메뉴 건너뛰기




Volumn 92, Issue , 2013, Pages 171-180

Actin carbonylation: From cell dysfunction to organism disorder

Author keywords

Actin; Cellular dysfunction; Cytoskeleton; Degenerative disorders; Proteasome; Protein carbonylation

Indexed keywords

ACROLEIN; ACTIN; ADVANCED GLYCATION END PRODUCT; MEVINOLIN; PROANTHOCYANIDIN; UBIQUITIN CONJUGATING ENZYME E2; UBIQUITIN PROTEIN LIGASE; UBIQUITIN PROTEIN LIGASE E3;

EID: 84886953660     PISSN: 18743919     EISSN: 18767737     Source Type: Journal    
DOI: 10.1016/j.jprot.2013.05.006     Document Type: Review
Times cited : (32)

References (120)
  • 1
    • 0142150051 scopus 로고    scopus 로고
    • Mitochondrial formation of reactive oxygen species
    • Turrens J.F. Mitochondrial formation of reactive oxygen species. J Physiol 2003, 552:335-344.
    • (2003) J Physiol , vol.552 , pp. 335-344
    • Turrens, J.F.1
  • 2
    • 0031721246 scopus 로고    scopus 로고
    • Localization at complex I and mechanism of the higher free radical production of brain nonsynaptic mitochondria in the short-lived rat than in the longevous pigeon
    • Barja G., Herrero A. Localization at complex I and mechanism of the higher free radical production of brain nonsynaptic mitochondria in the short-lived rat than in the longevous pigeon. J Bioenerg Biomembr 1998, 30:235-243.
    • (1998) J Bioenerg Biomembr , vol.30 , pp. 235-243
    • Barja, G.1    Herrero, A.2
  • 3
    • 4444268690 scopus 로고    scopus 로고
    • Mechanisms that regulate production of reactive oxygen species by cytochrome P450
    • Zangar R.C., Davydov D.R., Verma S. Mechanisms that regulate production of reactive oxygen species by cytochrome P450. Toxicol Appl Pharmacol 2004, 199:316-331.
    • (2004) Toxicol Appl Pharmacol , vol.199 , pp. 316-331
    • Zangar, R.C.1    Davydov, D.R.2    Verma, S.3
  • 5
    • 84859487532 scopus 로고    scopus 로고
    • Nitric oxide synthases: regulation and function
    • Förstermann U., Sessa W.C. Nitric oxide synthases: regulation and function. Eur Heart J 2012, 33:829-837.
    • (2012) Eur Heart J , vol.33 , pp. 829-837
    • Förstermann, U.1    Sessa, W.C.2
  • 7
    • 79952562826 scopus 로고    scopus 로고
    • Oxidative depolymerization of polysaccharides by reactive oxygen/nitrogen species
    • Duan J., Kasper D.L. Oxidative depolymerization of polysaccharides by reactive oxygen/nitrogen species. Glycobiology 2011, 21:401-409.
    • (2011) Glycobiology , vol.21 , pp. 401-409
    • Duan, J.1    Kasper, D.L.2
  • 9
    • 0034566190 scopus 로고    scopus 로고
    • Oxidative modifications of protein structures
    • Naskalski J.W., Bartosz G. Oxidative modifications of protein structures. Adv Clin Chem 2000, 35:161-253.
    • (2000) Adv Clin Chem , vol.35 , pp. 161-253
    • Naskalski, J.W.1    Bartosz, G.2
  • 10
    • 0030982143 scopus 로고    scopus 로고
    • Degradation of oxidized proteins in mammalian cells
    • Grune T., Reinheckel T., Davies K.J. Degradation of oxidized proteins in mammalian cells. FASEB J 1997, 11:526-534.
    • (1997) FASEB J , vol.11 , pp. 526-534
    • Grune, T.1    Reinheckel, T.2    Davies, K.J.3
  • 12
    • 84855217371 scopus 로고    scopus 로고
    • Protein oxidative modification in the aging organism and the role of the ubiquitin proteasomal system
    • Kastle M., Grune T. Protein oxidative modification in the aging organism and the role of the ubiquitin proteasomal system. Curr Pharm Des 2011, 17:4007-4022.
    • (2011) Curr Pharm Des , vol.17 , pp. 4007-4022
    • Kastle, M.1    Grune, T.2
  • 14
    • 0034798361 scopus 로고    scopus 로고
    • Protein oxidation and 20S proteasome-dependent proteolysis in mammalian cells
    • Shringarpure R., Grune T., Davies K.J. Protein oxidation and 20S proteasome-dependent proteolysis in mammalian cells. Cell Mol Life Sci 2001, 58:1442-1450.
    • (2001) Cell Mol Life Sci , vol.58 , pp. 1442-1450
    • Shringarpure, R.1    Grune, T.2    Davies, K.J.3
  • 16
    • 0036591853 scopus 로고    scopus 로고
    • Protein turnover by the proteasome in aging and disease
    • Shringarpure R., Davies K.J.A. Protein turnover by the proteasome in aging and disease. Free Radic Biol Med 2002, 32:1084-1089.
    • (2002) Free Radic Biol Med , vol.32 , pp. 1084-1089
    • Shringarpure, R.1    Davies, K.J.A.2
  • 18
    • 17844403545 scopus 로고    scopus 로고
    • Role of oxidative carbonylation in protein quality control and senescence
    • Nystrom T. Role of oxidative carbonylation in protein quality control and senescence. EMBO J 2005, 24:1311-1317.
    • (2005) EMBO J , vol.24 , pp. 1311-1317
    • Nystrom, T.1
  • 19
    • 80053041158 scopus 로고    scopus 로고
    • Protein carbonylation and metal-catalyzed protein oxidation in a cellular perspective
    • Møller I.M., Rogowska-Wrzesinska A., Rao R.S.P. Protein carbonylation and metal-catalyzed protein oxidation in a cellular perspective. J Proteomics 2011, 74:2228-2242.
    • (2011) J Proteomics , vol.74 , pp. 2228-2242
    • Møller, I.M.1    Rogowska-Wrzesinska, A.2    Rao, R.S.P.3
  • 21
    • 0038239701 scopus 로고    scopus 로고
    • Selective degradation of oxidatively modified protein substrates by the proteasome
    • Grune T., Merker K., Sandig G., Davies K.J.A. Selective degradation of oxidatively modified protein substrates by the proteasome. Biochem Biophys Res Commun 2003, 305:709-718.
