메뉴 건너뛰기




Volumn 42, Issue 2-3, 2012, Pages 1037-1043

Monitoring of transglutaminase2 under different oxidative stress conditions

Author keywords

Autoimmune diseases; Neurodegeneration; Oxidative stress; Transglutaminase 2

Indexed keywords

PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE 2; REACTIVE OXYGEN METABOLITE; SUMO PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE;

EID: 84861655173     PISSN: 09394451     EISSN: 14382199     Source Type: Journal    
DOI: 10.1007/s00726-011-1018-8     Document Type: Review
Times cited : (35)

References (52)
  • 1
    • 0035823548 scopus 로고    scopus 로고
    • Effects of tissue transglutaminase on retinoic acid-induced cellular differentiation and protection against apoptosis
    • Antonyak MA, Singh US, Lee DA, Boehm JE, Combs C, Zgola MM, Page RL, Cerione RA (2001) Effects of tissue transglutaminase on retinoic acid-induced cellular differentiation and protection against apoptosis. J Biol Chem 276(36):33582-33587
    • (2001) J Biol Chem , vol.276 , Issue.36 , pp. 33582-33587
    • Antonyak, M.A.1    Singh, U.S.2    Lee, D.A.3    Boehm, J.E.4    Combs, C.5    Zgola, M.M.6    Page, R.L.7    Cerione, R.A.8
  • 2
    • 0038521257 scopus 로고    scopus 로고
    • Activation of the Ras-ERK pathway inhibits retinoic acid-induced stimulation of tissue transglutaminase expression in NIH3T3 cells
    • DOI 10.1074/jbc.M300037200
    • Antonyak MA, McNeill CJ, Wakshlag JJ, Boehm JE, Cerione RA (2003) Activation of the Ras-ERK pathway inhibits retinoic acid-induced stimulation of tissue transglutaminase expression in NIH3T3 cells. J Biol Chem 278:15859-15866 (Pubitemid 36799701)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.18 , pp. 15859-15866
    • Antonyak, M.A.1    McNeill, C.J.2    Wakshlag, J.J.3    Boehm, J.E.4    Cerione, R.A.5
  • 3
    • 34548287996 scopus 로고    scopus 로고
    • Oxidative stress: A dead end or a laboratory hypothesis?
    • DOI 10.1016/j.bbrc.2007.07.124, PII S0006291X07016245
    • Azzi A (2007) Oxidative stress: a dead end or a laboratory hypothesis? Biochem Biophys Res Commun 362:230-232 (Pubitemid 47332408)
    • (2007) Biochemical and Biophysical Research Communications , vol.362 , Issue.2 , pp. 230-232
    • Azzi, A.1
  • 5
    • 0035695371 scopus 로고    scopus 로고
    • Oxidative stress to human lymphocytes by xanthine oxidoreductase activity
    • Battelli MG, Musiani S, Tazzari PL, Stirpe F (2001) Oxidative stress to human lymphocytes by xanthine oxidoreductase activity. Free Radic Res 35(6):665-679 (Pubitemid 34065658)
    • (2001) Free Radical Research , vol.35 , Issue.6 , pp. 665-679
    • Battelli, M.G.1    Musiani, S.2    Tazzari, P.L.3    Stirpe, F.4
  • 6
    • 0035399856 scopus 로고    scopus 로고
    • Activation of the nuclear factor-κB is a key event in brain tolerance
    • Blondeau N, Widmann C, Lazdunski M, Heurteaux C (2001) Activation of nuclear factor-kB is a key event in brain tolerance. J Neurosci 21:4668-4677 (Pubitemid 32565625)
    • (2001) Journal of Neuroscience , vol.21 , Issue.13 , pp. 4668-4677
    • Blondeau, N.1    Widmann, C.2    Lazdunski, M.3    Heurteaux, C.4
  • 7
    • 0027302430 scopus 로고
    • The relationship between excitotoxicity and oxidative stress in the central nervous system
    • DOI 10.1016/0891-5849(93)90144-J
    • Bondy SC, Le Bel CP (1993) The relationship between excitotoxicity and oxidative stress in the central nervous system. Free Radic Biol Med 14(6):633-642 (Pubitemid 23172570)
    • (1993) Free Radical Biology and Medicine , vol.14 , Issue.6 , pp. 633-642
    • Bondy, S.C.1    LeBel, C.P.2
  • 8
