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Volumn 7, Issue 5, 2012, Pages

Suppression of ribosomal function triggers innate immune signaling through activation of the NLRP3 inflammasome

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; ANISOMYCIN; CRYOPYRIN; CYCLOHEXIMIDE; DOUBLE STRANDED RNA; INFLAMMASOME; INTERLEUKIN 1BETA; INTERLEUKIN 1BETA CONVERTING ENZYME; NIGERICIN; PACTAMYCIN; POLYINOSINIC POLYCYTIDYLIC ACID; POTASSIUM; PUROMYCIN; RICIN; URATE; BENZYLOXYCARBONYLLEUCYL LEUCYL LEUCINE ALDEHYDE; BENZYLOXYCARBONYLLEUCYL-LEUCYL-LEUCINE ALDEHYDE; CARRIER PROTEIN; CIAS1 PROTEIN, MOUSE; LEUPEPTIN; PROTEASOME; URIC ACID;

EID: 84861010060     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0036044     Document Type: Article
Times cited : (47)

References (74)
  • 1
    • 77749304035 scopus 로고    scopus 로고
    • IL-1: discoveries, controversies and future directions
    • Dinarello CA, (2010) IL-1: discoveries, controversies and future directions. Eur J Immunol 40: 599-606.
    • (2010) Eur J Immunol , vol.40 , pp. 599-606
    • Dinarello, C.A.1
  • 2
    • 0036398446 scopus 로고    scopus 로고
    • The IL-1 family and inflammatory diseases
    • Dinarello CA, (2002) The IL-1 family and inflammatory diseases. Clin Exp Rheumatol 20: S1-13.
    • (2002) Clin Exp Rheumatol , vol.20 , pp. 1-13
    • Dinarello, C.A.1
  • 3
    • 0036671894 scopus 로고    scopus 로고
    • The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta
    • Martinon F, Burns K, Tschopp J, (2002) The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta. Mol Cell 10: 417-426.
    • (2002) Mol Cell , vol.10 , pp. 417-426
    • Martinon, F.1    Burns, K.2    Tschopp, J.3
  • 4
    • 0026507126 scopus 로고
    • A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes
    • Thornberry NA, Bull HG, Calaycay JR, Chapman KT, Howard AD, et al. (1992) A novel heterodimeric cysteine protease is required for interleukin-1 beta processing in monocytes. Nature 356: 768-774.
    • (1992) Nature , vol.356 , pp. 768-774
    • Thornberry, N.A.1    Bull, H.G.2    Calaycay, J.R.3    Chapman, K.T.4    Howard, A.D.5
  • 5
    • 0037077283 scopus 로고    scopus 로고
    • The PYRIN-CARD protein ASC is an activating adaptor for caspase-1
    • Srinivasula SM, Poyet JL, Razmara M, Datta P, Zhang Z, et al. (2002) The PYRIN-CARD protein ASC is an activating adaptor for caspase-1. J Biol Chem 277: 21119-21122.
    • (2002) J Biol Chem , vol.277 , pp. 21119-21122
    • Srinivasula, S.M.1    Poyet, J.L.2    Razmara, M.3    Datta, P.4    Zhang, Z.5
  • 6
    • 78249269470 scopus 로고    scopus 로고
    • Activation of the NLRP3 inflammasome by intracellular poly I:C
    • Rajan JV, Warren SE, Miao EA, Aderem A, (2010) Activation of the NLRP3 inflammasome by intracellular poly I:C. FEBS Lett 584: 4627-4632.
    • (2010) FEBS Lett , vol.584 , pp. 4627-4632
    • Rajan, J.V.1    Warren, S.E.2    Miao, E.A.3    Aderem, A.4
  • 7
    • 0028175838 scopus 로고
    • Interleukin-1 beta maturation and release in response to ATP and nigericin. Evidence that potassium depletion mediated by these agents is a necessary and common feature of their activity
    • Perregaux D, Gabel CA, (1994) Interleukin-1 beta maturation and release in response to ATP and nigericin. Evidence that potassium depletion mediated by these agents is a necessary and common feature of their activity. J Biol Chem 269: 15195-15203.
    • (1994) J Biol Chem , vol.269 , pp. 15195-15203
    • Perregaux, D.1    Gabel, C.A.2
  • 9
    • 36849056773 scopus 로고    scopus 로고
    • IL-1R1/MyD88 signaling and the inflammasome are essential in pulmonary inflammation and fibrosis in mice
    • Gasse P, Mary C, Guenon I, Noulin N, Charron S, et al. (2007) IL-1R1/MyD88 signaling and the inflammasome are essential in pulmonary inflammation and fibrosis in mice. J Clin Invest 117: 3786-3799.
