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Volumn 280, Issue 15, 2013, Pages 3551-3562

A role of intracellular mono-ADP-ribosylation in cancer biology

Author keywords

ADP ribosyltransferase; cancer; clostridial toxin like ADP ribosyltransferase (ARTC); diphtheria toxin like ADP ribosyltransferase (ARTD); diphtheria toxin like ADP ribosyltransferase 15 (ARTD15); mono ADP ribosylation; NAD; poly ADP ribose polymerase 16 (PARP16); post translational modification

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSE; ANTINEOPLASTIC AGENT; BMN 763; BRCA2 PROTEIN; CELL PROTEIN; CEP 9722; DIPHTHERIA TOXIN; GAMMA INTERFERON; GPI 21016; INIPARIB; INO 1001; INTERLEUKIN 4; KARYOPHERIN ALPHA; KARYOPHERIN BETA; KARYOPHERIN BETA1; MONO ADP RIBOSYLTRANSFERASE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 1; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 10; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 15; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 3; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 4; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 5; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE 8; NIRAPARIB; OLAPARIB; POLY ADP RIBOSYLTRANSFERASE; RUCAPARIB; UNCLASSIFIED DRUG; UNINDEXED DRUG; VELIPARIB;

EID: 84880333963     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.12290     Document Type: Review
Times cited : (54)

References (110)
  • 1
    • 25444495510 scopus 로고    scopus 로고
    • Physiological relevance of the endogenous mono(ADP-ribosyl)ation of cellular proteins
    • Di Girolamo M, Dani N, Stilla A, &, Corda D, (2005) Physiological relevance of the endogenous mono(ADP-ribosyl)ation of cellular proteins. FEBS J 272, 4565-4575.
    • (2005) FEBS J , vol.272 , pp. 4565-4575
    • Di Girolamo, M.1    Dani, N.2    Stilla, A.3    Corda, D.4
  • 2
    • 84876733507 scopus 로고    scopus 로고
    • ADP-ribosylated proteins as old and new drug targets for anticancer therapy: The example of ARF6
    • Dani N, Barbosa AJ, Del Rio A, &, Di Girolamo M, (2013) ADP-ribosylated proteins as old and new drug targets for anticancer therapy: the example of ARF6. Curr Pharm Des, 19, 624-633.
    • (2013) Curr Pharm des , vol.19 , pp. 624-633
    • Dani, N.1    Barbosa, A.J.2    Del Rio, A.3    Di Girolamo, M.4
  • 4
    • 38449088040 scopus 로고    scopus 로고
    • The diverse biological roles of mammalian PARPS, a small but powerful family of poly-ADP-ribose polymerases
    • Hassa PO, &, Hottiger MO, (2008) The diverse biological roles of mammalian PARPS, a small but powerful family of poly-ADP-ribose polymerases. Front Biosci 13, 3046-3082.
    • (2008) Front Biosci , vol.13 , pp. 3046-3082
    • Hassa, P.O.1    Hottiger, M.O.2
  • 5
    • 0028981421 scopus 로고
    • The family of bacterial ADP-ribosylating exotoxins
    • Krueger KM, &, Barbieri JT, (1995) The family of bacterial ADP-ribosylating exotoxins. Clin Microbiol Rev 8, 34-47.
    • (1995) Clin Microbiol Rev , vol.8 , pp. 34-47
    • Krueger, K.M.1    Barbieri, J.T.2
  • 6
    • 53849133471 scopus 로고    scopus 로고
    • Molecular mechanisms of the cytotoxicity of ADP-ribosylating toxins
    • Deng Q, &, Barbieri JT, (2008) Molecular mechanisms of the cytotoxicity of ADP-ribosylating toxins. Annu Rev Microbiol 62, 271-288.
    • (2008) Annu Rev Microbiol , vol.62 , pp. 271-288
    • Deng, Q.1    Barbieri, J.T.2
  • 7
    • 0035400143 scopus 로고    scopus 로고
    • An abundance of bacterial ADP-ribosyltransferases - Implications for the origin of exotoxins and their human homologues
    • discussion 308
    • Pallen MJ, Lam AC, Loman NJ, &, McBride A, (2001) An abundance of bacterial ADP-ribosyltransferases-implications for the origin of exotoxins and their human homologues. Trends Microbiol 9, 302-307.; discussion 308.
    • (2001) Trends Microbiol , vol.9 , pp. 302-307
    • Pallen, M.J.1    Lam, A.C.2    Loman, N.J.3    McBride, A.4
  • 8
    • 0038508358 scopus 로고    scopus 로고
    • Mono-ADP-Ribosylation of Heterotrimeric G Proteins
    • (Bradshaw R. & Dennis E. eds), Academic Press, San Diego
    • Di Girolamo M, &, Corda D, (2009) Mono-ADP-Ribosylation of Heterotrimeric G Proteins. In: Handbook of Cell Signalling, Vol. 2, (, Bradshaw R, &, Dennis E, eds), pp. 613-618. Academic Press, San Diego.
    • (2009) Handbook of Cell Signalling , vol.2 , pp. 613-618
    • Di Girolamo, M.1    Corda, D.2
  • 9
    • 0037881920 scopus 로고    scopus 로고
    • Functional aspects of protein mono-ADP-ribosylation
    • Corda D, &, Di Girolamo M, (2003) Functional aspects of protein mono-ADP-ribosylation. EMBO J 22, 1953-1958.
    • (2003) EMBO J , vol.22 , pp. 1953-1958
    • Corda, D.1    Di Girolamo, M.2
  • 10
    • 84862758175 scopus 로고    scopus 로고
    • New insights into the molecular and cellular functions of poly(ADP-ribose) and PARPs
    • Gibson BA, &, Kraus WL, (2012) New insights into the molecular and cellular functions of poly(ADP-ribose) and PARPs. Nat Rev Mol Cell Biol 13, 411-424.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 411-424
    • Gibson, B.A.1    Kraus, W.L.2
  • 11
    • 84867370386 scopus 로고    scopus 로고
    • Pleiotropic cellular functions of PARP1 in longevity and aging: Genome maintenance meets inflammation
    • Mangerich A, &, Burkle A, (2012) Pleiotropic cellular functions of PARP1 in longevity and aging: genome maintenance meets inflammation. Oxid Med Cell Longev 2012, 321653.