    • (2003) Biochem Biophys Res Commun , vol.305 , pp. 709-718
    • Grune, T.1    Merker, K.2    Sandig, G.3    Davies, K.J.A.4
  • 22
    • 4344677922 scopus 로고    scopus 로고
    • Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and 'aggresomes' during oxidative stress, aging, and disease
    • Grune T., Jung T., Merker K., Davies K.J.A. Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and 'aggresomes' during oxidative stress, aging, and disease. Int J Biochem Cell Biol 2004, 36:2519-2530.
    • (2004) Int J Biochem Cell Biol , vol.36 , pp. 2519-2530
    • Grune, T.1    Jung, T.2    Merker, K.3    Davies, K.J.A.4
  • 23
    • 79955703833 scopus 로고    scopus 로고
    • Microscopic analysis of protein oxidative damage: effect of carbonylation on structure, dynamics, and aggregability of villin headpiece
    • Petrov D., Zagrovic B. Microscopic analysis of protein oxidative damage: effect of carbonylation on structure, dynamics, and aggregability of villin headpiece. J Am Chem Soc 2011, 133:7016-7024.
    • (2011) J Am Chem Soc , vol.133 , pp. 7016-7024
    • Petrov, D.1    Zagrovic, B.2
  • 25
    • 84867347561 scopus 로고    scopus 로고
    • Lipofuscin is formed independently of macroautophagy and lysosomal activity in stress-induced prematurely senescent human fibroblasts
    • Höhn A., Sittig A., Jung T., Grimm S., Grune T. Lipofuscin is formed independently of macroautophagy and lysosomal activity in stress-induced prematurely senescent human fibroblasts. Free Radic Biol Med 2012, 53:1760-1769.
    • (2012) Free Radic Biol Med , vol.53 , pp. 1760-1769
    • Höhn, A.1    Sittig, A.2    Jung, T.3    Grimm, S.4    Grune, T.5
  • 26
    • 0036793581 scopus 로고    scopus 로고
    • Ezrin turnover and cell shape changes catalyzed by proteasome in oxidatively stressed cells
    • Grune T., Reinheckel T., Ja North, Li R., Pb Bescos, Shringarpure R., et al. Ezrin turnover and cell shape changes catalyzed by proteasome in oxidatively stressed cells. FASEB J 2002, 16:1602-1610.
    • (2002) FASEB J , vol.16 , pp. 1602-1610
    • Grune, T.1    Reinheckel, T.2    Ja, N.3    Li, R.4    Pb, B.5    Shringarpure, R.6
  • 27
    • 34548170503 scopus 로고    scopus 로고
    • Vimentin is the specific target in skin glycation. Structural prerequisites, functional consequences, and role in skin aging
    • Kueper T., Grune T., Prahl S., Lenz H., Welge V., Biernoth T., et al. Vimentin is the specific target in skin glycation. Structural prerequisites, functional consequences, and role in skin aging. J Biol Chem 2007, 282:23427-23436.
    • (2007) J Biol Chem , vol.282 , pp. 23427-23436
    • Kueper, T.1    Grune, T.2    Prahl, S.3    Lenz, H.4    Welge, V.5    Biernoth, T.6
  • 29
    • 0034117954 scopus 로고    scopus 로고
    • Protein oxidation and degradation during proliferative senescence of human MRC-5 fibroblasts
    • Sitte N., Merker K., von Zglinicki T., Grune T. Protein oxidation and degradation during proliferative senescence of human MRC-5 fibroblasts. Free Radic Biol Med 2000, 28:701-708.
    • (2000) Free Radic Biol Med , vol.28 , pp. 701-708
    • Sitte, N.1    Merker, K.2    von Zglinicki, T.3    Grune, T.4
  • 30
    • 0034571026 scopus 로고    scopus 로고
    • Oxidative stress, aging and the proteasomal system
    • Grune T. Oxidative stress, aging and the proteasomal system. Biogerontology 2000, 1:31-40.
    • (2000) Biogerontology , vol.1 , pp. 31-40
    • Grune, T.1
  • 31
    • 0033870001 scopus 로고    scopus 로고
    • Proteasome inhibition by lipofuscin/ceroid during postmitotic aging of fibroblasts
    • Sitte N., Huber M., Grune T., Ladhoff A., Doecke W.D., Von Zglinicki T., et al. Proteasome inhibition by lipofuscin/ceroid during postmitotic aging of fibroblasts. FASEB J 2000, 14:1490-1498.
    • (2000) FASEB J , vol.14 , pp. 1490-1498
    • Sitte, N.1    Huber, M.2    Grune, T.3    Ladhoff, A.4    Doecke, W.D.5    Von Zglinicki, T.6
  • 32
    • 0033712579 scopus 로고    scopus 로고
    • 4-Hydroxynonenal-modified amyloid-beta peptide inhibits the proteasome: possible importance in Alzheimer's disease
    • Shringarpure R., Grune T., Sitte N., Davies K.J. 4-Hydroxynonenal-modified amyloid-beta peptide inhibits the proteasome: possible importance in Alzheimer's disease. Cell Mol Life Sci 2000, 57:1802-1809.
    • (2000) Cell Mol Life Sci , vol.57 , pp. 1802-1809
    • Shringarpure, R.1    Grune, T.2    Sitte, N.3    Davies, K.J.4
  • 33
    • 0029563691 scopus 로고
    • Lipofuscin in bovine muscle and brain: a model for studying age pigment
    • Jolly R.D., Douglas B.V., Davey P.M., Roiri J.E. Lipofuscin in bovine muscle and brain: a model for studying age pigment. Gerontology 1995, 41(Suppl. 2):283-295.
    • (1995) Gerontology , vol.41 , Issue.SUPPL. 2 , pp. 283-295
    • Jolly, R.D.1    Douglas, B.V.2    Davey, P.M.3    Roiri, J.E.4
  • 34
    • 77950519040 scopus 로고    scopus 로고
    • Lipofuscin-bound iron is a major intracellular source of oxidants: role in senescent cells
    • Hohn A., Jung T., Grimm S., Grune T. Lipofuscin-bound iron is a major intracellular source of oxidants: role in senescent cells. Free Radic Biol Med 2010, 48:1100-1108.
