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Volumn 31, Issue 13, 2011, Pages 2696-2706

A hypoxia-induced positive feedback loop promotes hypoxia-inducible factor 1α stability through mir-210 suppression of glycerol-3-phosphate dehydrogenase 1-like

Author keywords

[No Author keywords available]

Indexed keywords

GLYCEROL 3 PHOSPHATE DEHYDROGENASE; HYPOXIA INDUCIBLE FACTOR 1ALPHA; MICRORNA; MICRORNA 210; PROCOLLAGEN PROLINE 2 OXOGLUTARATE 4 DIOXYGENASE; PROTEASOME; REGULATOR PROTEIN; REGULATOR PROTEIN GPD1L; UNCLASSIFIED DRUG;

EID: 79959425207     PISSN: 02707306     EISSN: 10985549     Source Type: Journal    
DOI: 10.1128/MCB.01242-10     Document Type: Article
Times cited : (195)

References (58)
  • 1
    • 57649178183 scopus 로고    scopus 로고
    • Identification of an alternative mechanism of degradation of the hypoxia-inducible factor-1alpha
    • Andre, H., and T. S. Pereira. 2008. Identification of an alternative mechanism of degradation of the hypoxia-inducible factor-1alpha. J. Biol. Chem. 283:29375-29384.
    • (2008) J. Biol. Chem. , vol.283 , pp. 29375-29384
    • Andre, H.1    Pereira, T.S.2
  • 2
    • 4644318828 scopus 로고    scopus 로고
    • Differential function of the prolyl hydroxylases PHD1, PHD2, and PHD3 in the regulation of hypoxia-inducible factor
    • Appelhoff, R. J., et al. 2004. Differential function of the prolyl hydroxylases PHD1, PHD2, and PHD3 in the regulation of hypoxia-inducible factor. J. Biol. Chem. 279:38458-38465.
    • (2004) J. Biol. Chem. , vol.279 , pp. 38458-38465
    • Appelhoff, R.J.1
  • 3
    • 13944276440 scopus 로고    scopus 로고
    • OS-9 interacts with hypoxia-inducible factor 1alpha and prolyl hydroxylases to promote oxygen-dependent degradation of HIF-1alpha
    • Baek, J. H., et al. 2005. OS-9 interacts with hypoxia-inducible factor 1alpha and prolyl hydroxylases to promote oxygen-dependent degradation of HIF-1alpha. Mol. Cell 17:503-512.
    • (2005) Mol. Cell , vol.17 , pp. 503-512
    • Baek, J.H.1
  • 5
    • 33746055678 scopus 로고    scopus 로고
    • mRNA degradation by miRNAs and GW182 requires both CCR4:NOT deadenylase and DCP1:DCP2 decapping complexes
    • Behm-Ansmant, I., et al. 2006. mRNA degradation by miRNAs and GW182 requires both CCR4:NOT deadenylase and DCP1:DCP2 decapping complexes. Genes Dev. 20:1885-1898.
    • (2006) Genes Dev , vol.20 , pp. 1885-1898
    • Behm-Ansmant, I.1
  • 6
    • 0041465022 scopus 로고    scopus 로고
    • HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1alpha in normoxia
    • Berra, E., et al. 2003. HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1alpha in normoxia. EMBO J. 22:4082-4090.
    • (2003) EMBO J , vol.22 , pp. 4082-4090
    • Berra, E.1
  • 7
    • 0005067144 scopus 로고
    • Low levels of soluble DPN-linked alpha-glycerophosphate dehydrogenase in tumors
    • Boxer, G. E., and C. E. Shonk. 1960. Low levels of soluble DPN-linked alpha-glycerophosphate dehydrogenase in tumors. Cancer Res. 20:85-91.
