메뉴 건너뛰기




Volumn 208, Issue 2, 2005, Pages 223-233

NO and transcriptional regulation: From signaling to death

Author keywords

Apoptosis; HIF 1 ; Hypoxia; Mdm2; p53; Proteasome; pVHL; Ubiquitination

Indexed keywords

GENE PRODUCT; HYPOXIA INDUCIBLE FACTOR 1ALPHA; NITRIC OXIDE; OXYGEN; PROTEIN P53; REACTIVE NITROGEN SPECIES;

EID: 13244255346     PISSN: 0300483X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tox.2004.11.021     Document Type: Article
Times cited : (37)

References (90)
  • 1
    • 0035425503 scopus 로고    scopus 로고
    • Nitric oxide synthases: Structure, function and inhibition
    • W.K. Alderton, C.E. Cooper, and R.G. Knowles Nitric oxide synthases: structure, function and inhibition Biochem. J. 357 2001 593 615
    • (2001) Biochem. J. , vol.357 , pp. 593-615
    • Alderton, W.K.1    Cooper, C.E.2    Knowles, R.G.3
  • 3
    • 0035253023 scopus 로고    scopus 로고
    • Nitric oxide and the regulation of gene expression
    • C. Bogdan Nitric oxide and the regulation of gene expression Trends Cell Biol. 11 2001 66 75
    • (2001) Trends Cell Biol. , vol.11 , pp. 66-75
    • Bogdan, C.1
  • 4
    • 0034282102 scopus 로고    scopus 로고
    • An intact HDM2 RING-finger domain is required for nuclear exclusion of p53
    • S.D. Boyd, K.Y. Tsai, and T. Jacks An intact HDM2 RING-finger domain is required for nuclear exclusion of p53 Nat. Cell Biol. 2 2000 563 568
    • (2000) Nat. Cell Biol. , vol.2 , pp. 563-568
    • Boyd, S.D.1    Tsai, K.Y.2    Jacks, T.3
  • 5
    • 0035834409 scopus 로고    scopus 로고
    • A conserved family of prolyl-4-hydroxylases that modify HIF
    • R.K. Bruick, and S.L. McKnight A conserved family of prolyl-4- hydroxylases that modify HIF Science 294 2001 1337 1340
    • (2001) Science , vol.294 , pp. 1337-1340
    • Bruick, R.K.1    McKnight, S.L.2
  • 6
    • 0034899785 scopus 로고    scopus 로고
    • Transcription factors p53 and HIF-1alpha as targets of nitric oxide
    • B. Brüne, A. von Knethen, and K.B. Sandau Transcription factors p53 and HIF-1alpha as targets of nitric oxide Cell. Signal. 13 2001 525 533
    • (2001) Cell. Signal. , vol.13 , pp. 525-533
    • Brüne, B.1    Von Knethen, A.2    Sandau, K.B.3
  • 7
    • 0042665423 scopus 로고    scopus 로고
    • Nitric oxide: NO apoptosis or turning it ON?
    • B. Brüne Nitric oxide: NO apoptosis or turning it ON? Cell Death Differ. 10 2003 864 869
    • (2003) Cell Death Differ. , vol.10 , pp. 864-869
    • Brüne, B.1
  • 8
    • 0037418602 scopus 로고    scopus 로고
    • Nitric oxide evoked p53-accumulation and apoptosis
    • B. Brüne, and N. Schneiderhan Nitric oxide evoked p53-accumulation and apoptosis Toxicol. Lett. 139 2003 119 123
    • (2003) Toxicol. Lett. , vol.139 , pp. 119-123
    • Brüne, B.1    Schneiderhan, N.2
  • 9
    • 0037262072 scopus 로고    scopus 로고
    • The role of nitric oxide (NO) in stability regulation of hypoxia inducible factor-1alpha (HIF-1alpha)
    • B. Brüne, and J. Zhou The role of nitric oxide (NO) in stability regulation of hypoxia inducible factor-1alpha (HIF-1alpha) Curr. Med. Chem. 10 2003 845 855
    • (2003) Curr. Med. Chem. , vol.10 , pp. 845-855
    • Brüne, B.1    Zhou, J.2
  • 10
    • 0028858786 scopus 로고
    • NO, nitrosonium ions, nitroxide ions, nitrosothiols and iron-nitrosyls in biology: A chemist's perspective
    • A.R. Butler, F.W. Flitney, and D.L. Williams NO, nitrosonium ions, nitroxide ions, nitrosothiols and iron-nitrosyls in biology: a chemist's perspective Trends Pharmacol. Sci. 16 1995 18 22
    • (1995) Trends Pharmacol. Sci. , vol.16 , pp. 18-22
    • Butler, A.R.1    Flitney, F.W.2    Williams, D.L.3
  • 11
    • 0029913730 scopus 로고    scopus 로고
    • Mdm-2 inhibits the G1 arrest and apoptosis functions of the p53 tumor suppressor protein
    • J. Chen, X. Wu, J. Lin, and A.J. Levine Mdm-2 inhibits the G1 arrest and apoptosis functions of the p53 tumor suppressor protein Mol. Cell Biol. 16 1996 2445 2452
