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Volumn 89, Issue 10, 2007, Pages 1221-1227

Inhibition of poly(A) polymerase by aminoglycosides

Author keywords

Aminoglycosides; Divalent metal ions; Inhibition; Polyadenylation

Indexed keywords

AMINOGLYCOSIDE ANTIBIOTIC AGENT; KANAMYCIN; NEOMYCIN; POLYNUCLEOTIDE ADENYLYLTRANSFERASE;

EID: 34848888610     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2007.06.001     Document Type: Article
Times cited : (4)

References (55)
  • 1
    • 0028397716 scopus 로고
    • New pathogens and old resistance genes
    • Davies J. New pathogens and old resistance genes. Microbiologia 10 (1994) 9-12
    • (1994) Microbiologia , vol.10 , pp. 9-12
    • Davies, J.1
  • 2
    • 0030792311 scopus 로고    scopus 로고
    • Bacterial resistance to aminoglycoside antibiotics
    • Davies J., and Wright G.D. Bacterial resistance to aminoglycoside antibiotics. Trends Microbiol. 5 (1997) 234-240
    • (1997) Trends Microbiol. , vol.5 , pp. 234-240
    • Davies, J.1    Wright, G.D.2
  • 5
    • 0034602848 scopus 로고    scopus 로고
    • Modulation of RNA function by aminoglycoside antibiotics
    • Schroeder R., Waldsich C., and Wank H. Modulation of RNA function by aminoglycoside antibiotics. EMBO J. 19 (2000) 1-9
    • (2000) EMBO J. , vol.19 , pp. 1-9
    • Schroeder, R.1    Waldsich, C.2    Wank, H.3
  • 6
    • 0029825658 scopus 로고    scopus 로고
    • Structure of the A site of Escherichia coli 16S ribosomal RNA complexed with an aminoglycoside antibiotic
    • Fourmy D., Recht M.I., Blanchard S.C., and Puglisi J.D. Structure of the A site of Escherichia coli 16S ribosomal RNA complexed with an aminoglycoside antibiotic. Science 274 (1996) 1367-1371
    • (1996) Science , vol.274 , pp. 1367-1371
    • Fourmy, D.1    Recht, M.I.2    Blanchard, S.C.3    Puglisi, J.D.4
  • 7
    • 0023238983 scopus 로고
    • Interaction of antibiotics with functional sites in 16S ribosomal RNA
    • Moazed D., and Noller H.F. Interaction of antibiotics with functional sites in 16S ribosomal RNA. Nature 327 (1987) 389-394
    • (1987) Nature , vol.327 , pp. 389-394
    • Moazed, D.1    Noller, H.F.2
  • 8
    • 0034886697 scopus 로고    scopus 로고
    • Crystal structure of paromomycin docked into the eubacterial ribosomal decoding a site
    • Vicens Q., and Westhof E. Crystal structure of paromomycin docked into the eubacterial ribosomal decoding a site. Structure (Camb.). 9 (2001) 647-658
    • (2001) Structure (Camb.). , vol.9 , pp. 647-658
    • Vicens, Q.1    Westhof, E.2
  • 9
    • 0035986708 scopus 로고    scopus 로고
    • Crystal structure of a complex between the aminoglycoside tobramycin and an oligonucleotide containing the ribosomal decoding a site
    • Vicens Q., and Westhof E. Crystal structure of a complex between the aminoglycoside tobramycin and an oligonucleotide containing the ribosomal decoding a site. Chem. Biol. 9 (2002) 747-755
    • (2002) Chem. Biol. , vol.9 , pp. 747-755
    • Vicens, Q.1    Westhof, E.2
  • 10
    • 0037470560 scopus 로고    scopus 로고
    • Crystal structure of geneticin bound to a bacterial 16S ribosomal RNA A site oligonucleotide
    • Vicens Q., and Westhof E. Crystal structure of geneticin bound to a bacterial 16S ribosomal RNA A site oligonucleotide. J. Mol. Biol. 326 (2003) 1175-1188
    • (2003) J. Mol. Biol. , vol.326 , pp. 1175-1188