    • (1960) Cancer Res , vol.20 , pp. 85-91
    • Boxer, G.E.1    Shonk, C.E.2
  • 8
    • 0032053823 scopus 로고    scopus 로고
    • The unique physiology of solid tumors: opportunities (and problems) for cancer therapy
    • Brown, J. M., and A. J. Giaccia. 1998. The unique physiology of solid tumors: opportunities (and problems) for cancer therapy. Cancer Res. 58:1408-1416.
    • (1998) Cancer Res , vol.58 , pp. 1408-1416
    • Brown, J.M.1    Giaccia, A.J.2
  • 9
    • 40949137731 scopus 로고    scopus 로고
    • hsa-miR-210 Is induced by hypoxia and is an independent prognostic factor in breast cancer
    • Camps, C., et al. 2008. hsa-miR-210 Is induced by hypoxia and is an independent prognostic factor in breast cancer. Clin. Cancer Res. 14:1340-1348.
    • (2008) Clin. Cancer Res. , vol.14 , pp. 1340-1348
    • Camps, C.1
  • 10
    • 0033986948 scopus 로고    scopus 로고
    • Redox-regulated recruitment of the transcriptional coactivators CREB-binding protein and SRC-1 to hypoxia-inducible factor 1alpha
    • Carrero, P., et al. 2000. Redox-regulated recruitment of the transcriptional coactivators CREB-binding protein and SRC-1 to hypoxia-inducible factor 1alpha. Mol. Cell. Biol. 20:402-415.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 402-415
    • Carrero, P.1
  • 11
    • 70349478990 scopus 로고    scopus 로고
    • MicroRNA-210 controls mitochondrial metabolism during hypoxia by repressing the iron-sulfur cluster assembly proteins ISCU1/2
    • Chan, S. Y., et al. 2009. MicroRNA-210 controls mitochondrial metabolism during hypoxia by repressing the iron-sulfur cluster assembly proteins ISCU1/2. Cell Metab. 10:273-284.
    • (2009) Cell Metab , vol.10 , pp. 273-284
    • Chan, S.Y.1
  • 12
    • 77955170881 scopus 로고    scopus 로고
    • Hypoxia-regulated microRNA-210 modulates mitochondrial function and decreases ISCU and COX10 expression
    • Chen, Z., Y. Li, H. Zhang, P. Huang, and R. Luthra. 2010. Hypoxia-regulated microRNA-210 modulates mitochondrial function and decreases ISCU and COX10 expression. Oncogene 29:4362-4368.
    • (2010) Oncogene , vol.29 , pp. 4362-4368
    • Chen, Z.1    Li, Y.2    Zhang, H.3    Huang, P.4    Luthra, R.5
  • 13
    • 34249282938 scopus 로고    scopus 로고
    • MicroRNA silencing through RISC recruitment of eIF6
    • Chendrimada, T. P., et al. 2007. MicroRNA silencing through RISC recruitment of eIF6. Nature 447:823-828.
    • (2007) Nature , vol.447 , pp. 823-828
    • Chendrimada, T.P.1
  • 14
    • 0037096732 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-1-dependent regulation of the multidrug resistance (MDR1) gene
    • Comerford, K. M., et al. 2002. Hypoxia-inducible factor-1-dependent regulation of the multidrug resistance (MDR1) gene. Cancer Res. 62:3387-3394.
    • (2002) Cancer Res , vol.62 , pp. 3387-3394
    • Comerford, K.M.1
  • 15
    • 34548316982 scopus 로고    scopus 로고
    • MicroRNA sponges: competitive inhibitors of small RNAs in mammalian cells
    • Ebert, M. S., J. R. Neilson, and P. A. Sharp. 2007. MicroRNA sponges: competitive inhibitors of small RNAs in mammalian cells. Nat. Methods 4:721-726.
    • (2007) Nat. Methods , vol.4 , pp. 721-726
    • Ebert, M.S.1    Neilson, J.R.2    Sharp, P.A.3
  • 16
    • 17944375360 scopus 로고    scopus 로고
    • C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation
    • Epstein, A. C., et al. 2001. C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation. Cell 107:43-54.