    • (2010) Free Radic Biol Med , vol.48 , pp. 1100-1108
    • Hohn, A.1    Jung, T.2    Grimm, S.3    Grune, T.4
  • 35
    • 71049176929 scopus 로고    scopus 로고
    • The proteasome is an integral part of solar ultraviolet a radiation-induced gene expression
    • Catalgol B., Ziaja I., Breusing N., Jung T., Hohn A., Alpertunga B., et al. The proteasome is an integral part of solar ultraviolet a radiation-induced gene expression. J Biol Chem 2009, 284:30076-30086.
    • (2009) J Biol Chem , vol.284 , pp. 30076-30086
    • Catalgol, B.1    Ziaja, I.2    Breusing, N.3    Jung, T.4    Hohn, A.5    Alpertunga, B.6
  • 36
    • 84868639366 scopus 로고    scopus 로고
    • Histone deacetylase 6 (HDAC6) plays a crucial role in p38MAPK-dependent induction of heme oxygenase-1 (HO-1) in response to proteasome inhibition
    • Kästle M., Woschee E., Grune T. Histone deacetylase 6 (HDAC6) plays a crucial role in p38MAPK-dependent induction of heme oxygenase-1 (HO-1) in response to proteasome inhibition. Free Radic Biol Med 2012, 53:2092-2101.
    • (2012) Free Radic Biol Med , vol.53 , pp. 2092-2101
    • Kästle, M.1    Woschee, E.2    Grune, T.3
  • 37
    • 78650348130 scopus 로고    scopus 로고
    • Conformational dynamics of actin: effectors and implications for biological function
    • Hild G., Bugyi B., Nyitrai M. Conformational dynamics of actin: effectors and implications for biological function. Cytoskeleton 2010, 67:609-629.
    • (2010) Cytoskeleton , vol.67 , pp. 609-629
    • Hild, G.1    Bugyi, B.2    Nyitrai, M.3
  • 38
    • 0035937396 scopus 로고    scopus 로고
    • Control of cell shape in bacteria: helical, actin-like filaments in Bacillus subtilis
    • Jones L.J.F., Carballido-López R., Errington J. Control of cell shape in bacteria: helical, actin-like filaments in Bacillus subtilis. Cell 2001, 104:913-922.
    • (2001) Cell , vol.104 , pp. 913-922
    • Jones, L.J.F.1    Carballido-López, R.2    Errington, J.3
  • 39
    • 70849098888 scopus 로고    scopus 로고
    • Actin, a central player in cell shape and movement
    • Pollard T.D., Cooper J.A. Actin, a central player in cell shape and movement. Science 2009, 326:1208-1212.
    • (2009) Science , vol.326 , pp. 1208-1212
    • Pollard, T.D.1    Cooper, J.A.2
  • 41
    • 0031571664 scopus 로고    scopus 로고
    • Modulation of yeast F-actin structure by a mutation in the nucleotide-binding cleft
    • Orlova A., Chen X., Rubenstein P.A., Egelman E.H. Modulation of yeast F-actin structure by a mutation in the nucleotide-binding cleft. J Mol Biol 1997, 271:235-243.
    • (1997) J Mol Biol , vol.271 , pp. 235-243
    • Orlova, A.1    Chen, X.2    Rubenstein, P.A.3    Egelman, E.H.4
  • 42
    • 0035500775 scopus 로고    scopus 로고
    • Actin carbonylation: from a simple marker of protein oxidation to relevant signs of severe functional impairment
    • Dalle-Donne I., Rossi R., Giustarini D., Gagliano N., Lusini L., Milzani A., et al. Actin carbonylation: from a simple marker of protein oxidation to relevant signs of severe functional impairment. Free Radic Biol Med 2001, 31:1075-1083.
    • (2001) Free Radic Biol Med , vol.31 , pp. 1075-1083
    • Dalle-Donne, I.1    Rossi, R.2    Giustarini, D.3    Gagliano, N.4    Lusini, L.5    Milzani, A.6
  • 44
  • 46
    • 84855175402 scopus 로고    scopus 로고
    • The cyclophosphamide metabolite, acrolein, induces cytoskeletal changes and oxidative stress in Sertoli cells
    • Liu F., Li X.L., Lin T., He D.W., Wei G.H., Liu J.H., et al. The cyclophosphamide metabolite, acrolein, induces cytoskeletal changes and oxidative stress in Sertoli cells. Mol Biol Rep 2012, 39:493-500.
    • (2012) Mol Biol Rep , vol.39 , pp. 493-500
    • Liu, F.1    Li, X.L.2    Lin, T.3    He, D.W.4    Wei, G.H.5    Liu, J.H.6
  • 47
    • 1342304174 scopus 로고    scopus 로고
    • Evidence of myofibrillar protein oxidation induced by postischemic reperfusion in isolated rat hearts
    • Canton M., Neverova I., Menabò R., Van Eyk J., Di Lisa F. Evidence of myofibrillar protein oxidation induced by postischemic reperfusion in isolated rat hearts. Am J Physiol Heart Circ Physiol 2004, 286:H870-H877.
    • (2004) Am J Physiol Heart Circ Physiol , vol.286
    • Canton, M.1    Neverova, I.2    Menabò, R.3    Van Eyk, J.4    Di Lisa, F.5
  • 48
    • 84864448289 scopus 로고    scopus 로고
    • Carbonylation of the cytoskeletal protein actin leads to aggregate formation
    • Castro J.P., Ott C., Jung T., Grune T., Almeida H. Carbonylation of the cytoskeletal protein actin leads to aggregate formation. Free Radic Biol Med 2012, 53:916-925.
    • (2012) Free Radic Biol Med , vol.53 , pp. 916-925
    • Castro, J.P.1    Ott, C.2    Jung, T.3    Grune, T.4    Almeida, H.5
  • 49
  • 51
    • 0036970951 scopus 로고    scopus 로고
    • Numerous proteins in mammalian cells are prone to iron-dependent oxidation and proteasomal degradation
    • Drake S.K., Bourdon E., Wehr N.B., Levine R.L., Backlund P.S., Yergey A.L., et al. Numerous proteins in mammalian cells are prone to iron-dependent oxidation and proteasomal degradation. Dev Neurosci 2002, 24:114-124.
    • (2002) Dev Neurosci , vol.24 , pp. 114-124
    • Drake, S.K.1    Bourdon, E.2    Wehr, N.B.3    Levine, R.L.4    Backlund, P.S.5    Yergey, A.L.6
  • 52
    • 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 2002, 99:3505-3510.