    • (2012) Oxid Med Cell Longev , vol.2012 , pp. 321653
    • Mangerich, A.1    Burkle, A.2
  • 14
    • 34548183836 scopus 로고    scopus 로고
    • PolyADP-ribosylation and cancer
    • Miwa M, &, Masutani M, (2007) PolyADP-ribosylation and cancer. Cancer Sci 98, 1528-1535.
    • (2007) Cancer Sci , vol.98 , pp. 1528-1535
    • Miwa, M.1    Masutani, M.2
  • 15
    • 0019332669 scopus 로고
    • Isolation and properties of an NAD- and guanidine-dependent ADP-ribosyltransferase from turkey erythrocytes
    • Moss J, Stanley SJ, &, Watkins PA, (1980) Isolation and properties of an NAD- and guanidine-dependent ADP-ribosyltransferase from turkey erythrocytes. J Biol Chem 255, 5838-5840.
    • (1980) J Biol Chem , vol.255 , pp. 5838-5840
    • Moss, J.1    Stanley, S.J.2    Watkins, P.A.3
  • 16
    • 0022920257 scopus 로고
    • Amino acid specific ADP-ribosylation: Specific NAD: Arginine mono-ADP-ribosyltransferases associated with turkey erythrocyte nuclei and plasma membranes
    • West RE Jr, &, Moss J, (1986) Amino acid specific ADP-ribosylation: specific NAD: arginine mono-ADP-ribosyltransferases associated with turkey erythrocyte nuclei and plasma membranes. Biochemistry 25, 8057-8062.
    • (1986) Biochemistry , vol.25 , pp. 8057-8062
    • West Jr., R.E.1    Moss, J.2
  • 17
    • 0019877184 scopus 로고
    • Amino acid-specific ADP-ribosylation. Identification of an arginine-dependent ADP-ribosyltransferase in rat liver
    • Moss J, &, Stanley SJ, (1981) Amino acid-specific ADP-ribosylation. Identification of an arginine-dependent ADP-ribosyltransferase in rat liver. J Biol Chem 256, 7830-7833.
    • (1981) J Biol Chem , vol.256 , pp. 7830-7833
    • Moss, J.1    Stanley, S.J.2
  • 18
    • 0020993941 scopus 로고
    • Xenopus mono(adenosine diphosphate ribosyl) transferase: Purification, assay, and properties
    • Godeau F, &, Koide SS, (1983) Xenopus mono(adenosine diphosphate ribosyl) transferase: purification, assay, and properties. Princess Takamatsu Symp 13, 111-118.
    • (1983) Princess Takamatsu Symp , vol.13 , pp. 111-118
    • Godeau, F.1    Koide, S.S.2
  • 19
    • 0026445547 scopus 로고
    • Molecular characterization of NAD:arginine ADP-ribosyltransferase from rabbit skeletal muscle
    • Zolkiewska A, Nightingale MS, &, Moss J, (1992) Molecular characterization of NAD:arginine ADP-ribosyltransferase from rabbit skeletal muscle. Proc Natl Acad Sci USA 89, 11352-11356.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 11352-11356
    • Zolkiewska, A.1    Nightingale, M.S.2    Moss, J.3
  • 20
    • 0029047630 scopus 로고
    • Cloning of a chicken gene homologous to the rabbit mono-ADP- ribosyltransferase gene
    • Davis T, &, Shall S, (1995) Cloning of a chicken gene homologous to the rabbit mono-ADP-ribosyltransferase gene. Biochem Soc Trans 23, 207S.
    • (1995) Biochem Soc Trans , vol.23
    • Davis, T.1    Shall, S.2
  • 21
    • 0030239668 scopus 로고    scopus 로고
    • Structure of the gene encoding the rat T cell ecto-ADP-ribosyltransferase RT6
    • Haag FA, Kuhlenbaumer G, Koch-Nolte F, Wingender E, &, Thiele HG, (1996) Structure of the gene encoding the rat T cell ecto-ADP-ribosyltransferase RT6. J Immunol 157, 2022-2030.
    • (1996) J Immunol , vol.157 , pp. 2022-2030
    • Haag, F.A.1    Kuhlenbaumer, G.2    Koch-Nolte, F.3    Wingender, E.4    Thiele, H.G.5
  • 22
    • 0029834653 scopus 로고    scopus 로고
    • Cloning and characterization of a novel membrane-associated lymphocyte NAD:arginine ADP-ribosyltransferase
    • Okazaki IJ, Kim HJ, &, Moss J, (1996) Cloning and characterization of a novel membrane-associated lymphocyte NAD:arginine ADP-ribosyltransferase. J Biol Chem 271, 22052-22057.
    • (1996) J Biol Chem , vol.271 , pp. 22052-22057
    • Okazaki, I.J.1    Kim, H.J.2    Moss, J.3
  • 23
    • 0030974292 scopus 로고    scopus 로고
    • Molecular cloning and characterization of arginine-specific ADP-ribosyltransferases from chicken bone marrow cells
    • Shimoyama M, Tsuchiya M, Hara N, Yamada K, &, Osago H, (1997) Molecular cloning and characterization of arginine-specific ADP- ribosyltransferases from chicken bone marrow cells. Adv Exp Med Biol 419, 137-144.
    • (1997) Adv Exp Med Biol , vol.419 , pp. 137-144
    • Shimoyama, M.1    Tsuchiya, M.2    Hara, N.3    Yamada, K.4    Osago, H.5
  • 24
  • 25
    • 0035913724 scopus 로고    scopus 로고
    • Structure, chromosomal localization, and expression of the gene for mouse ecto-mono(ADP-ribosyl)transferase ART5
    • Glowacki G, Braren R, Cetkovic-Cvrlje M, Leiter EH, Haag F, &, Koch-Nolte F, (2001) Structure, chromosomal localization, and expression of the gene for mouse ecto-mono(ADP-ribosyl)transferase ART5. Gene 275, 267-277.