    • Vicens, Q.1    Westhof, E.2
  • 11
    • 0025799785 scopus 로고
    • Interaction of antibiotics with A- and P-site-specific bases in 16S ribosomal RNA
    • Woodcock J., Moazed D., Cannon M., Davies J., and Noller H.F. Interaction of antibiotics with A- and P-site-specific bases in 16S ribosomal RNA. EMBO J. 10 (1991) 3099-3103
    • (1991) EMBO J. , vol.10 , pp. 3099-3103
    • Woodcock, J.1    Moazed, D.2    Cannon, M.3    Davies, J.4    Noller, H.F.5
  • 12
    • 0032513007 scopus 로고    scopus 로고
    • Aminoglycoside binding to the hammerhead ribozyme: a general model for the interaction of cationic antibiotics with RNA
    • Hermann T., and Westhof E. Aminoglycoside binding to the hammerhead ribozyme: a general model for the interaction of cationic antibiotics with RNA. J. Mol. Biol. 276 (1998) 903-912
    • (1998) J. Mol. Biol. , vol.276 , pp. 903-912
    • Hermann, T.1    Westhof, E.2
  • 13
    • 0032566484 scopus 로고    scopus 로고
    • Antibiotic inhibition of RNA catalysis: Neomycin B binds to the catalytic core of the td group I intron displacing essential metal ions
    • Hoch I., Berens C., Westhof E., and Schroeder R. Antibiotic inhibition of RNA catalysis: Neomycin B binds to the catalytic core of the td group I intron displacing essential metal ions. J. Mol. Biol. 282 (1998) 557-569
    • (1998) J. Mol. Biol. , vol.282 , pp. 557-569
    • Hoch, I.1    Berens, C.2    Westhof, E.3    Schroeder, R.4
  • 15
    • 0035005249 scopus 로고    scopus 로고
    • Aminoglycoside binding displaces a divalent metal ion in a tRNA-neomycin B complex
    • Mikkelsen N.E., Johansson K., Virtanen A., and Kirsebom L.A. Aminoglycoside binding displaces a divalent metal ion in a tRNA-neomycin B complex. Nat. Struct. Biol. 8 (2001) 510-514
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 510-514
    • Mikkelsen, N.E.1    Johansson, K.2    Virtanen, A.3    Kirsebom, L.A.4
  • 16
    • 0343799864 scopus 로고    scopus 로고
    • Inhibition of the self-cleavage reaction of the human hepatitis delta virus ribozyme by antibiotics
    • Rogers J., Chang A.H., von Ahsen U., Schroeder R., and Davies J. Inhibition of the self-cleavage reaction of the human hepatitis delta virus ribozyme by antibiotics. J. Mol. Biol. 259 (1996) 916-925
    • (1996) J. Mol. Biol. , vol.259 , pp. 916-925
    • Rogers, J.1    Chang, A.H.2    von Ahsen, U.3    Schroeder, R.4    Davies, J.5
  • 17
    • 0037084261 scopus 로고    scopus 로고
    • Binding of tobramycin leads to conformational changes in yeast tRNA(Asp) and inhibition of aminoacylation
    • Walter F., Putz J., Giege R., and Westhof E. Binding of tobramycin leads to conformational changes in yeast tRNA(Asp) and inhibition of aminoacylation. EMBO J. 21 (2002) 760-768
    • (2002) EMBO J. , vol.21 , pp. 760-768
    • Walter, F.1    Putz, J.2    Giege, R.3    Westhof, E.4
  • 19
    • 0034680167 scopus 로고    scopus 로고
    • Molecular mechanisms that confer antibacterial drug resistance
    • Walsh C. Molecular mechanisms that confer antibacterial drug resistance. Nature 406 (2000) 775-781
    • (2000) Nature , vol.406 , pp. 775-781
    • Walsh, C.1
  • 20
    • 0029558564 scopus 로고
    • Gentamicin nephrotoxicity in humans and animals: some recent research
    • Ali B.H. Gentamicin nephrotoxicity in humans and animals: some recent research. Gen. Pharmacol. 26 (1995) 1477-1487
