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Volumn 97, Issue , 2015, Pages 55-64

Hyperglycemia and redox status regulate RUNX2 DNA-binding and an angiogenic phenotype in endothelial cells

Author keywords

Angiogenesis; Antioxidant enzymes; Endothelial cell differentiation; Oxidative stress; Transcriptional factors

Indexed keywords

ALDEHYDE REDUCTASE; CYSTEINE; GLUTATHIONE REDUCTASE; METHIONINE; METHIONINE SULFOXIDE REDUCTASE A; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; TRANSCRIPTION FACTOR RUNX1; TRANSCRIPTION FACTOR RUNX2; ANGIOGENESIS INHIBITOR; ANTIOXIDANT; DNA; GLUCOSE; METHIONINE SULFOXIDE REDUCTASE; OXIDIZING AGENT; RUNX1 PROTEIN, HUMAN; RUNX2 PROTEIN, HUMAN;

EID: 84918500125     PISSN: 00262862     EISSN: 10959319     Source Type: Journal    
DOI: 10.1016/j.mvr.2014.09.008     Document Type: Article
Times cited : (21)

References (69)
  • 1
    • 65449120650 scopus 로고    scopus 로고
    • The role of methionine oxidation/reduction in the regulation of immune response
    • Agbas A., Moskovitz J. The role of methionine oxidation/reduction in the regulation of immune response. Curr. Signal Transduct. Ther. 2009, 4:46-50.
    • (2009) Curr. Signal Transduct. Ther. , vol.4 , pp. 46-50
    • Agbas, A.1    Moskovitz, J.2
  • 2
    • 0031013844 scopus 로고    scopus 로고
    • A simple screening for mutant DNA binding proteins: application to murine transcription factor PEBP2alpha subunit, a founding member of the Runt domain protein family
    • Akamatsu Y., et al. A simple screening for mutant DNA binding proteins: application to murine transcription factor PEBP2alpha subunit, a founding member of the Runt domain protein family. Gene 1997, 185:111-117.
    • (1997) Gene , vol.185 , pp. 111-117
    • Akamatsu, Y.1
  • 3
    • 43749084209 scopus 로고    scopus 로고
    • Hyperglycemia and the pathobiology of diabetic complications
    • Aronson D. Hyperglycemia and the pathobiology of diabetic complications. Adv. Cardiol. 2008, 45:1-16.
    • (2008) Adv. Cardiol. , vol.45 , pp. 1-16
    • Aronson, D.1
  • 4
    • 18344372018 scopus 로고    scopus 로고
    • The RUNX genes: gain or loss of function in cancer
    • Blyth K., et al. The RUNX genes: gain or loss of function in cancer. Nat. Rev. Cancer 2005, 5:376-387.
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 376-387
    • Blyth, K.1
  • 6
    • 84890285329 scopus 로고    scopus 로고
    • Glutaredoxin regulates vascular development by reversible glutathionylation of sirtuin 1
    • Brautigam L., et al. Glutaredoxin regulates vascular development by reversible glutathionylation of sirtuin 1. Proc. Natl. Acad. Sci. U. S. A. 2013, 110:20057-20062.
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 20057-20062
    • Brautigam, L.1
  • 7
    • 14344250739 scopus 로고    scopus 로고
    • Expression of Runx2/Cbfa1/Pebp2alphaA during angiogenesis in postnatal rodent and fetal human orofacial tissues
    • Bronckers A.L., et al. Expression of Runx2/Cbfa1/Pebp2alphaA during angiogenesis in postnatal rodent and fetal human orofacial tissues. J. Bone Miner. Res. 2005, 20:428-437.
    • (2005) J. Bone Miner. Res. , vol.20 , pp. 428-437
    • Bronckers, A.L.1
  • 8
    • 0035856980 scopus 로고    scopus 로고
    • Biochemistry and molecular cell biology of diabetic complications
    • Brownlee M. Biochemistry and molecular cell biology of diabetic complications. Nature 2001, 414:813-820.
