus 로고    scopus 로고
    • Mitochondrial Lon protease is a human stress protein
    • Ngo JK, Davies KJ. Mitochondrial Lon protease is a human stress protein. Free Radic Biol Med 46(8): 1042-8 (2009).
    • (2009) Free Radic Biol Med , vol.46 , Issue.8 , pp. 1042-1048
    • Ngo, J.K.1    Davies, K.J.2
  • 67
    • 67650091290 scopus 로고    scopus 로고
    • Increasing organismal healthspan by enhancing mitochondrial protein quality control
    • Luce K, Osiewacz HD. Increasing organismal healthspan by enhancing mitochondrial protein quality control. Nat Cell Biol 11(7): 852-8 (2009).
    • (2009) Nat Cell Biol , vol.11 , Issue.7 , pp. 852-858
    • Luce, K.1    Osiewacz, H.D.2
  • 69
    • 48349134855 scopus 로고    scopus 로고
    • Inactivation of brain mitochondrial Lon protease by peroxynitrite precedes electron transport chain dysfunction
    • Stanyer L, Jorgensen W, Hori O, Clark JB, Heales SJ. Inactivation of brain mitochondrial Lon protease by peroxynitrite precedes electron transport chain dysfunction. Neurochem Int 53(3-4): 95-101 (2008).
    • (2008) Neurochem Int , vol.53 , Issue.3-4 , pp. 95-101
    • Stanyer, L.1    Jorgensen, W.2    Hori, O.3    Clark, J.B.4    Heales, S.J.5
  • 71
    • 34447511284 scopus 로고    scopus 로고
    • ClpP: A distinctive family of cylindrical energy-dependent serine proteases
    • Yu AY, Houry WA. ClpP: a distinctive family of cylindrical energy-dependent serine proteases. FEBS Lett 581(19): 3749-57 (2007).
    • (2007) FEBS Lett , vol.581 , Issue.19 , pp. 3749-3757
    • Yu, A.Y.1    Houry, W.A.2
  • 72
    • 55249118150 scopus 로고    scopus 로고
    • ClpP hydrolyzes a protein substrate processively in the absence of the ClpA ATPase: Mechanistic studies of ATP-independent proteolysis
    • Jennings LD, Lun DS, Medard M, Licht S. ClpP hydrolyzes a protein substrate processively in the absence of the ClpA ATPase: mechanistic studies of ATP-independent proteolysis. Biochemistry 47(44): 11536-46 (2008).
    • (2008) Biochemistry , vol.47 , Issue.44 , pp. 11536-11546
    • Jennings, L.D.1    Lun, D.S.2    Medard, M.3    Licht, S.4
  • 74
    • 84855195754 scopus 로고    scopus 로고
    • ClpXP, an ATP-powered unfolding and protein-degradation machine
    • Baker TA, Sauer RT. ClpXP, an ATP-powered unfolding and protein-degradation machine. Biochim Biophys Acta 1823(1): 15-28 (2012).
    • (2012) Biochim Biophys Acta , vol.1823 , Issue.1 , pp. 15-28
    • Baker, T.A.1    Sauer, R.T.2
  • 75
    • 0031737552 scopus 로고    scopus 로고
    • Mcx1p, a ClpX homologue in mitochondria of Saccharomyces cerevisiae
    • van Dyck L, Dembowski M, Neupert W, Langer T. Mcx1p, a ClpX homologue in mitochondria of Saccharomyces cerevisiae. FEBS Lett 438(3): 250-4 (1998).
    • (1998) FEBS Lett , vol.438 , Issue.3 , pp. 250-254
    • van Dyck, L.1    Dembowski, M.2    Neupert, W.3    Langer, T.4
  • 76
    • 0029620843 scopus 로고
    • Human ClpP protease: CDNA sequence, tissue-specific expression and chromosomal assignment of the gene
    • Bross P, Andresen BS, Knudsen I, Kruse TA, Gregersen N. Human ClpP protease: cDNA sequence, tissue-specific expression and chromosomal assignment of the gene. FEBS Lett 377(2): 249-52 (1995).
    • (1995) FEBS Lett , vol.377 , Issue.2 , pp. 249-252
    • Bross, P.1    Resen, B.S.2    Knudsen, I.3    Kruse, T.A.4    Gregersen, N.5
  • 77
    • 27444440627 scopus 로고    scopus 로고
    • Human mitochondrial ClpP is a stable heptamer that assembles into a tetradecamer in the presence of ClpX
    • Kang SG, Dimitrova MN, Ortega J, Ginsburg A, Maurizi MR. Human mitochondrial ClpP is a stable heptamer that assembles into a tetradecamer in the presence of ClpX. J Biol Chem 280(42): 35424-32 (2005).
    • (2005) J Biol Chem , vol.280 , Issue.42 , pp. 35424-35432
    • Kang, S.G.1    Dimitrova, M.N.2    Ortega, J.3    Ginsburg, A.4    Maurizi, M.R.5
  • 78
    • 84888196854 scopus 로고    scopus 로고
    • Loss of mitochondrial peptidase Clpp leads to infertility, hearing loss plus growth retardation via accumulation of CLPX, mtDNA and inflammatory factors
    • Gispert S, Parganlija D, Klinkenberg M, Drose S, Wittig I, Mittelbronn M, et al. Loss of mitochondrial peptidase Clpp leads to infertility, hearing loss plus growth retardation via accumulation of CLPX, mtDNA and inflammatory factors. Hum Mol Genet 22(24): 4871-87 (2013).