    • (2007) J Clin Invest , vol.117 , pp. 3786-3799
    • Gasse, P.1    Mary, C.2    Guenon, I.3    Noulin, N.4    Charron, S.5
  • 10
    • 0037312509 scopus 로고    scopus 로고
    • NALPs: a novel protein family involved in inflammation
    • Tschopp J, Martinon F, Burns K, (2003) NALPs: a novel protein family involved in inflammation. Nat Rev Mol Cell Biol 4: 95-104.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 95-104
    • Tschopp, J.1    Martinon, F.2    Burns, K.3
  • 11
    • 34548027736 scopus 로고    scopus 로고
    • Activation of the NALP3 inflammasome is triggered by low intracellular potassium concentration
    • Petrilli V, Papin S, Dostert C, Mayor A, Martinon F, et al. (2007) Activation of the NALP3 inflammasome is triggered by low intracellular potassium concentration. Cell Death Differ 14: 1583-1589.
    • (2007) Cell Death Differ , vol.14 , pp. 1583-1589
    • Petrilli, V.1    Papin, S.2    Dostert, C.3    Mayor, A.4    Martinon, F.5
  • 12
    • 34047261260 scopus 로고    scopus 로고
    • ATP activates a reactive oxygen species-dependent oxidative stress response and secretion of proinflammatory cytokines in macrophages
    • Cruz CM, Rinna A, Forman HJ, Ventura AL, Persechini PM, et al. (2007) ATP activates a reactive oxygen species-dependent oxidative stress response and secretion of proinflammatory cytokines in macrophages. J Biol Chem 282: 2871-2879.
    • (2007) J Biol Chem , vol.282 , pp. 2871-2879
    • Cruz, C.M.1    Rinna, A.2    Forman, H.J.3    Ventura, A.L.4    Persechini, P.M.5
  • 13
    • 43249125839 scopus 로고    scopus 로고
    • Innate immune activation through Nalp3 inflammasome sensing of asbestos and silica
    • Dostert C, Petrilli V, Van Bruggen R, Steele C, Mossman BT, et al. (2008) Innate immune activation through Nalp3 inflammasome sensing of asbestos and silica. Science 320: 674-677.
    • (2008) Science , vol.320 , pp. 674-677
    • Dostert, C.1    Petrilli, V.2    van Bruggen, R.3    Steele, C.4    Mossman, B.T.5
  • 14
    • 79960542894 scopus 로고    scopus 로고
    • Cutting edge: reactive oxygen species inhibitors block priming, but not activation, of the NLRP3 inflammasome
    • Bauernfeind F, Bartok E, Rieger A, Franchi L, Nunez G, et al. (2011) Cutting edge: reactive oxygen species inhibitors block priming, but not activation, of the NLRP3 inflammasome. J Immunol 187: 613-617.
    • (2011) J Immunol , vol.187 , pp. 613-617
    • Bauernfeind, F.1    Bartok, E.2    Rieger, A.3    Franchi, L.4    Nunez, G.5
  • 15
    • 77955867246 scopus 로고    scopus 로고
    • Human NLRP3 inflammasome activation is Nox1-4 independent
    • van Bruggen R, Koker MY, Jansen M, van Houdt M, Roos D, et al. (2010) Human NLRP3 inflammasome activation is Nox1-4 independent. Blood 115: 5398-5400.
    • (2010) Blood , vol.115 , pp. 5398-5400
    • van Bruggen, R.1    Koker, M.Y.2    Jansen, M.3    van Houdt, M.4    Roos, D.5
  • 16
    • 77649260429 scopus 로고    scopus 로고
    • Reactive oxygen species-independent activation of the IL-1beta inflammasome in cells from patients with chronic granulomatous disease
    • van de Veerdonk FL, Smeekens SP, Joosten LA, Kullberg BJ, Dinarello CA, et al. (2010) Reactive oxygen species-independent activation of the IL-1beta inflammasome in cells from patients with chronic granulomatous disease. Proc Natl Acad Sci U S A 107: 3030-3033.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 3030-3033
    • van de Veerdonk, F.L.1    Smeekens, S.P.2    Joosten, L.A.3    Kullberg, B.J.4    Dinarello, C.A.5
  • 17
    • 0015244752 scopus 로고
    • Structural and functional defects in mammalian ribosomes after potassium deficiency
    • Naslund PH, Hultin T, (1971) Structural and functional defects in mammalian ribosomes after potassium deficiency. Biochim Biophys Acta 254: 104-116.