    • (2001) Gene , vol.275 , pp. 267-277
    • Glowacki, G.1    Braren, R.2    Cetkovic-Cvrlje, M.3    Leiter, E.H.4    Haag, F.5    Koch-Nolte, F.6
  • 26
    • 0027960632 scopus 로고
    • Premature stop codons inactivate the RT6 genes of the human and chimpanzee species
    • Haag F, Koch-Nolte F, Kuhl M, Lorenzen S, &, Thiele HG, (1994) Premature stop codons inactivate the RT6 genes of the human and chimpanzee species. J Mol Biol 243, 537-546.
    • (1994) J Mol Biol , vol.243 , pp. 537-546
    • Haag, F.1    Koch-Nolte, F.2    Kuhl, M.3    Lorenzen, S.4    Thiele, H.G.5
  • 27
    • 0031700924 scopus 로고    scopus 로고
    • Endogenous relatives of ADP-ribosylating bacterial toxins in mice and men: Potential regulators of immune cell function
    • Haag F, &, Koch-Nolte F, (1998) Endogenous relatives of ADP-ribosylating bacterial toxins in mice and men: potential regulators of immune cell function. J Biol Regul Homeost Agents 12, 53-62.
    • (1998) J Biol Regul Homeost Agents , vol.12 , pp. 53-62
    • Haag, F.1    Koch-Nolte, F.2
  • 28
    • 0030584706 scopus 로고    scopus 로고
    • Regulation of CTL by ecto-nicotinamide adenine dinucleotide (NAD) involves ADP-ribosylation of a p56lck-associated protein
    • Wang J, Nemoto E, &, Dennert G, (1996) Regulation of CTL by ecto-nicotinamide adenine dinucleotide (NAD) involves ADP-ribosylation of a p56lck-associated protein. J Immunol 156, 2819-2827.
    • (1996) J Immunol , vol.156 , pp. 2819-2827
    • Wang, J.1    Nemoto, E.2    Dennert, G.3
  • 29
    • 0033581006 scopus 로고    scopus 로고
    • A cell surface ADP-ribosyltransferase modulates T cell receptor association and signaling
    • Liu ZX, Yu Y, &, Dennert G, (1999) A cell surface ADP-ribosyltransferase modulates T cell receptor association and signaling. J Biol Chem 274, 17399-17401.
    • (1999) J Biol Chem , vol.274 , pp. 17399-17401
    • Liu, Z.X.1    Yu, Y.2    Dennert, G.3
  • 30
    • 0037126639 scopus 로고    scopus 로고
    • Mono-ADP-ribosylation: A tool for modulating immune response and cell signaling
    • Corda D, &, Di Girolamo M, (2002) Mono-ADP-ribosylation: a tool for modulating immune response and cell signaling. Sci STKE 2002, PE53.
    • (2002) Sci STKE , vol.2002
    • Corda, D.1    Di Girolamo, M.2
  • 31
    • 84880331568 scopus 로고    scopus 로고
    • The art of blocking ARTs: Nanobodies as experimental and therapeutic tools to block mammalian and toxin ADP-ribosyltransferases
    • in press
    • Koch-Nolte F, (2013) The art of blocking ARTs: Nanobodies as experimental and therapeutic tools to block mammalian and toxin ADP-ribosyltransferases. FEBS J in press.
    • (2013) FEBS J
    • Koch-Nolte, F.1
  • 32
    • 0031010494 scopus 로고    scopus 로고
    • Isolation and characterization of the cDNA encoding bovine poly(ADP-ribose) glycohydrolase
    • Lin W, Ame JC, Aboul-Ela N, Jacobson EL, &, Jacobson MK, (1997) Isolation and characterization of the cDNA encoding bovine poly(ADP-ribose) glycohydrolase. J Biol Chem 272, 11895-11901.
    • (1997) J Biol Chem , vol.272 , pp. 11895-11901
    • Lin, W.1    Ame, J.C.2    Aboul-Ela, N.3    Jacobson, E.L.4    Jacobson, M.K.5
  • 33
    • 0023753245 scopus 로고
    • Purification and characterization of ADP-ribosylarginine hydrolase from turkey erythrocytes
    • Moss J, Tsai SC, Adamik R, Chen HC, &, Stanley SJ, (1988) Purification and characterization of ADP-ribosylarginine hydrolase from turkey erythrocytes. Biochemistry 27, 5819-5823.
    • (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
  • 35
    • 84860844237 scopus 로고    scopus 로고
    • ADP-ribosylhydrolase 3 (ARH3), not poly-ADP-ribose glycohydrolase (PARG) isoforms, are responsible for degradation of mitochondrial matrix-associated poly-ADP-Ribose
    • Niere M, Mashimo M, Agledal L, Doelle C, Kasamatsu A, Kato J, Moss J, &, Ziegler M, (2012) ADP-ribosylhydrolase 3 (ARH3), not poly-ADP-ribose glycohydrolase (PARG) isoforms, are responsible for degradation of mitochondrial matrix-associated poly-ADP-Ribose. J Biol Chem 287, 16088-16102.
    • (2012) J Biol Chem , vol.287 , pp. 16088-16102
    • Niere, M.1    Mashimo, M.2    Agledal, L.3    Doelle, C.4    Kasamatsu, A.5    Kato, J.6    Moss, J.7    Ziegler, M.8
  • 36
    • 84863482663 scopus 로고    scopus 로고
    • Silencing poly(ADP-ribose) glycohydrolase (PARG) expression inhibits growth of human colon cancer cells in vitro via PI3K/Akt/NFkappa-B pathway
    • Fauzee NJ, Li Q, Wang YL, &, Pan J, (2012) Silencing poly(ADP-ribose) glycohydrolase (PARG) expression inhibits growth of human colon cancer cells in vitro via PI3K/Akt/NFkappa-B pathway. Pathol Oncol Res 18, 191-199.