    • 12144255196 scopus 로고    scopus 로고
    • Excitotoxic and post-ischemic neurodegeneration: Involvement of transglutaminases
    • DOI 10.1007/s00726-004-0117-1
    • Caccamo D, Campisi A, Currò M, Li Volti G, Vanella A, Ientile R (2004) Excitotoxic and post-ischemic neurodegeneration: involvement of transglutaminases. Amino Acids 27:373-379 (Pubitemid 40110083)
    • (2004) Amino Acids , vol.27 , Issue.3-4 , pp. 373-379
    • Caccamo, D.1    Campisi, A.2    Curro, M.3    Li Volti, G.4    Vanella, A.5    Ientile, R.6
  • 9
    • 26444448966 scopus 로고    scopus 로고
    • Antioxidant treatment inhibited glutamate-evoked NF-κB activation in primary astroglial cell cultures
    • DOI 10.1016/j.neuro.2005.01.010, PII S0161813X05000392, First International Porto Pirgos Conference on Advances in Neuroscience
    • Caccamo D, Campisi A, Currò M, Bramanti V, Tringali M, Li Volti G, Vanella A, Ientile R (2005a) Antioxidant treatment inhibited glutamate-evoked NF-kappaB activation in primary astroglial cell cultures. Neurotoxicology 26:915-921 (Pubitemid 41427531)
    • (2005) NeuroToxicology , vol.26 , Issue.5 , pp. 915-921
    • Caccamo, D.1    Campisi, A.2    Curro, M.3    Bramanti, V.4    Tringali, M.5    Volti, G.L.6    Vanella, A.7    Ientile, R.8
  • 10
    • 18144372746 scopus 로고    scopus 로고
    • Glutamate promotes NF-κB pathway in primary astrocytes: Protective effects of IRFI 016, a synthetic vitamin E analogue
    • DOI 10.1016/j.expneurol.2005.01.014
    • Caccamo D, Campisi A, Marini H, Adamo EB, Li Volti G, Squadrito F, Ientile R (2005b) Glutamate promotes NF-kappaB pathway in primary astrocytes: protective effects of IRFI 016, a synthetic vitamin E analogue. Exp Neurol 193:377-383 (Pubitemid 40616187)
    • (2005) Experimental Neurology , vol.193 , Issue.2 , pp. 377-383
    • Caccamo, D.1    Campisi, A.2    Marini, H.3    Adamo, E.B.4    Li Volti, G.5    Squadrito, F.6    Ientile, R.7
  • 11
    • 28544451599 scopus 로고    scopus 로고
    • Nuclear factor-κB activation is associated with glutamate-evoked tissue transglutaminase up-regulation in primary astrocyte cultures
    • DOI 10.1002/jnr.20683
    • Caccamo D, Campisi A, Currò M, Aguennouz M, Li Volti G, Avola R, Ientile R (2005c) Nuclear factor-kappab activation is associated with glutamate-evoked tissue transglutaminase upregulation in primary astrocyte cultures. J Neurosci Res 82:858-865 (Pubitemid 41746499)
    • (2005) Journal of Neuroscience Research , vol.82 , Issue.6 , pp. 858-865
    • Caccamo, D.1    Campisi, A.2    Curro, M.3    Aguennouz, M.4    Li Volti, G.5    Avola, R.6    Ientile, R.7
  • 12
    • 77953067720 scopus 로고    scopus 로고
    • Critical role of transglutaminase and other stress proteins during neurodegenerative processes
    • Caccamo D, Currò M, Condello S, Ferlazzo N, Ientile R, Caccamo D (2010) Critical role of transglutaminase and other stress proteins during neurodegenerative processes. Amino Acids 38(2):653-658
    • (2010) Amino Acids , vol.38 , Issue.2 , pp. 653-658
    • Caccamo, D.1    Currò, M.2    Condello, S.3    Ferlazzo, N.4    Ientile, R.5    Caccamo, D.6
  • 13
    • 77953716363 scopus 로고    scopus 로고
    • Cystamine protects from 3-nitropropionic acid lesioning via induction of nf-e2 related factor 2 mediated transcription
    • Calkins MJ, Townsend JA, Johnson DA, Johnson JA (2010) Cystamine protects from 3-nitropropionic acid lesioning via induction of nf-e2 related factor 2 mediated transcription. Exp Neurol 224(1):307-317
    • (2010) Exp Neurol , vol.224 , Issue.1 , pp. 307-317
    • Calkins, M.J.1    Townsend, J.A.2    Johnson, D.A.3    Johnson, J.A.4