    • (1996) Mol. Cell Biol. , vol.16 , pp. 2445-2452
    • Chen, J.1    Wu, X.2    Lin, J.3    Levine, A.J.4
  • 12
    • 0037083845 scopus 로고    scopus 로고
    • A dominant-negative isoform lacking exons 11 and 12 of the human hypoxia-inducible factor-1alpha gene
    • Y.S. Chun, E. Choi, T.Y. Kim, M.S. Kim, and J.W. Park A dominant-negative isoform lacking exons 11 and 12 of the human hypoxia-inducible factor-1alpha gene Biochem. J. 362 2002 71 79
    • (2002) Biochem. J. , vol.362 , pp. 71-79
    • Chun, Y.S.1    Choi, E.2    Kim, T.Y.3    Kim, M.S.4    Park, J.W.5
  • 13
    • 0033802982 scopus 로고    scopus 로고
    • Nitric oxide-dependent activation of p53 suppresses bleomycin-induced apoptosis in the lung
    • D.W. Davis, D.A. Weidner, A. Holian, and D.J. McConkey Nitric oxide-dependent activation of p53 suppresses bleomycin-induced apoptosis in the lung J. Exp. Med. 192 2000 857 869
    • (2000) J. Exp. Med. , vol.192 , pp. 857-869
    • Davis, D.W.1    Weidner, D.A.2    Holian, A.3    McConkey, D.J.4
  • 14
    • 0033572746 scopus 로고    scopus 로고
    • Serine15 phosphorylation stimulates p53 transactivation but does not directly influence interaction with HDM2
    • N. Dumaz, and D.W. Meek Serine15 phosphorylation stimulates p53 transactivation but does not directly influence interaction with HDM2 EMBO J. 18 1999 7002 7010
    • (1999) EMBO J. , vol.18 , pp. 7002-7010
    • Dumaz, N.1    Meek, D.W.2
  • 16
    • 0032512057 scopus 로고    scopus 로고
    • Mdm2 association with p53 targets its ubiquitination
    • S.Y. Fuchs, V. Adler, T. Buschmann, X. Wu, and Z. Ronai Mdm2 association with p53 targets its ubiquitination Oncogene 17 1998 2543 2547
    • (1998) Oncogene , vol.17 , pp. 2543-2547
    • Fuchs, S.Y.1    Adler, V.2    Buschmann, T.3    Wu, X.4    Ronai, Z.5
  • 17
    • 0030831534 scopus 로고    scopus 로고
    • CRM1 is responsible for intracellular transport mediated by the nuclear export signal
    • M. Fukuda, S. Asano, T. Nakamura, M. Adachi, M. Yoshida, M. Yanagida, and E. Nishida CRM1 is responsible for intracellular transport mediated by the nuclear export signal Nature 390 1997 308 311
    • (1997) Nature , vol.390 , pp. 308-311
    • Fukuda, M.1    Asano, S.2    Nakamura, T.3    Adachi, M.4    Yoshida, M.5    Yanagida, M.6    Nishida, E.7
  • 18
    • 0019195506 scopus 로고
    • The obligatory role of endothelial cells in the relaxation of arterial smooth muscle by acetylcholine
    • R.F. Furchgott, and J.V. Zawadzki The obligatory role of endothelial cells in the relaxation of arterial smooth muscle by acetylcholine Nature 288 1980 373 376
    • (1980) Nature , vol.288 , pp. 373-376
    • Furchgott, R.F.1    Zawadzki, J.V.2
  • 19
    • 0034282220 scopus 로고    scopus 로고
    • The MDM2 RING-finger domain is required to promote p53 nuclear export
    • R.K. Geyer, Z.K. Yu, and C.G. Maki The MDM2 RING-finger domain is required to promote p53 nuclear export Nat. Cell Biol. 2 2000 569 573
    • (2000) Nat. Cell Biol. , vol.2 , pp. 569-573
    • Geyer, R.K.1    Yu, Z.K.2    Maki, C.G.3
  • 21
    • 0035827308 scopus 로고    scopus 로고
    • Molecular biology. Getting p53 out of the nucleus
    • V. Gottifredi, and C. Prives Molecular biology. Getting p53 out of the nucleus Science 292 2001 1851 1852
    • (2001) Science , vol.292 , pp. 1851-1852
    • Gottifredi, V.1    Prives, C.2
  • 22
    • 0032910873 scopus 로고    scopus 로고
    • Nitric oxide. I. Physiological chemistry of nitric oxide and its metabolites: Implications in inflammation
    • M.B. Grisham, D. Jourd'Heuil, and D.A. Wink Nitric oxide. I. Physiological chemistry of nitric oxide and its metabolites: implications in inflammation Am. J. Physiol. 276 1999 G315 G321
    • (1999) Am. J. Physiol. , vol.276
    • Grisham, M.B.1    Jourd'Heuil, D.2    Wink, D.A.3