    • (2002) Proc Natl Acad Sci , vol.99 , pp. 3505-3510
    • Fratelli, M.1    Demol, H.2    Puype, M.3    Casagrande, S.4    Eberini, I.5    Salmona, M.6
  • 53
    • 2942586687 scopus 로고    scopus 로고
    • Identification of specific oxidatively modified proteins in chicken muscles using a combined immunologic and proteomic approach
    • Stagsted J., Bendixen E., Andersen H.J. Identification of specific oxidatively modified proteins in chicken muscles using a combined immunologic and proteomic approach. J Agric Food Chem 2004, 52:3967-3974.
    • (2004) J Agric Food Chem , vol.52 , pp. 3967-3974
    • Stagsted, J.1    Bendixen, E.2    Andersen, H.J.3
  • 54
    • 66749115646 scopus 로고    scopus 로고
    • Oats supplementation prevents alcohol-induced gut leakiness in rats by preventing alcohol-induced oxidative tissue damage
    • Tang Y., Forsyth C.B., Banan A., Fields J.Z., Keshavarzian A. Oats supplementation prevents alcohol-induced gut leakiness in rats by preventing alcohol-induced oxidative tissue damage. J Pharmacol Exp Ther 2009, 329:952-958.
    • (2009) J Pharmacol Exp Ther , vol.329 , pp. 952-958
    • Tang, Y.1    Forsyth, C.B.2    Banan, A.3    Fields, J.Z.4    Keshavarzian, A.5
  • 55
    • 60849109931 scopus 로고    scopus 로고
    • Hop proanthocyanidins induce apoptosis, protein carbonylation, and cytoskeleton disorganization in human colorectal adenocarcinoma cells via reactive oxygen species
    • Chung W.-G., Miranda C.L., Stevens J.F., Maier C.S. Hop proanthocyanidins induce apoptosis, protein carbonylation, and cytoskeleton disorganization in human colorectal adenocarcinoma cells via reactive oxygen species. Food Chem Toxicol 2009, 47:827-836.
    • (2009) Food Chem Toxicol , vol.47 , pp. 827-836
    • Chung, W.-G.1    Miranda, C.L.2    Stevens, J.F.3    Maier, C.S.4
  • 56
    • 0034069867 scopus 로고    scopus 로고
    • Carbonylation and disassembly of the F-actin cytoskeleton in oxidant induced barrier dysfunction and its prevention by epidermal growth factor and transforming growth factor α in a human colonic cell line
    • Banan A., Zhang Y., Losurdo J., Keshavarzian A. Carbonylation and disassembly of the F-actin cytoskeleton in oxidant induced barrier dysfunction and its prevention by epidermal growth factor and transforming growth factor α in a human colonic cell line. Gut 2000, 46:830-837.
    • (2000) Gut , vol.46 , pp. 830-837
    • Banan, A.1    Zhang, Y.2    Losurdo, J.3    Keshavarzian, A.4
  • 57
    • 67349164761 scopus 로고    scopus 로고
    • Proinflammatory cytokines provoke oxidative damage to actin in neuronal cells mediated by Rac1 and NADPH oxidase
    • Barth B.M., Stewart-Smeets S., Kuhn T.B. Proinflammatory cytokines provoke oxidative damage to actin in neuronal cells mediated by Rac1 and NADPH oxidase. Mol Cell Neurosci 2009, 41:274-285.
    • (2009) Mol Cell Neurosci , vol.41 , pp. 274-285
    • Barth, B.M.1    Stewart-Smeets, S.2    Kuhn, T.B.3
  • 58
    • 79960588383 scopus 로고    scopus 로고
    • Fish proteins as targets of ferrous-catalyzed oxidation: identification of protein carbonyls by fluorescent labeling on two-dimensional gels and MALDI-TOF/TOF mass spectrometry
    • Pazos M., da Rocha A.P., Roepstorff P., Rogowska-Wrzesinska A. Fish proteins as targets of ferrous-catalyzed oxidation: identification of protein carbonyls by fluorescent labeling on two-dimensional gels and MALDI-TOF/TOF mass spectrometry. J Agric Food Chem 2011, 59:7962-7977.
    • (2011) J Agric Food Chem , vol.59 , pp. 7962-7977
    • Pazos, M.1    da Rocha, A.P.2    Roepstorff, P.3    Rogowska-Wrzesinska, A.4
  • 59
    • 20444397400 scopus 로고    scopus 로고
    • Carbonylation and glutathionylation of proteins in the blue mussel Mytilus edulis detected by proteomic analysis and Western blotting: actin as a target for oxidative stress
    • McDonagh B., Tyther R., Sheehan D. Carbonylation and glutathionylation of proteins in the blue mussel Mytilus edulis detected by proteomic analysis and Western blotting: actin as a target for oxidative stress. Aquat Toxicol 2005, 73:315-326.
    • (2005) Aquat Toxicol , vol.73 , pp. 315-326
    • McDonagh, B.1    Tyther, R.2    Sheehan, D.3
  • 60
    • 80054862721 scopus 로고    scopus 로고
    • Identification of serum stress biomarkers in pigs housed at different stocking densities
    • Marco-Ramell A., Pato R., Peña R., Saco Y., Manteca X., Ruiz de la Torre J.L., et al. Identification of serum stress biomarkers in pigs housed at different stocking densities. Vet J 2011, 190:e66-e71.
    • (2011) Vet J , vol.190
    • Marco-Ramell, A.1    Pato, R.2    Peña, R.3    Saco, Y.4    Manteca, X.5    Ruiz de la Torre, J.L.6
  • 61
    • 0020079283 scopus 로고
    • Decreased actin content of lymphocytes from patients with chronic lymphocytic leukemia
    • Stark R., Liebes L., Nevrla D., Conklyn M., Silber R. Decreased actin content of lymphocytes from patients with chronic lymphocytic leukemia. Blood 1982, 59:536-541.
    • (1982) Blood , vol.59 , pp. 536-541
    • Stark, R.1    Liebes, L.2    Nevrla, D.3    Conklyn, M.4    Silber, R.5
  • 62
    • 0019306105 scopus 로고
    • Changes in contractile proteins during differentiation of myeloid leukemia cells. I. Polymerization of actin
    • Nagata K., Sagara J., Ichikawa Y. Changes in contractile proteins during differentiation of myeloid leukemia cells. I. Polymerization of actin. J Cell Biol 1980, 85:273-282.
    • (1980) J Cell Biol , vol.85 , pp. 273-282
    • Nagata, K.1    Sagara, J.2    Ichikawa, Y.3
  • 63
    • 0019794183 scopus 로고
    • Regulation of actin in rat adrenocortical cells by corticotropin
    • Cheitlin R., Ramachandran J. Regulation of actin in rat adrenocortical cells by corticotropin. J Biol Chem 1981, 256:3156-3158.