    • (1995) Gen. Pharmacol. , vol.26 , pp. 1477-1487
    • Ali, B.H.1
  • 22
  • 23
    • 0028797645 scopus 로고
    • Phosphoinositide hydrolysis by phospholipase C modulated by multivalent cations La(3+), Al(3+), neomycin, polyamines, and melittin
    • McDonald L.J., and Mamrack M.D. Phosphoinositide hydrolysis by phospholipase C modulated by multivalent cations La(3+), Al(3+), neomycin, polyamines, and melittin. J. Lipid Mediat. Cell Signal 11 (1995) 81-91
    • (1995) J. Lipid Mediat. Cell Signal , vol.11 , pp. 81-91
    • McDonald, L.J.1    Mamrack, M.D.2
  • 24
    • 0029896753 scopus 로고    scopus 로고
    • Phosphatidylinositol phospholipase C is activated allosterically by the aminoglycoside G418. 2-deoxy-2-fluoro-scyllo-inositol-1-O-dodecylphosphonate and its analogs inhibit glycosylphosphatidylinositol phospholipase C
    • Morris J.C., Ping-Sheng L., Zhai H.X., Shen T.Y., and Mensa-Wilmot K. Phosphatidylinositol phospholipase C is activated allosterically by the aminoglycoside G418. 2-deoxy-2-fluoro-scyllo-inositol-1-O-dodecylphosphonate and its analogs inhibit glycosylphosphatidylinositol phospholipase C. J. Biol. Chem. 271 (1996) 15468-15477
    • (1996) J. Biol. Chem. , vol.271 , pp. 15468-15477
    • Morris, J.C.1    Ping-Sheng, L.2    Zhai, H.X.3    Shen, T.Y.4    Mensa-Wilmot, K.5
  • 25
    • 0036847881 scopus 로고    scopus 로고
    • Inhibition of Klenow DNA polymerase and poly(A)-specific ribonuclease by aminoglycosides
    • Ren Y.G., Martinez J., Kirsebom L.A., and Virtanen A. Inhibition of Klenow DNA polymerase and poly(A)-specific ribonuclease by aminoglycosides. RNA 8 (2002) 1393-1400
    • (2002) RNA , vol.8 , pp. 1393-1400
    • Ren, Y.G.1    Martinez, J.2    Kirsebom, L.A.3    Virtanen, A.4
  • 26
    • 0033535566 scopus 로고    scopus 로고
    • Docking of cationic antibiotics to negatively charged pockets in RNA folds
    • Hermann T., and Westhof E. Docking of cationic antibiotics to negatively charged pockets in RNA folds. J. Med. Chem. 42 (1999) 1250-1261
    • (1999) J. Med. Chem. , vol.42 , pp. 1250-1261
    • Hermann, T.1    Westhof, E.2
  • 27
    • 0037093442 scopus 로고    scopus 로고
    • Substrate promiscuity of an aminoglycoside antibiotic resistance enzyme via target mimicry
    • Fong D.H., and Berghuis A.M. Substrate promiscuity of an aminoglycoside antibiotic resistance enzyme via target mimicry. EMBO J. 21 (2002) 2323-2331
    • (2002) EMBO J. , vol.21 , pp. 2323-2331
    • Fong, D.H.1    Berghuis, A.M.2
  • 28
    • 0028865333 scopus 로고
    • Structural investigation of the antibiotic and ATP-binding sites in kanamycin nucleotidyltransferase
    • Pedersen L.C., Benning M.M., and Holden H.M. Structural investigation of the antibiotic and ATP-binding sites in kanamycin nucleotidyltransferase. Biochemistry 34 (1995) 13305-13311
    • (1995) Biochemistry , vol.34 , pp. 13305-13311
    • Pedersen, L.C.1    Benning, M.M.2    Holden, H.M.3
  • 29
    • 0033059981 scopus 로고    scopus 로고
    • Formation of mRNA 3′ ends in eukaryotes: mechanism, regulation, and interrelationships with other steps in mRNA synthesis
    • Zhao J., Hyman L., and Moore C. Formation of mRNA 3′ ends in eukaryotes: mechanism, regulation, and interrelationships with other steps in mRNA synthesis. Microbiol. Mol. Biol. Rev. 63 (1999) 405-445
    • (1999) Microbiol. Mol. Biol. Rev. , vol.63 , pp. 405-445