    • (2001) Cell , vol.107 , pp. 43-54
    • Epstein, A.C.1
  • 17
    • 0030561363 scopus 로고    scopus 로고
    • The P-glycoprotein multidrug transporter
    • Fardel, O., V. Lecureur, and A. Guillouzo. 1996. The P-glycoprotein multidrug transporter. Gen. Pharmacol. 27:1283-1291.
    • (1996) Gen. Pharmacol. , vol.27 , pp. 1283-1291
    • Fardel, O.1    Lecureur, V.2    Guillouzo, A.3
  • 18
    • 47049119934 scopus 로고    scopus 로고
    • MicroRNA-210 modulates endothelial cell response to hypoxia and inhibits the receptor tyrosine kinase ligand Ephrin-A3
    • Fasanaro, P., et al. 2008. MicroRNA-210 modulates endothelial cell response to hypoxia and inhibits the receptor tyrosine kinase ligand Ephrin-A3. J. Biol. Chem. 283:15878-15883.
    • (2008) J. Biol. Chem. , vol.283 , pp. 15878-15883
    • Fasanaro, P.1
  • 19
    • 71749100911 scopus 로고    scopus 로고
    • An integrated approach for experimental target identification of hypoxia-induced miR-210
    • Fasanaro, P., et al. 2009. An integrated approach for experimental target identification of hypoxia-induced miR-210. J. Biol. Chem. 284:35134-35143.
    • (2009) J. Biol. Chem. , vol.284 , pp. 35134-35143
    • Fasanaro, P.1
  • 20
    • 77956402239 scopus 로고    scopus 로고
    • MicroRNA-210 regulates mitochondrial free radical response to hypoxia and krebs cycle in cancer cells by targeting iron sulfur cluster protein ISCU
    • Favaro, E., et al. 2010. MicroRNA-210 regulates mitochondrial free radical response to hypoxia and krebs cycle in cancer cells by targeting iron sulfur cluster protein ISCU. PLoS One 5:e10345.
    • (2010) PLoS One , vol.5
    • Favaro, E.1
  • 21
    • 51349103144 scopus 로고    scopus 로고
    • Four miRNAs associated with aggressiveness of lymph node-negative, estrogen receptor-positive human breast cancer
    • Foekens, J. A., et al. 2008. Four miRNAs associated with aggressiveness of lymph node-negative, estrogen receptor-positive human breast cancer. Proc. Natl. Acad. Sci. U. S. A. 105:13021-13026.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 13021-13026
    • Foekens, J.A.1
  • 22
    • 40949114950 scopus 로고    scopus 로고
    • Role and regulation of prolyl hydroxylase domain proteins
    • Fong, G. H., and K. Takeda. 2008. Role and regulation of prolyl hydroxylase domain proteins. Cell Death Differ. 15:635-641.
    • (2008) Cell Death Differ , vol.15 , pp. 635-641
    • Fong, G.H.1    Takeda, K.2
  • 23
    • 0029789568 scopus 로고    scopus 로고
    • Functional interference between hypoxia and dioxin signal transduction pathways: competition for recruitment of the Arnt transcription factor
    • Gradin, K., et al. 1996. Functional interference between hypoxia and dioxin signal transduction pathways: competition for recruitment of the Arnt transcription factor. Mol. Cell. Biol. 16:5221-5231.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5221-5231
    • Gradin, K.1
  • 24
    • 73449134501 scopus 로고    scopus 로고
    • Elevated expression of microRNAs 155 203 210 and 222 in pancreatic tumors is associated with poorer survival
    • Greither, T., et al. 2010. Elevated expression of microRNAs 155, 203, 210 and 222 in pancreatic tumors is associated with poorer survival. Int. J. Cancer 126:73-80.