    • (1981) J Biol Chem , vol.256 , pp. 3156-3158
    • Cheitlin, R.1    Ramachandran, J.2
  • 64
    • 0016837839 scopus 로고
    • The actin content of fibroblasts
    • Bray D., Thomas C. The actin content of fibroblasts. Biochem J 1975, 147:221-228.
    • (1975) Biochem J , vol.147 , pp. 221-228
    • Bray, D.1    Thomas, C.2
  • 65
    • 33846025822 scopus 로고    scopus 로고
    • Identification of yeast oxidized proteins: chromatographic top-down approach for identification of carbonylated, fragmented and cross-linked proteins in yeast
    • Mirzaei H., Regnier F. Identification of yeast oxidized proteins: chromatographic top-down approach for identification of carbonylated, fragmented and cross-linked proteins in yeast. J Chromatogr A 2007, 1141:22-31.
    • (2007) J Chromatogr A , vol.1141 , pp. 22-31
    • Mirzaei, H.1    Regnier, F.2
  • 66
    • 0032579371 scopus 로고    scopus 로고
    • Identification of the major oxidatively damaged proteins in Escherichia coli cells exposed to oxidative stress
    • Tamarit J., Cabiscol E., Ros J. Identification of the major oxidatively damaged proteins in Escherichia coli cells exposed to oxidative stress. J Biol Chem 1998, 273:3027-3032.
    • (1998) J Biol Chem , vol.273 , pp. 3027-3032
    • Tamarit, J.1    Cabiscol, E.2    Ros, J.3
  • 67
    • 59649127414 scopus 로고    scopus 로고
    • Methionine in proteins defends against oxidative stress
    • Luo S., Levine R.L. Methionine in proteins defends against oxidative stress. FASEB J 2009, 23:464-472.
    • (2009) FASEB J , vol.23 , pp. 464-472
    • Luo, S.1    Levine, R.L.2
  • 68
    • 0035890871 scopus 로고    scopus 로고
    • Selectivity of protein oxidative damage during aging in Drosophila melanogaster
    • Das N., Levine R.L., Orr W.C., Sohal R.S. Selectivity of protein oxidative damage during aging in Drosophila melanogaster. Biochem J 2001, 360:209-216.
    • (2001) Biochem J , vol.360 , pp. 209-216
    • Das, N.1    Levine, R.L.2    Orr, W.C.3    Sohal, R.S.4
  • 69
    • 0034635188 scopus 로고    scopus 로고
    • Cross-linked dimers with nucleating activity in actin prepared from muscle acetone powder
    • Selden L.A., Kinosian H.J., Estes J.E., Gershman L.C. Cross-linked dimers with nucleating activity in actin prepared from muscle acetone powder. Biochemistry 1999, 39:64-74.
    • (1999) Biochemistry , vol.39 , pp. 64-74
    • Selden, L.A.1    Kinosian, H.J.2    Estes, J.E.3    Gershman, L.C.4
  • 70
    • 33846148665 scopus 로고    scopus 로고
    • Identification of carbonylated protein in frozen rainbow trout (Oncorhynchus mykiss) fillets and development of protein oxidation during frozen storage
    • Nørrelykke M.R., Baron C.P., Jessen F. Identification of carbonylated protein in frozen rainbow trout (Oncorhynchus mykiss) fillets and development of protein oxidation during frozen storage. J Agric Food Chem 2006, 54:9437-9446.
    • (2006) J Agric Food Chem , vol.54 , pp. 9437-9446
    • Nørrelykke, M.R.1    Baron, C.P.2    Jessen, F.3
  • 71
    • 0031738101 scopus 로고    scopus 로고
    • Severing of F-actin by the amino-terminal half of gelsolin suggests internal cooperativity in gelsolin
    • Selden L.A., Kinosian H.J., Newman J., Lincoln B., Hurwitz C., Gershman L.C., et al. Severing of F-actin by the amino-terminal half of gelsolin suggests internal cooperativity in gelsolin. Biophys J 1998, 75:3092-3100.
    • (1998) Biophys J , vol.75 , pp. 3092-3100
    • Selden, L.A.1    Kinosian, H.J.2    Newman, J.3    Lincoln, B.4    Hurwitz, C.5    Gershman, L.C.6
  • 72
    • 9244235016 scopus 로고    scopus 로고
    • Cytoskeletal actin degradation induced by lovastatin in cardiomyocytes is mediated through caspase-2
    • Kong J.Y., Rabkin S.W. Cytoskeletal actin degradation induced by lovastatin in cardiomyocytes is mediated through caspase-2. Cell Biol Int 2004, 28:781-790.
    • (2004) Cell Biol Int , vol.28 , pp. 781-790
    • Kong, J.Y.1    Rabkin, S.W.2
  • 73
    • 0027272193 scopus 로고
    • Contractile activity modulates actin synthesis and turnover in cultured neonatal rat heart cells
    • Sharp W.W., Terracio L., Borg T.K., Samarel A.M. Contractile activity modulates actin synthesis and turnover in cultured neonatal rat heart cells. Circ Res 1993, 73:172-183.
    • (1993) Circ Res , vol.73 , pp. 172-183
    • Sharp, W.W.1    Terracio, L.2    Borg, T.K.3    Samarel, A.M.4
  • 74
    • 27644438336 scopus 로고    scopus 로고
    • Trim32 is a ubiquitin ligase mutated in limb girdle muscular dystrophy type 2H that binds to skeletal muscle myosin and ubiquitinates actin
    • Kudryashova E., Kudryashov D., Kramerova I., Spencer M.J. Trim32 is a ubiquitin ligase mutated in limb girdle muscular dystrophy type 2H that binds to skeletal muscle myosin and ubiquitinates actin. J Mol Biol 2005, 354:413-424.
    • (2005) J Mol Biol , vol.354 , pp. 413-424
    • Kudryashova, E.1    Kudryashov, D.2    Kramerova, I.3    Spencer, M.J.4
  • 75
    • 0028912676 scopus 로고
    • Proteolysis in cultured liver epithelial cells during oxidative stress: role of the multicatalytic proteinase complex, proteasome
    • Grune T., Reinheckel T., Joshi M., Davies K.J.A. Proteolysis in cultured liver epithelial cells during oxidative stress: role of the multicatalytic proteinase complex, proteasome. J Biol Chem 1995, 270:2344-2351.