    • (2012) Pathol Oncol Res , vol.18 , pp. 191-199
    • Fauzee, N.J.1    Li, Q.2    Wang, Y.L.3    Pan, J.4
  • 37
    • 84857945772 scopus 로고    scopus 로고
    • Inhibition of poly(ADP-ribose) glycohydrolase (PARG) specifically kills BRCA2-deficient tumor cells
    • Fathers C, Drayton RM, Solovieva S, &, Bryant HE, (2012) Inhibition of poly(ADP-ribose) glycohydrolase (PARG) specifically kills BRCA2-deficient tumor cells. Cell Cycle 11, 990-997.
    • (2012) Cell Cycle , vol.11 , pp. 990-997
    • Fathers, C.1    Drayton, R.M.2    Solovieva, S.3    Bryant, H.E.4
  • 41
    • 55549139051 scopus 로고    scopus 로고
    • The expanding field of poly(ADP-ribosyl)ation reactions. Protein Modifications: Beyond the usual suspects. Review Series
    • Hakme A, Wong HK, Dantzer F, &, Schreiber V, (2008) The expanding field of poly(ADP-ribosyl)ation reactions. Protein Modifications: beyond the usual suspects. Review Series. EMBO Rep 9, 1094-1100.
    • (2008) EMBO Rep , vol.9 , pp. 1094-1100
    • Hakme, A.1    Wong, H.K.2    Dantzer, F.3    Schreiber, V.4
  • 44
    • 77957743077 scopus 로고    scopus 로고
    • Evolutionary history of the poly(ADP-ribose) polymerase gene family in eukaryotes
    • Citarelli M, Teotia S, &, Lamb RS, (2010) Evolutionary history of the poly(ADP-ribose) polymerase gene family in eukaryotes. BMC Evol Biol 10, 308.
    • (2010) BMC Evol Biol , vol.10 , pp. 308
    • Citarelli, M.1    Teotia, S.2    Lamb, R.S.3
  • 45
    • 79953651847 scopus 로고    scopus 로고
    • PARP-3, a DNA-dependent PARP with emerging roles in double-strand break repair and mitotic progression
    • Boehler C, &, Dantzer F, (2011) PARP-3, a DNA-dependent PARP with emerging roles in double-strand break repair and mitotic progression. Cell Cycle 10, 1023-1024.
    • (2011) Cell Cycle , vol.10 , pp. 1023-1024
    • Boehler, C.1    Dantzer, F.2
  • 47
    • 85047693635 scopus 로고    scopus 로고
    • Tankyrase-1 polymerization of poly(ADP-ribose) is required for spindle structure and function
    • Chang P, Coughlin M, &, Mitchison TJ, (2005) Tankyrase-1 polymerization of poly(ADP-ribose) is required for spindle structure and function. Nat Cell Biol 7, 1133-1139.
    • (2005) Nat Cell Biol , vol.7 , pp. 1133-1139
    • Chang, P.1    Coughlin, M.2    Mitchison, T.J.3
  • 48
    • 0037379179 scopus 로고    scopus 로고
    • Involvement of poly(ADP-ribose) polymerase 1 and poly(ADP-ribosyl)ation in regulation of centrosome function
    • Kanai M, Tong WM, Sugihara E, Wang ZQ, Fukasawa K, &, Miwa M, (2003) Involvement of poly(ADP-ribose) polymerase 1 and poly(ADP-ribosyl)ation in regulation of centrosome function. Mol Cell Biol 23, 2451-2462.
    • (2003) Mol Cell Biol , vol.23 , pp. 2451-2462
    • Kanai, M.1    Tong, W.M.2    Sugihara, E.3    Wang, Z.Q.4    Fukasawa, K.5    Miwa, M.6
  • 49
    • 59449085305 scopus 로고    scopus 로고
    • Phase i study of the poly(ADP-ribose) polymerase inhibitor, AG014699, in combination with temozolomide in patients with advanced solid tumors
    • Plummer R, Jones C, Middleton M, Wilson R, Evans J, Olsen A, Curtin N, Boddy A, McHugh P, Newell D, et al,. (2008) Phase I study of the poly(ADP-ribose) polymerase inhibitor, AG014699, in combination with temozolomide in patients with advanced solid tumors. Clin Cancer Res 14, 7917-7923.
    • (2008) Clin Cancer Res , vol.14 , pp. 7917-7923
    • Plummer, R.1    Jones, C.2    Middleton, M.3    Wilson, R.4    Evans, J.5    Olsen, A.6    Curtin, N.7    Boddy, A.8    McHugh, P.9    Newell, D.10
  • 50
    • 19444375973 scopus 로고    scopus 로고
    • Chemopotentiation by PARP inhibitors in cancer therapy
    • Tentori L, &, Graziani G, (2005) Chemopotentiation by PARP inhibitors in cancer therapy. Pharmacol Res 52, 25-33.
    • (2005) Pharmacol Res , vol.52 , pp. 25-33
    • Tentori, L.1    Graziani, G.2
  • 51
    • 0036733355 scopus 로고    scopus 로고
    • The therapeutic potential of poly(ADP-ribose) polymerase inhibitors
    • Virag L, &, Szabo C, (2002) The therapeutic potential of poly(ADP-ribose) polymerase inhibitors. Pharmacol Rev 54, 375-429.
    • (2002) Pharmacol Rev , vol.54 , pp. 375-429
    • Virag, L.1    Szabo, C.2
  • 52
    • 18944390248 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase and the therapeutic effects of its inhibitors
    • Jagtap P, &, Szabo C, (2005) Poly(ADP-ribose) polymerase and the therapeutic effects of its inhibitors. Nat Rev Drug Discov 4, 421-440.
    • (2005) Nat Rev Drug Discov , vol.4 , pp. 421-440
    • Jagtap, P.1    Szabo, C.2
  • 53
    • 79960703030 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase-1 inhibition: Preclinical and clinical development of synthetic lethality
    • Leung M, Rosen D, Fields S, Cesano A, &, Budman DR, (2011) Poly(ADP-ribose) polymerase-1 inhibition: preclinical and clinical development of synthetic lethality. Mol Med 17, 854-862.
