메뉴 건너뛰기




Volumn 71, Issue 15, 2011, Pages 5327-5335

ADP-ribosylarginine hydrolase regulates cell proliferation and tumorigenesis

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSE; ADENOSINE DIPHOSPHATE RIBOSYLARGININE HYDROLASE; UNCLASSIFIED DRUG;

EID: 79960958113     PISSN: 00085472     EISSN: 15387445     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-10-0733     Document Type: Article
Times cited : (41)

References (37)
  • 1
    • 0000921719 scopus 로고
    • Mono-ADP-ribosyltransferases and ADPribosylarginine hydrolase: A mono-ADP-ribosylation cycle in animal cells
    • Moss J, Vaughan M, editors. Washington, D.C.: ASM Press
    • Williamson KC, Moss J. Mono-ADP-ribosyltransferases and ADPribosylarginine hydrolase: a mono-ADP-ribosylation cycle in animal cells. In: Moss J, Vaughan M, editors. ADP-ribosylating toxins and G proteins: insights into signal transduction. Washington, D.C.: ASM Press; 1990. p. 493-510.
    • (1990) ADP-ribosylating Toxins and G Proteins: Insights into Signal Transduction , pp. 493-510
    • Williamson, K.C.1    Moss, J.2
  • 2
    • 0032797983 scopus 로고    scopus 로고
    • Characterization of glycosylphosphatidylinositiol-anchored, secreted, and intracellular vertebrate mono-ADP-ribosyltransferases
    • DOI 10.1146/annurev.nutr.19.1.485
    • Okazaki IJ, Moss J. Characterization of glycosylphosphatidylinositiol- anchored, secreted, and intracellular vertebrate mono-ADP-ribosyltransferases. Annu Rev Nutr 1999;19:485-509. (Pubitemid 29380614)
    • (1999) Annual Review of Nutrition , vol.19 , pp. 485-509
    • Okazaki, I.J.1    Moss, J.2
  • 3
    • 0037881920 scopus 로고    scopus 로고
    • Functional aspects of protein mono-ADP-ribosylation
    • DOI 10.1093/emboj/cdg209
    • Corda D, Di Girolamo M. Functional aspects of protein mono-ADP-ribosylation. EMBO J 2003;22:1953-8. (Pubitemid 36565521)
    • (2003) EMBO Journal , vol.22 , Issue.9 , pp. 1953-1958
    • Corda, D.1    Di, G.M.2
  • 4
    • 0023742061 scopus 로고
    • ADP-ribosylation of guanyl nucleotide-binding regulatory proteins by bacterial toxins
    • Moss J, Vaughan M. ADP-ribosylation of guanyl nucleotide-binding regulatory proteins by bacterial toxins. Adv Enzymol Relat Areas Mol Biol 1988;61:303-79.
    • (1988) Adv Enzymol Relat Areas Mol Biol , vol.61 , pp. 303-379
    • Moss, J.1    Vaughan, M.2
  • 5
    • 0003085965 scopus 로고
    • Pertussis toxin as a valuable probe for G-protein involvement in signal transduction
    • Moss J, Vaughan M, editors. Washington, D.C.: ASM Press
    • Ui M. Pertussis toxin as a valuable probe for G-protein involvement in signal transduction. In: Moss J, Vaughan M, editors. ADP-ribosylating toxins and G proteins: insights into signal transduction. Washington, D.C.: ASM Press; 1990. p. 45-77.
    • (1990) ADP-ribosylating Toxins and G Proteins: Insights into Signal Transduction , pp. 45-77
    • Ui, M.1
  • 6
    • 0032508689 scopus 로고    scopus 로고
    • Glycosylphosphatidylinositol-anchored and secretory isoforms of mono-ADP-ribosyltransferases
    • Okazaki IJ, Moss J. Glycosylphosphatidylinositol-anchored and secretory isoforms of mono-ADP-ribosyltransferases. J Biol Chem 1998;273:23617-20.
    • (1998) J Biol Chem , vol.273 , pp. 23617-23620
    • Okazaki, I.J.1    Moss, J.2
  • 7
    • 0029684208 scopus 로고    scopus 로고
    • Structure and function of eukaryotic mono-ADP-ribosyltransferases
    • Okazaki IJ, Moss J. Structure and function of eukaryotic mono-ADP-ribosyltransferases. Rev Physiol Biochem Pharmacol 1996;129: 51-104.
    • (1996) Rev Physiol Biochem Pharmacol , vol.129 , pp. 51-104
    • Okazaki, I.J.1    Moss, J.2
  • 8
    • 0018801346 scopus 로고
    • Substrate specificity and partial purification of a stereospecific NAD- and guanidine-dependent ADP-ribosyltransferase from avian erythrocytes
    • Moss J, Stanley SJ, Oppenheimer NJ. Substrate specificity and partial purification of a stereospecific NAD- and guanidine-dependent ADP-ribosyltransferase from avian erythrocytes. J Biol Chem 1979;254: 8891-4.
