메뉴 건너뛰기




Volumn 370, Issue 2-3, 2004, Pages 224-229

The augmentation of brain thioredoxin-1 expression after severe hypobaric hypoxia by the preconditioning in rats

Author keywords

Antioxidants; Hypobaric hypoxia; Immunocytochemistry; Preconditioning; Thioredoxin 1

Indexed keywords

ANTIOXIDANT; THIOREDOXIN; THIOREDOXIN 1; UNCLASSIFIED DRUG;

EID: 5644227641     PISSN: 03043940     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.neulet.2004.08.022     Document Type: Article
Times cited : (35)

References (61)
  • 1
    • 0030903691 scopus 로고    scopus 로고
    • Redox regulation of the DNA binding activity in transcription factor PEBP2. The roles of two conserved cysteine residues
    • Y. Akamatsu, T. Ohno, K. Hirota, H. Kagoshima, J. Yodoi, and K. Shigesada Redox regulation of the DNA binding activity in transcription factor PEBP2. The roles of two conserved cysteine residues J. Biol. Chem. 272 1997 14497 14500
    • (1997) J. Biol. Chem. , vol.272 , pp. 14497-14500
    • Akamatsu, Y.1    Ohno, T.2    Hirota, K.3    Kagoshima, H.4    Yodoi, J.5    Shigesada, K.6
  • 2
    • 0037155817 scopus 로고    scopus 로고
    • The roles of thioredoxin in protection against oxidative stress-induced apoptosis in SH-SY5Y cells
    • T. Andoh, P.B. Chock, and C.C. Chiueh The roles of thioredoxin in protection against oxidative stress-induced apoptosis in SH-SY5Y cells J. Biol. Chem. 277 2002 9655 9660
    • (2002) J. Biol. Chem. , vol.277 , pp. 9655-9660
    • Andoh, T.1    Chock, P.B.2    Chiueh, C.C.3
  • 3
    • 0032578028 scopus 로고    scopus 로고
    • Hypoxia-induced apoptosis: Effect of hypoxic severity and role of p53 in neuronal cell death
    • K.J. Banasiak, and G.G. Haddad Hypoxia-induced apoptosis: effect of hypoxic severity and role of p53 in neuronal cell death Brain Res. 797 1998 295 304
    • (1998) Brain Res. , vol.797 , pp. 295-304
    • Banasiak, K.J.1    Haddad, G.G.2
  • 4
    • 0030499036 scopus 로고    scopus 로고
    • Thioredoxin and thioredoxin reductase gene expression in human tumors and cell lines, and the effects of serum stimulation and hypoxia
    • M. Berggren, A. Gallegos, J.R. Gasdaska, P.Y. Gasdaska, J. Warneke, and G. Powis Thioredoxin and thioredoxin reductase gene expression in human tumors and cell lines, and the effects of serum stimulation and hypoxia Anticancer Res. 16 1996 3459 3466
    • (1996) Anticancer Res. , vol.16 , pp. 3459-3466
    • Berggren, M.1    Gallegos, A.2    Gasdaska, J.R.3    Gasdaska, P.Y.4    Warneke, J.5    Powis, G.6
  • 5
    • 0033796250 scopus 로고    scopus 로고
    • Mitochondrial free radical generation, oxidative stress, and aging
    • E. Cadenas, and K.J. Davies Mitochondrial free radical generation, oxidative stress, and aging Free Radic. Biol. Med. 29 2000 222 230
    • (2000) Free Radic. Biol. Med. , vol.29 , pp. 222-230
    • Cadenas, E.1    Davies, K.J.2
  • 6
    • 0344154463 scopus 로고    scopus 로고
    • Oxidative damage to DNA: Formation, measurement and biochemical features
    • J. Cadet, T. Douki, D. Gasparutto, and J.L. Ravanat Oxidative damage to DNA: formation, measurement and biochemical features Mutat. Res. 531 2003 5 23
    • (2003) Mutat. Res. , vol.531 , pp. 5-23
    • Cadet, J.1    Douki, T.2    Gasparutto, D.3    Ravanat, J.L.4
  • 7
    • 0034765766 scopus 로고    scopus 로고
    • Time course of oxidative damage in different brain regions following transient cerebral ischemia in gerbils
    • E. Candelario-Jalil, N.H. Mhadu, S.M. Al-Dalain, G. Martinez, and O.S. Leon Time course of oxidative damage in different brain regions following transient cerebral ischemia in gerbils Neurosci. Res. 41 2001 233 241
    • (2001) Neurosci. Res. , vol.41 , pp. 233-241