    • (2013) Hum Mol Genet , vol.22 , Issue.24 , pp. 4871-4887
    • Gispert, S.1    Parganlija, D.2    Klinkenberg, M.3    Drose, S.4    Wittig, I.5    Mittelbronn, M.6
  • 79
    • 84865305875 scopus 로고    scopus 로고
    • Maintenance of mitochondrial genome distribution by mitochondrial AAA+ protein ClpX
    • Kasashima K, Sumitani M, Endo H. Maintenance of mitochondrial genome distribution by mitochondrial AAA+ protein ClpX. Exp Cell Res 318(18): 2335-43 (2012).
    • (2012) Exp Cell Res , vol.318 , Issue.18 , pp. 2335-2343
    • Kasashima, K.1    Sumitani, M.2    Endo, H.3
  • 80
    • 20444480246 scopus 로고    scopus 로고
    • Defense against protein carbonylation by DnaK/DnaJ and proteases of the heat shock regulon
    • Fredriksson A, Ballesteros M, Dukan S, Nystrom T. Defense against protein carbonylation by DnaK/DnaJ and proteases of the heat shock regulon. J Bacteriol 187(12): 4207-13 (2005).
    • (2005) J Bacteriol , vol.187 , Issue.12 , pp. 4207-4213
    • Fredriksson, A.1    Ballesteros, M.2    Dukan, S.3    Nystrom, T.4
  • 81
    • 84871729535 scopus 로고    scopus 로고
    • Protein quality control in organelles-AAA/FtsH story
    • Janska H, Kwasniak M, Szczepanowska J. Protein quality control in organelles-AAA/FtsH story. Biochim Biophys Acta 1833(2): 381-7 (2013).
    • (2013) Biochim Biophys Acta , vol.1833 , Issue.2 , pp. 381-387
    • Janska, H.1    Kwasniak, M.2    Szczepanowska, J.3
  • 82
    • 84855240784 scopus 로고    scopus 로고
    • Proteases--towards a molecular understanding of membrane-bound proteolytic machines
    • Gerdes F, Tatsuta T, Langer T. Mitochondrial AAA proteases--towards a molecular understanding of membrane-bound proteolytic machines. Biochim Biophys Acta 1823(1): 49-55 (2012).
    • (2012) Biochim Biophys Acta , vol.1823 , Issue.1 , pp. 49-55
    • Gerdes, F.1    Tatsuta, T.2    Langer, T.3    Mitochondrial, A.4
  • 83
    • 0035878402 scopus 로고    scopus 로고
    • Molecular and functional analyses of the human and mouse genes encoding AFG3L1, a mitochondrial metalloprotease homologous to the human spastic paraplegia protein
    • Kremmidiotis G, Gardner AE, Settasatian C, Savoia A, Sutherland GR, Callen DF. Molecular and functional analyses of the human and mouse genes encoding AFG3L1, a mitochondrial metalloprotease homologous to the human spastic paraplegia protein. Genomics 76(1-3): 58-65 (2001).
    • (2001) Genomics , vol.76 , Issue.1-3 , pp. 58-65
    • Kremmidiotis, G.1    Gardner, A.E.2    Settasatian, C.3    Savoia, A.4    Sutherland, G.R.5    Callen, D.F.6
  • 84
    • 0032954927 scopus 로고    scopus 로고
    • Prohibitins regulate membrane protein degradation by the m-AAA protease in mitochondria
    • Steglich G, Neupert W, Langer T. Prohibitins regulate membrane protein degradation by the m-AAA protease in mitochondria. Mol Cell Biol 19(5): 3435-42 (1999).
    • (1999) Mol Cell Biol , vol.19 , Issue.5 , pp. 3435-3442
    • Steglich, G.1    Neupert, W.2    Langer, T.3
  • 85
    • 0032541406 scopus 로고    scopus 로고
    • The formation of respiratory chain complexes in mitochondria is under the proteolytic control of the m-AAA protease
    • Arlt H, Steglich G, Perryman R, Guiard B, Neupert W, Langer T. The formation of respiratory chain complexes in mitochondria is under the proteolytic control of the m-AAA protease. EMBO J 17(16): 4837-47 (1998).
    • (1998) EMBO J , vol.17 , Issue.16 , pp. 4837-4847
    • Arlt, H.1    Steglich, G.2    Perryman, R.3    Guiard, B.4    Neupert, W.5    Langer, T.6
  • 86
    • 0030008581 scopus 로고    scopus 로고
    • The YTA10-12 complex, an AAA protease with chaperone-like activity in the inner membrane of mitochondria
    • Arlt H, Tauer R, Feldmann H, Neupert W, Langer T. The YTA10-12 complex, an AAA protease with chaperone-like activity in the inner membrane of mitochondria. Cell 85(6): 875-85 (1996).
    • (1996) Cell , vol.85 , Issue.6 , pp. 875-885
    • Arlt, H.1    Tauer, R.2    Feldmann, H.3    Neupert, W.4    Langer, T.5
  • 87
    • 33750986200 scopus 로고    scopus 로고
    • A new function in translocation for the mitochondrial i-AAA protease Yme1: Import of polynucleotide phosphorylase into the intermembrane space
    • Rainey RN, Glavin JD, Chen HW, French SW, Teitell MA, Koehler CM. A new function in translocation for the mitochondrial i-AAA protease Yme1: import of polynucleotide phosphorylase into the intermembrane space. Mol Cell Biol 26(22): 8488-97 (2006).