    • (2001) Nature , vol.414 , pp. 813-820
    • Brownlee, M.1
  • 9
    • 84885190209 scopus 로고    scopus 로고
    • Angiogenesis and vascular functions in modulation of obesity, adipose metabolism, and insulin sensitivity
    • Cao Y. Angiogenesis and vascular functions in modulation of obesity, adipose metabolism, and insulin sensitivity. Cell Metab. 2013, 18:478-489.
    • (2013) Cell Metab. , vol.18 , pp. 478-489
    • Cao, Y.1
  • 10
    • 85047694081 scopus 로고    scopus 로고
    • VEGF-targeted cancer therapeutics-paradoxical effects in endocrine organs
    • Cao Y. VEGF-targeted cancer therapeutics-paradoxical effects in endocrine organs. Nat. Rev. Endocrinol. 2014, 10:530-539.
    • (2014) Nat. Rev. Endocrinol. , vol.10 , pp. 530-539
    • Cao, Y.1
  • 11
    • 77952581069 scopus 로고    scopus 로고
    • Optimizing the delivery of cancer drugs that block angiogenesis
    • 15ps3
    • Cao Y., Langer R. Optimizing the delivery of cancer drugs that block angiogenesis. Sci. Transl. Med. 2010, 2:15ps3.
    • (2010) Sci. Transl. Med. , vol.2
    • Cao, Y.1    Langer, R.2
  • 12
    • 84255183765 scopus 로고    scopus 로고
    • Forty-year journey of angiogenesis translational research
    • 114rv3
    • Cao Y., et al. Forty-year journey of angiogenesis translational research. Sci. Transl. Med. 2011, 3:114rv3.
    • (2011) Sci. Transl. Med. , vol.3
    • Cao, Y.1
  • 13
    • 0032485416 scopus 로고    scopus 로고
    • Telomerase activity is restored in human cells by ectopic expression of hTERT (hEST2), the catalytic subunit of telomerase
    • Counter C.M., et al. Telomerase activity is restored in human cells by ectopic expression of hTERT (hEST2), the catalytic subunit of telomerase. Oncogene 1998, 16:1217-1222.
    • (1998) Oncogene , vol.16 , pp. 1217-1222
    • Counter, C.M.1
  • 14
    • 78649847916 scopus 로고    scopus 로고
    • Methionine sulfoxide reductase A down-regulation in human breast cancer cells results in a more aggressive phenotype
    • De Luca A., et al. Methionine sulfoxide reductase A down-regulation in human breast cancer cells results in a more aggressive phenotype. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:18628-18633.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 18628-18633
    • De Luca, A.1
  • 15
    • 67650519130 scopus 로고    scopus 로고
    • Hyperglycemia regulates RUNX2 activation and cellular wound healing through the aldose reductase polyol pathway
    • D'Souza D.R., et al. Hyperglycemia regulates RUNX2 activation and cellular wound healing through the aldose reductase polyol pathway. J. Biol. Chem. 2009, 284:17947-17955.
    • (2009) J. Biol. Chem. , vol.284 , pp. 17947-17955
    • D'Souza, D.R.1
  • 16
    • 65549095447 scopus 로고    scopus 로고
    • MsrB1 (methionine-R-sulfoxide reductase 1) knock-out mice: roles of MsrB1 in redox regulation and identification of a novel selenoprotein form
    • Fomenko D.E., et al. MsrB1 (methionine-R-sulfoxide reductase 1) knock-out mice: roles of MsrB1 in redox regulation and identification of a novel selenoprotein form. J. Biol. Chem. 2009, 284:5986-5993.
    • (2009) J. Biol. Chem. , vol.284 , pp. 5986-5993
    • Fomenko, D.E.1
  • 17
    • 41549160278 scopus 로고    scopus 로고
    • Runt-related transcription factor 2 (RUNX2) and RUNX2-related osteogenic genes are down-regulated throughout osteogenesis in type 1 diabetes mellitus
    • Fowlkes J.L., et al. Runt-related transcription factor 2 (RUNX2) and RUNX2-related osteogenic genes are down-regulated throughout osteogenesis in type 1 diabetes mellitus. Endocrinology 2008, 149:1697-1704.