  • 14
    • 9644310547 scopus 로고    scopus 로고
    • Glutamate-evoked redox state alterations are involved in tissue transglutaminase upregulation in primary astrocyte cultures
    • DOI 10.1016/j.febslet.2004.10.074, PII S0014579304013298
    • Campisi A, Caccamo D, Li Volti G, Currò M, Parisi G, Avola R, Vanella A, Ientile R (2004) Glutamate-evoked redox state alterations are involved in tissue transglutaminase up-regulation in primary astrocyte cultures. FEBS Lett 578:80-84 (Pubitemid 39576104)
    • (2004) FEBS Letters , vol.578 , Issue.1-2 , pp. 80-84
    • Campisi, A.1    Caccamo, D.2    Li Volti, G.3    Curro, M.4    Parisi, G.5    Avola, R.6    Vanella, A.7    Ientile, R.8
  • 17
    • 0036804796 scopus 로고    scopus 로고
    • Transglutaminase 2: An enigmatic enzyme with diverse functions
    • DOI 10.1016/S0968-0004(02)02182-5, PII S0968000402021825
    • Fesus L, Piacentini M (2002) Transglutaminase 2: an enigmatic enzyme with diverse functions. Trends Biochem Sci 27:534-539 (Pubitemid 35279599)
    • (2002) Trends in Biochemical Sciences , vol.27 , Issue.10 , pp. 534-539
    • Fesus, L.1    Piacentini, M.2
  • 18
    • 20444363472 scopus 로고    scopus 로고
    • Transglutaminase 2 in the balance of cell death and survival
    • DOI 10.1016/j.febslet.2005.03.063, PII S0014579305004151
    • Fésüs L, Szondy Z (2005) Transglutaminase 2 in the balance of cell death and survival. FEBS Lett 579(15):3297-3302 (Pubitemid 40804677)
    • (2005) FEBS Letters , vol.579 , Issue.15 , pp. 3297-3302
    • Fesus, L.1    Szondy, Z.2
  • 20
    • 0031968031 scopus 로고    scopus 로고
    • Alteration of enzymatic activities implicating neuronal degeneration in the spinal cord of the motor neuron degeneration mouse during postnatal development
    • DOI 10.1023/A:1022442904179
    • Fujita K, Shibayama K, Yamauchi M, Kato T, Ando M, Takahashi H, Iritani K, Yoshimoto N, Nagata Y (1998) Alteration of enzymatic activities implicating neuronal degeneration in the spinal cord of the motor neuron degeneration mouse during postnatal development. Neurochem Res 23(4):557-562 (Pubitemid 28177622)
    • (1998) Neurochemical Research , vol.23 , Issue.4 , pp. 557-562
    • Fujita, K.1    Shibayama, K.2    Yamauchi, M.3    Kato, T.4    Ando, M.5    Takahashi, H.6    Iritani, K.7    Yoshimoto, N.8    Nagata, Y.9
  • 21
    • 0036901574 scopus 로고    scopus 로고
    • Transglutaminases: Nature's biological glues
    • DOI 10.1042/BJ20021234
    • Griffin M, Casadio R, Bergamini CM (2002) Transglutaminases: nature's biological glues. Biochem J 368:377-396 (Pubitemid 35454517)
    • (2002) Biochemical Journal , vol.368 , Issue.2 , pp. 377-396
    • Griffin, M.1    Casadio, R.2    Bergamini, C.M.3
  • 22
    • 0027424329 scopus 로고
    • Exposure of βH-crystallin to hydroxyl radicals enhances the transglutaminase-susceptibility of its existing amine-donor and amine-acceptor sites
    • Groenen PJ, Seccia M, Smulders RH, Gravela E, Cheeseman KH, Bloemendal H, de Jong WW (1993) Exposure of beta H-crystallin to hydroxyl radicals enhances the transglutaminasesusceptibility of its existing amine-donor and amine-acceptor sites. Biochem J 295(Pt 2):399-404 (Pubitemid 23315177)
    • (1993) Biochemical Journal , vol.295 , Issue.2 , pp. 399-404
    • Groenen, P.J.T.A.1    Seccia, M.2    Smulders, R.H.P.H.3    Gravela, E.4    Cheeseman, K.H.5    Bloemendal, H.6    De Jong, W.W.7
  • 23
    • 0043124302 scopus 로고    scopus 로고
    • Importance of tissue transglutaminase in repair of extracellular matrices and cell death of dermal fibroblasts after exposure to a solarium ultraviolet a source