    • (1995) J Biol Chem , vol.270 , pp. 2344-2351
    • Grune, T.1    Reinheckel, T.2    Joshi, M.3    Davies, K.J.A.4
  • 76
    • 0029984892 scopus 로고    scopus 로고
    • Degradation of oxidized proteins in K562 human hematopoietic cells by proteasome
    • Grune T., Reinheckel T., Davies K.J.A. Degradation of oxidized proteins in K562 human hematopoietic cells by proteasome. J Biol Chem 1996, 271:15504-15509.
    • (1996) J Biol Chem , vol.271 , pp. 15504-15509
    • Grune, T.1    Reinheckel, T.2    Davies, K.J.A.3
  • 77
    • 33644859926 scopus 로고    scopus 로고
    • Preferential degradation of oxidized proteins by the 20S proteasome may be inhibited in aging and in inflammatory neuromuscular diseases
    • Davies K.J., Shringarpure R. Preferential degradation of oxidized proteins by the 20S proteasome may be inhibited in aging and in inflammatory neuromuscular diseases. Neurology 2006, 66:S93-S96.
    • (2006) Neurology , vol.66
    • Davies, K.J.1    Shringarpure, R.2
  • 80
    • 0033033698 scopus 로고    scopus 로고
    • Poly-ADP ribose polymerase activates nuclear proteasome to degrade oxidatively damaged histones
    • Ullrich O., Reinheckel T., Sitte N., Hass R., Grune T., Davies K.J.A. Poly-ADP ribose polymerase activates nuclear proteasome to degrade oxidatively damaged histones. Proc Natl Acad Sci 1999, 96:6223-6228.
    • (1999) Proc Natl Acad Sci , vol.96 , pp. 6223-6228
    • Ullrich, O.1    Reinheckel, T.2    Sitte, N.3    Hass, R.4    Grune, T.5    Davies, K.J.A.6
  • 81
    • 79955063530 scopus 로고    scopus 로고
    • Proteins bearing oxidation-induced carbonyl groups are not preferentially ubiquitinated
    • Kästle M., Grune T. Proteins bearing oxidation-induced carbonyl groups are not preferentially ubiquitinated. Biochimie 2011, 93:1076-1079.
    • (2011) Biochimie , vol.93 , pp. 1076-1079
    • Kästle, M.1    Grune, T.2
  • 82
    • 84866389666 scopus 로고    scopus 로고
    • Chaperones, but not oxidized proteins, are ubiquitinated after oxidative stress
    • Kästle M., Reeg S., Rogowska-Wrzesinska A., Grune T. Chaperones, but not oxidized proteins, are ubiquitinated after oxidative stress. Free Radic Biol Med 2012, 53:1468-1477.
    • (2012) Free Radic Biol Med , vol.53 , pp. 1468-1477
    • Kästle, M.1    Reeg, S.2    Rogowska-Wrzesinska, A.3    Grune, T.4
  • 83
    • 0032212875 scopus 로고    scopus 로고
    • Comparative resistance of the 20S and 26S proteasome to oxidative stress
    • Reinheckel T., Sitte N., Ullrich O., Kuckelkorn U., Davies K.J., Grune T. Comparative resistance of the 20S and 26S proteasome to oxidative stress. Biochem J 1998, 335(Pt 3):637-642.
    • (1998) Biochem J , vol.335 , Issue.PART 3 , pp. 637-642
    • Reinheckel, T.1    Sitte, N.2    Ullrich, O.3    Kuckelkorn, U.4    Davies, K.J.5    Grune, T.6
  • 84
    • 0037414834 scopus 로고    scopus 로고
    • Ubiquitin conjugation is not required for the degradation of oxidized proteins by proteasome
    • Shringarpure R., Grune T., Mehlhase J., Davies K.J.A. Ubiquitin conjugation is not required for the degradation of oxidized proteins by proteasome. J Biol Chem 2003, 278:311-318.
    • (2003) J Biol Chem , vol.278 , pp. 311-318
    • Shringarpure, R.1    Grune, T.2    Mehlhase, J.3    Davies, K.J.A.4
  • 85
    • 79959534486 scopus 로고    scopus 로고
    • Oxidative protein damage and the proteasome
    • Grimm S., Hohn A., Grune T. Oxidative protein damage and the proteasome. Amino Acids 2012, 42:23-38.
    • (2012) Amino Acids , vol.42 , pp. 23-38
    • Grimm, S.1    Hohn, A.2    Grune, T.3
  • 87
    • 28744453336 scopus 로고    scopus 로고
    • Proteasome mediates removal of proteins oxidized during myocardial ischemia
    • Divald A., Powell S.R. Proteasome mediates removal of proteins oxidized during myocardial ischemia. Free Radic Biol Med 2006, 40:156-164.
    • (2006) Free Radic Biol Med , vol.40 , pp. 156-164
    • Divald, A.1    Powell, S.R.2
  • 89
    • 0033592425 scopus 로고    scopus 로고
    • The tert-butyl hydroperoxide-induced oxidation of actin Cys-374 is coupled with structural changes in distant regions of the protein
    • DalleDonne I., Milzani A., Colombo R. The tert-butyl hydroperoxide-induced oxidation of actin Cys-374 is coupled with structural changes in distant regions of the protein. Biochemistry 1999, 38:12471-12480.
    • (1999) Biochemistry , vol.38 , pp. 12471-12480
    • DalleDonne, I.1    Milzani, A.2    Colombo, R.3
  • 90
    • 0033673408 scopus 로고    scopus 로고
    • Protein oxidation and degradation during cellular senescence of human BJ fibroblasts: part I-effects of proliferative senescence
    • Sitte N., Merker K., Von Zglinicki T., Grune T., Davies K.J. Protein oxidation and degradation during cellular senescence of human BJ fibroblasts: part I-effects of proliferative senescence. FASEB J 2000, 14:2495-2502.
    • (2000) FASEB J , vol.14 , pp. 2495-2502
    • Sitte, N.1    Merker, K.2    Von Zglinicki, T.3    Grune, T.4    Davies, K.J.5
  • 91
    • 0033674181 scopus 로고    scopus 로고
    • Protein oxidation and degradation during cellular senescence of human BJ fibroblasts: part II-aging of nondividing cells
    • Sitte N., Merker K., Von Zglinicki T., Davies K.J., Grune T. Protein oxidation and degradation during cellular senescence of human BJ fibroblasts: part II-aging of nondividing cells. FASEB J 2000, 14:2503-2510.
