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Volumn 36, Issue 12, 2004, Pages 1542-1554

Catalase binds Grb2 in tumor cells when stimulated with serum or ligands for integrin receptors

Author keywords

3 aminotrizole; 3 AT; 4 (2 aminoethyl)benzenesulfonyl fluoride; adenosine 5 triphosphate; AEBSF; American Tissue Culture Collection; ATCC; ATP; Butyrate; Catalase; DTT; Fibrinogen; Fibronectin; Free radicals; Grb2; Laminin; SH2 binding motif; Tet off HeLa

Indexed keywords

AMITROLE; BUTYRIC ACID; CATALASE; COLLAGEN TYPE 1; COLLAGEN TYPE 2; COLLAGEN TYPE 3; COLLAGEN TYPE 4; COLLAGEN TYPE 5; ELASTIN; EPIDERMAL GROWTH FACTOR; FIBRINOGEN; FIBRONECTIN; GROWTH FACTOR RECEPTOR BOUND PROTEIN 2; HERBIMYCIN A; HYALURONIC ACID; INSULIN; INTEGRIN RECEPTOR; LAMININ; LIGAND; NERVE GROWTH FACTOR; PHENYLALANINE; PLATELET DERIVED GROWTH FACTOR; SOMATOMEDIN C; THREONYLVALYLALANYLVALINE; TYROSINE; UNCLASSIFIED DRUG;

EID: 2942555270     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2004.04.006     Document Type: Article
Times cited : (19)

References (58)
  • 3
    • 0026515446 scopus 로고
    • Active oxygen species stimulate vascular smooth muscle cell growth and protooncogene expression
    • Rao G.N., Berk B.C. Active oxygen species stimulate vascular smooth muscle cell growth and protooncogene expression. Circ. Res. 70:1992;593-599
    • (1992) Circ. Res. , vol.70 , pp. 593-599
    • Rao, G.N.1    Berk, B.C.2
  • 4
    • 0024389273 scopus 로고
    • Free radicals and regulation of mammalian cell proliferation
    • Burdon R.H., Rice-Evance C. Free radicals and regulation of mammalian cell proliferation. Free Radic. Res. Commun. 6:1989;345-358
    • (1989) Free Radic. Res. Commun. , vol.6 , pp. 345-358
    • Burdon, R.H.1    Rice-Evance, C.2
  • 5
    • 0026021362 scopus 로고
    • Production of large amount of hydrogen peroxide by human tumor cells
    • Szatrowski T.P., Nathan C.F. Production of large amount of hydrogen peroxide by human tumor cells. Cancer Res. 51:1991;794-798
    • (1991) Cancer Res. , vol.51 , pp. 794-798
    • Szatrowski, T.P.1    Nathan, C.F.2
  • 6
    • 0027296444 scopus 로고
    • Depression of catalase gene expression after immortalization and transformation of mouse liver cells
    • Sun Y., Colburn N.H., Oberley L.W. Depression of catalase gene expression after immortalization and transformation of mouse liver cells. Carcinogenesis. 14:1993;1505-1510
    • (1993) Carcinogenesis , vol.14 , pp. 1505-1510
    • Sun, Y.1    Colburn, N.H.2    Oberley, L.W.3
  • 7
    • 0001952829 scopus 로고    scopus 로고
    • Redox signaling: Hydrogen peroxide as intracellular messenger
    • Rhee S.G. Redox signaling: hydrogen peroxide as intracellular messenger. Exp. Mol. Med. 31:1999;53-59
    • (1999) Exp. Mol. Med. , vol.31 , pp. 53-59
    • Rhee, S.G.1
  • 8
    • 0025945823 scopus 로고
    • Evidence for protein-tyrosine-phosphatase catalysis proceeding via a cysteine-phosphate intermediate
    • Guan K.L., Dixon J.E. Evidence for protein-tyrosine-phosphatase catalysis proceeding via a cysteine-phosphate intermediate. J. Biol. Chem. 266:1991;17026-17030
    • (1991) J. Biol. Chem. , vol.266 , pp. 17026-17030
    • Guan, K.L.1    Dixon, J.E.2
  • 9
    • 0032554611 scopus 로고    scopus 로고
    • Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: Evidence for a sulfenic acid intermediate and implication for redox regulation
    • Denu J.M., Tanner K.G. Specific and reversible inactivation of protein tyrosine phosphatases by hydrogen peroxide: evidence for a sulfenic acid intermediate and implication for redox regulation. Biochemistry. 37:1998;5633-5642