    • (2010) Int. J. Cancer , vol.126 , pp. 73-80
    • Greither, T.1
  • 25
    • 0029753008 scopus 로고    scopus 로고
    • Activation of hypoxia-inducible transcription factor depends primarily upon redox-sensitive stabilization of its alpha subunit
    • Huang, L. E., Z. Arany, D. M. Livingston, and H. F. Bunn. 1996. Activation of hypoxia-inducible transcription factor depends primarily upon redox-sensitive stabilization of its alpha subunit. J. Biol. Chem. 271:32253-32259.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32253-32259
    • Huang, L.E.1    Arany, Z.2    Livingston, D.M.3    Bunn, H.F.4
  • 26
    • 0037119415 scopus 로고    scopus 로고
    • Hsp90 regulates a von Hippel Lindau-independent hypoxia-inducible factor-1 alpha-degradative pathway
    • Isaacs, J. S., et al. 2002. Hsp90 regulates a von Hippel Lindau-independent hypoxia-inducible factor-1 alpha-degradative pathway. J. Biol. Chem. 277: 29936-29944.
    • (2002) J. Biol. Chem. , vol.277 , pp. 29936-29944
    • Isaacs, J.S.1
  • 27
    • 0035917808 scopus 로고    scopus 로고
    • Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation
    • Jaakkola, P., et al. 2001. Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation. Science 292: 468-472.
    • (2001) Science , vol.292 , pp. 468-472
    • Jaakkola, P.1
  • 28
    • 0035347260 scopus 로고    scopus 로고
    • Induction of HIF-1alpha in response to hypoxia is instantaneous
    • Jewell, U. R., et al. 2001. Induction of HIF-1alpha in response to hypoxia is instantaneous. FASEB J. 15:1312-1314.
    • (2001) FASEB J , vol.15 , pp. 1312-1314
    • Jewell, U.R.1
  • 29
    • 43649093915 scopus 로고    scopus 로고
    • Oxygen sensing by metazoans: the central role of the HIF hydroxylase pathway
    • Kaelin, W. G., Jr., and P. J. Ratcliffe. 2008. Oxygen sensing by metazoans: the central role of the HIF hydroxylase pathway. Mol. Cell 30:393-402.
    • (2008) Mol. Cell , vol.30 , pp. 393-402
    • Kaelin Jr., W.G.1    Ratcliffe, P.J.2
  • 30
    • 0032538797 scopus 로고    scopus 로고
    • Signal transduction in hypoxic cells: inducible nuclear translocation and recruitment of the CBP/p300 coactivator by the hypoxia-inducible factor-1alpha
    • Kallio, P. J., et al. 1998. Signal transduction in hypoxic cells: inducible nuclear translocation and recruitment of the CBP/p300 coactivator by the hypoxia-inducible factor-1alpha. EMBO J. 17:6573-6586.
    • (1998) EMBO J , vol.17 , pp. 6573-6586
    • Kallio, P.J.1
  • 31
    • 34250017082 scopus 로고    scopus 로고
    • An mRNA m7G cap binding-like motif within human Ago2 represses translation
    • Kiriakidou, M., et al. 2007. An mRNA m7G cap binding-like motif within human Ago2 represses translation. Cell 129:1141-1151.
    • (2007) Cell , vol.129 , pp. 1141-1151
    • Kiriakidou, M.1
  • 32
    • 33847234988 scopus 로고    scopus 로고
    • A microRNA signature of hypoxia
    • Kulshreshtha, R., et al. 2007. A microRNA signature of hypoxia. Mol. Cell. Biol. 27:1859-1867.
    • (2007) Mol. Cell. Biol. , vol.27 , pp. 1859-1867
    • Kulshreshtha, R.1
  • 33
    • 11844278458 scopus 로고    scopus 로고
    • Conserved seed pairing, often flanked by adenosines, indicates that thousands of human genes are microRNA targets
    • Lewis, B. P., C. B. Burge, and D. P. Bartel. 2005. Conserved seed pairing, often flanked by adenosines, indicates that thousands of human genes are microRNA targets. Cell 120:15-20.