    • (1971) Biochim Biophys Acta , vol.254 , pp. 104-116
    • Naslund, P.H.1    Hultin, T.2
  • 18
    • 0018265538 scopus 로고
    • Inhibition of elongation steps of protein synthesis at reduced potassium concentrations in reticulocytes and reticulocyte lysate
    • Cahn F, Lubin M, (1978) Inhibition of elongation steps of protein synthesis at reduced potassium concentrations in reticulocytes and reticulocyte lysate. J Biol Chem 253: 7798-7803.
    • (1978) J Biol Chem , vol.253 , pp. 7798-7803
    • Cahn, F.1    Lubin, M.2
  • 19
    • 0014284690 scopus 로고
    • Studies on salt-treated reticulocyte ribosomes
    • Yang PC, Hamada K, Schweet R, (1968) Studies on salt-treated reticulocyte ribosomes. Arch Biochem Biophys 125: 506-513.
    • (1968) Arch Biochem Biophys , vol.125 , pp. 506-513
    • Yang, P.C.1    Hamada, K.2    Schweet, R.3
  • 20
    • 0014192217 scopus 로고
    • Intracellular potassium and macromolecular synthesis in mammalian cells
    • Lubin M, (1967) Intracellular potassium and macromolecular synthesis in mammalian cells. Nature 213: 451-453.
    • (1967) Nature , vol.213 , pp. 451-453
    • Lubin, M.1
  • 21
    • 0017365519 scopus 로고
    • Control of protein synthesis in human fibroblasts by intracellular potassium
    • Ledbetter ML, Lubin M, (1977) Control of protein synthesis in human fibroblasts by intracellular potassium. Exp Cell Res 105: 223-236.
    • (1977) Exp Cell Res , vol.105 , pp. 223-236
    • Ledbetter, M.L.1    Lubin, M.2
  • 22
    • 70249139539 scopus 로고    scopus 로고
    • Pulmonary inflammation triggered by ricin toxin requires macrophages and IL-1 signaling
    • Lindauer ML, Wong J, Iwakura Y, Magun BE, (2009) Pulmonary inflammation triggered by ricin toxin requires macrophages and IL-1 signaling. J Immunol 183: 1419-1426.
    • (2009) J Immunol , vol.183 , pp. 1419-1426
    • Lindauer, M.L.1    Wong, J.2    Iwakura, Y.3    Magun, B.E.4
  • 23
    • 79952076264 scopus 로고    scopus 로고
    • Ricin toxin activates the NALP3 inflammasome
    • Lindauer M, Wong J, Magun B, (2010) Ricin toxin activates the NALP3 inflammasome. Toxins 2: 1500-1514.
    • (2010) Toxins , vol.2 , pp. 1500-1514
    • Lindauer, M.1    Wong, J.2    Magun, B.3
  • 24
    • 0015498972 scopus 로고
    • The effects of nigericin, valinomycin, and 2,4-dinitrophenol on intracellular pH, glycolysis, and K + concentration of Ehrlich ascites tumor cells
    • Poole DT, Butler TC, Williams ME, (1972) The effects of nigericin, valinomycin, and 2,4-dinitrophenol on intracellular pH, glycolysis, and K + concentration of Ehrlich ascites tumor cells. Biochim Biophys Acta 266: 463-470.
    • (1972) Biochim Biophys Acta , vol.266 , pp. 463-470
    • Poole, D.T.1    Butler, T.C.2    Williams, M.E.3
  • 25
    • 79952747168 scopus 로고    scopus 로고
    • Cutting edge: cyclic polypeptide and aminoglycoside antibiotics trigger IL-1beta secretion by activating the NLRP3 inflammasome
    • Allam R, Darisipudi MN, Rupanagudi KV, Lichtnekert J, Tschopp J, et al. (2011) Cutting edge: cyclic polypeptide and aminoglycoside antibiotics trigger IL-1beta secretion by activating the NLRP3 inflammasome. J Immunol 186: 2714-2718.
    • (2011) J Immunol , vol.186 , pp. 2714-2718
    • Allam, R.1    Darisipudi, M.N.2    Rupanagudi, K.V.3    Lichtnekert, J.4    Tschopp, J.5
  • 26
    • 79956358982 scopus 로고    scopus 로고
    • Polyene macrolide antifungal drugs trigger interleukin-1beta secretion by activating the NLRP3 inflammasome
    • Darisipudi MN, Allam R, Rupanagudi KV, Anders HJ, (2011) Polyene macrolide antifungal drugs trigger interleukin-1beta secretion by activating the NLRP3 inflammasome. PLoS One 6: e19588.