    • (2006) Mol Cell Biol , vol.26 , Issue.22 , pp. 8488-8497
    • Rainey, R.N.1    Glavin, J.D.2    Chen, H.W.3    French, S.W.4    Teitell, M.A.5    Koehler, C.M.6
  • 89
    • 1342310772 scopus 로고    scopus 로고
    • Axonal degeneration in paraplegin-deficient mice is associated with abnormal mitochondria and impairment of axonal transport
    • Ferreirinha F, Quattrini A, Pirozzi M, Valsecchi V, Dina G, Broccoli V, et al. Axonal degeneration in paraplegin-deficient mice is associated with abnormal mitochondria and impairment of axonal transport. J Clin Invest 113(2): 231-42 (2004).
    • (2004) J Clin Invest , vol.113 , Issue.2 , pp. 231-242
    • Ferreirinha, F.1    Quattrini, A.2    Pirozzi, M.3    Valsecchi, V.4    Dina, G.5    Broccoli, V.6
  • 90
    • 67651154308 scopus 로고    scopus 로고
    • Haploinsufficiency of AFG3L2, the gene responsible for spinocerebellar ataxia type 28, causes mitochondria-mediated Purkinje cell dark degeneration
    • Maltecca F, Magnoni R, Cerri F, Cox GA, Quattrini A, Casari G. Haploinsufficiency of AFG3L2, the gene responsible for spinocerebellar ataxia type 28, causes mitochondria-mediated Purkinje cell dark degeneration. J Neurosci 29(29): 9244-54 (2009).
    • (2009) J Neurosci , vol.29 , Issue.29 , pp. 9244-9254
    • Maltecca, F.1    Magnoni, R.2    Cerri, F.3    Cox, G.A.4    Quattrini, A.5    Casari, G.6
  • 91
    • 84858411560 scopus 로고    scopus 로고
    • YME1L controls the accumulation of respiratory chain subunits and is required for apoptotic resistance, cristae morphogenesis, and cell proliferation
    • Stiburek L, Cesnekova J, Kostkova O, Fornuskova D, Vinsova K, Wenchich L, et al. YME1L controls the accumulation of respiratory chain subunits and is required for apoptotic resistance, cristae morphogenesis, and cell proliferation. Mol Biol Cell 23(6): 1010-23 (2012).
    • (2012) Mol Biol Cell , vol.23 , Issue.6 , pp. 1010-1023
    • Stiburek, L.1    Cesnekova, J.2    Kostkova, O.3    Fornuskova, D.4    Vinsova, K.5    Wenchich, L.6
  • 92
    • 84924853843 scopus 로고    scopus 로고
    • YME1L degradation reduces mitochondrial proteolytic capacity during oxidative stress
    • Rainbolt TK, Saunders JM, Wiseman RL. YME1L degradation reduces mitochondrial proteolytic capacity during oxidative stress. EMBO Rep 16(1): 97-106 (2014).
    • (2014) EMBO Rep , vol.16 , Issue.1 , pp. 97-106
    • Rainbolt, T.K.1    Saunders, J.M.2    Wiseman, R.L.3
  • 93
    • 0344736798 scopus 로고    scopus 로고
    • Loss of m-AAA protease in mitochondria causes complex I deficiency and increased sensitivity to oxidative stress in hereditary spastic paraplegia
    • Atorino L, Silvestri L, Koppen M, Cassina L, Ballabio A, Marconi R, et al. Loss of m-AAA protease in mitochondria causes complex I deficiency and increased sensitivity to oxidative stress in hereditary spastic paraplegia. J Cell Biol 163(4): 777-87 (2003).
    • (2003) J Cell Biol , vol.163 , Issue.4 , pp. 777-787
    • Atorino, L.1    Silvestri, L.2    Koppen, M.3    Cassina, L.4    Ballabio, A.5    Marconi, R.6
  • 94
    • 39449115415 scopus 로고    scopus 로고
    • The mitochondrial serine protease HtrA2/Omi: An overview
    • Vande Walle L, Lamkanfi M, Vandenabeele P. The mitochondrial serine protease HtrA2/Omi: an overview. Cell Death Differ 15(3): 453-60 (2008).
    • (2008) Cell Death Differ , vol.15 , Issue.3 , pp. 453-460
    • Vande Walle, L.1    Lamkanfi, M.2    Vandenabeele, P.3
  • 95
    • 25444491980 scopus 로고    scopus 로고
    • Structure and function of HtrA family proteins, the key players in protein quality control
    • Kim DY, Kim KK. Structure and function of HtrA family proteins, the key players in protein quality control. J Biochem Mol Biol 38(3): 266-74 (2005).
    • (2005) J Biochem Mol Biol , vol.38 , Issue.3 , pp. 266-274
    • Kim, D.Y.1    Kim, K.K.2
  • 96
    • 60849097548 scopus 로고    scopus 로고
    • Mitochondrial dysfunction triggered by loss of HtrA2 results in the activation of a brain-specific transcriptional stress response
    • Moisoi N, Klupsch K, Fedele V, East P, Sharma S, Renton A, et al. Mitochondrial dysfunction triggered by loss of HtrA2 results in the activation of a brain-specific transcriptional stress response. Cell Death Differ 16(3): 449-64 (2009).