    • Zhao, J.1    Hyman, L.2    Moore, C.3
  • 30
    • 0029962371 scopus 로고    scopus 로고
    • Mutational analysis of mammalian poly(A) polymerase identifies a region for primer binding and a catalytic domain, homologous to the family X polymerases, and to other nucleotidyltransferases
    • Martin G., and Keller W. Mutational analysis of mammalian poly(A) polymerase identifies a region for primer binding and a catalytic domain, homologous to the family X polymerases, and to other nucleotidyltransferases. EMBO J. 15 (1996) 2593-2603
    • (1996) EMBO J. , vol.15 , pp. 2593-2603
    • Martin, G.1    Keller, W.2
  • 31
    • 0034714329 scopus 로고    scopus 로고
    • Structure of yeast poly(A) polymerase alone and in complex with 3′-dATP
    • Bard J., Zhelkovsky A.M., Helmling S., Earnest T.N., Moore C.L., and Bohm A. Structure of yeast poly(A) polymerase alone and in complex with 3′-dATP. Science 289 (2000) 1346-1349
    • (2000) Science , vol.289 , pp. 1346-1349
    • Bard, J.1    Zhelkovsky, A.M.2    Helmling, S.3    Earnest, T.N.4    Moore, C.L.5    Bohm, A.6
  • 32
    • 0034664049 scopus 로고    scopus 로고
    • Crystal structure of mammalian poly(A) polymerase in complex with an analog of ATP
    • Martin G., Keller W., and Doublie S. Crystal structure of mammalian poly(A) polymerase in complex with an analog of ATP. EMBO J. 19 (2000) 4193-4203
    • (2000) EMBO J. , vol.19 , pp. 4193-4203
    • Martin, G.1    Keller, W.2    Doublie, S.3
  • 33
    • 0033119535 scopus 로고    scopus 로고
    • DNA polymerase beta-like nucleotidyltransferase superfamily: identification of three new families, classification and evolutionary history
    • Aravind L., and Koonin E.V. DNA polymerase beta-like nucleotidyltransferase superfamily: identification of three new families, classification and evolutionary history. Nucleic Acids Res. 27 (1999) 1609-1618
    • (1999) Nucleic Acids Res. , vol.27 , pp. 1609-1618
    • Aravind, L.1    Koonin, E.V.2
  • 34
    • 0029360327 scopus 로고
    • DNA polymerase β belongs to an ancient nucleotidyltransferase superfamily
    • Holm L., and Sander C. DNA polymerase β belongs to an ancient nucleotidyltransferase superfamily. Trends Biochem. Sci. 20 (1995) 345-347
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 345-347
    • Holm, L.1    Sander, C.2
  • 35
    • 0035823480 scopus 로고    scopus 로고
    • A novel nuclear human poly(A) polymerase (PAP), PAP gamma
    • Kyriakopoulou C.B., Nordvarg H., and Virtanen A. A novel nuclear human poly(A) polymerase (PAP), PAP gamma. J. Biol. Chem. 276 (2001) 33504-33511
    • (2001) J. Biol. Chem. , vol.276 , pp. 33504-33511
    • Kyriakopoulou, C.B.1    Nordvarg, H.2    Virtanen, A.3
  • 36
    • 0025987814 scopus 로고
    • Isolation and expression of cDNA clones encoding mammalian poly(A) polymerase
    • Wahle E., Martin G., Schiltz E., and Keller W. Isolation and expression of cDNA clones encoding mammalian poly(A) polymerase. EMBO J. 10 (1991) 4251-4257
    • (1991) EMBO J. , vol.10 , pp. 4251-4257
    • Wahle, E.1    Martin, G.2    Schiltz, E.3    Keller, W.4
  • 37
    • 0016721973 scopus 로고
    • Purification of terminal riboadenylate transferase from calf thymus gland
    • Tsiapalis C.M., Dorson J.W., and Bollum F.J. Purification of terminal riboadenylate transferase from calf thymus gland. J. Biol. Chem. 250 (1975) 4486-4496