    • (2011) PLoS One , vol.6
    • Darisipudi, M.N.1    Allam, R.2    Rupanagudi, K.V.3    Anders, H.J.4
  • 27
    • 84856857478 scopus 로고    scopus 로고
    • ER stress activates the NLRP3 inflammasome via an UPR-independent pathway
    • Menu P, Mayor A, Zhou R, Tardivel A, Ichijo H, et al. (2012) ER stress activates the NLRP3 inflammasome via an UPR-independent pathway. Cell Death Dis 3: e261.
    • (2012) Cell Death Dis , vol.3
    • Menu, P.1    Mayor, A.2    Zhou, R.3    Tardivel, A.4    Ichijo, H.5
  • 28
    • 84860997598 scopus 로고    scopus 로고
    • Double-walled carbon nanotubes trigger IL-1beta release in human monocytes through Nlrp3 inflammasome activation
    • Meunier E, Coste A, Olagnier D, Authier H, Lefevre L, et al. (2011) Double-walled carbon nanotubes trigger IL-1beta release in human monocytes through Nlrp3 inflammasome activation. Nanomedicine.
    • (2011) Nanomedicine
    • Meunier, E.1    Coste, A.2    Olagnier, D.3    Authier, H.4    Lefevre, L.5
  • 29
    • 84863726706 scopus 로고    scopus 로고
    • Mycobacterium abscessus activates the NLRP3 inflammasome via Dectin-1-Syk and p62/SQSTM1
    • Lee HM, Yuk JM, Kim KH, Jang J, Kang G, et al. (2011) Mycobacterium abscessus activates the NLRP3 inflammasome via Dectin-1-Syk and p62/SQSTM1. Immunol Cell Biol.
    • (2011) Immunol Cell Biol
    • Lee, H.M.1    Yuk, J.M.2    Kim, K.H.3    Jang, J.4    Kang, G.5
  • 30
    • 80052581043 scopus 로고    scopus 로고
    • NLRP3 inflammasome plays a critical role in the pathogenesis of hydroxyapatite-associated arthropathy
    • Jin C, Frayssinet P, Pelker R, Cwirka D, Hu B, et al. (2011) NLRP3 inflammasome plays a critical role in the pathogenesis of hydroxyapatite-associated arthropathy. Proc Natl Acad Sci U S A 108: 14867-14872.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 14867-14872
    • Jin, C.1    Frayssinet, P.2    Pelker, R.3    Cwirka, D.4    Hu, B.5
  • 31
    • 0015195582 scopus 로고
    • Inhibitors of ribosome functions
    • Pestka S, (1971) Inhibitors of ribosome functions. Annu Rev Microbiol 25: 487-562.
    • (1971) Annu Rev Microbiol , vol.25 , pp. 487-562
    • Pestka, S.1
  • 33
    • 0030973162 scopus 로고    scopus 로고
    • Ribotoxic stress response: activation of the stress-activated protein kinase JNK1 by inhibitors of the peptidyl transferase reaction and by sequence-specific RNA damage to the alpha-sarcin/ricin loop in the 28S rRNA
    • Iordanov MS, Pribnow D, Magun JL, Dinh TH, Pearson JA, et al. (1997) Ribotoxic stress response: activation of the stress-activated protein kinase JNK1 by inhibitors of the peptidyl transferase reaction and by sequence-specific RNA damage to the alpha-sarcin/ricin loop in the 28S rRNA. Mol Cell Biol 17: 3373-3381.
    • (1997) Mol Cell Biol , vol.17 , pp. 3373-3381
    • Iordanov, M.S.1    Pribnow, D.2    Magun, J.L.3    Dinh, T.H.4    Pearson, J.A.5
  • 34
    • 0018367463 scopus 로고
    • Coupling between K efflux, ATP metabolism and protein synthesis in reticulocytes
    • Panet R, Atlan H, (1979) Coupling between K efflux, ATP metabolism and protein synthesis in reticulocytes. Biochem Biophys Res Commun 88: 619-626.
    • (1979) Biochem Biophys Res Commun , vol.88 , pp. 619-626
    • Panet, R.1    Atlan, H.2
  • 35
    • 0019379799 scopus 로고
    • Reversion by hypotonic medium of the shutoff of protein synthesis induced by encephalomyocarditis virus
    • Alonso MA, Carrasco L, (1981) Reversion by hypotonic medium of the shutoff of protein synthesis induced by encephalomyocarditis virus. J Virol 37: 535-540.
    • (1981) J Virol , vol.37 , pp. 535-540
    • Alonso, M.A.1    Carrasco, L.2
  • 36
    • 0019731673 scopus 로고
    • Effect of ionophores and metabolic inhibitors on protein synthesis in rabbit reticulocytes
    • Breitbart H, (1981) Effect of ionophores and metabolic inhibitors on protein synthesis in rabbit reticulocytes. Biochim Biophys Acta 656: 160-166.