    • (2009) Cell Death Differ , vol.16 , Issue.3 , pp. 449-464
    • Moisoi, N.1    Klupsch, K.2    Fedele, V.3    East, P.4    Sharma, S.5    Renton, A.6
  • 97
    • 7644230386 scopus 로고    scopus 로고
    • Neuroprotective role of the Reaper-related serine protease HtrA2/Omi revealed by targeted deletion in mice
    • Martins LM, Morrison A, Klupsch K, Fedele V, Moisoi N, Teismann P, et al. Neuroprotective role of the Reaper-related serine protease HtrA2/Omi revealed by targeted deletion in mice. Mol Cell Biol 24(22): 9848-62 (2004).
    • (2004) Mol Cell Biol , vol.24 , Issue.22 , pp. 9848-9862
    • Martins, L.M.1    Morrison, A.2    Klupsch, K.3    Fedele, V.4    Moisoi, N.5    Teismann, P.6
  • 98
    • 84905696703 scopus 로고    scopus 로고
    • Inactivation of Omi/HtrA2 protease leads to the deregulation of mitochondrial Mulan E3 ubiquitin ligase and increased mitophagy
    • Cilenti L, Ambivero CT, Ward N, Alnemri ES, Germain D, Zervos AS. Inactivation of Omi/HtrA2 protease leads to the deregulation of mitochondrial Mulan E3 ubiquitin ligase and increased mitophagy. Biochim Biophys Acta 1843(7): 1295-307 (2014).
    • (2014) Biochim Biophys Acta , vol.1843 , Issue.7 , pp. 1295-1307
    • Cilenti, L.1    Ambivero, C.T.2    Ward, N.3    Alnemri, E.S.4    Germain, D.5    Zervos, A.S.6
  • 99
    • 84908237888 scopus 로고    scopus 로고
    • HtrA2/Omi influences the stability of LON protease 1 and prohibitin, proteins involved in mitochondrial homeostasis
    • Goo HG, Rhim H, Kang S. HtrA2/Omi influences the stability of LON protease 1 and prohibitin, proteins involved in mitochondrial homeostasis. Exp Cell Res 328(2): 456-65 (2014).
    • (2014) Exp Cell Res , vol.328 , Issue.2 , pp. 456-465
    • Goo, H.G.1    Rhim, H.2    Kang, S.3
  • 100
    • 52949142730 scopus 로고    scopus 로고
    • Mpv17l protects against mitochondrial oxidative stress and apoptosis by activation of Omi/HtrA2 protease
    • Krick S, Shi S, Ju W, Faul C, Tsai SY, Mundel P, et al. Mpv17l protects against mitochondrial oxidative stress and apoptosis by activation of Omi/HtrA2 protease. Proc Natl Acad Sci U S A 105(37): 14106-11 (2008).
    • (2008) Proc Natl Acad Sci U S A , vol.105 , Issue.37 , pp. 14106-14111
    • Krick, S.1    Shi, S.2    Ju, W.3    Faul, C.4    Tsai, S.Y.5    Mundel, P.6
  • 101
    • 70349581640 scopus 로고    scopus 로고
    • Enhanced HtrA2/Omi expression in oxidative injury to retinal pigment epithelial cells and murine models of neurodegeneration
    • Ding X, Patel M, Shen D, Herzlich AA, Cao X, Villasmil R, et al. Enhanced HtrA2/Omi expression in oxidative injury to retinal pigment epithelial cells and murine models of neurodegeneration. Invest Ophthalmol Vis Sci 50(10): 4957-66 (2009).
    • (2009) Invest Ophthalmol Vis Sci , vol.50 , Issue.10 , pp. 4957-4966
    • Ding, X.1    Patel, M.2    Shen, D.3    Herzlich, A.A.4    Cao, X.5    Villasmil, R.6
  • 102
    • 42749087763 scopus 로고    scopus 로고
    • The mitochondrial impairment, oxidative stress and neurodegeneration connection: Reality or just an attractive hypothesis?
    • Fukui H, Moraes CT. The mitochondrial impairment, oxidative stress and neurodegeneration connection: reality or just an attractive hypothesis? Trends Neurosci 31(5): 251-6 (2008).
    • (2008) Trends Neurosci , vol.31 , Issue.5 , pp. 251-256
    • Fukui, H.1    Moraes, C.T.2
  • 103
    • 0028856460 scopus 로고
    • An English translation of Alzheimer’s 1907 paper, “Uber eine eigenartige Erkankung der Hirnrinde
    • Alzheimer A, Stelzmann RA, Schnitzlein HN, Murtagh FR. An English translation of Alzheimer’s 1907 paper, “Uber eine eigenartige Erkankung der Hirnrinde”. Clin Anat 8(6): 429-31 (1995).
    • (1995) Clin Anat , vol.8 , Issue.6 , pp. 429-431
    • Alzheimer, A.1    Stelzmann, R.A.2    Schnitzlein, H.N.3    Murtagh, F.R.4
  • 104
    • 84907149261 scopus 로고    scopus 로고
    • Intracellular accumulation of amyloid-beta (Abeta) protein plays a major role in Abeta-induced alterations of glutamatergic synaptic transmission and plasticity
    • Ripoli C, Cocco S, Li Puma DD, Piacentini R, Mastrodonato A, Scala F, et al. Intracellular accumulation of amyloid-beta (Abeta) protein plays a major role in Abeta-induced alterations of glutamatergic synaptic transmission and plasticity. J Neurosci 34(38): 12893-903.