    • (2011) Mol Med , vol.17 , pp. 854-862
    • Leung, M.1    Rosen, D.2    Fields, S.3    Cesano, A.4    Budman, D.R.5
  • 54
    • 80052535308 scopus 로고    scopus 로고
    • PARP inhibitors stumble in breast cancer
    • Guha M, (2011) PARP inhibitors stumble in breast cancer. Nat Biotechnol 29, 373-374.
    • (2011) Nat Biotechnol , vol.29 , pp. 373-374
    • Guha, M.1
  • 57
    • 79551582236 scopus 로고    scopus 로고
    • Docking study and binding free energy calculation of poly(ADP-ribose) polymerase inhibitors
    • Ohno K, Mitsui T, Tanida Y, Matsuura A, Fujitani H, Niimi T, &, Orita M, (2011) Docking study and binding free energy calculation of poly(ADP-ribose) polymerase inhibitors. J Mol Model 17, 383-389.
    • (2011) J Mol Model , vol.17 , pp. 383-389
    • Ohno, K.1    Mitsui, T.2    Tanida, Y.3    Matsuura, A.4    Fujitani, H.5    Niimi, T.6    Orita, M.7
  • 58
    • 0035829430 scopus 로고    scopus 로고
    • Modeling of poly(ADP-ribose)polymerase (PARP) inhibitors. Docking of ligands and quantitative structure-activity relationship analysis
    • Costantino G, Macchiarulo A, Camaioni E, &, Pellicciari R, (2001) Modeling of poly(ADP-ribose)polymerase (PARP) inhibitors. Docking of ligands and quantitative structure-activity relationship analysis. J Med Chem 44, 3786-3794.
    • (2001) J Med Chem , vol.44 , pp. 3786-3794
    • Costantino, G.1    Macchiarulo, A.2    Camaioni, E.3    Pellicciari, R.4
  • 59
    • 12844260196 scopus 로고    scopus 로고
    • Docking studies on PARP-1 inhibitors: Insights into the role of a binding pocket water molecule
    • Bellocchi D, Macchiarulo A, Costantino G, &, Pellicciari R, (2005) Docking studies on PARP-1 inhibitors: insights into the role of a binding pocket water molecule. Bioorg Med Chem 13, 1151-1157.
    • (2005) Bioorg Med Chem , vol.13 , pp. 1151-1157
    • Bellocchi, D.1    Macchiarulo, A.2    Costantino, G.3    Pellicciari, R.4
  • 60
    • 74049112025 scopus 로고    scopus 로고
    • Discovery and SAR of substituted 3-oxoisoindoline-4-carboxamides as potent inhibitors of poly(ADP-ribose) polymerase (PARP) for the treatment of cancer
    • Gandhi VB, Luo Y, Liu X, Shi Y, Klinghofer V, Johnson EF, Park C, Giranda VL, Penning TD, &, Zhu GD, (2010) Discovery and SAR of substituted 3-oxoisoindoline-4-carboxamides as potent inhibitors of poly(ADP-ribose) polymerase (PARP) for the treatment of cancer. Bioorg Med Chem Lett 20, 1023-1026.
    • (2010) Bioorg Med Chem Lett , vol.20 , pp. 1023-1026
    • Gandhi, V.B.1    Luo, Y.2    Liu, X.3    Shi, Y.4    Klinghofer, V.5    Johnson, E.F.6    Park, C.7    Giranda, V.L.8    Penning, T.D.9    Zhu, G.D.10
  • 61
    • 84880330905 scopus 로고    scopus 로고
    • Tankyrases as drug targets
    • in press
    • Lehtio L, &, Krauss S, (2013) Tankyrases as drug targets. FEBS J in press.
    • (2013) FEBS J
    • Lehtio, L.1    Krauss, S.2
  • 65
    • 84869786773 scopus 로고    scopus 로고
    • PARP6, a mono(ADP-ribosyl) transferase and a negative regulator of cell proliferation, is involved in colorectal cancer development
    • Tuncel H, Tanaka S, Oka S, Nakai S, Fukutomi R, Okamoto M, Ota T, Kaneko H, Tatsuka M, &, Shimamoto F, (2012) PARP6, a mono(ADP-ribosyl) transferase and a negative regulator of cell proliferation, is involved in colorectal cancer development. Int J Oncol 41, 2079-2086.
    • (2012) Int J Oncol , vol.41 , pp. 2079-2086
    • Tuncel, H.1    Tanaka, S.2    Oka, S.3    Nakai, S.4    Fukutomi, R.5    Okamoto, M.6    Ota, T.7    Kaneko, H.8    Tatsuka, M.9    Shimamoto, F.10
  • 66
    • 33645243011 scopus 로고    scopus 로고
    • Selective potentiation of Stat-dependent gene expression by collaborator of Stat6 (CoaSt6), a transcriptional cofactor
    • Goenka S, &, Boothby M, (2006) Selective potentiation of Stat-dependent gene expression by collaborator of Stat6 (CoaSt6), a transcriptional cofactor. Proc Natl Acad Sci USA 103, 4210-4215.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 4210-4215
    • Goenka, S.1    Boothby, M.2
  • 67
    • 84862233980 scopus 로고    scopus 로고
    • PARP16/ARTD15 is a novel endoplasmic-reticulum-associated mono-ADP-ribosyltransferase that interacts with, and modifies karyopherin-1
    • Di Paola S, Micaroni M, Di Tullio G, Buccione R, &, Di Girolamo M, (2012) PARP16/ARTD15 is a novel endoplasmic-reticulum-associated mono-ADP-ribosyltransferase that interacts with, and modifies karyopherin-1. PLoS ONE 7, e37352.