    • (1979) J Biol Chem , vol.254 , pp. 8891-8894
    • Moss, J.1    Stanley, S.J.2    Oppenheimer, N.J.3
  • 11
    • 73949112004 scopus 로고    scopus 로고
    • ADP-ribosylation of human defensin HNP-1 results in the replacement of the modified arginine with the noncoded amino acid ornithine
    • Stevens LA, Levine RL, Gochuico BR, Moss J. ADP-ribosylation of human defensin HNP-1 results in the replacement of the modified arginine with the noncoded amino acid ornithine. Proc Natl Acad Sci U S A 2009; 106:19796-800.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 19796-19800
    • Stevens, L.A.1    Levine, R.L.2    Gochuico, B.R.3    Moss, J.4
  • 12
    • 0028901021 scopus 로고
    • Processing of ADP-ribosylated integrin alpha 7 in skeletal muscle myotubes
    • Zolkiewska A, Moss J. Processing of ADP-ribosylated integrin alpha 7 in skeletal muscle myotubes. J Biol Chem 1995;270:9227-33.
    • (1995) J Biol Chem , vol.270 , pp. 9227-9233
    • Zolkiewska, A.1    Moss, J.2
  • 13
    • 0027331555 scopus 로고
    • Integrin alpha 7 as substrate for a glycosylphosphatidylinositol- anchored ADP-ribosyltransferase on the surface of skeletal muscle cells
    • Zolkiewska A, Moss J. Integrin alpha 7 as substrate for a glycosylphosphatidylinositol- anchored ADP-ribosyltransferase on the surface of skeletal muscle cells. J Biol Chem 1993;268:25273-6.
    • (1993) J Biol Chem , vol.268 , pp. 25273-25276
    • Zolkiewska, A.1    Moss, J.2
  • 14
    • 0026445547 scopus 로고
    • Molecular characterization of NAD:Arginine ADP-ribosyltransferase from rabbit skeletal muscle
    • Zolkiewska A, Nightingale MS, Moss J. Molecular characterization of NAD:arginine ADP-ribosyltransferase from rabbit skeletal muscle. Proc Natl Acad Sci U S A 1992;89:11352-6.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 11352-11356
    • Zolkiewska, A.1    Nightingale, M.S.2    Moss, J.3
  • 15
    • 0028131940 scopus 로고
    • Regulation of cytotoxic T cells by ecto-nicotinamide adenine dinucleotide (NAD) correlates with cell surface GPI-anchored/arginine ADP-ribosyltransferase
    • Wang J, Nemoto E, Kots AY, Kaslow HR, Dennert G. Regulation of cytotoxic T cells by ecto-nicotinamide adenine dinucleotide (NAD) correlates with cell surface GPI-anchored/arginine ADP-ribosyltransferase. J Immunol 1994;153:4048-58.
    • (1994) J Immunol , vol.153 , pp. 4048-4058
    • Wang, J.1    Nemoto, E.2    Kots, A.Y.3    Kaslow, H.R.4    Dennert, G.5
  • 16
    • 0030584706 scopus 로고    scopus 로고
    • Regulation of CTL by ecto-nictinamide adenine dinucleotide (NAD) involves ADP-ribosylation of a p56lck-associated protein
    • Wang J, Nemoto E, Dennert G. Regulation of CTL by ecto-nictinamide adenine dinucleotide (NAD) involves ADP-ribosylation of a p56lck-associated protein. J Immunol 1996;156:2819-27.
    • (1996) J Immunol , vol.156 , pp. 2819-2827
    • Wang, J.1    Nemoto, E.2    Dennert, G.3
  • 18
    • 0023055764 scopus 로고
    • Amino acid specific ADP-ribosylation: Substrate specificity of an ADP-ribosylarginine hydrolase from turkey erythrocytes
    • Moss J, Oppenheimer NJ, West RE Jr, Stanley SJ. Amino acid specific ADP-ribosylation: substrate specificity of an ADP-ribosylarginine hydrolase from turkey erythrocytes. Biochemistry 1986;25:5408-14.
    • (1986) Biochemistry , vol.25 , pp. 5408-5414
    • Moss, J.1    Oppenheimer, N.J.2    West Jr., R.E.3    Stanley, S.J.4
  • 21
    • 0023753245 scopus 로고
    • Purification and characterization of ADP-ribosylarginine hydrolase from turkey erythrocytes
    • Moss J, Tsai SC, Adamik R, Chen HC, Stanley SJ. Purification and characterization of ADP-ribosylarginine hydrolase from turkey erythrocytes. Biochemistry 1988;27:5819-23.
    • (1988) Biochemistry , vol.27 , pp. 5819-5823
    • Moss, J.1    Tsai, S.C.2    Adamik, R.3    Chen, H.C.4    Stanley, S.J.5
  • 22
    • 0027198328 scopus 로고
    • Cloning and site-directed mutagenesis of human ADP-ribosylarginine hydrolase