  • 23
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Y. Haupt, R. Maya, A. Kazaz, and M. Oren Mdm2 promotes the rapid degradation of p53 Nature 387 1997 296 299
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 24
    • 0037191916 scopus 로고    scopus 로고
    • Deconstruction of p53 functions and regulation
    • Y. Haupt, A.I. Robles, C. Prives, and V. Rotter Deconstruction of p53 functions and regulation Oncogene 21 2002 8223 8231
    • (2002) Oncogene , vol.21 , pp. 8223-8231
    • Haupt, Y.1    Robles, A.I.2    Prives, C.3    Rotter, V.4
  • 25
    • 0031574232 scopus 로고    scopus 로고
    • The 2-His-1-carboxylate facial triad-an emerging structural motif in mononuclear non-heme iron(II) enzymes
    • E.L. Hegg, and L. Que Jr. The 2-His-1-carboxylate facial triad-an emerging structural motif in mononuclear non-heme iron(II) enzymes Eur. J. Biochem. 250 1997 625 629
    • (1997) Eur. J. Biochem. , vol.250 , pp. 625-629
    • Hegg, E.L.1    Que Jr., L.2
  • 26
    • 0142242181 scopus 로고    scopus 로고
    • Nitric oxide activates diverse signaling pathways to regulate gene expression
    • J. Hemish, N. Nakaya, V. Mittal, and G. Enikolopov Nitric oxide activates diverse signaling pathways to regulate gene expression J. Biol. Chem. 278 2003 42321 42329
    • (2003) J. Biol. Chem. , vol.278 , pp. 42321-42329
    • Hemish, J.1    Nakaya, N.2    Mittal, V.3    Enikolopov, G.4
  • 28
    • 0031583962 scopus 로고    scopus 로고
    • Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53
    • R. Honda, H. Tanaka, and H. Yasuda Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53 FEBS Lett. 420 1997 25 27
    • (1997) FEBS Lett. , vol.420 , pp. 25-27
    • Honda, R.1    Tanaka, H.2    Yasuda, H.3
  • 29
    • 0033605676 scopus 로고    scopus 로고
    • Inhibition of hypoxia-inducible factor 1 activation by carbon monoxide and nitric oxide
    • L.E. Huang, W.G. Willmore, J. Gu, M.A. Goldberg, and H.F. Bunn Inhibition of hypoxia-inducible factor 1 activation by carbon monoxide and nitric oxide J. Biol. Chem. 274 1999 9038 9044
    • (1999) J. Biol. Chem. , vol.274 , pp. 9038-9044
    • Huang, L.E.1    Willmore, W.G.2    Gu, J.3    Goldberg, M.A.4    Bunn, H.F.5
  • 30
    • 0037490210 scopus 로고    scopus 로고
    • Hypoxia-inducible factor and its biomedical relevance
    • L.E. Huang, and H.F. Bunn Hypoxia-inducible factor and its biomedical relevance J. Biol. Chem. 278 2003 19575 19578
    • (2003) J. Biol. Chem. , vol.278 , pp. 19575-19578
    • Huang, L.E.1    Bunn, H.F.2
  • 31
    • 0032756587 scopus 로고    scopus 로고
    • Tumor suppressor p53 but not cGMP mediates NO-induced expression of p21 (Waf1/Cip1/Sdi1) in vascular smooth muscle cells
    • A. Ishida, T. Sasaguri, Y. Miwa, C. Kosaka, Y. Taba, and T. Abumiya Tumor suppressor p53 but not cGMP mediates NO-induced expression of p21 (Waf1/Cip1/Sdi1) in vascular smooth muscle cells Mol. Pharmacol. 56 1999 938 946
    • (1999) Mol. Pharmacol. , vol.56 , pp. 938-946
    • Ishida, A.1    Sasaguri, T.2    Miwa, Y.3    Kosaka, C.4    Taba, Y.5    Abumiya, T.6
  • 34
    • 0037098081 scopus 로고    scopus 로고
    • How oxygen makes its presence felt
    • W.G. Kaelin Jr. How oxygen makes its presence felt Genes Dev. 16 2002 1441 1445
    • (2002) Genes Dev. , vol.16 , pp. 1441-1445
    • Kaelin Jr., W.G.1
  • 35
    • 0033525830 scopus 로고    scopus 로고
    • Regulation of the hypoxia-inducible transcription factor 1alpha by the ubiquitin-proteasome pathway
    • P.J. Kallio, W.J. Wilson, S. O'Brien, Y. Makino, and L. Poellinger Regulation of the hypoxia-inducible transcription factor 1alpha by the ubiquitin-proteasome pathway J. Biol. Chem. 274 1999 6519 6525
    • (1999) J. Biol. Chem. , vol.274 , pp. 6519-6525
    • Kallio, P.J.1    Wilson, W.J.2    O'Brien, S.3    Makino, Y.4    Poellinger, L.5
  • 36
    • 1642453685 scopus 로고    scopus 로고