    • Candelario-Jalil, E.1    Mhadu, N.H.2    Al-Dalain, S.M.3    Martinez, G.4    Leon, O.S.5
  • 8
    • 0034656846 scopus 로고    scopus 로고
    • Cerebral ischemia: Gene activation, neuronal injury, and the protective role of antioxidants
    • J.A. Clemens Cerebral ischemia: gene activation, neuronal injury, and the protective role of antioxidants Free Radic. Biol. Med. 28 2000 1526 1531
    • (2000) Free Radic. Biol. Med. , vol.28 , pp. 1526-1531
    • Clemens, J.A.1
  • 9
    • 0035895885 scopus 로고    scopus 로고
    • C-Jun NH2-terminal kinase-mediated redox-dependent degradation of IkappaB: Role of thioredoxin in NF-kappaB activation
    • K.C. Das c-Jun NH2-terminal kinase-mediated redox-dependent degradation of IkappaB: role of thioredoxin in NF-kappaB activation J. Biol. Chem. 276 2001 4662 4670
    • (2001) J. Biol. Chem. , vol.276 , pp. 4662-4670
    • Das, K.C.1
  • 10
    • 0031302910 scopus 로고    scopus 로고
    • Elevation of manganese superoxide dismutase gene expression by thioredoxin
    • K.C. Das, Y. Lewis-Molock, and C.W. White Elevation of manganese superoxide dismutase gene expression by thioredoxin Am. J. Respir. Cell Mol. Biol. 17 1997 713 726
    • (1997) Am. J. Respir. Cell Mol. Biol. , vol.17 , pp. 713-726
    • Das, K.C.1    Lewis-Molock, Y.2    White, C.W.3
  • 11
    • 0034655765 scopus 로고    scopus 로고
    • The cytosolic antioxidant copper/zinc-superoxide dismutase prevents the early release of mitochondrial cytochrome c in ischemic brain after transient focal cerebral ischemia in mice
    • M. Fujimura, Y. Morita-Fujimura, N. Noshita, T. Sugawara, M. Kawase, and P.H. Chan The cytosolic antioxidant copper/zinc-superoxide dismutase prevents the early release of mitochondrial cytochrome c in ischemic brain after transient focal cerebral ischemia in mice J. Neurosci. 20 2000 2817 2824
    • (2000) J. Neurosci. , vol.20 , pp. 2817-2824
    • Fujimura, M.1    Morita-Fujimura, Y.2    Noshita, N.3    Sugawara, T.4    Kawase, M.5    Chan, P.H.6
  • 12
    • 0027496935 scopus 로고
    • The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases
    • J.W. Harper, G.R. Adami, N. Wei, K. Keyomarsi, and S.J. Elledge The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases Cell 75 1993 805 816
    • (1993) Cell , vol.75 , pp. 805-816
    • Harper, J.W.1    Adami, G.R.2    Wei, N.3    Keyomarsi, K.4    Elledge, S.J.5
  • 15
  • 16
    • 0027217531 scopus 로고
    • Oxidoreductive regulation of nuclear factor kappa B. Involvement of a cellular reducing catalyst thioredoxin
    • T. Hayashi, Y. Ueno, and T. Okamoto Oxidoreductive regulation of nuclear factor kappa B. Involvement of a cellular reducing catalyst thioredoxin J. Biol. Chem. 268 1993 11380 11388
    • (1993) J. Biol. Chem. , vol.268 , pp. 11380-11388
    • Hayashi, T.1    Ueno, Y.2    Okamoto, T.3
  • 17
    • 0030838711 scopus 로고    scopus 로고
    • Functional modulation of estrogen receptor by redox state with reference to thioredoxin as a mediator
    • S. Hayashi, K. Hajiro-Nakanishi, Y. Makino, H. Eguchi, J. Yodoi, and H. Tanaka Functional modulation of estrogen receptor by redox state with reference to thioredoxin as a mediator Nucleic Acids Res. 25 1997 4035 4040
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4035-4040
    • Hayashi, S.1    Hajiro-Nakanishi, K.2    Makino, Y.3    Eguchi, H.4    Yodoi, J.5    Tanaka, H.6
  • 18
    • 0642375804 scopus 로고    scopus 로고
    • Chromosomal DNA fragmentation in apoptosis and necrosis induced by oxidative stress
    • Y. Higuchi Chromosomal DNA fragmentation in apoptosis and necrosis induced by oxidative stress Biochem. Pharmacol. 66 2003 1527 1535