    • (2012) PLoS ONE , vol.7
    • Di Paola, S.1    Micaroni, M.2    Di Tullio, G.3    Buccione, R.4    Di Girolamo, M.5
  • 69
    • 27644577665 scopus 로고    scopus 로고
    • In silico characterization of the family of PARP-like poly(ADP-ribosyl)transferases (pARTs)
    • Otto H, Reche PA, Bazan F, Dittmar K, Haag F, &, Koch-Nolte F, (2005) In silico characterization of the family of PARP-like poly(ADP-ribosyl) transferases (pARTs). BMC Genomics 6, 139.
    • (2005) BMC Genomics , vol.6 , pp. 139
    • Otto, H.1    Reche, P.A.2    Bazan, F.3    Dittmar, K.4    Haag, F.5    Koch-Nolte, F.6
  • 70
    • 0026737922 scopus 로고
    • MacroH2A, a core histone containing a large nonhistone region
    • Pehrson JR, &, Fried VA, (1992) MacroH2A, a core histone containing a large nonhistone region. Science 257, 1398-1400.
    • (1992) Science , vol.257 , pp. 1398-1400
    • Pehrson, J.R.1    Fried, V.A.2
  • 71
    • 0032507949 scopus 로고    scopus 로고
    • Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals
    • Costanzi C, &, Pehrson JR, (1998) Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals. Nature 393, 599-601.
    • (1998) Nature , vol.393 , pp. 599-601
    • Costanzi, C.1    Pehrson, J.R.2
  • 72
    • 0037961635 scopus 로고    scopus 로고
    • The histone variant macroH2A interferes with transcription factor binding and SWI/SNF nucleosome remodeling
    • Angelov D, Molla A, Perche PY, Hans F, Cote J, Khochbin S, Bouvet P, &, Dimitrov S, (2003) The histone variant macroH2A interferes with transcription factor binding and SWI/SNF nucleosome remodeling. Mol Cell 11, 1033-1041.
    • (2003) Mol Cell , vol.11 , pp. 1033-1041
    • Angelov, D.1    Molla, A.2    Perche, P.Y.3    Hans, F.4    Cote, J.5    Khochbin, S.6    Bouvet, P.7    Dimitrov, S.8
  • 74
    • 63149116496 scopus 로고    scopus 로고
    • Combining affinity purification by ADP-ribose-binding macro domains with mass spectrometry to define the mammalian ADP-ribosyl proteome
    • Dani N, Stilla A, Marchegiani A, Tamburro A, Till S, Ladurner AG, Corda D, &, Di Girolamo M, (2009) Combining affinity purification by ADP-ribose-binding macro domains with mass spectrometry to define the mammalian ADP-ribosyl proteome. Proc Natl Acad Sci USA 106, 4243-4248.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 4243-4248
    • Dani, N.1    Stilla, A.2    Marchegiani, A.3    Tamburro, A.4    Till, S.5    Ladurner, A.G.6    Corda, D.7    Di Girolamo, M.8
  • 76
    • 34250359929 scopus 로고    scopus 로고
    • Poly(ADP-ribose) polymerase 1 is inhibited by a histone H2A variant, MacroH2A, and contributes to silencing of the inactive X chromosome
    • Nusinow DA, Hernandez-Munoz I, Fazzio TG, Shah GM, Kraus WL, &, Panning B, (2007) Poly(ADP-ribose) polymerase 1 is inhibited by a histone H2A variant, MacroH2A, and contributes to silencing of the inactive X chromosome. J Biol Chem 282, 12851-12859.
    • (2007) J Biol Chem , vol.282 , pp. 12851-12859
    • Nusinow, D.A.1    Hernandez-Munoz, I.2    Fazzio, T.G.3    Shah, G.M.4    Kraus, W.L.5    Panning, B.6
  • 77
    • 26644446700 scopus 로고    scopus 로고
    • B-aggressive lymphoma family proteins have unique domains that modulate transcription and exhibit poly(ADP-ribose) polymerase activity
    • Aguiar RC, Takeyama K, He C, Kreinbrink K, &, Shipp MA, (2005) B-aggressive lymphoma family proteins have unique domains that modulate transcription and exhibit poly(ADP-ribose) polymerase activity. J Biol Chem 280, 33756-33765.
    • (2005) J Biol Chem , vol.280 , pp. 33756-33765
    • Aguiar, R.C.1    Takeyama, K.2    He, C.3    Kreinbrink, K.4    Shipp, M.A.5
  • 78
    • 0034672418 scopus 로고    scopus 로고
    • BAL is a novel risk-related gene in diffuse large B-cell lymphomas that enhances cellular migration
    • Aguiar RC, Yakushijin Y, Kharbanda S, Salgia R, Fletcher JA, &, Shipp MA, (2000) BAL is a novel risk-related gene in diffuse large B-cell lymphomas that enhances cellular migration. Blood 96, 4328-4334.
    • (2000) Blood , vol.96 , pp. 4328-4334
    • Aguiar, R.C.1    Yakushijin, Y.2    Kharbanda, S.3    Salgia, R.4    Fletcher, J.A.5    Shipp, M.A.6
  • 79
    • 33745848147 scopus 로고    scopus 로고
    • BAL1 and BBAP are regulated by a gamma interferon-responsive bidirectional promoter and are overexpressed in diffuse large B-cell lymphomas with a prominent inflammatory infiltrate
    • Juszczynski P, Kutok JL, Li C, Mitra J, Aguiar RC, &, Shipp MA, (2006) BAL1 and BBAP are regulated by a gamma interferon-responsive bidirectional promoter and are overexpressed in diffuse large B-cell lymphomas with a prominent inflammatory infiltrate. Mol Cell Biol 26, 5348-5359.
    • (2006) Mol Cell Biol , vol.26 , pp. 5348-5359
    • Juszczynski, P.1    Kutok, J.L.2    Li, C.3    Mitra, J.4    Aguiar, R.C.5    Shipp, M.A.6
  • 81
    • 0345575181 scopus 로고    scopus 로고
    • Cytokines and STAT signaling
    • Schindler C, &, Strehlow I, (2000) Cytokines and STAT signaling. Adv Pharmacol 47, 113-174.