    • (1998) Biochemistry , vol.37 , pp. 5633-5642
    • Denu, J.M.1    Tanner, K.G.2
  • 10
    • 0028952140 scopus 로고
    • Selective activation of the rat hepatic endosomal insulin receptor kinase: Role for the endosome in insulin signaling
    • Bevan A.P., Burgess J.W., Drake P.G., Shaver A., Bergeron J.J., Posner B.I. Selective activation of the rat hepatic endosomal insulin receptor kinase: role for the endosome in insulin signaling. J. Biol. Chem. 270:1995;10784-10791
    • (1995) J. Biol. Chem. , vol.270 , pp. 10784-10791
    • Bevan, A.P.1    Burgess, J.W.2    Drake, P.G.3    Shaver, A.4    Bergeron, J.J.5    Posner, B.I.6
  • 11
    • 0029828638 scopus 로고    scopus 로고
    • A role for tyrosine phosphorylation in both activation and inhibition of the insulin receptor tyrosine kinase in vivo
    • Drake P.G., Bevan A.P., Burgess J.W., Bergeron J.J., Posner B.I. A role for tyrosine phosphorylation in both activation and inhibition of the insulin receptor tyrosine kinase in vivo. Endocrinology. 137:1996;4960-4969
    • (1996) Endocrinology , vol.137 , pp. 4960-4969
    • Drake, P.G.1    Bevan, A.P.2    Burgess, J.W.3    Bergeron, J.J.4    Posner, B.I.5
  • 12
    • 0036855560 scopus 로고    scopus 로고
    • Regulation of catalase enzyme activity by cell signaling molecules
    • Yano S., Yano N. Regulation of catalase enzyme activity by cell signaling molecules. Mol. Cell. Biochem. 240:2002;119-130
    • (2002) Mol. Cell. Biochem. , vol.240 , pp. 119-130
    • Yano, S.1    Yano, N.2
  • 13
    • 0033430085 scopus 로고    scopus 로고
    • Amyloid-beta binds catalase with high affinity and inhibits hydrogen peroxide breakdown
    • Milton N.G. Amyloid-beta binds catalase with high affinity and inhibits hydrogen peroxide breakdown. Biochem. J. 344:1999;293-296
    • (1999) Biochem. J. , vol.344 , pp. 293-296
    • Milton, N.G.1
  • 14
    • 0030963022 scopus 로고    scopus 로고
    • Multiplicity of antioxidant enzyme catalase in mouse liver cells
    • Sun Y. Multiplicity of antioxidant enzyme catalase in mouse liver cells. Free Radic. Res. 26:1997;343-350
    • (1997) Free Radic. Res. , vol.26 , pp. 343-350
    • Sun, Y.1
  • 16
    • 0032483575 scopus 로고    scopus 로고
    • A requirement for caveolin-1 and associated kinase Fyn in integrin signaling and anchorage-dependent cell growth
    • Wary K.K., Mariotti A., Zurzolo C., Giancotti F.G. A requirement for caveolin-1 and associated kinase Fyn in integrin signaling and anchorage-dependent cell growth. Cell. 94:1998;625-634
    • (1998) Cell , vol.94 , pp. 625-634
    • Wary, K.K.1    Mariotti, A.2    Zurzolo, C.3    Giancotti, F.G.4
  • 19
    • 0034672394 scopus 로고    scopus 로고
    • LiSa-2, a novel human liposarcoma cell line with a high capacity for terminal adipose differentiation
    • Wabitsch M., Brüderlein S., Melzner I., Braun M., Mechtersheimer G., Möller P. LiSa-2, a novel human liposarcoma cell line with a high capacity for terminal adipose differentiation. Int. J. Cancer. 88:2000;889-894
    • (2000) Int. J. Cancer , vol.88 , pp. 889-894
    • Wabitsch, M.1    Brüderlein, S.2    Melzner, I.3    Braun, M.4    Mechtersheimer, G.5    Möller, P.6
  • 22
    • 18644367141 scopus 로고    scopus 로고
    • Induction and superinduction of growth arrest and DNA damage gene 45 (GADD45) alpha and beta messenger RNAs by histone deacetylase inhibitors trichostatin a and butyrate in SW620 human colon carcinoma cells
    • Chen Z., Clarks S., Birkeland M., Sung C.M., Lago A., Liu R., Kirkpatrick R., Johanson K., Winkler J.D., Hu E. Induction and superinduction of growth arrest and DNA damage gene 45 (GADD45) alpha and beta messenger RNAs by histone deacetylase inhibitors trichostatin A and butyrate in SW620 human colon carcinoma cells. Cancer Lett. 188:2002;127-140