    • Takada T, Iida K, Moss J. Cloning and site-directed mutagenesis of human ADP-ribosylarginine hydrolase. J Biol Chem 1993;268: 17837-43. (Pubitemid 23260294)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.24 , pp. 17837-17843
    • Takada, T.1    Iida, K.2    Moss, J.3
  • 23
    • 0028938731 scopus 로고
    • Conservation of a common motif in enzymes catalyzing ADP-ribose transfer. Identification of domains in mammalian transferases
    • Takada T, Iida K, Moss J. Conservation of a common motif in enzymes catalyzing ADP-ribose transfer. Identification of domains in mammalian transferases. J Biol Chem 1995;270:541-4.
    • (1995) J Biol Chem , vol.270 , pp. 541-544
    • Takada, T.1    Iida, K.2    Moss, J.3
  • 24
    • 0033546332 scopus 로고    scopus 로고
    • Identification of critical, conserved vicinal aspartate residues in mammalian and bacterial ADP-ribosylarginine hydrolases
    • Konczalik P, Moss J. Identification of critical, conserved vicinal aspartate residues in mammalian and bacterial ADP-ribosylarginine hydrolases. J Biol Chem 1999;274:16736-40.
    • (1999) J Biol Chem , vol.274 , pp. 16736-16740
    • Konczalik, P.1    Moss, J.2
  • 25
    • 34547207148 scopus 로고    scopus 로고
    • Enhanced sensitivity to cholera toxin in ADP-ribosylarginine hydrolase-deficient mice
    • DOI 10.1128/MCB.00302-07
    • Kato J, Zhu J, Liu C, Moss J. Enhanced sensitivity to cholera toxin in ADP-ribosylarginine hydrolase-deficient mice. Mol Cell Biol 2007;27: 5534-43. (Pubitemid 47124405)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.15 , pp. 5534-5543
    • Kato, J.1    Zhu, J.2    Liu, C.3    Moss, J.4
  • 26
    • 79960936946 scopus 로고    scopus 로고
    • Growth of transformed cells in soft agar
    • Bonifacino JS, Dasso M, Harford JB, Schwartz JL, Yamada KM, editors. Hoboken, NJ: John Wiley &Sons
    • Sato JD, Kan M. Growth of transformed cells in soft agar. In: Bonifacino JS, Dasso M, Harford JB, Schwartz JL, Yamada KM, editors. Current protocols in cell biology. Hoboken, NJ: John Wiley &Sons; 1998. p. 1.2.1-1.2.15
    • (1998) Current Protocols in Cell Biology
    • Sato, J.D.1    Kan, M.2
  • 27
    • 84858830785 scopus 로고    scopus 로고
    • Intraperitoneal and subcutaneous tumor models for assessing anti-neoplastic agents in rodent
    • Enna SJ, Williams M, Ferkany JW, Frechette R, Kenakin T, Moser P, Ruggeri B, editors. Hoboken, NJ: John Wiley &Sons
    • Hollingshead M. Intraperitoneal and subcutaneous tumor models for assessing anti-neoplastic agents in rodent. In: Enna SJ, Williams M, Ferkany JW, Frechette R, Kenakin T, Moser P, Ruggeri B, editors. Current protocols in Pharmacology. Hoboken, NJ: John Wiley &Sons; 2002. p. 5.28.1-5.28.13.
    • (2002) Current Protocols in Pharmacology
    • Hollingshead, M.1
  • 28
    • 0028568315 scopus 로고
    • Cell cycle control and cancer
    • Hartwell LH, Kastan MB. Cell cycle control and cancer. Science 1994;266:1821-28.
    • (1994) Science , vol.266 , pp. 1821-1828
    • Hartwell, L.H.1    Kastan, M.B.2
  • 34
    • 4944255743 scopus 로고    scopus 로고
    • Post-translational modification of p53 in tumorigenesis
    • DOI 10.1038/nrc1455
    • Bode AM, Dong Z. Post-translational modification of p53 in tumorigenesis. Nat Rev Cancer 2004;4:793-805. (Pubitemid 39331151)
    • (2004) Nature Reviews Cancer , vol.4 , Issue.10 , pp. 793-805
    • Bode, A.M.1    Dong, Z.2
  • 35
    • 35548930209 scopus 로고    scopus 로고
    • The emerging roles of forkhead box (Fox) proteins in cancer
    • DOI 10.1038/nrc2223, PII NRC2223
    • Myatt SS, Lam EW. The emerging roles of forkhead box (Fox) proteins in cancer. Nat Rev Cancer 2007;7:847-59. (Pubitemid 350006253)
    • (2007) Nature Reviews Cancer , vol.7 , Issue.11 , pp. 847-859
    • Myatt, S.S.1    Lam, E.W.-F.2
  • 37
    • 34548183836 scopus 로고    scopus 로고
    • PolyADP-ribosylation and cancer
    • DOI 10.1111/j.1349-7006.2007.00567.x
    • Miwa M, Masutani M. PolyADP-ribosylation and cancer. Cancer Sci 2007;98:1528-35. (Pubitemid 47308446)
    • (2007) Cancer Science , vol.98 , Issue.10 , pp. 1528-1535
    • Miwa, M.1    Masutani, M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.