    • (2000) Adv Pharmacol , vol.47 , pp. 113-174
    • Schindler, C.1    Strehlow, I.2
  • 82
    • 0030840464 scopus 로고    scopus 로고
    • STATs and gene regulation
    • Darnell JE Jr, (1997) STATs and gene regulation. Science 277, 1630-1635.
    • (1997) Science , vol.277 , pp. 1630-1635
    • Darnell Jr., J.E.1
  • 83
    • 0036476551 scopus 로고    scopus 로고
    • Stat1-dependent and -independent pathways in IFN-gamma-dependent signaling
    • Ramana CV, Gil MP, Schreiber RD, &, Stark GR, (2002) Stat1-dependent and -independent pathways in IFN-gamma-dependent signaling. Trends Immunol 23, 96-101.
    • (2002) Trends Immunol , vol.23 , pp. 96-101
    • Ramana, C.V.1    Gil, M.P.2    Schreiber, R.D.3    Stark, G.R.4
  • 85
    • 34547112062 scopus 로고    scopus 로고
    • Collaborator of Stat6 (CoaSt6)-associated poly(ADP-ribose) polymerase activity modulates Stat6-dependent gene transcription
    • Goenka S, Cho SH, &, Boothby M, (2007) Collaborator of Stat6 (CoaSt6)-associated poly(ADP-ribose) polymerase activity modulates Stat6-dependent gene transcription. J Biol Chem 282, 18732-18739.
    • (2007) J Biol Chem , vol.282 , pp. 18732-18739
    • Goenka, S.1    Cho, S.H.2    Boothby, M.3
  • 86
    • 78751543911 scopus 로고    scopus 로고
    • PARP-14 functions as a transcriptional switch for Stat6-dependent gene activation
    • Mehrotra P, Riley JP, Patel R, Li F, Voss L, &, Goenka S, (2011) PARP-14 functions as a transcriptional switch for Stat6-dependent gene activation. J Biol Chem 286, 1767-1776.
    • (2011) J Biol Chem , vol.286 , pp. 1767-1776
    • Mehrotra, P.1    Riley, J.P.2    Patel, R.3    Li, F.4    Voss, L.5    Goenka, S.6
  • 88
    • 80053158632 scopus 로고    scopus 로고
    • Glycolytic rate and lymphomagenesis depend on PARP14, an ADP ribosyltransferase of the B aggressive lymphoma (BAL) family
    • Cho SH, Ahn AK, Bhargava P, Lee CH, Eischen CM, McGuinness O, &, Boothby M, (2011) Glycolytic rate and lymphomagenesis depend on PARP14, an ADP ribosyltransferase of the B aggressive lymphoma (BAL) family. Proc Natl Acad Sci USA 108, 15972-15977.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 15972-15977
    • Cho, S.H.1    Ahn, A.K.2    Bhargava, P.3    Lee, C.H.4    Eischen, C.M.5    McGuinness, O.6    Boothby, M.7
  • 89
    • 34548757447 scopus 로고    scopus 로고
    • Regulation of phosphoglucose isomerase/autocrine motility factor activities by the poly(ADP-ribose) polymerase family-14
    • Yanagawa T, Funasaka T, Tsutsumi S, Hu H, Watanabe H, &, Raz A, (2007) Regulation of phosphoglucose isomerase/autocrine motility factor activities by the poly(ADP-ribose) polymerase family-14. Cancer Res 67, 8682-8689.
    • (2007) Cancer Res , vol.67 , pp. 8682-8689
    • Yanagawa, T.1    Funasaka, T.2    Tsutsumi, S.3    Hu, H.4    Watanabe, H.5    Raz, A.6
  • 90
    • 0027937653 scopus 로고
    • Isolation of a protein that is essential for the first step of nuclear protein import
    • Gorlich D, Prehn S, Laskey RA, &, Hartmann E, (1994) Isolation of a protein that is essential for the first step of nuclear protein import. Cell 79, 767-778.
    • (1994) Cell , vol.79 , pp. 767-778
    • Gorlich, D.1    Prehn, S.2    Laskey, R.A.3    Hartmann, E.4
  • 91
    • 0042830859 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport: Taking an inventory
    • Fried H, &, Kutay U, (2003) Nucleocytoplasmic transport: taking an inventory. Cell Mol Life Sci 60, 1659-1688.
    • (2003) Cell Mol Life Sci , vol.60 , pp. 1659-1688
    • Fried, H.1    Kutay, U.2
  • 92
    • 0035370948 scopus 로고    scopus 로고
    • Nucleocytoplasmic transport enters the atomic age
    • Conti E, &, Izaurralde E, (2001) Nucleocytoplasmic transport enters the atomic age. Curr Opin Cell Biol 13, 310-319.
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 310-319
    • Conti, E.1    Izaurralde, E.2
  • 93
    • 8644262258 scopus 로고    scopus 로고
    • Importin beta: Conducting a much larger cellular symphony
    • Harel A, &, Forbes DJ, (2004) Importin beta: conducting a much larger cellular symphony. Mol Cell 16, 319-330.
    • (2004) Mol Cell , vol.16 , pp. 319-330
    • Harel, A.1    Forbes, D.J.2
  • 94
    • 0033587167 scopus 로고    scopus 로고
    • Structure of importin-beta bound to the IBB domain of importin-alpha
    • Cingolani G, Petosa C, Weis K, &, Muller CW, (1999) Structure of importin-beta bound to the IBB domain of importin-alpha. Nature 399, 221-229.
    • (1999) Nature , vol.399 , pp. 221-229
    • Cingolani, G.1    Petosa, C.2    Weis, K.3    Muller, C.W.4
  • 95
    • 0029278621 scopus 로고
    • Two different subunits of importin cooperate to recognize nuclear localization signals and bind them to the nuclear envelope
    • Gorlich D, Kostka S, Kraft R, Dingwall C, Laskey RA, Hartmann E, &, Prehn S, (1995) Two different subunits of importin cooperate to recognize nuclear localization signals and bind them to the nuclear envelope. Curr Biol 5, 383-392.