    • (1981) Biochim Biophys Acta , vol.656 , pp. 160-166
    • Breitbart, H.1
  • 37
    • 77749304032 scopus 로고    scopus 로고
    • Signaling by ROS drives inflammasome activation
    • Martinon F, (2010) Signaling by ROS drives inflammasome activation. Eur J Immunol 40: 616-619.
    • (2010) Eur J Immunol , vol.40 , pp. 616-619
    • Martinon, F.1
  • 38
    • 78650926948 scopus 로고    scopus 로고
    • Sodium overload and water influx activate the NALP3 inflammasome
    • Schorn C, Frey B, Lauber K, Janko C, Strysio M, et al. (2011) Sodium overload and water influx activate the NALP3 inflammasome. J Biol Chem 286: 35-41.
    • (2011) J Biol Chem , vol.286 , pp. 35-41
    • Schorn, C.1    Frey, B.2    Lauber, K.3    Janko, C.4    Strysio, M.5
  • 39
    • 0027323010 scopus 로고
    • Reversal of the double-stranded-RNA-induced inhibition of protein synthesis by a catalytically inactive mutant of the protein kinase PKR
    • Sharp TV, Xiao Q, Jeffrey I, Gewert DR, Clemens MJ, (1993) Reversal of the double-stranded-RNA-induced inhibition of protein synthesis by a catalytically inactive mutant of the protein kinase PKR. Eur J Biochem 214: 945-948.
    • (1993) Eur J Biochem , vol.214 , pp. 945-948
    • Sharp, T.V.1    Xiao, Q.2    Jeffrey, I.3    Gewert, D.R.4    Clemens, M.J.5
  • 40
    • 36349019887 scopus 로고    scopus 로고
    • Proteasomes control caspase-1 activation in anthrax lethal toxin-mediated cell killing
    • Squires RC, Muehlbauer SM, Brojatsch J, (2007) Proteasomes control caspase-1 activation in anthrax lethal toxin-mediated cell killing. J Biol Chem 282: 34260-34267.
    • (2007) J Biol Chem , vol.282 , pp. 34260-34267
    • Squires, R.C.1    Muehlbauer, S.M.2    Brojatsch, J.3
  • 44
    • 0030147202 scopus 로고    scopus 로고
    • Lesions of acute inhaled lethal ricin intoxication in rhesus monkeys
    • Wilhelmsen CL, Pitt ML, (1996) Lesions of acute inhaled lethal ricin intoxication in rhesus monkeys. Vet Pathol 33: 296-302.
    • (1996) Vet Pathol , vol.33 , pp. 296-302
    • Wilhelmsen, C.L.1    Pitt, M.L.2
  • 45
    • 34250807925 scopus 로고    scopus 로고
    • Intrapulmonary delivery of ricin at high dosage triggers a systemic inflammatory response and glomerular damage
    • Wong J, Korcheva V, Jacoby DB, Magun B, (2007) Intrapulmonary delivery of ricin at high dosage triggers a systemic inflammatory response and glomerular damage. Am J Pathol 170: 1497-1510.
    • (2007) Am J Pathol , vol.170 , pp. 1497-1510
    • Wong, J.1    Korcheva, V.2    Jacoby, D.B.3    Magun, B.4
  • 46
    • 0018632325 scopus 로고
    • Compounds affecting membranes that inhibit protein synthesis in yeast
    • Alonso MA, Vazquez D, Carrasco L, (1979) Compounds affecting membranes that inhibit protein synthesis in yeast. Antimicrob Agents Chemother 16: 750-756.
    • (1979) Antimicrob Agents Chemother , vol.16 , pp. 750-756
    • Alonso, M.A.1    Vazquez, D.2    Carrasco, L.3
  • 47
    • 0032488926 scopus 로고    scopus 로고
    • Loss of cellular K+ mimics ribotoxic stress. Inhibition of protein synthesis and activation of the stress kinases SEK1/MKK4, stress-activated protein kinase/c-Jun NH2-terminal kinase 1, and p38/HOG1 by palytoxin
    • Iordanov MS, Magun BE, (1998) Loss of cellular K+ mimics ribotoxic stress. Inhibition of protein synthesis and activation of the stress kinases SEK1/MKK4, stress-activated protein kinase/c-Jun NH2-terminal kinase 1, and p38/HOG1 by palytoxin. J Biol Chem 273: 3528-3534.