    • (2008) Endocrinology , vol.149 , pp. 1697-1704
    • Fowlkes, J.L.1
  • 18
    • 7944238041 scopus 로고    scopus 로고
    • Redox-sensitive signaling factors and antioxidants: how tumor cells respond to ionizing radiation
    • Gius D. Redox-sensitive signaling factors and antioxidants: how tumor cells respond to ionizing radiation. J. Nutr. 2004, 134:3213S-3214S.
    • (2004) J. Nutr. , vol.134 , pp. 3213S-3214S
    • Gius, D.1
  • 19
    • 40049100344 scopus 로고    scopus 로고
    • Impaired skin and hair follicle development in Runx2 deficient mice
    • Glotzer D.J., et al. Impaired skin and hair follicle development in Runx2 deficient mice. Dev. Biol. 2008, 315:459-473.
    • (2008) Dev. Biol. , vol.315 , pp. 459-473
    • Glotzer, D.J.1
  • 20
    • 77956186783 scopus 로고    scopus 로고
    • Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes
    • Hamanaka R.B., Chandel N.S. Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes. Trends Biochem. Sci. 2010, 35:505-513.
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 505-513
    • Hamanaka, R.B.1    Chandel, N.S.2
  • 21
    • 14944378159 scopus 로고    scopus 로고
    • Redox factor 1 (Ref-1) enhances specific DNA binding of p53 by promoting p53 tetramerization
    • Hanson S., et al. Redox factor 1 (Ref-1) enhances specific DNA binding of p53 by promoting p53 tetramerization. Oncogene 2005, 24:1641-1647.
    • (2005) Oncogene , vol.24 , pp. 1641-1647
    • Hanson, S.1
  • 22
    • 55149107716 scopus 로고    scopus 로고
    • Radical-free biology of oxidative stress
    • Jones D.P. Radical-free biology of oxidative stress. Am. J. Physiol. Cell Physiol. 2008, 295:C849-C868.
    • (2008) Am. J. Physiol. Cell Physiol. , vol.295 , pp. C849-C868
    • Jones, D.P.1
  • 23
    • 34250005695 scopus 로고    scopus 로고
    • High-dose estrogen-induced osteogenesis is decreased in aged RUNX2(+/-) mice
    • Juttner K.V., Perry M.J. High-dose estrogen-induced osteogenesis is decreased in aged RUNX2(+/-) mice. Bone 2007, 41:25-32.
    • (2007) Bone , vol.41 , pp. 25-32
    • Juttner, K.V.1    Perry, M.J.2
  • 24
    • 33646178955 scopus 로고    scopus 로고
    • Reciprocal relationships between insulin resistance and endothelial dysfunction: molecular and pathophysiological mechanisms
    • Kim J.A., et al. Reciprocal relationships between insulin resistance and endothelial dysfunction: molecular and pathophysiological mechanisms. Circulation 2006, 113:1888-1904.
    • (2006) Circulation , vol.113 , pp. 1888-1904
    • Kim, J.A.1
  • 25
    • 0036867895 scopus 로고    scopus 로고
    • Oxidation of biological systems: oxidative stress phenomena, antioxidants, redox reactions, and methods for their quantification
    • Kohen R., Nyska A. Oxidation of biological systems: oxidative stress phenomena, antioxidants, redox reactions, and methods for their quantification. Toxicol. Pathol. 2002, 30:620-650.
    • (2002) Toxicol. Pathol. , vol.30 , pp. 620-650
    • Kohen, R.1    Nyska, A.2
  • 26
    • 0030684749 scopus 로고    scopus 로고
    • Targeted disruption of Cbfa1 results in a complete lack of bone formation owing to maturational arrest of osteoblasts [see comments]
    • Komori T., et al. Targeted disruption of Cbfa1 results in a complete lack of bone formation owing to maturational arrest of osteoblasts [see comments]. Cell 1997, 89:755-764.