    • (2005) Cell , vol.120 , pp. 15-20
    • Lewis, B.P.1    Burge, C.B.2    Bartel, D.P.3
  • 35
    • 36049001507 scopus 로고    scopus 로고
    • Mutation in glycerol-3-phosphate dehydrogenase 1 like gene (GPD1-L) decreases cardiac Na current and causes inherited arrhythmias
    • London, B., et al. 2007. Mutation in glycerol-3-phosphate dehydrogenase 1 like gene (GPD1-L) decreases cardiac Na current and causes inherited arrhythmias. Circulation 116:2260-2268.
    • (2007) Circulation , vol.116 , pp. 2260-2268
    • London, B.1
  • 36
    • 0035903468 scopus 로고    scopus 로고
    • Independent function of two destruction domains in hypoxia-inducible factor-alpha chains activated by prolyl hydroxylation
    • Masson, N., C. Willam, P. H. Maxwell, C. W. Pugh, and P. J. Ratcliffe. 2001. Independent function of two destruction domains in hypoxia-inducible factor-alpha chains activated by prolyl hydroxylation. EMBO J. 20:5197-5206.
    • (2001) EMBO J , vol.20 , pp. 5197-5206
    • Masson, N.1    Willam, C.2    Maxwell, P.H.3    Pugh, C.W.4    Ratcliffe, P.J.5
  • 37
    • 0037035851 scopus 로고    scopus 로고
    • Structure of an HIF-1alpha-pVHL complex: hydroxyproline recognition in signaling
    • Min, J. H., et al. 2002. Structure of an HIF-1alpha-pVHL complex: hydroxyproline recognition in signaling. Science 296:1886-1889.
    • (2002) Science , vol.296 , pp. 1886-1889
    • Min, J.H.1
  • 38
    • 67649381623 scopus 로고    scopus 로고
    • miR-210 promotes osteoblastic differentiation through inhibition of AcvR1b
    • Mizuno, Y., et al. 2009. miR-210 promotes osteoblastic differentiation through inhibition of AcvR1b. FEBS Lett. 583:2263-2268.
    • (2009) FEBS Lett , vol.583 , pp. 2263-2268
    • Mizuno, Y.1
  • 39
    • 0029955714 scopus 로고    scopus 로고
    • The pCL vector system: rapid production of helper-free, high-titer, recombinant retroviruses
    • Naviaux, R. K., E. Costanzi, M. Haas, and I. M. Verma. 1996. The pCL vector system: rapid production of helper-free, high-titer, recombinant retroviruses. J. Virol. 70:5701-5705.
    • (1996) J. Virol. , vol.70 , pp. 5701-5705
    • Naviaux, R.K.1    Costanzi, E.2    Haas, M.3    Verma, I.M.4
  • 40
    • 0017684404 scopus 로고
    • Isolation and characterization of multiple molecular forms of cytosolic NAD-linked glycerol-3-phosphate dehydrogenase from normal and neoplastic rabbit tissues
    • Ostro, M. J., and T. P. Fondy. 1977. Isolation and characterization of multiple molecular forms of cytosolic NAD-linked glycerol-3-phosphate dehydrogenase from normal and neoplastic rabbit tissues. J. Biol. Chem. 252: 5575-5583.
    • (1977) J. Biol. Chem. , vol.252 , pp. 5575-5583
    • Ostro, M.J.1    Fondy, T.P.2
  • 41
    • 33645038728 scopus 로고    scopus 로고
    • Crystal structures of human glycerol 3-phosphate dehydrogenase 1 (GPD1)
    • Ou, X., et al. 2006. Crystal structures of human glycerol 3-phosphate dehydrogenase 1 (GPD1). J. Mol. Biol. 357:858-869.
    • (2006) J. Mol. Biol. , vol.357 , pp. 858-869
    • Ou, X.1
  • 42
    • 34250374820 scopus 로고    scopus 로고
    • Carbodiimide-mediated cross-linking of RNA to nylon membranes improves the detection of siRNA, miRNA and piRNA by northern blot
    • Pall, G. S., C. Codony-Servat, J. Byrne, L. Ritchie, and A. Hamilton. 2007. Carbodiimide-mediated cross-linking of RNA to nylon membranes improves the detection of siRNA, miRNA and piRNA by northern blot. Nucleic Acids Res. 35:e60.