    • J Neurosci , vol.34 , Issue.38
    • Ripoli, C.1    Cocco, S.2    Li Puma, D.D.3    Piacentini, R.4    Mastrodonato, A.5    Scala, F.6
  • 105
    • 0032568534 scopus 로고    scopus 로고
    • Alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson’s disease and dementia with lewy bodies
    • Spillantini MG, Crowther RA, Jakes R, Hasegawa M, Goedert M. alpha-Synuclein in filamentous inclusions of Lewy bodies from Parkinson’s disease and dementia with lewy bodies. Proc Natl Acad Sci U S A 95(11): 6469-73 (1998).
    • (1998) Proc Natl Acad Sci U S A , vol.95 , Issue.11 , pp. 6469-6473
    • Spillantini, M.G.1    Crowther, R.A.2    Jakes, R.3    Hasegawa, M.4    Goedert, M.5
  • 106
    • 33749543406 scopus 로고    scopus 로고
    • Differential effects of mitochondrial heat shock protein 60 and related molecular chaperones to prevent intracellular betaamyloid-induced inhibition of complex IV and limit apoptosis
    • Veereshwarayya V, Kumar P, Rosen KM, Mestril R, Querfurth HW. Differential effects of mitochondrial heat shock protein 60 and related molecular chaperones to prevent intracellular betaamyloid-induced inhibition of complex IV and limit apoptosis. J Biol Chem 281(40): 29468-78 (2006).
    • (2006) J Biol Chem , vol.281 , Issue.40 , pp. 29468-29478
    • Veereshwarayya, V.1    Kumar, P.2    Rosen, K.M.3    Mestril, R.4    Querfurth, H.W.5
  • 107
    • 84878752125 scopus 로고    scopus 로고
    • Increased heat shock transcription factor 1 in the cerebellum reverses the deficiency of Purkinje cells in Alzheimer’s disease
    • Jiang YQ, Wang XL, Cao XH, Ye ZY, Li L, Cai WQ. Increased heat shock transcription factor 1 in the cerebellum reverses the deficiency of Purkinje cells in Alzheimer’s disease. Brain Res 1519: 105-11 (2013).
    • (2013) Brain Res , vol.1519 , pp. 105-111
    • Jiang, Y.Q.1    Wang, X.L.2    Cao, X.H.3    Ye, Z.Y.4    Li, L.5    Cai, W.Q.6
  • 108
    • 84873055610 scopus 로고    scopus 로고
    • Proteomic analysis of the hippocampus in Alzheimer’s disease model mice by using two-dimensional fluorescence difference in gel electrophoresis
    • Takano M, Yamashita T, Nagano K, Otani M, Maekura K, Kamada H, et al. Proteomic analysis of the hippocampus in Alzheimer’s disease model mice by using two-dimensional fluorescence difference in gel electrophoresis. Neurosci Lett 534: 85-9 (2013).
    • (2013) Neurosci Lett , vol.534 , pp. 85-89
    • Takano, M.1    Yamashita, T.2    Nagano, K.3    Otani, M.4    Maekura, K.5    Kamada, H.6
  • 109
    • 77952107755 scopus 로고    scopus 로고
    • Protein levels of heat shock proteins 27, 32, 60, 70, 90 and thioredoxin-1 in amnestic mild cognitive impairment: An investigation on the role of cellular stress response in the progression of Alzheimer disease
    • Di Domenico F, Sultana R, Tiu GF, Scheff NN, Perluigi M, Cini C, et al. Protein levels of heat shock proteins 27, 32, 60, 70, 90 and thioredoxin-1 in amnestic mild cognitive impairment: an investigation on the role of cellular stress response in the progression of Alzheimer disease. Brain Res 1333: 72-81 (2010).
    • (2010) Brain Res , vol.1333 , pp. 72-81
    • Di Domenico, F.1    Sultana, R.2    Tiu, G.F.3    Scheff, N.N.4    Perluigi, M.5    Cini, C.6
  • 110
    • 84865721919 scopus 로고    scopus 로고
    • Swedish Alzheimer mutation induces mitochondrial dysfunction mediated by HSP60 mislocalization of amyloid precursor protein (APP) and beta-amyloid
    • Walls KC, Coskun P, Gallegos-Perez JL, Zadourian N, Freude K, Rasool S, et al. Swedish Alzheimer mutation induces mitochondrial dysfunction mediated by HSP60 mislocalization of amyloid precursor protein (APP) and beta-amyloid. J Biol Chem 287(36): 30317-27 (2012).
    • (2012) J Biol Chem , vol.287 , Issue.36 , pp. 30317-30327
    • Walls, K.C.1    Coskun, P.2    Gallegos-Perez, J.L.3    Zadourian, N.4    Freude, K.5    Rasool, S.6
  • 111
    • 0034650427 scopus 로고    scopus 로고
    • Cutting edge: Heat shock protein 60 is a putative endogenous ligand of the toll-like receptor-4 complex
    • Ohashi K, Burkart V, Flohe S, Kolb H. Cutting edge: heat shock protein 60 is a putative endogenous ligand of the toll-like receptor-4 complex. J Immunol 164(2): 558-61 (2000).
    • (2000) J Immunol , vol.164 , Issue.2 , pp. 558-561
    • Ohashi, K.1    Burkart, V.2    Flohe, S.3    Kolb, H.4
  • 112
    • 40449097556 scopus 로고    scopus 로고
    • A vicious cycle involving release of heat shock protein 60 from injured cells and activation of toll-like receptor 4 mediates neurodegeneration in the CNS
    • Lehnardt S, Schott E, Trimbuch T, Laubisch D, Krueger C, Wulczyn G, et al. A vicious cycle involving release of heat shock protein 60 from injured cells and activation of toll-like receptor 4 mediates neurodegeneration in the CNS. J Neurosci 28(10): 2320-31 (2008).