    • (2003) Biochem. Pharmacol. , vol.66 , pp. 1527-1535
    • Higuchi, Y.1
  • 19
    • 0030936568 scopus 로고    scopus 로고
    • AP-1 transcriptional activity is regulated by a direct association between thioredoxin and Ref-1
    • K. Hirota, M. Matsui, S. Iwata, A. Nishiyama, K. Mori, and J. Yodoi AP-1 transcriptional activity is regulated by a direct association between thioredoxin and Ref-1 Proc. Natl. Acad. Sci. U.S.A. 94 1997 3633 3638
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 3633-3638
    • Hirota, K.1    Matsui, M.2    Iwata, S.3    Nishiyama, A.4    Mori, K.5    Yodoi, J.6
  • 21
    • 0033600744 scopus 로고    scopus 로고
    • Distinct roles of thioredoxin in the cytoplasm and in the nucleus. A two-step mechanism of redox regulation of transcription factor NF-kappaB
    • K. Hirota, M. Murata, Y. Sachi, H. Nakamura, J. Takeuchi, K. Mori, and J. Yodoi Distinct roles of thioredoxin in the cytoplasm and in the nucleus. A two-step mechanism of redox regulation of transcription factor NF-kappaB J. Biol. Chem. 274 1999 27891 27897
    • (1999) J. Biol. Chem. , vol.274 , pp. 27891-27897
    • Hirota, K.1    Murata, M.2    Sachi, Y.3    Nakamura, H.4    Takeuchi, J.5    Mori, K.6    Yodoi, J.7
  • 23
    • 0024393963 scopus 로고
    • Thioredoxin and glutaredoxin systems
    • A. Holmgren Thioredoxin and glutaredoxin systems J. Biol. Chem. 264 1989 13963 13966
    • (1989) J. Biol. Chem. , vol.264 , pp. 13963-13966
    • Holmgren, A.1
  • 24
    • 0028234644 scopus 로고
    • Neuroprotection by glial cells through adult T cell leukemia-derived factor/human thioredoxin (ADF/TRX)
    • K. Hori, M. Katayama, N. Sato, K. Ishii, S. Waga, and J. Yodoi Neuroprotection by glial cells through adult T cell leukemia-derived factor/human thioredoxin (ADF/TRX) Brain Res. 652 1994 304 310
    • (1994) Brain Res. , vol.652 , pp. 304-310
    • Hori, K.1    Katayama, M.2    Sato, N.3    Ishii, K.4    Waga, S.5    Yodoi, J.6
  • 26
    • 0033988731 scopus 로고    scopus 로고
    • Human thioredoxin attenuates hypoxia-reoxygenation injury of murine endothelial cells in a thiol-free condition
    • N. Isowa, T. Yoshimura, S. Kosaka, M. Liu, S. Hitomi, J. Yodoi, and H. Wada Human thioredoxin attenuates hypoxia-reoxygenation injury of murine endothelial cells in a thiol-free condition J. Cell Physiol. 182 2000 33 40
    • (2000) J. Cell Physiol. , vol.182 , pp. 33-40
    • Isowa, N.1    Yoshimura, T.2    Kosaka, S.3    Liu, M.4    Hitomi, S.5    Yodoi, J.6    Wada, H.7
  • 27
    • 0028873415 scopus 로고
    • Temporal profile of nuclear DNA fragmentation in situ in gerbil hippocampus following transient forebrain ischemia
    • T. Iwai, A. Hara, M. Niwa, M. Nozaki, T. Uematsu, N. Sakai, and H. Yamada Temporal profile of nuclear DNA fragmentation in situ in gerbil hippocampus following transient forebrain ischemia Brain Res. 671 1995 305 308
    • (1995) Brain Res. , vol.671 , pp. 305-308
    • Iwai, T.1    Hara, A.2    Niwa, M.3    Nozaki, M.4    Uematsu, T.5    Sakai, N.6    Yamada, H.7
  • 28
    • 0033805442 scopus 로고    scopus 로고
    • Oxidative stress and apoptosis
    • K. Kannan, and S.K. Jain Oxidative stress and apoptosis Pathophysiology 7 2000 153 163
    • (2000) Pathophysiology , vol.7 , pp. 153-163
    • Kannan, K.1    Jain, S.K.2
  • 30
    • 0029804576 scopus 로고    scopus 로고
    • Thioredoxin: A redox-regulating cellular cofactor for glucocorticoid hormone action. Cross talk between endocrine control of stress response and cellular antioxidant defense system
    • Y. Makino, K. Okamoto, N. Yoshikawa, M. Aoshima, K. Hirota, J. Yodoi, K. Umesono, I. Makino, and H. Tanaka Thioredoxin: a redox-regulating cellular cofactor for glucocorticoid hormone action. Cross talk between endocrine control of stress response and cellular antioxidant defense system J. Clin. Invest. 98 1996 2469 2477