    • (1998) J Biol Chem , vol.273 , pp. 3528-3534
    • Iordanov, M.S.1    Magun, B.E.2
  • 48
    • 32944468985 scopus 로고    scopus 로고
    • Gout-associated uric acid crystals activate the NALP3 inflammasome
    • Martinon F, Petrilli V, Mayor A, Tardivel A, Tschopp J, (2006) Gout-associated uric acid crystals activate the NALP3 inflammasome. Nature 440: 237-241.
    • (2006) Nature , vol.440 , pp. 237-241
    • Martinon, F.1    Petrilli, V.2    Mayor, A.3    Tardivel, A.4    Tschopp, J.5
  • 50
    • 0032504212 scopus 로고    scopus 로고
    • Increased mature interleukin-1beta (IL-1beta) secretion from THP-1 cells induced by nigericin is a result of activation of p45 IL-1beta-converting enzyme processing
    • Cheneval D, Ramage P, Kastelic T, Szelestenyi T, Niggli H, et al. (1998) Increased mature interleukin-1beta (IL-1beta) secretion from THP-1 cells induced by nigericin is a result of activation of p45 IL-1beta-converting enzyme processing. J Biol Chem 273: 17846-17851.
    • (1998) J Biol Chem , vol.273 , pp. 17846-17851
    • Cheneval, D.1    Ramage, P.2    Kastelic, T.3    Szelestenyi, T.4    Niggli, H.5
  • 51
    • 0019083215 scopus 로고
    • Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria
    • Turrens JF, Boveris A, (1980) Generation of superoxide anion by the NADH dehydrogenase of bovine heart mitochondria. Biochem J 191: 421-427.
    • (1980) Biochem J , vol.191 , pp. 421-427
    • Turrens, J.F.1    Boveris, A.2
  • 52
    • 0021996572 scopus 로고
    • Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria
    • Turrens JF, Alexandre A, Lehninger AL, (1985) Ubisemiquinone is the electron donor for superoxide formation by complex III of heart mitochondria. Arch Biochem Biophys 237: 408-414.
    • (1985) Arch Biochem Biophys , vol.237 , pp. 408-414
    • Turrens, J.F.1    Alexandre, A.2    Lehninger, A.L.3
  • 53
    • 0030969868 scopus 로고    scopus 로고
    • Superoxide production by the mitochondrial respiratory chain
    • Turrens JF, (1997) Superoxide production by the mitochondrial respiratory chain. Biosci Rep 17: 3-8.
    • (1997) Biosci Rep , vol.17 , pp. 3-8
    • Turrens, J.F.1
  • 54
    • 79951642032 scopus 로고    scopus 로고
    • Autophagy proteins regulate innate immune responses by inhibiting the release of mitochondrial DNA mediated by the NALP3 inflammasome
    • Nakahira K, Haspel JA, Rathinam VA, Lee SJ, Dolinay T, et al. (2011) Autophagy proteins regulate innate immune responses by inhibiting the release of mitochondrial DNA mediated by the NALP3 inflammasome. Nat Immunol 12: 222-230.
    • (2011) Nat Immunol , vol.12 , pp. 222-230
    • Nakahira, K.1    Haspel, J.A.2    Rathinam, V.A.3    Lee, S.J.4    Dolinay, T.5
  • 55
    • 0014495519 scopus 로고
    • A steroid inhibitory effect on adrenal mitochondria
    • Burrow GN, (1969) A steroid inhibitory effect on adrenal mitochondria. Endocrinology 84: 979-985.
    • (1969) Endocrinology , vol.84 , pp. 979-985
    • Burrow, G.N.1
  • 56
    • 0842285401 scopus 로고    scopus 로고
    • Cytoprotection by pre-emptive conditional phosphorylation of translation initiation factor 2
    • Lu PD, Jousse C, Marciniak SJ, Zhang Y, Novoa I, et al. (2004) Cytoprotection by pre-emptive conditional phosphorylation of translation initiation factor 2. EMBO J 23: 169-179.
    • (2004) EMBO J , vol.23 , pp. 169-179
    • Lu, P.D.1    Jousse, C.2    Marciniak, S.J.3    Zhang, Y.4    Novoa, I.5
  • 57
    • 0036314780 scopus 로고    scopus 로고
    • Cellular stresses profoundly inhibit protein synthesis and modulate the states of phosphorylation of multiple translation factors
    • Patel J, McLeod LE, Vries RG, Flynn A, Wang X, et al. (2002) Cellular stresses profoundly inhibit protein synthesis and modulate the states of phosphorylation of multiple translation factors. Eur J Biochem 269: 3076-3085.