    • (2007) Nucleic Acids Res , vol.35
    • Pall, G.S.1    Codony-Servat, C.2    Byrne, J.3    Ritchie, L.4    Hamilton, A.5
  • 43
    • 79951678403 scopus 로고    scopus 로고
    • miR-210 is overexpressed in late stages of lung cancer and mediates mitochondrial alterations associated with modulation of HIF-1 activity
    • Puissegur, M. P., et al. 2011. miR-210 is overexpressed in late stages of lung cancer and mediates mitochondrial alterations associated with modulation of HIF-1 activity. Cell Death Differ. 18:465-478.
    • (2011) Cell Death Differ , vol.18 , pp. 465-478
    • Puissegur, M.P.1
  • 44
    • 0030961006 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1alpha (HIF-1alpha) protein is rapidly degraded by the ubiquitin-proteasome system under normoxic conditions. Its stabilization by hypoxia depends on redoxinduced changes
    • Salceda, S., and J. Caro. 1997. Hypoxia-inducible factor 1alpha (HIF-1alpha) protein is rapidly degraded by the ubiquitin-proteasome system under normoxic conditions. Its stabilization by hypoxia depends on redoxinduced changes. J. Biol. Chem. 272:22642-22647.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22642-22647
    • Salceda, S.1    Caro, J.2
  • 45
    • 19944433653 scopus 로고    scopus 로고
    • Succinate links TCA cycle dysfunction to oncogenesis by inhibiting HIF-alpha prolyl hydroxylase
    • Selak, M. A., et al. 2005. Succinate links TCA cycle dysfunction to oncogenesis by inhibiting HIF-alpha prolyl hydroxylase. Cancer Cell 7:77-85.
    • (2005) Cancer Cell , vol.7 , pp. 77-85
    • Selak, M.A.1
  • 46
    • 76349095132 scopus 로고    scopus 로고
    • Defining the role of hypoxia-inducible factor 1 in cancer biology and therapeutics
    • Semenza, G. L. 2010. Defining the role of hypoxia-inducible factor 1 in cancer biology and therapeutics. Oncogene 29:625-634.
    • (2010) Oncogene , vol.29 , pp. 625-634
    • Semenza, G.L.1
  • 47
    • 35148828429 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1 (HIF-1) pathway
    • Semenza, G. L. 2007. Hypoxia-inducible factor 1 (HIF-1) pathway. Sci. STKE 2007:cm8.
    • (2007) Sci. STKE , vol.2007
    • Semenza, G.L.1
  • 48
    • 60549083256 scopus 로고    scopus 로고
    • Regulation of cancer cell metabolism by hypoxiainducible factor 1
    • Semenza, G. L. 2009. Regulation of cancer cell metabolism by hypoxiainducible factor 1. Semin. Cancer Biol. 19:12-16.
    • (2009) Semin. Cancer Biol. , vol.19 , pp. 12-16
    • Semenza, G.L.1
  • 49
    • 0142166332 scopus 로고    scopus 로고
    • Targeting HIF-1 for cancer therapy
    • Semenza, G. L. 2003. Targeting HIF-1 for cancer therapy. Nat. Rev. Cancer 3:721-732.
    • (2003) Nat. Rev. Cancer , vol.3 , pp. 721-732
    • Semenza, G.L.1
  • 50
    • 0344375083 scopus 로고    scopus 로고
    • Lentivirus-delivered stable gene silencing by RNAi in primary cells
    • Stewart, S. A., et al. 2003. Lentivirus-delivered stable gene silencing by RNAi in primary cells. RNA 9:493-501.