    • (1997) Cell , vol.89 , pp. 755-764
    • Komori, T.1
  • 27
    • 0030012618 scopus 로고    scopus 로고
    • A conserved cysteine residue in the runt homology domain of AML1 is required for the DNA binding ability and the transforming activity on fibroblasts
    • Kurokawa M., et al. A conserved cysteine residue in the runt homology domain of AML1 is required for the DNA binding ability and the transforming activity on fibroblasts. J. Biol. Chem. 1996, 271:16870-16876.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16870-16876
    • Kurokawa, M.1
  • 28
    • 0032402945 scopus 로고    scopus 로고
    • Caloric restriction prevents age-associated accrual of oxidative damage to mouse skeletal muscle mitochondria
    • Lass A., et al. Caloric restriction prevents age-associated accrual of oxidative damage to mouse skeletal muscle mitochondria. Free Radic. Biol. Med. 1998, 25:1089-1097.
    • (1998) Free Radic. Biol. Med. , vol.25 , pp. 1089-1097
    • Lass, A.1
  • 29
    • 35148844229 scopus 로고    scopus 로고
    • Identification of MSRA gene on chromosome 8p as a candidate metastasis suppressor for human hepatitis B virus-positive hepatocellular carcinoma
    • Lei K.F., et al. Identification of MSRA gene on chromosome 8p as a candidate metastasis suppressor for human hepatitis B virus-positive hepatocellular carcinoma. BMC Cancer 2007, 7:172.
    • (2007) BMC Cancer , vol.7 , pp. 172
    • Lei, K.F.1
  • 30
    • 33750926794 scopus 로고    scopus 로고
    • Role of Nox family NADPH oxidases in host defense
    • Leto T.L., Geiszt M. Role of Nox family NADPH oxidases in host defense. Antioxid. Redox Signal. 2006, 8:1549-1561.
    • (2006) Antioxid. Redox Signal. , vol.8 , pp. 1549-1561
    • Leto, T.L.1    Geiszt, M.2
  • 31
    • 0037230153 scopus 로고    scopus 로고
    • Diabetes interferes with the bone formation by affecting the expression of transcription factors that regulate osteoblast differentiation
    • Lu H., et al. Diabetes interferes with the bone formation by affecting the expression of transcription factors that regulate osteoblast differentiation. Endocrinology 2003, 144:346-352.
    • (2003) Endocrinology , vol.144 , pp. 346-352
    • Lu, H.1
  • 32
    • 84858218213 scopus 로고    scopus 로고
    • Regulation of intracellular signalling through cysteine oxidation by reactive oxygen species
    • Miki H., Funato Y. Regulation of intracellular signalling through cysteine oxidation by reactive oxygen species. J. Biochem. 2012, 151:255-261.
    • (2012) J. Biochem. , vol.151 , pp. 255-261
    • Miki, H.1    Funato, Y.2
  • 33
    • 12844267504 scopus 로고    scopus 로고
    • Methionine sulfoxide reductases: ubiquitous enzymes involved in antioxidant defense, protein regulation, and prevention of aging-associated diseases
    • Moskovitz J. Methionine sulfoxide reductases: ubiquitous enzymes involved in antioxidant defense, protein regulation, and prevention of aging-associated diseases. Biochim. Biophys. Acta 2005, 1703:213-219.
    • (2005) Biochim. Biophys. Acta , vol.1703 , pp. 213-219
    • Moskovitz, J.1
  • 34
    • 0028967490 scopus 로고
    • Escherichia coli peptide methionine sulfoxide reductase gene: regulation of expression and role in protecting against oxidative damage
    • Moskovitz J., et al. Escherichia coli peptide methionine sulfoxide reductase gene: regulation of expression and role in protecting against oxidative damage. J. Bacteriol. 1995, 177:502-507.