    • (2002) Cancer Lett. , vol.188 , pp. 127-140
    • Chen, Z.1    Clarks, S.2    Birkeland, M.3    Sung, C.M.4    Lago, A.5    Liu, R.6    Kirkpatrick, R.7    Johanson, K.8    Winkler, J.D.9    Hu, E.10
  • 23
    • 0037362060 scopus 로고    scopus 로고
    • Alpha-lipoic acid induces p27Kip-dependent cell cycle arrest in non-transformed cell lines and apoptosis in tumor cell lines
    • Mark K.K., Chen J.S., Steliou K., Perrine S.P., Faller D.V. Alpha-lipoic acid induces p27Kip-dependent cell cycle arrest in non-transformed cell lines and apoptosis in tumor cell lines. J. Cell. Physiol. 194:2003;325-340
    • (2003) J. Cell. Physiol. , vol.194 , pp. 325-340
    • Mark, K.K.1    Chen, J.S.2    Steliou, K.3    Perrine, S.P.4    Faller, D.V.5
  • 24
    • 0034806431 scopus 로고    scopus 로고
    • Alterations of MAPK activities with intestinal cell differentiation
    • Ding Q., Wang Q., Evers B.M. Alterations of MAPK activities with intestinal cell differentiation. Biochem. Biophys. Res. Commun. 284:2001;282-288
    • (2001) Biochem. Biophys. Res. Commun. , vol.284 , pp. 282-288
    • Ding, Q.1    Wang, Q.2    Evers, B.M.3
  • 25
    • 0035045908 scopus 로고    scopus 로고
    • Inhibition of the phosphatidylinositol 3-kinase pathway contributes to HT29 and Caco-2 intestinal cell differentiation
    • Wang Q., Wang X., Hernandez A., Kim S., Evers B.M. Inhibition of the phosphatidylinositol 3-kinase pathway contributes to HT29 and Caco-2 intestinal cell differentiation. Gastroenterology. 120:2001;1381-1392
    • (2001) Gastroenterology , vol.120 , pp. 1381-1392
    • Wang, Q.1    Wang, X.2    Hernandez, A.3    Kim, S.4    Evers, B.M.5
  • 26
    • 0031439247 scopus 로고    scopus 로고
    • Cellular functions regulated by Src family kinases
    • Thomas S.M., Brugge J.S. Cellular functions regulated by Src family kinases. Annu. Rev. Cell. Dev. Biol. 13:1997;513-609
    • (1997) Annu. Rev. Cell. Dev. Biol. , vol.13 , pp. 513-609
    • Thomas, S.M.1    Brugge, J.S.2
  • 27
    • 0032921366 scopus 로고    scopus 로고
    • Discoidin domain receptors: Structural relations and functional implications
    • Vogel W. Discoidin domain receptors: structural relations and functional implications. FASEB J. 13:1999;S77-S82
    • (1999) FASEB J. , vol.13 , pp. 77-S82
    • Vogel, W.1
  • 28
    • 0036840511 scopus 로고    scopus 로고
    • Discoidin domain receptor 1 controls growth and adhesion of mesangial cells
    • Curat C.A., Vogel W.F. Discoidin domain receptor 1 controls growth and adhesion of mesangial cells. J. Am. Soc. Nephrol. 13:2002;1648-2656
    • (2002) J. Am. Soc. Nephrol. , vol.13 , pp. 1648-2656
    • Curat, C.A.1    Vogel, W.F.2
  • 29
    • 0036480050 scopus 로고    scopus 로고
    • Functional analysis of discoidin domain receptor 1: Effect of adhesion on DDR 1 phosphorylation
    • L'hote C.G., Thomas P.H., Ganesan T.S. Functional analysis of discoidin domain receptor 1: effect of adhesion on DDR 1 phosphorylation. FASEB J. 16:2002;234-236
    • (2002) FASEB J. , vol.16 , pp. 234-236
    • L'Hote, C.G.1    Thomas, P.H.2    Ganesan, T.S.3
  • 30
    • 0023839836 scopus 로고
    • Inhibition of in vitro tumor cell invasion by Arg-Gly-Asp-containing synthetic peptides
    • Gehlsen K.R., Argraves W.S., Pierschbacher M.D., Ruoslahti E. Inhibition of in vitro tumor cell invasion by Arg-Gly-Asp-containing synthetic peptides. J. Cell. Biol. 106:1988;925-930
    • (1988) J. Cell. Biol. , vol.106 , pp. 925-930
    • Gehlsen, K.R.1    Argraves, W.S.2    Pierschbacher, M.D.3    Ruoslahti, E.4