    • DOI 10.1046/j.1523-1747.2003.12353.x
    • Gross SR, Balklava Z, Griffin M (2003) Importance of tissue transglutaminase in repair of extracellular matrices and cell death of dermal fibroblasts after exposure to a solarium ultraviolet A source. J Invest Dermatol 121:412-423 (Pubitemid 36969917)
    • (2003) Journal of Investigative Dermatology , vol.121 , Issue.2 , pp. 412-423
    • Gross, S.R.1    Balklava, Z.2    Griffin, M.3
  • 24
    • 67651246845 scopus 로고    scopus 로고
    • Intracellular localization and conformational state of transglutaminase 2: Implications for cell death
    • Gundemir S, Johnson GV (2009) Intracellular localization and conformational state of transglutaminase 2: implications for cell death. PLoS One 4(7):e6123
    • (2009) PLoS One , vol.4 , Issue.7
    • Gundemir, S.1    Johnson, G.V.2
  • 25
    • 34547697884 scopus 로고    scopus 로고
    • Tissue transglutaminase and the stress response
    • DOI 10.1007/s00726-007-0517-0, Special Issue: Polyamines and their Analogs in Cancer and other Diseases
    • Ientile R, Caccamo D, Griffin M (2007) Tissue transglutaminase and the stress response. Amino Acids 33:385-394 (Pubitemid 47222963)
    • (2007) Amino Acids , vol.33 , Issue.2 , pp. 385-394
    • Ientile, R.1    Caccamo, D.2    Griffin, M.3
  • 26
    • 67651071286 scopus 로고    scopus 로고
    • Transglutaminases and disease: Lessons from genetically engineered mouse models and inherited disorders
    • Iismaa SE, Mearns BM, Lorand L, Graham RM (2009) Transglutaminases and disease: lessons from genetically engineered mouse models and inherited disorders. Physiol Rev 89:991-1023
    • (2009) Physiol Rev , vol.89 , pp. 991-1023
    • Iismaa, S.E.1    Mearns, B.M.2    Lorand, L.3    Graham, R.M.4
  • 27
    • 60049098220 scopus 로고    scopus 로고
    • Degradation of transglutaminase 2 by calcium-mediated ubiquitination responding to high oxidative stress
    • Jeong EM, Kim CW, Cho SY, Jang GY, Shin DM, Jeon JH, Kim IG (2009) Degradation of transglutaminase 2 by calcium-mediated ubiquitination responding to high oxidative stress. FEBS Lett 583(4):648-654
    • (2009) FEBS Lett , vol.583 , Issue.4 , pp. 648-654
    • Jeong, E.M.1    Kim, C.W.2    Cho, S.Y.3    Jang, G.Y.4    Shin, D.M.5    Jeon, J.H.6    Kim, I.G.7
  • 28
    • 51249086028 scopus 로고    scopus 로고
    • Pathophysiological and pharmacological implications of mitochondria-targeted reactive oxygen-species generation in astrocytes
    • Jou MJ (2008) Pathophysiological and pharmacological implications of mitochondria-targeted reactive oxygen-species generation in astrocytes. Adv Drug Deliv Rev 60(13-14): 1512-1526
    • (2008) Adv Drug Deliv Rev , vol.60 , Issue.13-14 , pp. 1512-1526
    • Jou, M.J.1
  • 29
  • 30
    • 0033794508 scopus 로고    scopus 로고
    • Impaired mitochondrial function results in increased tissue transglutaminase activity in situ
    • Lesort M, Tucholski J, Zhang J, Johnson GV (2000) Impaired mitochondrial function results in increased tissue transglutaminase activity in situ. J Neurochem 75:1951-1961
    • (2000) J Neurochem , vol.75 , pp. 1951-1961
    • Lesort, M.1    Tucholski, J.2    Zhang, J.3    Johnson, G.V.4
  • 32
    • 77749318553 scopus 로고    scopus 로고
    • Lysosomal accumulation of gliadin p31-43 peptide induces oxidative stress and tissue transglutaminase-mediated PPARgamma down-regulation in intestinal epithelial cells and coeliac mucosa
    • Luciani A, Villella VR, Vasaturo A, Giardino I, Pettoello-Mantovani M, Guido S, Cexus ON, Peake N, Londei M, Quaratino S, Maiuri L (2010a) Lysosomal accumulation of gliadin p31-43 peptide induces oxidative stress and tissue transglutaminase-mediated PPARgamma down-regulation in intestinal epithelial cells and coeliac mucosa. Gut 59(3):311-319