    • (2008) J Neurosci , vol.28 , Issue.10 , pp. 2320-2331
    • Lehnardt, S.1    Schott, E.2    Trimbuch, T.3    Laubisch, D.4    Krueger, C.5    Wulczyn, G.6
  • 113
    • 0023789193 scopus 로고
    • Reactive microglia are positive for HLA-DR in the substantia nigra of Parkinson’s and Alzheimer’s disease brains
    • McGeer PL, Itagaki S, Boyes BE, McGeer EG. Reactive microglia are positive for HLA-DR in the substantia nigra of Parkinson’s and Alzheimer’s disease brains. Neurology 38(8): 1285-91 (1988).
    • (1988) Neurology , vol.38 , Issue.8 , pp. 1285-1291
    • McGeer, P.L.1    Itagaki, S.2    Boyes, B.E.3    McGeer, E.G.4
  • 115
    • 84884908194 scopus 로고    scopus 로고
    • The expression and release of Hsp60 in 6-OHDA induced in vivo and in vitro models of Parkinson’s disease
    • Feng M, Zhang L, Liu Z, Zhou P, Lu X. The expression and release of Hsp60 in 6-OHDA induced in vivo and in vitro models of Parkinson’s disease. Neurochem Res 38(10): 2180-9 (2013).
    • (2013) Neurochem Res , vol.38 , Issue.10 , pp. 2180-2189
    • Feng, M.1    Zhang, L.2    Liu, Z.3    Zhou, P.4    Lu, X.5
  • 116
    • 84927175748 scopus 로고    scopus 로고
    • APOE epsilon4: The most prevalent yet understudied risk factor for Alzheimer’s disease
    • Michaelson DM. APOE epsilon4: the most prevalent yet understudied risk factor for Alzheimer’s disease. Alzheimers Dement 10(6): 861-8 (2014).
    • (2014) Alzheimers Dement , vol.10 , Issue.6 , pp. 861-868
    • Michaelson, D.M.1
  • 117
    • 35148859811 scopus 로고    scopus 로고
    • Mortalin is regulated by APOE in hippocampus of AD patients and by human APOE in TR mice
    • Osorio C, Sullivan PM, He DN, Mace BE, Ervin JF, Strittmatter WJ, et al. Mortalin is regulated by APOE in hippocampus of AD patients and by human APOE in TR mice. Neurobiol Aging 28(12): 1853-62 (2007).
    • (2007) Neurobiol Aging , vol.28 , Issue.12 , pp. 1853-1862
    • Osorio, C.1    Sullivan, P.M.2    He, D.N.3    Mace, B.E.4    Ervin, J.F.5    Strittmatter, W.J.6
  • 118
    • 11844251260 scopus 로고    scopus 로고
    • Regulation of gene expression by the amyloid precursor protein: Inhibition of the JNK/c-Jun pathway
    • Kogel D, Schomburg R, Copanaki E, Prehn JH. Regulation of gene expression by the amyloid precursor protein: inhibition of the JNK/c-Jun pathway. Cell Death Differ 12(1): 1-9 (2005).
    • (2005) Cell Death Differ , vol.12 , Issue.1 , pp. 1-9
    • Kogel, D.1    Schomburg, R.2    Copanaki, E.3    Prehn, J.H.4
  • 119
    • 1842634504 scopus 로고    scopus 로고
    • Proteomic identification of specific oxidized proteins in ApoE-knockout mice: Relevance to Alzheimer’s disease
    • Choi J, Forster MJ, McDonald SR, Weintraub ST, Carroll CA, Gracy RW. Proteomic identification of specific oxidized proteins in ApoE-knockout mice: relevance to Alzheimer’s disease. Free Radic Biol Med 36(9): 1155-62 (2004).
    • (2004) Free Radic Biol Med , vol.36 , Issue.9 , pp. 1155-1162
    • Choi, J.1    Forster, M.J.2    McDonald, S.R.3    Weintraub, S.T.4    Carroll, C.A.5    Gracy, R.W.6
  • 120
    • 77952085938 scopus 로고    scopus 로고
    • Differential effects of wild-type and A53T mutant isoform of alpha-synuclein on the mitochondrial proteome of differentiated SH-SY5Y cells
    • Pennington K, Peng J, Hung CC, Banks RE, Robinson PA. Differential effects of wild-type and A53T mutant isoform of alpha-synuclein on the mitochondrial proteome of differentiated SH-SY5Y cells. J Proteome Res 9(5): 2390-401 (2010).
    • (2010) J Proteome Res , vol.9 , Issue.5 , pp. 2390-2401
    • Pennington, K.1    Peng, J.2    Hung, C.C.3    Banks, R.E.4    Robinson, P.A.5
  • 123
    • 33746296891 scopus 로고    scopus 로고
    • Proteomic identification of a stress protein, mortalin/mthsp70/GRP75: Relevance to Parkinson disease
    • Jin J, Hulette C, Wang Y, Zhang T, Pan C, Wadhwa R, et al. Proteomic identification of a stress protein, mortalin/mthsp70/GRP75: relevance to Parkinson disease. Mol Cell Proteomics 5(7): 1193-204 (2006).