    • (1996) J. Clin. Invest. , vol.98 , pp. 2469-2477
    • Makino, Y.1    Okamoto, K.2    Yoshikawa, N.3    Aoshima, M.4    Hirota, K.5    Yodoi, J.6    Umesono, K.7    Makino, I.8    Tanaka, H.9
  • 31
    • 0033613871 scopus 로고    scopus 로고
    • Direct association with thioredoxin allows redox regulation of glucocorticoid receptor function
    • Y. Makino, N. Yoshikawa, K. Okamoto, K. Hirota, J. Yodoi, I. Makino, and H. Tanaka Direct association with thioredoxin allows redox regulation of glucocorticoid receptor function J. Biol. Chem. 274 1999 3182 3188
    • (1999) J. Biol. Chem. , vol.274 , pp. 3182-3188
    • Makino, Y.1    Yoshikawa, N.2    Okamoto, K.3    Hirota, K.4    Yodoi, J.5    Makino, I.6    Tanaka, H.7
  • 32
    • 0031816990 scopus 로고    scopus 로고
    • Oxidative stress leads to a rapid alteration of transferrin receptor intravesicular trafficking
    • W. Malorni, U. Testa, G. Rainaldi, E. Tritarelli, and C. Peschle Oxidative stress leads to a rapid alteration of transferrin receptor intravesicular trafficking Exp. Cell Res. 241 1998 102 116
    • (1998) Exp. Cell Res. , vol.241 , pp. 102-116
    • Malorni, W.1    Testa, U.2    Rainaldi, G.3    Tritarelli, E.4    Peschle, C.5
  • 34
    • 0028883179 scopus 로고
    • Tumor suppressor p53 is a direct transcriptional activator of the human bax gene
    • T. Miyashita, and J.C. Reed Tumor suppressor p53 is a direct transcriptional activator of the human bax gene Cell 80 1995 293 299
    • (1995) Cell , vol.80 , pp. 293-299
    • Miyashita, T.1    Reed, J.C.2
  • 35
    • 0028106431 scopus 로고
    • Adult T cell leukemia-derived factor/human thioredoxin protects endothelial F-2 cell injury caused by activated neutrophils or hydrogen peroxide
    • H. Nakamura, M. Matsuda, K. Furuke, Y. Kitaoka, S. Iwata, K. Toda, T. Inamoto, Y. Yamaoka, K. Ozawa, and J. Yodoi Adult T cell leukemia-derived factor/human thioredoxin protects endothelial F-2 cell injury caused by activated neutrophils or hydrogen peroxide Immunol. Lett. 42 1994 75 80
    • (1994) Immunol. Lett. , vol.42 , pp. 75-80
    • Nakamura, H.1    Matsuda, M.2    Furuke, K.3    Kitaoka, Y.4    Iwata, S.5    Toda, K.6    Inamoto, T.7    Yamaoka, Y.8    Ozawa, K.9    Yodoi, J.10
  • 36
    • 0033988716 scopus 로고    scopus 로고
    • Cytochrome c release from mitochondria to the cytosol was suppressed in the ischemia-tolerance-induced hippocampal CA1 region after 5-min forebrain ischemia in gerbils
    • H. Nakatsuka, S. Ohta, J. Tanaka, K. Toku, Y. Kumon, N. Maeda, M. Sakanaka, and S. Sakaki Cytochrome c release from mitochondria to the cytosol was suppressed in the ischemia-tolerance-induced hippocampal CA1 region after 5-min forebrain ischemia in gerbils Neurosci. Lett. 278 2000 53 56
    • (2000) Neurosci. Lett. , vol.278 , pp. 53-56
    • Nakatsuka, H.1    Ohta, S.2    Tanaka, J.3    Toku, K.4    Kumon, Y.5    Maeda, N.6    Sakanaka, M.7    Sakaki, S.8
  • 38
    • 0035029131 scopus 로고    scopus 로고
    • Properties and biological activities of thioredoxins
    • G. Powis, and W.R. Montfort Properties and biological activities of thioredoxins Annu. Rev. Pharmacol. Toxicol. 41 2001 261 295
    • (2001) Annu. Rev. Pharmacol. Toxicol. , vol.41 , pp. 261-295
    • Powis, G.1    Montfort, W.R.2
  • 39
    • 5644284041 scopus 로고    scopus 로고
    • The action of hypobaric hypoxia on the expression of immediate early gene products and the morphological alterations in rat brain neurons: A correcting effect of preconditioning
    • in press.