    • (1995) J. Bacteriol. , vol.177 , pp. 502-507
    • Moskovitz, J.1
  • 35
    • 0034640506 scopus 로고    scopus 로고
    • Identification and characterization of a putative active site for peptide methionine sulfoxide reductase (MsrA) and its substrate stereospecificity
    • Moskovitz J., et al. Identification and characterization of a putative active site for peptide methionine sulfoxide reductase (MsrA) and its substrate stereospecificity. J. Biol. Chem. 2000, 275:14167-14172.
    • (2000) J. Biol. Chem. , vol.275 , pp. 14167-14172
    • Moskovitz, J.1
  • 36
    • 0035818520 scopus 로고    scopus 로고
    • Methionine sulfoxide reductase (MsrA) is a regulator of antioxidant defense and lifespan in mammals
    • Moskovitz J., et al. Methionine sulfoxide reductase (MsrA) is a regulator of antioxidant defense and lifespan in mammals. Proc. Natl. Acad. Sci. U. S. A. 2001, 98:12920-12925.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 12920-12925
    • Moskovitz, J.1
  • 37
    • 0036297758 scopus 로고    scopus 로고
    • Purification and characterization of methionine sulfoxide reductases from mouse and Staphylococcus aureus and their substrate stereospecificity
    • Moskovitz J., et al. Purification and characterization of methionine sulfoxide reductases from mouse and Staphylococcus aureus and their substrate stereospecificity. Biochem. Biophys. Res. Commun. 2002, 290:62-65.
    • (2002) Biochem. Biophys. Res. Commun. , vol.290 , pp. 62-65
    • Moskovitz, J.1
  • 38
    • 0034610754 scopus 로고    scopus 로고
    • Indispensable role of the transcription factor PEBP2/CBF in angiogenic activity of a murine endothelial cell MSS31
    • Namba K., et al. Indispensable role of the transcription factor PEBP2/CBF in angiogenic activity of a murine endothelial cell MSS31. Oncogene 2000, 19:106-114.
    • (2000) Oncogene , vol.19 , pp. 106-114
    • Namba, K.1
  • 39
    • 59949097619 scopus 로고    scopus 로고
    • Oxidation of methionine residue at hydrophobic core destabilizes p53 tetrameric structure
    • Nomura T., et al. Oxidation of methionine residue at hydrophobic core destabilizes p53 tetrameric structure. Biopolymers 2009, 91:78-84.
    • (2009) Biopolymers , vol.91 , pp. 78-84
    • Nomura, T.1
  • 40
    • 35348903730 scopus 로고    scopus 로고
    • Substrates of the methionine sulfoxide reductase system and their physiological relevance
    • Oien D.B., Moskovitz J. Substrates of the methionine sulfoxide reductase system and their physiological relevance. Curr. Top. Dev. Biol. 2008, 80:93-133.
    • (2008) Curr. Top. Dev. Biol. , vol.80 , pp. 93-133
    • Oien, D.B.1    Moskovitz, J.2
  • 41
    • 44649170935 scopus 로고    scopus 로고
    • MsrA knockout mouse exhibits abnormal behavior and brain dopamine levels
    • Oien D.B., et al. MsrA knockout mouse exhibits abnormal behavior and brain dopamine levels. Free Radic. Biol. Med. 2008, 45:193-200.
    • (2008) Free Radic. Biol. Med. , vol.45 , pp. 193-200
    • Oien, D.B.1
  • 42
    • 64549133370 scopus 로고    scopus 로고
    • Detection of oxidized methionine in selected proteins, cellular extracts and blood serums by novel anti-methionine sulfoxide antibodies
    • Oien D.B., et al. Detection of oxidized methionine in selected proteins, cellular extracts and blood serums by novel anti-methionine sulfoxide antibodies. Arch. Biochem. Biophys. 2009, 485:35-40.
    • (2009) Arch. Biochem. Biophys. , vol.485 , pp. 35-40
    • Oien, D.B.1
  • 43
    • 73849134745 scopus 로고    scopus 로고
    • Clearance and phosphorylation of alpha-synuclein are inhibited in methionine sulfoxide reductase a null yeast cells
    • Oien D.B., et al. Clearance and phosphorylation of alpha-synuclein are inhibited in methionine sulfoxide reductase a null yeast cells. J. Mol. Neurosci. 2009, 39:323-332.