    • (2006) Mol Cell Proteomics , vol.5 , Issue.7 , pp. 1193-1204
    • Jin, J.1    Hulette, C.2    Wang, Y.3    Zhang, T.4    Pan, C.5    Wadhwa, R.6
  • 124
    • 79959886270 scopus 로고    scopus 로고
    • Amyloid precursor protein processing and Alzheimer’s disease
    • O’Brien RJ, Wong PC. Amyloid precursor protein processing and Alzheimer’s disease. Annu Rev Neurosci 34: 185-204.
    • Annu Rev Neurosci , vol.34 , pp. 185-204
    • O’Brien, R.J.1    Wong, P.C.2
  • 125
    • 0033825336 scopus 로고    scopus 로고
    • Characterization of human HtrA2, a novel serine protease involved in the mammalian cellular stress response
    • Gray CW, Ward RV, Karran E, Turconi S, Rowles A, Viglienghi D, et al. Characterization of human HtrA2, a novel serine protease involved in the mammalian cellular stress response. Eur J Biochem 267(18): 5699-710 (2000).
    • (2000) Eur J Biochem , vol.267 , Issue.18 , pp. 5699-5710
    • Gray, C.W.1    Ward, R.V.2    Karran, E.3    Turconi, S.4    Rowles, A.5    Viglienghi, D.6
  • 126
    • 8544245734 scopus 로고    scopus 로고
    • The Cterminal tail of presenilin regulates Omi/HtrA2 protease activity
    • Gupta S, Singh R, Datta P, Zhang Z, Orr C, Lu Z, et al. The Cterminal tail of presenilin regulates Omi/HtrA2 protease activity. J Biol Chem 279(44): 45844-54 (2004).
    • (2004) J Biol Chem , vol.279 , Issue.44 , pp. 45844-45854
    • Gupta, S.1    Singh, R.2    Datta, P.3    Zhang, Z.4    Orr, C.5    Lu, Z.6
  • 128
    • 0442323503 scopus 로고    scopus 로고
    • Alzheimer’s disease-associated amyloid beta interacts with the human serine protease HtrA2/Omi
    • Park HJ, Seong YM, Choi JY, Kang S, Rhim H. Alzheimer’s disease-associated amyloid beta interacts with the human serine protease HtrA2/Omi. Neurosci Lett 357(1): 63-7 (2004).
    • (2004) Neurosci Lett , vol.357 , Issue.1 , pp. 63-67
    • Park, H.J.1    Seong, Y.M.2    Choi, J.Y.3    Kang, S.4    Rhim, H.5
  • 129
    • 67849129079 scopus 로고    scopus 로고
    • A new function of human HtrA2 as an amyloid-beta oligomerization inhibitor
    • Kooistra J, Milojevic J, Melacini G, Ortega J. A new function of human HtrA2 as an amyloid-beta oligomerization inhibitor. J Alzheimers Dis 17(2): 281-94 (2009).
    • (2009) J Alzheimers Dis , vol.17 , Issue.2 , pp. 281-294
    • Kooistra, J.1    Milojevic, J.2    Melacini, G.3    Ortega, J.4
  • 130
    • 34948867875 scopus 로고    scopus 로고
    • HtrA2 regulates beta-amyloid precursor protein (APP) metabolism through endoplasmic reticulum-associated degradation
    • Huttunen HJ, Guenette SY, Peach C, Greco C, Xia W, Kim DY, et al. HtrA2 regulates beta-amyloid precursor protein (APP) metabolism through endoplasmic reticulum-associated degradation. J Biol Chem 282(38): 28285-95 (2007).
    • (2007) J Biol Chem , vol.282 , Issue.38 , pp. 28285-28295
    • Huttunen, H.J.1    Guenette, S.Y.2    Peach, C.3    Greco, C.4    Xia, W.5    Kim, D.Y.6
  • 131
    • 33845918450 scopus 로고    scopus 로고
    • Beta-amyloid precursor protein is a direct cleavage target of HtrA2 serine protease. Implications for the physiological function of HtrA2 in the mitochondria
    • Park HJ, Kim SS, Seong YM, Kim KH, Goo HG, Yoon EJ, et al. Beta-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 281(45): 34277-87 (2006).
    • (2006) J Biol Chem , vol.281 , Issue.45 , 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
  • 132
    • 78349313844 scopus 로고    scopus 로고
    • Localization of HtrA2/Omi immunoreactivity in brains affected by Alzheimer’s disease
    • Kawamoto Y, Ito H, Kobayashi Y, Suzuki Y, Takahashi R. Localization of HtrA2/Omi immunoreactivity in brains affected by Alzheimer’s disease. Neuroreport 21(17): 1121-5 (2010).
    • (2010) Neuroreport , vol.21 , Issue.17 , pp. 1121-1125
    • Kawamoto, Y.1    Ito, H.2    Kobayashi, Y.3    Suzuki, Y.4    Takahashi, R.5
  • 133
    • 79954625572 scopus 로고    scopus 로고
    • Altered enzymatic activity and allele frequency of OMI/HTRA2 in Alzheimer’s disease
    • Westerlund M, Behbahani H, Gellhaar S, Forsell C, Belin AC, Anvret A, et al. Altered enzymatic activity and allele frequency of OMI/HTRA2 in Alzheimer’s disease. FASEB J 25(4): 1345-52 (2011).