  • 31
    • 1242348060 scopus 로고
    • Sequence of MET protooncogene cDNA has features characteristic of the tyrosine kinase family of growth-factor receptors
    • Park M., Dean M., Kaul M.J., Gonda M.A., Vande Wounde G. Sequence of MET protooncogene cDNA has features characteristic of the tyrosine kinase family of growth-factor receptors. Proc. Natl. Acad. Sci. USA. 84:1987;6379-6383
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6379-6383
    • Park, M.1    Dean, M.2    Kaul, M.J.3    Gonda, M.A.4    Vande Wounde, G.5
  • 32
    • 0030297898 scopus 로고    scopus 로고
    • Uncoupling of Grb2 from the Met receptor in vivo reveals complex roles in muscle development
    • Maina F., Casagrande F., Audera E., Simeone A., Comoglio P.M., Klein R., Ponzetto C. Uncoupling of Grb2 from the Met receptor in vivo reveals complex roles in muscle development. Cell. 87:1996;531-542
    • (1996) Cell , vol.87 , pp. 531-542
    • Maina, F.1    Casagrande, F.2    Audera, E.3    Simeone, A.4    Comoglio, P.M.5    Klein, R.6    Ponzetto, C.7
  • 35
    • 0010066582 scopus 로고
    • A v-erbB-related protooncogene, c-erbB-2, is distinct from the c-erbB-1/epidermal growth factor-receptor gene and is amplified in a human salivary gland adenocarcinoma
    • Semba K., Kamata N., Toyoshima K., Yamamoto T. A v-erbB-related protooncogene, c-erbB-2, is distinct from the c-erbB-1/epidermal growth factor-receptor gene and is amplified in a human salivary gland adenocarcinoma. Proc. Natl. Acad. Sci. USA. 82:1985;6497-6501
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 6497-6501
    • Semba, K.1    Kamata, N.2    Toyoshima, K.3    Yamamoto, T.4
  • 36
    • 0025259592 scopus 로고
    • Nucleotide sequence and expression of a novel human receptor-type tyrosine kinase gene (flt) closely related to the fms family
    • Shibuya M., Yamaguchi S., Yamane A., Ikeda T., Tojo A., Matsushima H., Sato M. Nucleotide sequence and expression of a novel human receptor-type tyrosine kinase gene (flt) closely related to the fms family. Oncogene. 5:1990;519-524
    • (1990) Oncogene , vol.5 , pp. 519-524
    • Shibuya, M.1    Yamaguchi, S.2    Yamane, A.3    Ikeda, T.4    Tojo, A.5    Matsushima, H.6    Sato, M.7
  • 37
    • 0023235631 scopus 로고
    • A possible new member of tyrosine kinase family, human frt sequence, is highly conserved in vertebrates and located on human chromosome 13
    • Matsushime H., Yashida M.C., Sasaki M., Shibuya M. A possible new member of tyrosine kinase family, human frt sequence, is highly conserved in vertebrates and located on human chromosome 13. Jpn. J. Cancer Res. 78:1987;655-661
    • (1987) Jpn. J. Cancer Res. , vol.78 , pp. 655-661
    • Matsushime, H.1    Yashida, M.C.2    Sasaki, M.3    Shibuya, M.4
  • 39
    • 0027294981 scopus 로고
    • The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSos1
    • Rozakis-Adcock M., Fernley R., Wade J., Pawson T., Bowtell D. The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSos1. Nature. 363:1993;83-85
    • (1993) Nature , vol.363 , pp. 83-85
    • Rozakis-Adcock, M.1    Fernley, R.2    Wade, J.3    Pawson, T.4    Bowtell, D.5
  • 40
    • 0034405696 scopus 로고    scopus 로고
    • Relationship between exopolysaccharide production and protein-tyrosine phosphorylation in gram-negative bacteria
    • Vincent C., Duclos B., Grangeasse C., Vaganay E., Riberty M., Cozzone A.J., Doublet P. Relationship between exopolysaccharide production and protein-tyrosine phosphorylation in gram-negative bacteria. J. Mol. Biol. 304:2000;311-321
    • (2000) J. Mol. Biol. , vol.304 , pp. 311-321