    • Nitric oxide induces hypoxia-inducible factor 1 activation that is dependent on MAP kinase and phosphatidylinositol 3-kinase signaling
    • K. Kasuno, S. Takabuchi, K. Fukuda, S. Kizaka-Kondoh, J. Yodoi, T. Adachi, G.L. Semenza, and K. Hirota Nitric oxide induces hypoxia-inducible factor 1 activation that is dependent on MAP kinase and phosphatidylinositol 3-kinase signaling J. Biol. Chem. 279 2004 2550 2558
    • (2004) J. Biol. Chem. , vol.279 , pp. 2550-2558
    • Kasuno, K.1    Takabuchi, S.2    Fukuda, K.3    Kizaka-Kondoh, S.4    Yodoi, J.5    Adachi, T.6    Semenza, G.L.7    Hirota, K.8
  • 37
    • 0033975850 scopus 로고    scopus 로고
    • Hypoxia response element of the human vascular endothelial growth factor gene mediates transcriptional regulation by nitric oxide: Control of hypoxia-inducible factor-1 activity by nitric oxide
    • H. Kimura, A. Weisz, Y. Kurashima, K. Hashimoto, T. Ogura, F. D'Acquisto, R. Addeo, M. Makuuchi, and H. Esumi Hypoxia response element of the human vascular endothelial growth factor gene mediates transcriptional regulation by nitric oxide: control of hypoxia-inducible factor-1 activity by nitric oxide Blood 95 2000 189 197
    • (2000) Blood , vol.95 , pp. 189-197
    • Kimura, H.1    Weisz, A.2    Kurashima, Y.3    Hashimoto, K.4    Ogura, T.5    D'Acquisto, F.6    Addeo, R.7    Makuuchi, M.8    Esumi, H.9
  • 38
    • 0035910429 scopus 로고    scopus 로고
    • Identification of hypoxia-inducible factor 1 ancillary sequence and its function in vascular endothelial growth factor gene induction by hypoxia and nitric oxide
    • H. Kimura, A. Weisz, T. Ogura, Y. Hitomi, Y. Kurashima, K. Hashimoto, F. D'Acquisto, M. Makuuchi, and H. Esumi Identification of hypoxia-inducible factor 1 ancillary sequence and its function in vascular endothelial growth factor gene induction by hypoxia and nitric oxide J. Biol. Chem. 276 2001 2292 2298
    • (2001) J. Biol. Chem. , vol.276 , pp. 2292-2298
    • Kimura, H.1    Weisz, A.2    Ogura, T.3    Hitomi, Y.4    Kurashima, Y.5    Hashimoto, K.6    D'Acquisto, F.7    Makuuchi, M.8    Esumi, H.9
  • 39
    • 0036324335 scopus 로고    scopus 로고
    • NO nomenclature?
    • W.H. Koppenol NO nomenclature? Nitric Oxide 6 2002 96 98
    • (2002) Nitric Oxide , vol.6 , pp. 96-98
    • Koppenol, W.H.1
  • 40
    • 0030965946 scopus 로고    scopus 로고
    • Regulation of p53 stability by Mdm2
    • M.H. Kubbutat, S.N. Jones, and K.H. Vousden Regulation of p53 stability by Mdm2 Nature 387 1997 299 303
    • (1997) Nature , vol.387 , pp. 299-303
    • Kubbutat, M.H.1    Jones, S.N.2    Vousden, K.H.3
  • 41
    • 0031702817 scopus 로고    scopus 로고
    • Regulation of Mdm2-directed degradation by the C terminus of p53
    • M.H. Kubbutat, R.L. Ludwig, M. Ashcroft, and K.H. Vousden Regulation of Mdm2-directed degradation by the C terminus of p53 Mol. Cell Biol. 18 1998 5690 5698
    • (1998) Mol. Cell Biol. , vol.18 , pp. 5690-5698
    • Kubbutat, M.H.1    Ludwig, R.L.2    Ashcroft, M.3    Vousden, K.H.4
  • 43
    • 0036469038 scopus 로고    scopus 로고
    • Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch
    • D. Lando, D.J. Peet, D.A. Whelan, J.J. Gorman, and M.L. Whitelaw Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch Science 295 2002 858 861
    • (2002) Science , vol.295 , pp. 858-861
    • Lando, D.1    Peet, D.J.2    Whelan, D.A.3    Gorman, J.J.4    Whitelaw, M.L.5
  • 44
    • 0036679174 scopus 로고    scopus 로고
    • Nitric oxide-induced genotoxicity, mitochondrial damage, and apoptosis in human lymphoblastoid cells expressing wild-type and mutant p53
    • C.Q. Li, L.J. Trudel, and G.N. Wogan Nitric oxide-induced genotoxicity, mitochondrial damage, and apoptosis in human lymphoblastoid cells expressing wild-type and mutant p53 Proc. Natl. Acad. Sci. U.S.A. 99 2002 10364 10369