    • (2003) RNA , vol.9 , pp. 493-501
    • Stewart, S.A.1
  • 51
    • 0033870281 scopus 로고    scopus 로고
    • The expression and distribution of the hypoxiainducible factors HIF-1alpha and HIF-2alpha in normal human tissues, cancers, and tumor-associated macrophages
    • Talks, K. L., et al. 2000. The expression and distribution of the hypoxiainducible factors HIF-1alpha and HIF-2alpha in normal human tissues, cancers, and tumor-associated macrophages. Am. J. Pathol. 157:411-421.
    • (2000) Am. J. Pathol. , vol.157 , pp. 411-421
    • Talks, K.L.1
  • 52
    • 34249282243 scopus 로고    scopus 로고
    • Drosophila miR2 induces pseudopolysomes and inhibits translation initiation
    • Thermann, R., and M. W. Hentze. 2007. Drosophila miR2 induces pseudopolysomes and inhibits translation initiation. Nature 447:875-878.
    • (2007) Nature , vol.447 , pp. 875-878
    • Thermann, R.1    Hentze, M.W.2
  • 53
    • 70349628999 scopus 로고    scopus 로고
    • GPD1L links redox state to cardiac excitability by PKC-dependent phosphorylation of the sodium channel SCN5A
    • Valdivia, C. R., K. Ueda, M. J. Ackerman, and J. C. Makielski. 2009. GPD1L links redox state to cardiac excitability by PKC-dependent phosphorylation of the sodium channel SCN5A. Am. J. Physiol. Heart Circ. Physiol. 297: H1446-H1452.
    • (2009) Am. J. Physiol. Heart Circ. Physiol. , vol.297
    • Valdivia, C.R.1    Ueda, K.2    Ackerman, M.J.3    Makielski, J.C.4
  • 54
    • 36048965546 scopus 로고    scopus 로고
    • Molecular and functional characterization of novel glycerol-3-phosphate dehydrogenase 1 like gene (GPD1-L) mutations in sudden infant death syndrome
    • Van Norstrand, D. W., et al. 2007. Molecular and functional characterization of novel glycerol-3-phosphate dehydrogenase 1 like gene (GPD1-L) mutations in sudden infant death syndrome. Circulation 116:2253-2259.
    • (2007) Circulation , vol.116 , pp. 2253-2259
    • Van Norstrand, D.W.1
  • 55
    • 4043181214 scopus 로고    scopus 로고
    • Cancer genes and the pathways they control
    • Vogelstein, B., and K. W. Kinzler. 2004. Cancer genes and the pathways they control. Nat. Med. 10:789-799.
    • (2004) Nat. Med. , vol.10 , pp. 789-799
    • Vogelstein, B.1    Kinzler, K.W.2
  • 56
    • 58149136865 scopus 로고    scopus 로고
    • Roles of p53, MYC and HIF-1 in regulating glycolysis-the seventh hallmark of cancer
    • Yeung, S. J., J. Pan, and M. H. Lee. 2008. Roles of p53, MYC and HIF-1 in regulating glycolysis-the seventh hallmark of cancer. Cell. Mol. Life Sci. 65:3981-3999.
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 3981-3999
    • Yeung, S.J.1    Pan, J.2    Lee, M.H.3
  • 57
    • 69749107748 scopus 로고    scopus 로고
    • MicroRNA miR-210 modulates cellular response to hypoxia through the MYC antagonist MNT
    • Zhang, Z., et al. 2009. MicroRNA miR-210 modulates cellular response to hypoxia through the MYC antagonist MNT. Cell Cycle 8:2756-2768.
    • (2009) Cell Cycle , vol.8 , pp. 2756-2768
    • Zhang, Z.1
  • 58
    • 0033571682 scopus 로고    scopus 로고
    • Overexpression of hypoxia-inducible factor 1alpha in common human cancers and their metastases
    • Zhong, H., et al. 1999. Overexpression of hypoxia-inducible factor 1alpha in common human cancers and their metastases. Cancer Res. 59:5830-5835.
    • (1999) Cancer Res , vol.59 , pp. 5830-5835
    • Zhong, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.