    • (2010) Gut , vol.59 , Issue.3 , pp. 311-319
    • Luciani, A.1    Villella, V.R.2    Vasaturo, A.3    Giardino, I.4    Pettoello-Mantovani, M.5    Guido, S.6    Cexus, O.N.7    Peake, N.8    Londei, M.9    Quaratino, S.10    Maiuri, L.11
  • 34
    • 1542335670 scopus 로고    scopus 로고
    • Intracellular localization and activity state of tissue transglutaminase differentially impacts cell death
    • DOI 10.1074/jbc.M308479200
    • Milakovic T, Tucholski J, McCoy E, Johnson GV (2004) Intracellular localization and activity state of tissue transglutaminase differentially impacts cell death. J Biol Chem 279:8715-8722 (Pubitemid 38295927)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.10 , pp. 8715-8722
    • Milakovic, T.1    Tucholski, J.2    McCoy, E.3    Johnson, G.V.W.4
  • 36
    • 21344433622 scopus 로고    scopus 로고
    • Intracellular glutathione levels determine cell sensitivity to apoptosis induced by the antineoplasic agent N-(4-hydroxyphenyl)retinamide
    • Morales MC, Pérez-Yarza G, Nieto-Rementeria N, Boyano MD, Jangi M, Atencia R, Asumendi A (2005) Intracellular glutathione levels determine cell sensitivity to apoptosis induced by the antineoplasic agent N-(4-hydroxyphenyl) retinamide. Anticancer Res 25(3B):1945-1951 (Pubitemid 40904589)
    • (2005) Anticancer Research , vol.25 , Issue.3 B , pp. 1945-1951
    • Morales, M.-C.1    Perez-Yarza, G.2    Nieto-Rementeria, N.3    Boyano, M.-D.4    Jangi, M.5    Atencia, R.6    Asumendi, A.7
  • 38
    • 77956916373 scopus 로고    scopus 로고
    • Transglutaminase 2: A multifunctional protein in multiple subcellular compartments
    • Park D, Choi SS, Ha KS (2010) Transglutaminase 2: a multifunctional protein in multiple subcellular compartments. Amino Acids 39:619-631
    • (2010) Amino Acids , vol.39 , pp. 619-631
    • Park, D.1    Choi, S.S.2    Ha, K.S.3
  • 40
    • 34249808244 scopus 로고    scopus 로고
    • Transglutaminase 2 in neurodegenerative disorders
    • DOI 10.2741/2111
    • Ruan Q, Johnson GV (2007) Transglutaminase 2 in neurodegenerative disorders. Front Biosci 12:891-904 (Pubitemid 46846864)
    • (2007) Frontiers in Bioscience , vol.12 , Issue.3 , pp. 891-904
    • Ruan, Q.1    Johnson, G.V.W.2
  • 41
    • 2442607838 scopus 로고    scopus 로고
    • Cell type-specific activation of intracellular transglutaminase 2 by oxidative stress or ultraviolet irradiation: Implications of transglutaminase 2 in age-related cataractogenesis
    • Shin DM, Jeon JH, Kim CW, Cho SY, Kwon JC, Lee HJ, Choi KH, Park SC, Kim IG (2004) Cell type-specific activation of intracellular transglutaminase 2 by oxidative stress or ultraviolet irradiation: implications of transglutaminase 2 in age-related cataractogenesis. J Biol Chem 279:15032-15039
    • (2004) J Biol Chem , vol.279 , pp. 15032-15039
    • Shin, D.M.1    Jeon, J.H.2    Kim, C.W.3    Cho, S.Y.4    Kwon, J.C.5    Lee, H.J.6    Choi, K.H.7    Park, S.C.8    Kim, I.G.9
  • 43
    • 0030032813 scopus 로고    scopus 로고
    • Measurement of tissue transglutaminase activity in a permeabilized cell system: Its regulation by Ca2+ and nucleotides
    • Smethurst PA, Griffin M (1996) Measurement of tissue transglutaminase activity in a permeabilized cell system: its regulation by Ca2+ and nucleotides. Biochem J 313:803-808
    • (1996) Biochem J , vol.313 , pp. 803-808
    • Smethurst, P.A.1    Griffin, M.2
  • 45
    • 77958091268 scopus 로고    scopus 로고