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 10364-10369
    • Li, C.Q.1    Trudel, L.J.2    Wogan, G.N.3
  • 45
    • 0034823780 scopus 로고    scopus 로고
    • Regulation of p53 localization
    • S.H. Liang, and M.F. Clarke Regulation of p53 localization Eur. J. Biochem. 268 2001 2779 2783
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2779-2783
    • Liang, S.H.1    Clarke, M.F.2
  • 46
    • 0032511014 scopus 로고    scopus 로고
    • Carbon monoxide and nitric oxide suppress the hypoxic induction of vascular endothelial growth factor gene via the 5′ enhancer
    • Y. Liu, H. Christou, T. Morita, E. Laughner, G.L. Semenza, and S. Kourembanas Carbon monoxide and nitric oxide suppress the hypoxic induction of vascular endothelial growth factor gene via the 5′ enhancer J. Biol. Chem. 273 1998 15257 15262
    • (1998) J. Biol. Chem. , vol.273 , pp. 15257-15262
    • Liu, Y.1    Christou, H.2    Morita, T.3    Laughner, E.4    Semenza, G.L.5    Kourembanas, S.6
  • 47
    • 0029952441 scopus 로고    scopus 로고
    • In vivo ubiquitination and proteasome-mediated degradation of p53
    • C.G. Maki, J.M. Huibregtse, and P.M. Howley In vivo ubiquitination and proteasome-mediated degradation of p53 Cancer Res. 56 1996 2649 2654
    • (1996) Cancer Res. , vol.56 , pp. 2649-2654
    • Maki, C.G.1    Huibregtse, J.M.2    Howley, P.M.3
  • 48
    • 0033523015 scopus 로고    scopus 로고
    • Oligomerization is required for p53 to be efficiently ubiquitinated by MDM2
    • C.G. Maki Oligomerization is required for p53 to be efficiently ubiquitinated by MDM2 J. Biol. Chem. 274 1999 16531 16535
    • (1999) J. Biol. Chem. , vol.274 , pp. 16531-16535
    • Maki, C.G.1
  • 49
    • 0033815334 scopus 로고    scopus 로고
    • Nitrosation and oxidation in the regulation of gene expression
    • H.E. Marshall, K. Merchant, and J.S. Stamler Nitrosation and oxidation in the regulation of gene expression FASEB J. 14 2000 1889 1900
    • (2000) FASEB J. , vol.14 , pp. 1889-1900
    • Marshall, H.E.1    Merchant, K.2    Stamler, J.S.3
  • 50
    • 0346027211 scopus 로고    scopus 로고
    • Regulation of hypoxia-inducible factor-1alpha by nitric oxide through mitochondria-dependent and -independent pathways
    • J. Mateo, M. Garcia-Lecea, S. Cadenas, C. Hernandez, and S. Moncada Regulation of hypoxia-inducible factor-1alpha by nitric oxide through mitochondria-dependent and -independent pathways Biochem. J. 376 2003 537 544
    • (2003) Biochem. J. , vol.376 , pp. 537-544
    • Mateo, J.1    Garcia-Lecea, M.2    Cadenas, S.3    Hernandez, C.4    Moncada, S.5
  • 51
    • 0034805815 scopus 로고    scopus 로고
    • Cadmium induces phosphorylation of p53 at serine 15 in MCF-7 cells
    • M. Matsuoka, and H. Igisu Cadmium induces phosphorylation of p53 at serine 15 in MCF-7 cells Biochem. Biophys. Res. Commun. 282 2001 1120 1125
    • (2001) Biochem. Biophys. Res. Commun. , vol.282 , pp. 1120-1125
    • Matsuoka, M.1    Igisu, H.2
  • 53
    • 0035573882 scopus 로고    scopus 로고
    • The pVHL-HIF-1 system. A key mediator of oxygen homeostasis
    • P.H. Maxwell, C.W. Pugh, and P.J. Ratcliffe The pVHL-HIF-1 system. A key mediator of oxygen homeostasis Adv. Exp. Med. Biol. 502 2001 365 376
    • (2001) Adv. Exp. Med. Biol. , vol.502 , pp. 365-376
    • Maxwell, P.H.1    Pugh, C.W.2    Ratcliffe, P.J.3
  • 55
    • 0042469448 scopus 로고    scopus 로고
    • Nitric oxide impairs normoxic degradation of HIF-1alpha by inhibition of prolyl hydroxylases
    • E. Metzen, J. Zhou, W. Jelkmann, J. Fandrey, and B. Brüne Nitric oxide impairs normoxic degradation of HIF-1alpha by inhibition of prolyl hydroxylases Mol. Biol. Cell 14 2003 3470 3481
    • (2003) Mol. Biol. Cell , vol.14 , pp. 3470-3481
    • Metzen, E.1    Zhou, J.2    Jelkmann, W.3    Fandrey, J.4    Brüne, B.5
  • 56
    • 0028863627 scopus 로고
    • Molecular mechanisms and therapeutic strategies related to nitric oxide