    • (1975) J. Biol. Chem. , vol.250 , pp. 4486-4496
    • Tsiapalis, C.M.1    Dorson, J.W.2    Bollum, F.J.3
  • 38
    • 0035931347 scopus 로고    scopus 로고
    • Which aminoglycoside ring is most important for binding? A hydropathic analysis of gentamicin, paromomycin, and analogues
    • Cashman D.J., Rife J.P., and Kellogg G.E. Which aminoglycoside ring is most important for binding? A hydropathic analysis of gentamicin, paromomycin, and analogues. Bioorg. Med. Chem. Lett. 11 (2001) 119-122
    • (2001) Bioorg. Med. Chem. Lett. , vol.11 , pp. 119-122
    • Cashman, D.J.1    Rife, J.P.2    Kellogg, G.E.3
  • 39
    • 0037138652 scopus 로고    scopus 로고
    • Binding of aminoglycoside antibiotics to the small ribosomal subunit: a continuum electrostatics investigation
    • Ma C., Baker N.A., Joseph S., and McCammon J.A. Binding of aminoglycoside antibiotics to the small ribosomal subunit: a continuum electrostatics investigation. J. Am. Chem. Soc. 124 (2002) 1438-1442
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 1438-1442
    • Ma, C.1    Baker, N.A.2    Joseph, S.3    McCammon, J.A.4
  • 40
    • 27244458194 scopus 로고    scopus 로고
    • Crystal structures of complexes between aminoglycosides and decoding A site oligonucleotides: role of the number of rings and positive charges in the specific binding leading to miscoding
    • Francois B., Russell R.J., Murray J.B., Aboul-ela F., Masquida B., Vicens Q., and Westhof E. Crystal structures of complexes between aminoglycosides and decoding A site oligonucleotides: role of the number of rings and positive charges in the specific binding leading to miscoding. Nucleic Acids Res. 33 (2005) 5677-5690
    • (2005) Nucleic Acids Res. , vol.33 , pp. 5677-5690
    • Francois, B.1    Russell, R.J.2    Murray, J.B.3    Aboul-ela, F.4    Masquida, B.5    Vicens, Q.6    Westhof, E.7
  • 41
    • 0029258393 scopus 로고
    • Inhibition of the hammerhead ribozyme by neomycin
    • Stage T.K., Hertel K.J., and Uhlenbeck O.C. Inhibition of the hammerhead ribozyme by neomycin. RNA 1 (1995) 95-101
    • (1995) RNA , vol.1 , pp. 95-101
    • Stage, T.K.1    Hertel, K.J.2    Uhlenbeck, O.C.3
  • 42
    • 0032212026 scopus 로고    scopus 로고
    • Deciphering RNA recognition: aminoglycoside binding to the hammerhead ribozyme
    • Tor Y., Hermann T., and Westhof E. Deciphering RNA recognition: aminoglycoside binding to the hammerhead ribozyme. Chem. Biol. 5 (1998) R277-R283
    • (1998) Chem. Biol. , vol.5
    • Tor, Y.1    Hermann, T.2    Westhof, E.3
  • 43
    • 0030930212 scopus 로고    scopus 로고
    • Electrostatic interactions in RNA aminoglycosides binding
    • Wang H., and Tor Y. Electrostatic interactions in RNA aminoglycosides binding. J. Am. Chem. Soc. 119 (1997) 8734-8735
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 8734-8735
    • Wang, H.1    Tor, Y.2
  • 44
    • 0030087981 scopus 로고    scopus 로고
    • A non-canonical base pair within the human immunodeficiency virus rev- responsive element is involved in both rev and small molecule recognition
    • Werstuck G., Zapp M.L., and Green M.R. A non-canonical base pair within the human immunodeficiency virus rev- responsive element is involved in both rev and small molecule recognition. Chem. Biol. 3 (1996) 129-137
    • (1996) Chem. Biol. , vol.3 , pp. 129-137