    • Vincent, C.1    Duclos, B.2    Grangeasse, C.3    Vaganay, E.4    Riberty, M.5    Cozzone, A.J.6    Doublet, P.7
  • 41
    • 0035951884 scopus 로고    scopus 로고
    • Phosphorylation of Wzc, a tyrosine autokinase, is essential for assembly of group 1 capsular polysaccharides in Escherichia coli
    • Wugeditsch T., Paiment A., Hocking J., Drummelsmith J., Forrester C., Whitfield C. Phosphorylation of Wzc, a tyrosine autokinase, is essential for assembly of group 1 capsular polysaccharides in Escherichia coli. J. Biol. Chem. 276:2001;2361-2371
    • (2001) J. Biol. Chem. , vol.276 , pp. 2361-2371
    • Wugeditsch, T.1    Paiment, A.2    Hocking, J.3    Drummelsmith, J.4    Forrester, C.5    Whitfield, C.6
  • 42
    • 0035930626 scopus 로고    scopus 로고
    • CpsB is a modulator of capsule-associated tyrosine kinase activity in Streptococcus pneumoniae
    • Bender M.H., Yother J. CpsB is a modulator of capsule-associated tyrosine kinase activity in Streptococcus pneumoniae. J. Biol. Chem. 276:2001;47966-47974
    • (2001) J. Biol. Chem. , vol.276 , pp. 47966-47974
    • Bender, M.H.1    Yother, J.2
  • 43
    • 0036510550 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of protein kinase Wzc from Escherichia coli K12 occurs through a two-step process
    • Grangeasse C., Doublet P., Cozzone A.J. Tyrosine phosphorylation of protein kinase Wzc from Escherichia coli K12 occurs through a two-step process. J. Biol. Chem. 277:2002;7127-7135
    • (2002) J. Biol. Chem. , vol.277 , pp. 7127-7135
    • Grangeasse, C.1    Doublet, P.2    Cozzone, A.J.3
  • 45
    • 0030738546 scopus 로고    scopus 로고
    • Ectopic expression of platelet integrin alphaIIb beta3 in tumor cells from various species and histological origin
    • Chen Y.Q., Trikha M., Gao X., Bazaz R., Porter A.T., Timar J., Honn K.V. Ectopic expression of platelet integrin alphaIIb beta3 in tumor cells from various species and histological origin. Int. J. Cancer. 72:1997;642-648
    • (1997) Int. J. Cancer , vol.72 , pp. 642-648
    • Chen, Y.Q.1    Trikha, M.2    Gao, X.3    Bazaz, R.4    Porter, A.T.5    Timar, J.6    Honn, K.V.7
  • 46
    • 0036114872 scopus 로고    scopus 로고
    • Immunohistochemical analysis of beta3 integrin (CD61): Expression in pig tissues and human tumors
    • Merono A., Lucena C., Lopez A., Garrido J.J., de Perez L.L., Llanes D. Immunohistochemical analysis of beta3 integrin (CD61): expression in pig tissues and human tumors. Histol. Histopathol. 17:2002;347-352
    • (2002) Histol. Histopathol. , vol.17 , pp. 347-352
    • Merono, A.1    Lucena, C.2    Lopez, A.3    Garrido, J.J.4    De Perez, L.L.5    Llanes, D.6
  • 47
    • 0035979337 scopus 로고    scopus 로고
    • Mechanism of integrin activation by disulfide bond reduction
    • Yan B., Smith J.W. Mechanism of integrin activation by disulfide bond reduction. Biochemistry. 40:2001;8861-8867
    • (2001) Biochemistry , vol.40 , pp. 8861-8867
    • Yan, B.1    Smith, J.W.2
  • 49
    • 0025940313 scopus 로고
    • The balance between Cu,Zn-superoxide dismutase and catalase affects the sensitivity of mouse epidermal cells to oxidative stress
    • Amstad P., Peskin A., Shah G., Mirault M.E., Moret R., Zbinden I., Cerutti P. The balance between Cu, Zn-superoxide dismutase and catalase affects the sensitivity of mouse epidermal cells to oxidative stress. Biochemistry. 30:1991;9305-9313
    • (1991) Biochemistry , vol.30 , pp. 9305-9313
    • Amstad, P.1    Peskin, A.2    Shah, G.3    Mirault, M.E.4    Moret, R.5    Zbinden, I.6    Cerutti, P.7
  • 50
    • 0036909108 scopus 로고    scopus 로고
    • Oxidative stress as a pathogenic factor in inflammatory bowel disease - Radicals or ridiculous?