    • S. Moncada, and E.A. Higgs Molecular mechanisms and therapeutic strategies related to nitric oxide FASEB J. 9 1995 1319 1330
    • (1995) FASEB J. , vol.9 , pp. 1319-1330
    • Moncada, S.1    Higgs, E.A.2
  • 57
    • 0034649496 scopus 로고    scopus 로고
    • Specific pattern of p53 phosphorylation during nitric oxide-induced cell cycle arrest
    • N. Nakaya, S.W. Lowe, Y. Taya, A. Chenchik, and G. Enikolopov Specific pattern of p53 phosphorylation during nitric oxide-induced cell cycle arrest Oncogene 19 2000 6369 6375
    • (2000) Oncogene , vol.19 , pp. 6369-6375
    • Nakaya, N.1    Lowe, S.W.2    Taya, Y.3    Chenchik, A.4    Enikolopov, G.5
  • 58
    • 0026629902 scopus 로고
    • Nitric oxide as a secretory product of mammalian cells
    • C. Nathan Nitric oxide as a secretory product of mammalian cells FASEB J. 6 1992 3051 3064
    • (1992) FASEB J. , vol.6 , pp. 3051-3064
    • Nathan, C.1
  • 59
    • 0034255209 scopus 로고    scopus 로고
    • Reactive oxygen and nitrogen intermediates in the relationship between mammalian hosts and microbial pathogens
    • C. Nathan, and M.U. Shiloh Reactive oxygen and nitrogen intermediates in the relationship between mammalian hosts and microbial pathogens Proc. Natl. Acad. Sci. U.S.A. 97 2000 8841 8848
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 8841-8848
    • Nathan, C.1    Shiloh, M.U.2
  • 61
    • 0026740449 scopus 로고
    • Amplification of a gene encoding a p53-associated protein in human sarcomas
    • J.D. Oliner, K.W. Kinzler, P.S. Meltzer, D.L. George, and B. Vogelstein Amplification of a gene encoding a p53-associated protein in human sarcomas Nature 358 1992 80 83
    • (1992) Nature , vol.358 , pp. 80-83
    • Oliner, J.D.1    Kinzler, K.W.2    Meltzer, P.S.3    George, D.L.4    Vogelstein, B.5
  • 62
    • 0038075338 scopus 로고    scopus 로고
    • Decision making by p53: Life, death and cancer
    • M. Oren Decision making by p53: life, death and cancer Cell Death Differ. 10 2003 431 442
    • (2003) Cell Death Differ. , vol.10 , pp. 431-442
    • Oren, M.1
  • 63
    • 0033673457 scopus 로고    scopus 로고
    • Normoxic stabilization of hypoxia-inducible factor-1 expression and activity: Redox-dependent effect of nitrogen oxides
    • L.A. Palmer, B. Gaston, and R.A. Johns Normoxic stabilization of hypoxia-inducible factor-1 expression and activity: redox-dependent effect of nitrogen oxides Mol. Pharmacol. 58 2000 1197 1203
    • (2000) Mol. Pharmacol. , vol.58 , pp. 1197-1203
    • Palmer, L.A.1    Gaston, B.2    Johns, R.A.3
  • 64
    • 0037326037 scopus 로고    scopus 로고
    • The von Hippel-Lindau tumor suppressor, hypoxia-inducible factor-1 (HIF-1) degradation, and cancer pathogenesis
    • C.W. Pugh, and P.J. Ratcliffe The von Hippel-Lindau tumor suppressor, hypoxia-inducible factor-1 (HIF-1) degradation, and cancer pathogenesis Semin. Cancer Biol. 13 2003 83 89
    • (2003) Semin. Cancer Biol. , vol.13 , pp. 83-89
    • Pugh, C.W.1    Ratcliffe, P.J.2
  • 66
    • 0344011603 scopus 로고    scopus 로고
    • Disruption of the nucleolus mediates stabilization of p53 in response to DNA damage and other stresses
    • C.P. Rubbi, and J. Milner Disruption of the nucleolus mediates stabilization of p53 in response to DNA damage and other stresses EMBO J. 22 2003 6068 6077
    • (2003) EMBO J. , vol.22 , pp. 6068-6077
    • Rubbi, C.P.1    Milner, J.2
  • 67
    • 0030961006 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1alpha (HIF-1alpha) protein is rapidly degraded by the ubiquitin-proteasome system under normoxic conditions
    • S. Salceda, and J. Caro Hypoxia-inducible factor 1alpha (HIF-1alpha) protein is rapidly degraded by the ubiquitin-proteasome system under normoxic conditions J. Biol. Chem. 272 1997 22642 22647
    • (1997) J. Biol. Chem. , vol.272 , pp. 22642-22647