    • (2002) Eur J Biochem , vol.269 , pp. 3076-3085
    • Patel, J.1    McLeod, L.E.2    Vries, R.G.3    Flynn, A.4    Wang, X.5
  • 58
    • 26644450729 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha (TNFalpha) induces the unfolded protein response (UPR) in a reactive oxygen species (ROS)-dependent fashion, and the UPR counteracts ROS accumulation by TNFalpha
    • Xue X, Piao JH, Nakajima A, Sakon-Komazawa S, Kojima Y, et al. (2005) Tumor necrosis factor alpha (TNFalpha) induces the unfolded protein response (UPR) in a reactive oxygen species (ROS)-dependent fashion, and the UPR counteracts ROS accumulation by TNFalpha. J Biol Chem 280: 33917-33925.
    • (2005) J Biol Chem , vol.280 , pp. 33917-33925
    • Xue, X.1    Piao, J.H.2    Nakajima, A.3    Sakon-Komazawa, S.4    Kojima, Y.5
  • 59
    • 80053179453 scopus 로고    scopus 로고
    • Mitochondrial Respiration Inhibitors Suppress Protein Translation and Hypoxic Signaling via the Hyperphosphorylation and Inactivation of Translation Initiation Factor eIF2alpha and Elongation Factor eEF2
    • Li J, Mahdi F, Du L, Datta S, Nagle DG, et al. (2011) Mitochondrial Respiration Inhibitors Suppress Protein Translation and Hypoxic Signaling via the Hyperphosphorylation and Inactivation of Translation Initiation Factor eIF2alpha and Elongation Factor eEF2. J Nat Prod 74: 1894-1901.
    • (2011) J Nat Prod , vol.74 , pp. 1894-1901
    • Li, J.1    Mahdi, F.2    Du, L.3    Datta, S.4    Nagle, D.G.5
  • 60
    • 57649221592 scopus 로고    scopus 로고
    • Hypoxic reactive oxygen species regulate the integrated stress response and cell survival
    • Liu L, Wise DR, Diehl JA, Simon MC, (2008) Hypoxic reactive oxygen species regulate the integrated stress response and cell survival. J Biol Chem 283: 31153-31162.
    • (2008) J Biol Chem , vol.283 , pp. 31153-31162
    • Liu, L.1    Wise, D.R.2    Diehl, J.A.3    Simon, M.C.4
  • 61
    • 0024437487 scopus 로고
    • Protein synthesis and protein phosphorylation during heat stress, recovery, and adaptation
    • Duncan RF, Hershey JW, (1989) Protein synthesis and protein phosphorylation during heat stress, recovery, and adaptation. J Cell Biol 109: 1467-1481.
    • (1989) J Cell Biol , vol.109 , pp. 1467-1481
    • Duncan, R.F.1    Hershey, J.W.2
  • 62
    • 0024797894 scopus 로고
    • Protein phosphorylation controls translation rates
    • Hershey JW, (1989) Protein phosphorylation controls translation rates. J Biol Chem 264: 20823-20826.
    • (1989) J Biol Chem , vol.264 , pp. 20823-20826
    • Hershey, J.W.1
  • 63
    • 32444433450 scopus 로고    scopus 로고
    • Hypoxia-induced energy stress regulates mRNA translation and cell growth
    • Liu L, Cash TP, Jones RG, Keith B, Thompson CB, et al. (2006) Hypoxia-induced energy stress regulates mRNA translation and cell growth. Mol Cell 21: 521-531.
    • (2006) Mol Cell , vol.21 , pp. 521-531
    • Liu, L.1    Cash, T.P.2    Jones, R.G.3    Keith, B.4    Thompson, C.B.5
  • 64
    • 77956706423 scopus 로고    scopus 로고
    • Phosphorylation of eIF2alpha at serine 51 is an important determinant of cell survival and adaptation to glucose deficiency
    • Muaddi H, Majumder M, Peidis P, Papadakis AI, Holcik M, et al. (2010) Phosphorylation of eIF2alpha at serine 51 is an important determinant of cell survival and adaptation to glucose deficiency. Mol Biol Cell 21: 3220-3231.
    • (2010) Mol Biol Cell , vol.21 , pp. 3220-3231
    • Muaddi, H.1    Majumder, M.2    Peidis, P.3    Papadakis, A.I.4    Holcik, M.5
  • 65
    • 78049314880 scopus 로고    scopus 로고
    • eIF2{alpha} Kinase PKR modulates the hypoxic response by Stat3-dependent transcriptional suppression of HIF-1{alpha}
    • Papadakis AI, Paraskeva E, Peidis P, Muaddi H, Li S, et al. (2010) eIF2{alpha} Kinase PKR modulates the hypoxic response by Stat3-dependent transcriptional suppression of HIF-1{alpha}. Cancer Res 70: 7820-7829.