    • (1995) Curr Biol , vol.5 , pp. 383-392
    • Gorlich, D.1    Kostka, S.2    Kraft, R.3    Dingwall, C.4    Laskey, R.A.5    Hartmann, E.6    Prehn, S.7
  • 97
    • 0037268889 scopus 로고    scopus 로고
    • Nucleo-cytoplasmic transport of proteins as a target for therapeutic drugs
    • Yashiroda Y, &, Yoshida M, (2003) Nucleo-cytoplasmic transport of proteins as a target for therapeutic drugs. Curr Med Chem 10, 741-748.
    • (2003) Curr Med Chem , vol.10 , pp. 741-748
    • Yashiroda, Y.1    Yoshida, M.2
  • 98
    • 14544272335 scopus 로고    scopus 로고
    • Regulation of nuclear transport: Central role in development and transformation?
    • Poon IK, &, Jans DA, (2005) Regulation of nuclear transport: central role in development and transformation? Traffic 6, 173-186.
    • (2005) Traffic , vol.6 , pp. 173-186
    • Poon, I.K.1    Jans, D.A.2
  • 99
    • 33845414955 scopus 로고    scopus 로고
    • Controlling protein compartmentalization to overcome disease
    • Davis JR, Kakar M, &, Lim CS, (2007) Controlling protein compartmentalization to overcome disease. Pharm Res 24, 17-27.
    • (2007) Pharm Res , vol.24 , pp. 17-27
    • Davis, J.R.1    Kakar, M.2    Lim, C.S.3
  • 100
    • 62449215108 scopus 로고    scopus 로고
    • The karyopherin proteins, Crm1 and karyopherin beta1, are overexpressed in cervical cancer and are critical for cancer cell survival and proliferation
    • van der Watt PJ, Maske CP, Hendricks DT, Parker MI, Denny L, Govender D, Birrer MJ, &, Leaner VD, (2009) The karyopherin proteins, Crm1 and karyopherin beta1, are overexpressed in cervical cancer and are critical for cancer cell survival and proliferation. Int J Cancer 124, 1829-1840.
    • (2009) Int J Cancer , vol.124 , pp. 1829-1840
    • Van Der Watt, P.J.1    Maske, C.P.2    Hendricks, D.T.3    Parker, M.I.4    Denny, L.5    Govender, D.6    Birrer, M.J.7    Leaner, V.D.8
  • 101
    • 77957221380 scopus 로고    scopus 로고
    • Overexpression of karyopherin-2 in epithelial ovarian cancer and correlation with poor prognosis
    • Zheng M, Tang L, Huang L, Ding H, Liao WT, Zeng MS, &, Wang HY, (2010) Overexpression of karyopherin-2 in epithelial ovarian cancer and correlation with poor prognosis. Obstet Gynecol 116, 884-891.
    • (2010) Obstet Gynecol , vol.116 , pp. 884-891
    • Zheng, M.1    Tang, L.2    Huang, L.3    Ding, H.4    Liao, W.T.5    Zeng, M.S.6    Wang, H.Y.7
  • 105
    • 84863804147 scopus 로고    scopus 로고
    • Crystal structure of human ADP-ribose transferase ARTD15/PARP16 reveals a novel putative regulatory domain
    • Karlberg T, Thorsell AG, Kallas A, &, Schuler H, (2012) Crystal structure of human ADP-ribose transferase ARTD15/PARP16 reveals a novel putative regulatory domain. J Biol Chem 287, 24077-24081.
    • (2012) J Biol Chem , vol.287 , pp. 24077-24081
    • Karlberg, T.1    Thorsell, A.G.2    Kallas, A.3    Schuler, H.4
  • 106
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • Ron D, &, Walter P, (2007) Signal integration in the endoplasmic reticulum unfolded protein response. Nat Rev Mol Cell Biol 8, 519-529.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 107
    • 77951177952 scopus 로고    scopus 로고
    • The UPR and cell fate at a glance
    • Merksamer PI, &, Papa FR, (2010) The UPR and cell fate at a glance. J Cell Sci 123, 1003-1006.
    • (2010) J Cell Sci , vol.123 , pp. 1003-1006
    • Merksamer, P.I.1    Papa, F.R.2
  • 108
    • 84869094697 scopus 로고    scopus 로고
    • PARP16 is a tail-anchored endoplasmic reticulum protein required for the PERK- and IRE1α-mediated unfolded protein response
    • Jwa M, &, Chang P, (2012) PARP16 is a tail-anchored endoplasmic reticulum protein required for the PERK- and IRE1α-mediated unfolded protein response. Nat Cell Biol 14, 1223-1230.
    • (2012) Nat Cell Biol , vol.14 , pp. 1223-1230
    • Jwa, M.1    Chang, P.2
  • 109
    • 47949099916 scopus 로고    scopus 로고
    • From endoplasmic-reticulum stress to the inflammatory response
    • Zhang K, &, Kaufman RJ, (2008) From endoplasmic-reticulum stress to the inflammatory response. Nature 454, 455-462.
    • (2008) Nature , vol.454 , pp. 455-462
    • Zhang, K.1    Kaufman, R.J.2
  • 110
    • 80053176398 scopus 로고    scopus 로고
    • Importin β interacts with the endoplasmic reticulum-associated degradation machinery and promotes ubiquitination and degradation of mutant α1-antitrypsin
    • Zhong Y, Wang Y, Yang H, Ballar P, Lee J, Ye Y, Monteiro MJ, &, Fang S, (2011) Importin β interacts with the endoplasmic reticulum-associated degradation machinery and promotes ubiquitination and degradation of mutant α1-antitrypsin. J Biol Chem 286, 33921-33930.
    • (2011) J Biol Chem , vol.286 , pp. 33921-33930
    • Zhong, Y.1    Wang, Y.2    Yang, H.3    Ballar, P.4    Lee, J.5    Ye, Y.6    Monteiro, M.J.7    Fang, S.8


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