    • Salceda, S.1    Caro, J.2
  • 68
    • 0035864361 scopus 로고    scopus 로고
    • Accumulation of HIF-1alpha under the influence of nitric oxide
    • K.B. Sandau, J. Fandrey, and B. Brüne Accumulation of HIF-1alpha under the influence of nitric oxide Blood 97 2001 1009 1015
    • (2001) Blood , vol.97 , pp. 1009-1015
    • Sandau, K.B.1    Fandrey, J.2    Brüne, B.3
  • 69
    • 0035955663 scopus 로고    scopus 로고
    • Regulation of the hypoxia-inducible factor 1alpha by the inflammatory mediators nitric oxide and tumor necrosis factor-alpha in contrast to desferroxamine and phenylarsine oxide
    • K.B. Sandau, J. Zhou, T. Kietzmann, and B. Brüne Regulation of the hypoxia-inducible factor 1alpha by the inflammatory mediators nitric oxide and tumor necrosis factor-alpha in contrast to desferroxamine and phenylarsine oxide J. Biol. Chem. 276 2001 39805 39811
    • (2001) J. Biol. Chem. , vol.276 , pp. 39805-39811
    • Sandau, K.B.1    Zhou, J.2    Kietzmann, T.3    Brüne, B.4
  • 70
    • 0028128416 scopus 로고
    • NO at work
    • H.H. Schmidt, and U. Walter NO at work Cell 78 1994 919 925
    • (1994) Cell , vol.78 , pp. 919-925
    • Schmidt, H.H.1    Walter, U.2
  • 71
    • 0038359369 scopus 로고    scopus 로고
    • Nitric oxide induces phosphorylation of p53 and impairs nuclear export
    • N. Schneiderhan, A. Budde, Y. Zhang, and B. Brüne Nitric oxide induces phosphorylation of p53 and impairs nuclear export Oncogene 22 2003 2857 2868
    • (2003) Oncogene , vol.22 , pp. 2857-2868
    • Schneiderhan, N.1    Budde, A.2    Zhang, Y.3    Brüne, B.4
  • 72
    • 0026468180 scopus 로고
    • A nuclear factor induced by hypoxia via de novo protein synthesis binds to the human erythropoietin gene enhancer at a site required for transcriptional activation
    • G.L. Semenza, and G.L. Wang A nuclear factor induced by hypoxia via de novo protein synthesis binds to the human erythropoietin gene enhancer at a site required for transcriptional activation Mol. Cell Biol. 12 1992 5447 5454
    • (1992) Mol. Cell Biol. , vol.12 , pp. 5447-5454
    • Semenza, G.L.1    Wang, G.L.2
  • 73
    • 0034663989 scopus 로고    scopus 로고
    • HIF-1 and human disease: One highly involved factor
    • G.L. Semenza HIF-1 and human disease: one highly involved factor Genes Dev. 14 2000 1983 1991
    • (2000) Genes Dev. , vol.14 , pp. 1983-1991
    • Semenza, G.L.1
  • 74
    • 0036216692 scopus 로고    scopus 로고
    • HIF-1 and tumor progression: Pathophysiology and therapeutics
    • G.L. Semenza HIF-1 and tumor progression: pathophysiology and therapeutics Trends Mol. Med. 8 2002 62 67
    • (2002) Trends Mol. Med. , vol.8 , pp. 62-67
    • Semenza, G.L.1
  • 75
    • 85047695603 scopus 로고    scopus 로고
    • Cell density mediated pericellular hypoxia leads to induction of HIF-1alpha via nitric oxide and Ras/MAP kinase mediated signaling pathways
    • E.A. Sheta, H. Trout, J.J. Gildea, M.A. Harding, and D. Theodorescu Cell density mediated pericellular hypoxia leads to induction of HIF-1alpha via nitric oxide and Ras/MAP kinase mediated signaling pathways Oncogene 20 2001 7624 7634
    • (2001) Oncogene , vol.20 , pp. 7624-7634
    • Sheta, E.A.1    Trout, H.2    Gildea, J.J.3    Harding, M.A.4    Theodorescu, D.5
  • 76
    • 0030667702 scopus 로고    scopus 로고
    • DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2
    • S.Y. Shieh, M. Ikeda, Y. Taya, and C. Prives DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2 Cell 91 1997 325 334
    • (1997) Cell , vol.91 , pp. 325-334
    • Shieh, S.Y.1    Ikeda, M.2    Taya, Y.3    Prives, C.4
  • 79
    • 0028132836 scopus 로고
    • Redox signaling: Nitrosylation and related target interactions of nitric oxide
    • J.S. Stamler Redox signaling: nitrosylation and related target interactions of nitric oxide Cell 78 1994 931 936
    • (1994) Cell , vol.78 , pp. 931-936