    • (2010) Cancer Res , vol.70 , pp. 7820-7829
    • Papadakis, A.I.1    Paraskeva, E.2    Peidis, P.3    Muaddi, H.4    Li, S.5
  • 66
    • 0021993110 scopus 로고
    • Regional variation and differential sensitivity of rat heart protein synthesis in vivo and in vitro
    • Preedy VR, Smith DM, Kearney NF, Sugden PH, (1985) Regional variation and differential sensitivity of rat heart protein synthesis in vivo and in vitro. Biochem J 225: 487-492.
    • (1985) Biochem J , vol.225 , pp. 487-492
    • Preedy, V.R.1    Smith, D.M.2    Kearney, N.F.3    Sugden, P.H.4
  • 67
    • 0034973982 scopus 로고    scopus 로고
    • Translational control is required for the unfolded protein response and in vivo glucose homeostasis
    • Scheuner D, Song B, McEwen E, Liu C, Laybutt R, et al. (2001) Translational control is required for the unfolded protein response and in vivo glucose homeostasis. Mol Cell 7: 1165-1176.
    • (2001) Mol Cell , vol.7 , pp. 1165-1176
    • Scheuner, D.1    Song, B.2    McEwen, E.3    Liu, C.4    Laybutt, R.5
  • 68
    • 75749108288 scopus 로고    scopus 로고
    • Double-stranded RNA-dependent protein kinase links pathogen sensing with stress and metabolic homeostasis
    • Nakamura T, Furuhashi M, Li P, Cao H, Tuncman G, et al. (2010) Double-stranded RNA-dependent protein kinase links pathogen sensing with stress and metabolic homeostasis. Cell 140: 338-348.
    • (2010) Cell , vol.140 , pp. 338-348
    • Nakamura, T.1    Furuhashi, M.2    Li, P.3    Cao, H.4    Tuncman, G.5
  • 69
    • 8644282751 scopus 로고    scopus 로고
    • Translational repression mediates activation of nuclear factor kappa B by phosphorylated translation initiation factor 2
    • Deng J, Lu PD, Zhang Y, Scheuner D, Kaufman RJ, et al. (2004) Translational repression mediates activation of nuclear factor kappa B by phosphorylated translation initiation factor 2. Mol Cell Biol 24: 10161-10168.
    • (2004) Mol Cell Biol , vol.24 , pp. 10161-10168
    • Deng, J.1    Lu, P.D.2    Zhang, Y.3    Scheuner, D.4    Kaufman, R.J.5
  • 71
    • 0034574498 scopus 로고    scopus 로고
    • The ubiquitin-dependent proteolytic system and other potential targets for the modulation of nuclear factor-kB (NF-kB)
    • Magnani M, Crinelli R, Bianchi M, Antonelli A, (2000) The ubiquitin-dependent proteolytic system and other potential targets for the modulation of nuclear factor-kB (NF-kB). Curr Drug Targets 1: 387-399.
    • (2000) Curr Drug Targets , vol.1 , pp. 387-399
    • Magnani, M.1    Crinelli, R.2    Bianchi, M.3    Antonelli, A.4
  • 72
    • 1642564569 scopus 로고    scopus 로고
    • Regulation of p53 by Mdm2: fate is in the numbers
    • Shmueli A, Oren M, (2004) Regulation of p53 by Mdm2: fate is in the numbers. Mol Cell 13: 4-5.
    • (2004) Mol Cell , vol.13 , pp. 4-5
    • Shmueli, A.1    Oren, M.2
  • 73
    • 4544253996 scopus 로고    scopus 로고
    • Ultraviolet light activates NFkappaB through translational inhibition of IkappaBalpha synthesis
    • Wu S, Tan M, Hu Y, Wang JL, Scheuner D, et al. (2004) Ultraviolet light activates NFkappaB through translational inhibition of IkappaBalpha synthesis. J Biol Chem 279: 34898-34902.
    • (2004) J Biol Chem , vol.279 , pp. 34898-34902
    • Wu, S.1    Tan, M.2    Hu, Y.3    Wang, J.L.4    Scheuner, D.5
  • 74
    • 70749097815 scopus 로고    scopus 로고
    • Sodium and potassium urate crystals differ in their inflammatory potential
    • Schorn C, Janko C, Munoz L, Schulze C, Strysio M, et al. (2009) Sodium and potassium urate crystals differ in their inflammatory potential. Autoimmunity 42: 314-316.
    • (2009) Autoimmunity , vol.42 , pp. 314-316
    • Schorn, C.1    Janko, C.2    Munoz, L.3    Schulze, C.4    Strysio, M.5


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