    • E.A. Rybnikova, L.I. Hozhai, E.I. Tjulkova, T.S. Gluschenko, N.A. Sitnik, M. Pelto-Huikko, V.A. Otellin, M.O. Samoilov, The action of hypobaric hypoxia on the expression of immediate early gene products and the morphological alterations in rat brain neurons: a correcting effect of preconditioning, Morphologia 2 (2004) in press.
    • (2004) Morphologia , vol.2
    • Rybnikova, E.A.1    Hozhai, L.I.2    Tjulkova, E.I.3    Gluschenko, T.S.4    Sitnik, N.A.5    Pelto-Huikko, M.6    Otellin, V.A.7    Samoilov, M.O.8
  • 42
  • 43
    • 0028903502 scopus 로고
    • Thiol-mediated redox regulation of apoptosis. Possible roles of cellular thiols other than glutathione in T cell apoptosis
    • N. Sato, S. Iwata, K. Nakamura, T. Hori, K. Mori, and J. Yodoi Thiol-mediated redox regulation of apoptosis. Possible roles of cellular thiols other than glutathione in T cell apoptosis J. Immunol. 154 1995 3194 3203
    • (1995) J. Immunol. , vol.154 , pp. 3194-3203
    • Sato, N.1    Iwata, S.2    Nakamura, K.3    Hori, T.4    Mori, K.5    Yodoi, J.6
  • 44
    • 0344585940 scopus 로고    scopus 로고
    • The interacting pathways for prevention and repair of oxidative DNA damage
    • G. Slupphaug, B. Kavli, and H.E. Krokan The interacting pathways for prevention and repair of oxidative DNA damage Mutat. Res. 531 2003 231 251
    • (2003) Mutat. Res. , vol.531 , pp. 231-251
    • Slupphaug, G.1    Kavli, B.2    Krokan, H.E.3
  • 46
    • 0142139346 scopus 로고    scopus 로고
    • Reactive oxygen radicals and pathogenesis of neuronal death after cerebral ischemia
    • T. Sugawara, and P.H. Chan Reactive oxygen radicals and pathogenesis of neuronal death after cerebral ischemia Antioxid. Redox Signal. 5 2003 597 607
    • (2003) Antioxid. Redox Signal. , vol.5 , pp. 597-607
    • Sugawara, T.1    Chan, P.H.2
  • 47
    • 0032540857 scopus 로고    scopus 로고
    • Expression and distribution of redox regulatory protein, thioredoxin during transient focal brain ischemia in the rat
    • Y. Takagi, F. Horikawa, K. Nozaki, T. Sugino, N. Hashimoto, and J. Yodoi Expression and distribution of redox regulatory protein, thioredoxin during transient focal brain ischemia in the rat Neurosci. Lett. 251 1998 25 28
    • (1998) Neurosci. Lett. , vol.251 , pp. 25-28
    • Takagi, Y.1    Horikawa, F.2    Nozaki, K.3    Sugino, T.4    Hashimoto, N.5    Yodoi, J.6
  • 49
    • 0031918327 scopus 로고    scopus 로고
    • Redox control of neuronal damage during brain ischemia after middle cerebral artery occlusion in the rat: Immunohistochemical and hybridization studies of thioredoxin
    • Y. Takagi, T. Tokime, K. Nozaki, Y. Gon, H. Kikuchi, and J. Yodoi Redox control of neuronal damage during brain ischemia after middle cerebral artery occlusion in the rat: immunohistochemical and hybridization studies of thioredoxin J. Cereb. Blood Flow Metab. 18 1998 206 214
    • (1998) J. Cereb. Blood Flow Metab. , vol.18 , pp. 206-214
    • Takagi, Y.1    Tokime, T.2    Nozaki, K.3    Gon, Y.4    Kikuchi, H.5    Yodoi, J.6
  • 50
    • 0027436461 scopus 로고
    • Astroglial expression of ATL-derived factor, a human thioredoxin homologue, in the gerbil brain after transient global ischemia