    • Stamler, J.S.1
  • 80
    • 0037472651 scopus 로고    scopus 로고
    • HIF-1alpha protein as a target for S-nitrosation
    • V.V. Sumbayev, A. Budde, J. Zhou, and B. Brüne HIF-1alpha protein as a target for S-nitrosation FEBS Lett. 535 2003 106 112
    • (2003) FEBS Lett. , vol.535 , pp. 106-112
    • Sumbayev, V.V.1    Budde, A.2    Zhou, J.3    Brüne, B.4
  • 82
    • 0037075898 scopus 로고    scopus 로고
    • Activation of the p53 tumor suppressor protein
    • K.H. Vousden Activation of the p53 tumor suppressor protein Biochim. Biophys. Acta 1602 2002 47 59
    • (2002) Biochim. Biophys. Acta , vol.1602 , pp. 47-59
    • Vousden, K.H.1
  • 83
    • 0028816847 scopus 로고
    • Purification and characterization of hypoxia-inducible factor 1
    • G.L. Wang, and G.L. Semenza Purification and characterization of hypoxia-inducible factor 1 J. Biol. Chem. 270 1995 1230 1237
    • (1995) J. Biol. Chem. , vol.270 , pp. 1230-1237
    • Wang, G.L.1    Semenza, G.L.2
  • 84
    • 0037013199 scopus 로고    scopus 로고
    • P53 Activation by nitric oxide involves down-regulation of Mdm2
    • X. Wang, D. Michael, G. de Murcia, and M. Oren p53 Activation by nitric oxide involves down-regulation of Mdm2 J. Biol. Chem. 277 2002 15697 15702
    • (2002) J. Biol. Chem. , vol.277 , pp. 15697-15702
    • Wang, X.1    Michael, D.2    De Murcia, G.3    Oren, M.4
  • 85
    • 0038188668 scopus 로고    scopus 로고
    • Nitric oxide promotes p53 nuclear retention and sensitizes neuroblastoma cells to apoptosis by ionizing radiation
    • X. Wang, A. Zalcenstein, and M. Oren Nitric oxide promotes p53 nuclear retention and sensitizes neuroblastoma cells to apoptosis by ionizing radiation Cell Death Differ. 10 2003 468 476
    • (2003) Cell Death Differ. , vol.10 , pp. 468-476
    • Wang, X.1    Zalcenstein, A.2    Oren, M.3
  • 86
    • 0036320934 scopus 로고    scopus 로고
    • 2- regulated gene expression
    • 2-regulated gene expression FASEB J. 16 2002 1151 1162
    • (2002) FASEB J. , vol.16 , pp. 1151-1162
    • Wenger, R.H.1
  • 87
    • 0031876304 scopus 로고    scopus 로고
    • Production of vascular endothelial growth factor by murine macrophages: Regulation by hypoxia, lactate, and the inducible nitric oxide synthase pathway
    • M. Xiong, G. Elson, D. Legarda, and S.J. Leibovich Production of vascular endothelial growth factor by murine macrophages: regulation by hypoxia, lactate, and the inducible nitric oxide synthase pathway Am. J. Pathol. 153 1998 587 598
    • (1998) Am. J. Pathol. , vol.153 , pp. 587-598
    • Xiong, M.1    Elson, G.2    Legarda, D.3    Leibovich, S.J.4
  • 88
    • 0035827335 scopus 로고    scopus 로고
    • A p53 amino-terminal nuclear export signal inhibited by DNA damage-induced phosphorylation
    • Y. Zhang, and Y. Xiong A p53 amino-terminal nuclear export signal inhibited by DNA damage-induced phosphorylation Science 292 2001 1910 1915
    • (2001) Science , vol.292 , pp. 1910-1915
    • Zhang, Y.1    Xiong, Y.2
  • 89
    • 0034915032 scopus 로고    scopus 로고
    • Control of p53 ubiquitination and nuclear export by MDM2 and ARF
    • Y. Zhang, and Y. Xiong Control of p53 ubiquitination and nuclear export by MDM2 and ARF Cell Growth Differ. 12 2001 175 186
    • (2001) Cell Growth Differ. , vol.12 , pp. 175-186
    • Zhang, Y.1    Xiong, Y.2
  • 90
    • 0037303047 scopus 로고    scopus 로고
    • NO and TNF-alpha released from activated macrophages stabilize HIF-1alpha in resting tubular LLC-PK1 cells
    • J. Zhou, J. Fandrey, J. Schumann, G. Tiegs, and B. Brüne NO and TNF-alpha released from activated macrophages stabilize HIF-1alpha in resting tubular LLC-PK1 cells Am. J. Physiol. Cell Physiol. 284 2003 C439 C446
    • (2003) Am. J. Physiol. Cell Physiol. , vol.284
    • Zhou, J.1    Fandrey, J.2    Schumann, J.3    Tiegs, G.4    Brüne, B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.