    • (2009) J. Mol. Neurosci. , vol.39 , pp. 323-332
    • Oien, D.B.1
  • 44
    • 70449517524 scopus 로고    scopus 로고
    • Caloric restriction alleviates abnormal locomotor activity and dopamine levels in the brain of the methionine sulfoxide reductase A knockout mouse
    • Oien D.B., et al. Caloric restriction alleviates abnormal locomotor activity and dopamine levels in the brain of the methionine sulfoxide reductase A knockout mouse. Neurosci. Lett. 2010, 468:38-41.
    • (2010) Neurosci. Lett. , vol.468 , pp. 38-41
    • Oien, D.B.1
  • 45
    • 79952009445 scopus 로고    scopus 로고
    • Quantification of reserve pool dopamine in methionine sulfoxide reductase A null mice
    • Ortiz A.N., et al. Quantification of reserve pool dopamine in methionine sulfoxide reductase A null mice. Neuroscience 2011, 177:223-229.
    • (2011) Neuroscience , vol.177 , pp. 223-229
    • Ortiz, A.N.1
  • 46
    • 84055222576 scopus 로고    scopus 로고
    • Glucose-activated RUNX2 phosphorylation promotes endothelial cell proliferation and an angiogenic phenotype
    • Pierce A.D., et al. Glucose-activated RUNX2 phosphorylation promotes endothelial cell proliferation and an angiogenic phenotype. J. Cell. Biochem. 2012, 113:218-292.
    • (2012) J. Cell. Biochem. , vol.113 , pp. 218-292
    • Pierce, A.D.1
  • 47
    • 0028129545 scopus 로고
    • Altered angiogenesis underlying age-dependent changes in tumor growth
    • Pili R., et al. Altered angiogenesis underlying age-dependent changes in tumor growth. J. Natl. Cancer Inst. 1994, 86:1303-1314.
    • (1994) J. Natl. Cancer Inst. , vol.86 , pp. 1303-1314
    • Pili, R.1
  • 48
    • 80052933197 scopus 로고    scopus 로고
    • Basic and therapeutic aspects of angiogenesis
    • Potente M., et al. Basic and therapeutic aspects of angiogenesis. Cell 2011, 146:873-887.
    • (2011) Cell , vol.146 , pp. 873-887
    • Potente, M.1
  • 49
    • 5644236459 scopus 로고    scopus 로고
    • Insulin-like growth factor-1 regulates endogenous RUNX2 activity in endothelial cells through a PI3K/ERK-dependent and Akt-independent signaling pathway
    • Qiao M., et al. Insulin-like growth factor-1 regulates endogenous RUNX2 activity in endothelial cells through a PI3K/ERK-dependent and Akt-independent signaling pathway. J. Biol. Chem. 2004, 279:42709-42718.
    • (2004) J. Biol. Chem. , vol.279 , pp. 42709-42718
    • Qiao, M.1
  • 50
    • 33646350024 scopus 로고    scopus 로고
    • Cell cycle-dependent phosphorylation of the RUNX2 transcription factor by cdc2 regulates endothelial cell proliferation
    • Qiao M., et al. Cell cycle-dependent phosphorylation of the RUNX2 transcription factor by cdc2 regulates endothelial cell proliferation. J. Biol. Chem. 2006, 281:7118-7128.
    • (2006) J. Biol. Chem. , vol.281 , pp. 7118-7128
    • Qiao, M.1
  • 51
    • 49449117608 scopus 로고    scopus 로고
    • Reactive oxygen species regulate hypoxia-inducible factor 1alpha differentially in cancer and ischemia
    • Qutub A.A., Popel A.S. Reactive oxygen species regulate hypoxia-inducible factor 1alpha differentially in cancer and ischemia. Mol. Cell. Biol. 2008, 28:5106-5119.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 5106-5119
    • Qutub, A.A.1    Popel, A.S.2
  • 52
    • 0035866185 scopus 로고    scopus 로고
    • Development of a sensitive multi-well colorimetric assay for active NFkappaB
    • Renard P., et al. Development of a sensitive multi-well colorimetric assay for active NFkappaB. Nucleic Acids Res. 2001, 29:E21.