    • H. Tomimoto, I. Akiguchi, H. Wakita, J. Kimura, K. Hori, and J. Yodoi Astroglial expression of ATL-derived factor, a human thioredoxin homologue, in the gerbil brain after transient global ischemia Brain Res. 625 1993 1 8
    • (1993) Brain Res. , vol.625 , pp. 1-8
    • Tomimoto, H.1    Akiguchi, I.2    Wakita, H.3    Kimura, J.4    Hori, K.5    Yodoi, J.6
  • 55
    • 0034708684 scopus 로고    scopus 로고
    • Oxidative stress disrupts glucocorticoid hormone-dependent transcription of the amiloride-sensitive epithelial sodium channel alpha-subunit in lung epithelial cells through ERK-dependent and thioredoxin-sensitive pathways
    • H.C. Wang, M.D. Zentner, H.T. Deng, K.J. Kim, R. Wu, P.C. Yang, and D.K. Ann Oxidative stress disrupts glucocorticoid hormone-dependent transcription of the amiloride-sensitive epithelial sodium channel alpha-subunit in lung epithelial cells through ERK-dependent and thioredoxin-sensitive pathways J. Biol. Chem. 275 2000 8600 8609
    • (2000) J. Biol. Chem. , vol.275 , pp. 8600-8609
    • Wang, H.C.1    Zentner, M.D.2    Deng, H.T.3    Kim, K.J.4    Wu, R.5    Yang, P.C.6    Ann, D.K.7
  • 57
    • 0036735392 scopus 로고    scopus 로고
    • The redox protein thioredoxin-1 (Trx-1) increases hypoxia-inducible factor 1alpha protein expression: Trx-1 overexpression results in increased vascular endothelial growth factor production and enhanced tumor angiogenesis
    • S.J. Welsh, W.T. Bellamy, M.M. Briehl, and G. Powis The redox protein thioredoxin-1 (Trx-1) increases hypoxia-inducible factor 1alpha protein expression: Trx-1 overexpression results in increased vascular endothelial growth factor production and enhanced tumor angiogenesis Cancer Res. 62 2002 5089 5095
    • (2002) Cancer Res. , vol.62 , pp. 5089-5095
    • Welsh, S.J.1    Bellamy, W.T.2    Briehl, M.M.3    Powis, G.4
  • 58
    • 0142144338 scopus 로고    scopus 로고
    • The thioredoxin redox inhibitors 1-methylpropyl 2-imidazolyl disulfide and pleurotin inhibit hypoxia-induced factor 1alpha and vascular endothelial growth factor formation
    • S.J. Welsh, R.R. Williams, A. Birmingham, D.J. Newman, D.L. Kirkpatrick, and G. Powis The thioredoxin redox inhibitors 1-methylpropyl 2-imidazolyl disulfide and pleurotin inhibit hypoxia-induced factor 1alpha and vascular endothelial growth factor formation Mol. Cancer Ther. 2 2003 235 243
    • (2003) Mol. Cancer Ther. , vol.2 , pp. 235-243
    • Welsh, S.J.1    Williams, R.R.2    Birmingham, A.3    Newman, D.J.4    Kirkpatrick, D.L.5    Powis, G.6
  • 61
    • 0035012926 scopus 로고    scopus 로고
    • Both caspase-dependent and caspase-independent pathways may be involved in hippocampal CA1 neuronal death because of loss of cytochrome c from mitochondria in a rat forebrain ischemia model
    • R.Z. Zhan, C. Wu, H. Fujihara, K. Taga, S. Qi, M. Naito, and K. Shimoji Both caspase-dependent and caspase-independent pathways may be involved in hippocampal CA1 neuronal death because of loss of cytochrome c From mitochondria in a rat forebrain ischemia model J. Cereb. Blood Flow Metab. 21 2001 529 540
    • (2001) J. Cereb. Blood Flow Metab. , vol.21 , pp. 529-540
    • Zhan, R.Z.1    Wu, C.2    Fujihara, H.3    Taga, K.4    Qi, S.5    Naito, M.6    Shimoji, K.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.