    • (2000) FASEB J , vol.14 , pp. 2503-2510
    • Sitte, N.1    Merker, K.2    Von Zglinicki, T.3    Davies, K.J.4    Grune, T.5
  • 92
    • 59849107267 scopus 로고    scopus 로고
    • Age-related differences in oxidative protein-damage in young and senescent fibroblasts
    • Jung T., Hohn A., Catalgol B., Grune T. Age-related differences in oxidative protein-damage in young and senescent fibroblasts. Arch Biochem Biophys 2009, 483:127-135.
    • (2009) Arch Biochem Biophys , vol.483 , pp. 127-135
    • Jung, T.1    Hohn, A.2    Catalgol, B.3    Grune, T.4
  • 93
    • 71849099982 scopus 로고    scopus 로고
    • Inverse correlation of protein oxidation and proteasome activity in liver and lung
    • Breusing N., Arndt J., Voss P., Bresgen N., Wiswedel I., Gardemann A., et al. Inverse correlation of protein oxidation and proteasome activity in liver and lung. Mech Ageing Dev 2009, 130:748-753.
    • (2009) Mech Ageing Dev , vol.130 , pp. 748-753
    • Breusing, N.1    Arndt, J.2    Voss, P.3    Bresgen, N.4    Wiswedel, I.5    Gardemann, A.6
  • 94
    • 0034891783 scopus 로고    scopus 로고
    • Oxidative modification of proteins during aging
    • Levine R.L., Stadtman E.R. Oxidative modification of proteins during aging. Exp Gerontol 2001, 36:1495-1502.
    • (2001) Exp Gerontol , vol.36 , pp. 1495-1502
    • Levine, R.L.1    Stadtman, E.R.2
  • 95
    • 71349088664 scopus 로고    scopus 로고
    • About "origin and evolution of the free radical theory of aging: a brief personal history, 1954-2009"
    • Harman D. About "origin and evolution of the free radical theory of aging: a brief personal history, 1954-2009". Biogerontology 2009, 10:783.
    • (2009) Biogerontology , vol.10 , pp. 783
    • Harman, D.1
  • 96
    • 33646517324 scopus 로고    scopus 로고
    • Quantitative proteomics analysis of differential protein expression and oxidative modification of specific proteins in the brains of old mice
    • Poon H.F., Vaishnav R.A., Getchell T.V., Getchell M.L., Butterfield D.A. Quantitative proteomics analysis of differential protein expression and oxidative modification of specific proteins in the brains of old mice. Neurobiol Aging 2006, 27:1010-1019.
    • (2006) Neurobiol Aging , vol.27 , pp. 1010-1019
    • Poon, H.F.1    Vaishnav, R.A.2    Getchell, T.V.3    Getchell, M.L.4    Butterfield, D.A.5
  • 97
    • 35848956857 scopus 로고    scopus 로고
    • Lipid peroxidation scavengers prevent the carbonylation of cytoskeletal brain proteins induced by glutathione depletion
    • Bizzozero O., Reyes S., Ziegler J., Smerjac S. Lipid peroxidation scavengers prevent the carbonylation of cytoskeletal brain proteins induced by glutathione depletion. Neurochem Res 2007, 32:2114-2122.
    • (2007) Neurochem Res , vol.32 , pp. 2114-2122
    • Bizzozero, O.1    Reyes, S.2    Ziegler, J.3    Smerjac, S.4
  • 98
    • 84871601359 scopus 로고    scopus 로고
    • Glutamate system, amyloid ss peptides and tau protein: functional interrelationships and relevance to Alzheimer disease pathology
    • Revett T.J., Baker G.B., Jhamandas J., Kar S. Glutamate system, amyloid ss peptides and tau protein: functional interrelationships and relevance to Alzheimer disease pathology. J Psychiatry Neurosci 2013, 38:6-23.
    • (2013) J Psychiatry Neurosci , vol.38 , pp. 6-23
    • Revett, T.J.1    Baker, G.B.2    Jhamandas, J.3    Kar, S.4
  • 99
    • 0037381710 scopus 로고    scopus 로고
    • Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer's disease
    • Keck S., Nitsch R., Grune T., Ullrich O. Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer's disease. J Neurochem 2003, 85:115-122.
    • (2003) J Neurochem , vol.85 , pp. 115-122
    • Keck, S.1    Nitsch, R.2    Grune, T.3    Ullrich, O.4
  • 100
    • 33845757628 scopus 로고    scopus 로고
    • Phosphorylation inhibits turnover of the tau protein by the proteasome: influence of RCAN1 and oxidative stress
    • Poppek D., Keck S., Ermak G., Jung T., Stolzing A., Ullrich O., et al. Phosphorylation inhibits turnover of the tau protein by the proteasome: influence of RCAN1 and oxidative stress. Biochem J 2006, 400:511-520.
    • (2006) Biochem J , vol.400 , pp. 511-520
    • Poppek, D.1    Keck, S.2    Ermak, G.3    Jung, T.4    Stolzing, A.5    Ullrich, O.6
  • 101
    • 77954622545 scopus 로고    scopus 로고
    • Tau protein degradation is catalyzed by the ATP/ubiquitin-independent 20S proteasome under normal cell conditions
    • Grune T., Botzen D., Engels M., Voss P., Kaiser B., Jung T., et al. Tau protein degradation is catalyzed by the ATP/ubiquitin-independent 20S proteasome under normal cell conditions. Arch Biochem Biophys 2010, 500:181-188.
    • (2010) Arch Biochem Biophys , vol.500 , pp. 181-188
    • Grune, T.1    Botzen, D.2    Engels, M.3    Voss, P.4    Kaiser, B.5    Jung, T.6
  • 102
    • 33947286683 scopus 로고    scopus 로고
    • Abnormal bundling and accumulation of F-actin mediates tau-induced neuronal degeneration in vivo
    • Fulga T.A., Elson-Schwab I., Khurana V., Steinhilb M.L., Spires T.L., Hyman B.T., et al. Abnormal bundling and accumulation of F-actin mediates tau-induced neuronal degeneration in vivo. Nat Cell Biol 2007, 9:139-148.