    • (2011) FASEB J , vol.25 , Issue.4 , pp. 1345-1352
    • Westerlund, M.1    Behbahani, H.2    Gellhaar, S.3    Forsell, C.4    Belin, A.C.5    Anvret, A.6
  • 134
    • 54449090491 scopus 로고    scopus 로고
    • Accumulation of HtrA2/Omi in neuronal and glial inclusions in brains with alpha-synucleinopathies
    • Kawamoto Y, Kobayashi Y, Suzuki Y, Inoue H, Tomimoto H, Akiguchi I, et al. Accumulation of HtrA2/Omi in neuronal and glial inclusions in brains with alpha-synucleinopathies. J Neuropathol Exp Neurol 67(10): 984-93 (2008).
    • (2008) J Neuropathol Exp Neurol , vol.67 , Issue.10 , pp. 984-993
    • Kawamoto, Y.1    Kobayashi, Y.2    Suzuki, Y.3    Inoue, H.4    Tomimoto, H.5    Akiguchi, I.6
  • 136
    • 0142246441 scopus 로고    scopus 로고
    • Loss of Omi mitochondrial protease activity causes the neuromuscular disorder of mnd2 mutant mice
    • Jones JM, Datta P, Srinivasula SM, Ji W, Gupta S, Zhang Z, et al. Loss of Omi mitochondrial protease activity causes the neuromuscular disorder of mnd2 mutant mice. Nature 425(6959): 721-7 (2003).
    • (2003) Nature , vol.425 , Issue.6959 , pp. 721-727
    • Jones, J.M.1    Datta, P.2    Srinivasula, S.M.3    Ji, W.4    Gupta, S.5    Zhang, Z.6
  • 137
  • 138
    • 35748935851 scopus 로고    scopus 로고
    • The mitochondrial protease HtrA2 is regulated by Parkinson’s disease-associated kinase PINK1
    • Plun-Favreau H, Klupsch K, Moisoi N, Gandhi S, Kjaer S, Frith D, et al. The mitochondrial protease HtrA2 is regulated by Parkinson’s disease-associated kinase PINK1. Nat Cell Biol 9(11): 1243-52 (2007).
    • (2007) Nat Cell Biol , vol.9 , Issue.11 , pp. 1243-1252
    • Plun-Favreau, H.1    Klupsch, K.2    Moisoi, N.3    Gandhi, S.4    Kjaer, S.5    Frith, D.6
  • 139
    • 58149397651 scopus 로고    scopus 로고
    • Rhomboid-7 and HtrA2/Omi act in a common pathway with the Parkinson’s disease factors Pink1 and Parkin
    • discussion 73
    • Whitworth AJ, Lee JR, Ho VM, Flick R, Chowdhury R, McQuibban GA. Rhomboid-7 and HtrA2/Omi act in a common pathway with the Parkinson’s disease factors Pink1 and Parkin. Dis Model Mech 1(2-3): 168-74; discussion 73 (2008).
    • (2008) Dis Model Mech , vol.1 , Issue.2-3 , pp. 168-174
    • Whitworth, A.J.1    Lee, J.R.2    Ho, V.M.3    Flick, R.4    Chowdhury, R.5    McQuibban, G.A.6
  • 140
    • 67650718212 scopus 로고    scopus 로고
    • Drosophila HtrA2 is dispensable for apoptosis but acts downstream of PINK1 independently from Parkin
    • Tain LS, Chowdhury RB, Tao RN, Plun-Favreau H, Moisoi N, Martins LM, et al. Drosophila HtrA2 is dispensable for apoptosis but acts downstream of PINK1 independently from Parkin. Cell Death Differ 16(8): 1118-25 (2009).
    • (2009) Cell Death Differ , vol.16 , Issue.8 , pp. 1118-1125
    • Tain, L.S.1    Chowdhury, R.B.2    Tao, R.N.3    Plun-Favreau, H.4    Moisoi, N.5    Martins, L.M.6
  • 141
    • 58149375389 scopus 로고    scopus 로고
    • Loss-of-function analysis suggests that Omi/HtrA2 is not an essential component of the PINK1/PARKIN pathway in vivo
    • Yun J, Cao JH, Dodson MW, Clark IE, Kapahi P, Chowdhury RB, et al. Loss-of-function analysis suggests that Omi/HtrA2 is not an essential component of the PINK1/PARKIN pathway in vivo. J Neurosci 28(53): 14500-10 (2008).
    • (2008) J Neurosci , vol.28 , Issue.53 , pp. 14500-14510
    • Yun, J.1    Cao, J.H.2    Dodson, M.W.3    Clark, I.E.4    Kapahi, P.5    Chowdhury, R.B.6
  • 142
    • 34547127902 scopus 로고    scopus 로고
    • PINK1 protects against oxidative stress by phosphorylating mitochondrial chaperone TRAP1
    • Pridgeon JW, Olzmann JA, Chin LS, Li L. PINK1 protects against oxidative stress by phosphorylating mitochondrial chaperone TRAP1. PLoS Biol 5(7): e172 (2007).
    • (2007) Plos Biol , vol.5 , Issue.7
    • Pridgeon, J.W.1    Olzmann, J.A.2    Chin, L.S.3    Li, L.4
  • 143
  • 144
    • 84901494659 scopus 로고    scopus 로고
    • Mitochondrial matrix proteases as novel therapeutic targets in malignancy
    • Goard CA, Schimmer AD. Mitochondrial matrix proteases as novel therapeutic targets in malignancy. Oncogene 33(21): 2690-9.
    • Oncogene , vol.33 , Issue.21 , pp. 2690-2699
    • Goard, C.A.1    Schimmer, A.D.2


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