    • (2001) Nucleic Acids Res. , vol.29 , pp. E21
    • Renard, P.1
  • 53
    • 0141680285 scopus 로고    scopus 로고
    • Molecular diagnosis of tumor angiogenesis and anti-angiogenic cancer therapy
    • Sato Y. Molecular diagnosis of tumor angiogenesis and anti-angiogenic cancer therapy. Int. J. Clin. Oncol. 2003, 8:200-206.
    • (2003) Int. J. Clin. Oncol. , vol.8 , pp. 200-206
    • Sato, Y.1
  • 54
    • 0031852850 scopus 로고    scopus 로고
    • Role of oxidative stress in senescence
    • Sohal R.S., Orr W.C. Role of oxidative stress in senescence. Aging (Milano) 1998, 10:149-151.
    • (1998) Aging (Milano) , vol.10 , pp. 149-151
    • Sohal, R.S.1    Orr, W.C.2
  • 55
    • 18844369302 scopus 로고    scopus 로고
    • Role of aldose reductase and oxidative damage in diabetes and the consequent potential for therapeutic options
    • Srivastava S.K., et al. Role of aldose reductase and oxidative damage in diabetes and the consequent potential for therapeutic options. Endocr. Rev. 2005, 26:380-392.
    • (2005) Endocr. Rev. , vol.26 , pp. 380-392
    • Srivastava, S.K.1
  • 56
    • 0142151375 scopus 로고    scopus 로고
    • Oxidation of methionine residues of proteins: biological consequences
    • Stadtman E.R., et al. Oxidation of methionine residues of proteins: biological consequences. Antioxid. Redox Signal. 2003, 5:577-582.
    • (2003) Antioxid. Redox Signal. , vol.5 , pp. 577-582
    • Stadtman, E.R.1
  • 57
    • 12844268130 scopus 로고    scopus 로고
    • Methionine oxidation and aging
    • Stadtman E.R., et al. Methionine oxidation and aging. Biochim. Biophys. Acta 2005, 1703:135-140.
    • (2005) Biochim. Biophys. Acta , vol.1703 , pp. 135-140
    • Stadtman, E.R.1
  • 58
    • 0035393430 scopus 로고    scopus 로고
    • Runt-related gene 2 in endothelial cells: inducible expression and specific regulation of cell migration and invasion
    • Sun L., et al. Runt-related gene 2 in endothelial cells: inducible expression and specific regulation of cell migration and invasion. Cancer Res. 2001, 61:4994-5001.
    • (2001) Cancer Res. , vol.61 , pp. 4994-5001
    • Sun, L.1
  • 59
    • 2942752288 scopus 로고    scopus 로고
    • Regulation of TGFß1-mediated growth inhibition and apoptosis by RUNX2 isoforms
    • Sun L., et al. Regulation of TGFß1-mediated growth inhibition and apoptosis by RUNX2 isoforms. Oncogene 2004, 23:4722-4734.
    • (2004) Oncogene , vol.23 , pp. 4722-4734
    • Sun, L.1
  • 60
    • 0029831907 scopus 로고    scopus 로고
    • Regulation of reactive-oxygen-species generation in fibroblasts by Rac1
    • Sundaresan M., et al. Regulation of reactive-oxygen-species generation in fibroblasts by Rac1. Biochem. J. 1996, 318(Pt 2):379-382.
    • (1996) Biochem. J. , vol.318 , pp. 379-382
    • Sundaresan, M.1
  • 61
    • 0035831044 scopus 로고    scopus 로고
    • Structural analyses of DNA recognition by the AML1/Runx-1 Runt domain and its allosteric control by CBFbeta
    • Tahirov T.H., et al. Structural analyses of DNA recognition by the AML1/Runx-1 Runt domain and its allosteric control by CBFbeta. Cell 2001, 104:755-767.