    • (2007) Nat Cell Biol , vol.9 , pp. 139-148
    • Fulga, T.A.1    Elson-Schwab, I.2    Khurana, V.3    Steinhilb, M.L.4    Spires, T.L.5    Hyman, B.T.6
  • 103
    • 0035880007 scopus 로고    scopus 로고
    • Brain protein oxidation in age-related neurodegenerative disorders that are associated with aggregated proteins
    • Butterfield D.A., Kanski J. Brain protein oxidation in age-related neurodegenerative disorders that are associated with aggregated proteins. Mech Ageing Dev 2001, 122:945-962.
    • (2001) Mech Ageing Dev , vol.122 , pp. 945-962
    • Butterfield, D.A.1    Kanski, J.2
  • 104
    • 0028807137 scopus 로고
    • Brain regional correspondence between Alzheimer's disease histopathology and biomarkers of protein oxidation
    • Hensley K., Hall N., Subramaniam R., Cole P., Harris M., Aksenov M., et al. Brain regional correspondence between Alzheimer's disease histopathology and biomarkers of protein oxidation. J Neurochem 1995, 65:2146-2156.
    • (1995) J Neurochem , vol.65 , pp. 2146-2156
    • Hensley, K.1    Hall, N.2    Subramaniam, R.3    Cole, P.4    Harris, M.5    Aksenov, M.6
  • 106
    • 40849120274 scopus 로고    scopus 로고
    • Redox proteomic identification of 4-hydroxy-2-nonenal-modified brain proteins in amnestic mild cognitive impairment: insight into the role of lipid peroxidation in the progression and pathogenesis of Alzheimer's disease
    • Reed T., Perluigi M., Sultana R., Pierce W.M., Klein J.B., Turner D.M., et al. Redox proteomic identification of 4-hydroxy-2-nonenal-modified brain proteins in amnestic mild cognitive impairment: insight into the role of lipid peroxidation in the progression and pathogenesis of Alzheimer's disease. Neurobiol Dis 2008, 30:107-120.
    • (2008) Neurobiol Dis , vol.30 , pp. 107-120
    • Reed, T.1    Perluigi, M.2    Sultana, R.3    Pierce, W.M.4    Klein, J.B.5    Turner, D.M.6
  • 108
    • 84864317471 scopus 로고    scopus 로고
    • Effects of left ventricular assist device (LVAD) placement on myocardial oxidative stress markers
    • Templeton D.L., Mosser K.H.H., Chen C.N., Stone M.D., John R., Dengel D.R., et al. Effects of left ventricular assist device (LVAD) placement on myocardial oxidative stress markers. Heart Lung Circ 2012, 21:586-597.
    • (2012) Heart Lung Circ , vol.21 , pp. 586-597
    • Templeton, D.L.1    Mosser, K.H.H.2    Chen, C.N.3    Stone, M.D.4    John, R.5    Dengel, D.R.6
  • 109
    • 67349091434 scopus 로고    scopus 로고
    • Proteomic identification of carbonylated proteins in the monkey hippocampus after ischemia-reperfusion
    • Oikawa S., Yamada T., Minohata T., Kobayashi H., Furukawa A., Tada-Oikawa S., et al. Proteomic identification of carbonylated proteins in the monkey hippocampus after ischemia-reperfusion. Free Radic Biol Med 2009, 46:1472-1477.
    • (2009) Free Radic Biol Med , vol.46 , pp. 1472-1477
    • Oikawa, S.1    Yamada, T.2    Minohata, T.3    Kobayashi, H.4    Furukawa, A.5    Tada-Oikawa, S.6
  • 112
    • 42449141602 scopus 로고    scopus 로고
    • Cytoskeletal protein carbonylation and degradation in experimental autoimmune encephalomyelitis
    • Smerjac S.M., Bizzozero O.A. Cytoskeletal protein carbonylation and degradation in experimental autoimmune encephalomyelitis. J Neurochem 2008, 105:763-772.
    • (2008) J Neurochem , vol.105 , pp. 763-772
    • Smerjac, S.M.1    Bizzozero, O.A.2
  • 114
    • 84859020443 scopus 로고    scopus 로고
    • Oxidative stress in HPV-driven viral carcinogenesis: redox proteomics analysis of HPV-16 dysplastic and neoplastic tissues
    • De Marco F., Bucaj E., Foppoli C., Fiorini A., Blarzino C., Filipi K., et al. Oxidative stress in HPV-driven viral carcinogenesis: redox proteomics analysis of HPV-16 dysplastic and neoplastic tissues. PLoS One 2012, 7:e34366.
    • (2012) PLoS One , vol.7
    • De Marco, F.1    Bucaj, E.2    Foppoli, C.3    Fiorini, A.4    Blarzino, C.5    Filipi, K.6
  • 115
  • 116
    • 78651233641 scopus 로고    scopus 로고
    • Combination of PDT and inhibitor treatment affects melanoma cells and spares keratinocytes
    • Kästle M., Grimm S., Nagel R., Breusing N., Grune T. Combination of PDT and inhibitor treatment affects melanoma cells and spares keratinocytes. Free Radic Biol Med 2011, 50:305-312.
    • (2011) Free Radic Biol Med , vol.50 , pp. 305-312
    • Kästle, M.1    Grimm, S.2    Nagel, R.3    Breusing, N.4    Grune, T.5
  • 117
    • 79951587207 scopus 로고    scopus 로고
    • The outcome of 5-ALA-mediated photodynamic treatment in melanoma cells is influenced by vitamin C and heme oxygenase-1
    • Grimm S., Mvondo D., Grune T., Breusing N. The outcome of 5-ALA-mediated photodynamic treatment in melanoma cells is influenced by vitamin C and heme oxygenase-1. BioFactors 2011, 37:17-24.
    • (2011) BioFactors , vol.37 , pp. 17-24
    • Grimm, S.1    Mvondo, D.2    Grune, T.3    Breusing, N.4
  • 118
    • 79959849335 scopus 로고    scopus 로고
    • Photodynamic therapy with hexyl aminolevulinate induces carbonylation, posttranslational modifications and changed expression of proteins in cell survival and cell death pathways
    • Baglo Y., Sousa M.M.L., Slupphaug G., Hagen L., Havag S., Helander L., et al. Photodynamic therapy with hexyl aminolevulinate induces carbonylation, posttranslational modifications and changed expression of proteins in cell survival and cell death pathways. Photochem Photobiol Sci 2011, 10:1137-1145.
    • (2011) Photochem Photobiol Sci , vol.10 , pp. 1137-1145
    • Baglo, Y.1    Sousa, M.M.L.2    Slupphaug, G.3    Hagen, L.4    Havag, S.5    Helander, L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.