    • Kruidenier L., Verspaget H.W. Oxidative stress as a pathogenic factor in inflammatory bowel disease - radicals or ridiculous? Aliment. Pharmacol. Ther. 16:2002;1997-2015
    • (2002) Aliment. Pharmacol. Ther. , vol.16 , pp. 1997-2015
    • Kruidenier, L.1    Verspaget, H.W.2
  • 52
    • 0034683031 scopus 로고    scopus 로고
    • Status of myocardial antioxidants in ischemia-reperfusion injury
    • Dhalla N.S., Elmoselhi A.B., Hata T., Makino N. Status of myocardial antioxidants in ischemia-reperfusion injury. Cardiovasc. Res. 47:2000;446-456
    • (2000) Cardiovasc. Res. , vol.47 , pp. 446-456
    • Dhalla, N.S.1    Elmoselhi, A.B.2    Hata, T.3    Makino, N.4
  • 53
    • 0029869726 scopus 로고    scopus 로고
    • Cytoplasmic and peroxisomal catalases of the guinea pig liver: Evidence for two distinct proteins
    • Bulitta C., Ganea C., Fahimi H.D., Volkl A. Cytoplasmic and peroxisomal catalases of the guinea pig liver: evidence for two distinct proteins. Biochim. Biophys. Acta. 1293:1996;55-62
    • (1996) Biochim. Biophys. Acta , vol.1293 , pp. 55-62
    • Bulitta, C.1    Ganea, C.2    Fahimi, H.D.3    Volkl, A.4
  • 54
    • 0028207535 scopus 로고
    • Changes in the localization of catalase during differentiation of neutrophilic granulocytes
    • Ballinger C.A., Mendis-Handagama C., Kalmar J.R., Arnold R.R., Kinkade J.M. Jr. Changes in the localization of catalase during differentiation of neutrophilic granulocytes. Blood. 83:1994;2654-2668
    • (1994) Blood , vol.83 , pp. 2654-2668
    • Ballinger, C.A.1    Mendis-Handagama, C.2    Kalmar, J.R.3    Arnold, R.R.4    Kinkade Jr., J.M.5
  • 55
    • 0023988178 scopus 로고
    • Catalase in guinea pig hepatocytes is localized in cytoplasm, nuclear matrix and peroxisomes
    • Yamamoto K., Volkl A., Hashimoto T., Fahimi H.D. Catalase in guinea pig hepatocytes is localized in cytoplasm, nuclear matrix and peroxisomes. Eur. J. Cell. Biol. 46:1988;129-135
    • (1988) Eur. J. Cell. Biol. , vol.46 , pp. 129-135
    • Yamamoto, K.1    Volkl, A.2    Hashimoto, T.3    Fahimi, H.D.4
  • 56
    • 0029613812 scopus 로고
    • Immunocytochemical localization of peroxisomal proteins in human liver and kidney
    • Espeel M., Van Limbergen G. Immunocytochemical localization of peroxisomal proteins in human liver and kidney. J. Inherited Metab. Dis. 18(Suppl. 1):1995;135-154
    • (1995) J. Inherited Metab. Dis. , vol.18 , Issue.SUPPL. 1 , pp. 135-154
    • Espeel, M.1    Van Limbergen, G.2
  • 57
    • 0026663644 scopus 로고
    • Is the cytosolic catalase induced by peroxisome proliferators in mouse liver on its way to the peroxisomes?
    • Eriksson A.M., Lundgren B., Andersson K., DePierre J.W. Is the cytosolic catalase induced by peroxisome proliferators in mouse liver on its way to the peroxisomes? FEBS Lett. 308:1992;211-214
    • (1992) FEBS Lett. , vol.308 , pp. 211-214
    • Eriksson, A.M.1    Lundgren, B.2    Andersson, K.3    Depierre, J.W.4
  • 58
    • 0026766935 scopus 로고
    • Changes in catalase activity and concentration during ovarian development and differentiation
    • Peterson S.L., Stevenson P.M. Changes in catalase activity and concentration during ovarian development and differentiation. Biochim. Biophys. Acta. 1135:1992;207-214
    • (1992) Biochim. Biophys. Acta , vol.1135 , pp. 207-214
    • Peterson, S.L.1    Stevenson, P.M.2


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