    • (2001) Cell , vol.104 , pp. 755-767
    • Tahirov, T.H.1
  • 62
    • 14144253246 scopus 로고    scopus 로고
    • Aged mice require full transcription factor, Runx2/Cbfa1, gene dosage for cancellous bone regeneration after bone marrow ablation
    • Tsuji K., et al. Aged mice require full transcription factor, Runx2/Cbfa1, gene dosage for cancellous bone regeneration after bone marrow ablation. J. Bone Miner. Res. 2004, 19:1481-1489.
    • (2004) J. Bone Miner. Res. , vol.19 , pp. 1481-1489
    • Tsuji, K.1
  • 63
    • 84858734844 scopus 로고    scopus 로고
    • Regulation of RUNX2 transcription factor-DNA interactions and cell proliferation by Vitamin D3 (cholecalciferol) prohormone activity
    • Underwood K.F., et al. Regulation of RUNX2 transcription factor-DNA interactions and cell proliferation by Vitamin D3 (cholecalciferol) prohormone activity. J. Bone Miner. Res. 2012, 27:913-925.
    • (2012) J. Bone Miner. Res. , vol.27 , pp. 913-925
    • Underwood, K.F.1
  • 64
    • 84883628313 scopus 로고    scopus 로고
    • A quantitative assay to study protein:DNA interactions, discover transcriptional regulators of gene expression, and identify novel anti-tumor agents
    • (Aug 31)
    • Underwood K.F., et al. A quantitative assay to study protein:DNA interactions, discover transcriptional regulators of gene expression, and identify novel anti-tumor agents. J. Vis. Exp. 2013, (78). (Aug 31).
    • (2013) J. Vis. Exp. , Issue.78
    • Underwood, K.F.1
  • 65
    • 42449103970 scopus 로고    scopus 로고
    • The RUNX2 transcription factor cooperates with the YES-associated protein, YAP65, to promote cell transformation
    • Vitolo M.I., et al. The RUNX2 transcription factor cooperates with the YES-associated protein, YAP65, to promote cell transformation. Cancer Biol. Ther. 2007, 6:856-863.
    • (2007) Cancer Biol. Ther. , vol.6 , pp. 856-863
    • Vitolo, M.I.1
  • 66
    • 12844264123 scopus 로고    scopus 로고
    • Methionine sulfoxide reductases: history and cellular role in protecting against oxidative damage
    • Weissbach H., et al. Methionine sulfoxide reductases: history and cellular role in protecting against oxidative damage. Biochim. Biophys. Acta 2005, 1703:203-212.
    • (2005) Biochim. Biophys. Acta , vol.1703 , pp. 203-212
    • Weissbach, H.1
  • 67
    • 48449107159 scopus 로고    scopus 로고
    • Thiol chemistry and specificity in redox signaling
    • Winterbourn C.C., Hampton M.B. Thiol chemistry and specificity in redox signaling. Free Radic. Biol. Med. 2008, 45:549-561.
    • (2008) Free Radic. Biol. Med. , vol.45 , pp. 549-561
    • Winterbourn, C.C.1    Hampton, M.B.2
  • 68
    • 0037252642 scopus 로고    scopus 로고
    • Biomarkers of lipid peroxidation, airway inflammation and asthma
    • Wood L.G., et al. Biomarkers of lipid peroxidation, airway inflammation and asthma. Eur. Respir. J. 2003, 21:177-186.
    • (2003) Eur. Respir. J. , vol.21 , pp. 177-186
    • Wood, L.G.1
  • 69
    • 0034914814 scopus 로고    scopus 로고
    • Tissue specific regulation of VEGF expression during bone development requires Cbfa1/Runx2
    • Zelzer E., et al. Tissue specific regulation of VEGF expression during bone development requires Cbfa1/Runx2. Mech. Dev. 2001, 106:97-106.
    • (2001) Mech. Dev. , vol.106 , pp. 97-106
    • Zelzer, E.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.