    • Transglutaminase 2 expression induced by lipopolysaccharide stimulation together with NO synthase induction in cultured astrocytes
    • Takano K, Shiraiwa K, Moriyama M, Nakamura Y (2010) Transglutaminase 2 expression induced by lipopolysaccharide stimulation together with NO synthase induction in cultured astrocytes. Neurochem Int 57(7):812-818
    • (2010) Neurochem Int , vol.57 , Issue.7 , pp. 812-818
    • Takano, K.1    Shiraiwa, K.2    Moriyama, M.3    Nakamura, Y.4
  • 46
    • 32944463725 scopus 로고    scopus 로고
    • Tissue transglutaminase (TG2) - A wound response enzyme
    • Telci D, Griffin M (2006) Tissue transglutaminase (TG2)-a wound response enzyme. Front Biosci 11:867-882 (Pubitemid 43258187)
    • (2006) Frontiers in Bioscience , vol.11 , Issue.1 , pp. 867-882
    • Telci, D.1    Griffin, M.2
  • 47
    • 0036319364 scopus 로고    scopus 로고
    • Tissue transglutaminase differentially modulates apoptosis in a stimuli-dependent manner
    • DOI 10.1046/j.1471-4159.2002.00859.x
    • Tucholski J, Johnson GVW (2002) Tissue transglutaminase differentially modulates apoptosis in a stimuli-dependent manner. J Neurochem 81:780-791 (Pubitemid 34809306)
    • (2002) Journal of Neurochemistry , vol.81 , Issue.4 , pp. 780-791
    • Tucholski, J.1    Johnson, G.V.W.2
  • 48
    • 0035863525 scopus 로고    scopus 로고
    • Tissue transglutaminase is essential for neurite outgrowth in human neuroblastoma SH-SY5Y cells
    • DOI 10.1016/S0306-4522(00)00482-6, PII S0306452200004826
    • Tucholski J, Lesort M, Johnson GV (2001) Tissue transglutaminase is essential for neurite outgrowth in human neuroblastoma SHSY5Y cells. Neuroscience 102(2):481-491 (Pubitemid 32126502)
    • (2001) Neuroscience , vol.102 , Issue.2 , pp. 481-491
    • Tucholski, J.1    Lesort, M.2    Johnson, G.V.W.3
  • 49
    • 0031869591 scopus 로고    scopus 로고
    • Regulated expression of tissue transglutaminase in Swiss 3T3 fibroblasts: Effects on the processing of fibronectin, cell attachment, and cell death
    • DOI 10.1006/excr.1997.3874
    • Verderio E, Nicholas B, Gross S, Griffin M (1998) Regulated expression of tissue transglutaminase in Swiss 3T3 fibroblasts: effects on the processing of fibronectin, cell attachment, and cell death. Exp Cell Res 239:119-138 (Pubitemid 28368484)
    • (1998) Experimental Cell Research , vol.239 , Issue.1 , pp. 119-138
    • Verderio, E.1    Nicholas, B.2    Gross, S.3    Griffin, M.4
  • 50
    • 3242794297 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a maize transglutaminase complementary DNA
    • DOI 10.1016/j.gene.2004.03.025, PII S0378111904001830
    • Villalobos E, Santos M, Talavera D, Rodríguez-Falcón M, Torné JM (2004) Molecular cloning and characterization of a maize transglutaminase complementary DNA. Gene 336(1):93-104 (Pubitemid 38968828)
    • (2004) Gene , vol.336 , Issue.1 , pp. 93-104
    • Villalobos, E.1    Santos, M.2    Talavera, D.3    Rodriguez-Falcon, M.4    Torne, J.M.5
  • 51
    • 33748750998 scopus 로고    scopus 로고
    • Dual effects of antioxidants in neurodegeneration: Direct neuroprotection against oxidative stress and indirect protection via suppression of glia-mediated inflammation
    • Wang JY, Wen LL, Huang YN, Chen YT, Ku MC (2006) Dual effects of antioxidants in neurodegeneration: direct neuroprotection against oxidative stress and indirect protection via suppression of glia-mediated inflammation. Curr Pharm Des 12(27):3521-3533
    • (2006) Curr Pharm des , vol.12 , Issue.27 , pp. 3521-3533
    • Wang, J.Y.1    Wen, L.L.2    Huang, Y.N.3    Chen, Y.T.4    Ku, M.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.