    • Werstuck, G.1    Zapp, M.L.2    Green, M.R.3
  • 45
    • 0026447727 scopus 로고
    • Non-competitive inhibition of group I intron RNA self-splicing by aminoglycoside antibiotics
    • von Ahsen U., Davies J., and Schroeder R. Non-competitive inhibition of group I intron RNA self-splicing by aminoglycoside antibiotics. J. Mol. Biol. 226 (1992) 935-941
    • (1992) J. Mol. Biol. , vol.226 , pp. 935-941
    • von Ahsen, U.1    Davies, J.2    Schroeder, R.3
  • 46
    • 0027370433 scopus 로고
    • Small molecules that selectively block RNA binding of HIV-1 Rev protein inhibit Rev function and viral production
    • Zapp M.L., Stern S., and Green M.R. Small molecules that selectively block RNA binding of HIV-1 Rev protein inhibit Rev function and viral production. Cell 74 (1993) 969-978
    • (1993) Cell , vol.74 , pp. 969-978
    • Zapp, M.L.1    Stern, S.2    Green, M.R.3
  • 47
    • 0020708497 scopus 로고
    • Nitrogen-15 nuclear magnetic resonance spectroscopy of neomycin B and related aminoglycosides
    • Botto R.E., and Coxon B. Nitrogen-15 nuclear magnetic resonance spectroscopy of neomycin B and related aminoglycosides. J. Am. Chem. Soc. 105 (1983) 1021-1028
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 1021-1028
    • Botto, R.E.1    Coxon, B.2
  • 48
    • 0027906281 scopus 로고
    • Microscopic protonation constants in tobramycin. An NMR and pH study with the aid of partially N-acetylated derivatives
    • Szilagyi L., Pusztahelyi Z.S., Jakab S., and Kovacs I. Microscopic protonation constants in tobramycin. An NMR and pH study with the aid of partially N-acetylated derivatives. Carbohydr. Res. 247 (1993) 99-109
    • (1993) Carbohydr. Res. , vol.247 , pp. 99-109
    • Szilagyi, L.1    Pusztahelyi, Z.S.2    Jakab, S.3    Kovacs, I.4
  • 50
    • 34247397853 scopus 로고    scopus 로고
    • Molecular determinants of antibiotic recognition and resistance by aminoglycoside phosphotransferase (3′)-IIIa: a calorimetric and mutational analysis
    • Kaul M., Barbieri C.M., Srinivasan A.R., and Pilch D.S. Molecular determinants of antibiotic recognition and resistance by aminoglycoside phosphotransferase (3′)-IIIa: a calorimetric and mutational analysis. J. Mol. Biol. 369 (2007) 142-156
    • (2007) J. Mol. Biol. , vol.369 , pp. 142-156
    • Kaul, M.1    Barbieri, C.M.2    Srinivasan, A.R.3    Pilch, D.S.4
  • 51
    • 0029857320 scopus 로고    scopus 로고
    • Cell-cycle related regulation of poly(A) polymerase by phosphorylation
    • Colgan D.F., Murthy K.G.K., Prives C., and Manley J.L. Cell-cycle related regulation of poly(A) polymerase by phosphorylation. Nature 384 (1996) 282-285
    • (1996) Nature , vol.384 , pp. 282-285
    • Colgan, D.F.1    Murthy, K.G.K.2    Prives, C.3    Manley, J.L.4
  • 52
    • 0023256533 scopus 로고
    • Increase in the levels of activity of polyadenylic acid-metabolizing enzymes following phytohaemagglutinin stimulation of human lymphocytes
    • Courtis N.C., Trangas T.T., and Tsiapalis C.M. Increase in the levels of activity of polyadenylic acid-metabolizing enzymes following phytohaemagglutinin stimulation of human lymphocytes. Mol. Cell. Biochem. 75 (1987) 33-42
    • (1987) Mol. Cell. Biochem. , vol.75 , pp. 33-42
    • Courtis, N.C.1    Trangas, T.T.2    Tsiapalis, C.M.3
  • 53
    • 0024402589 scopus 로고
    • Polyadenylate polymerases from normal and cancer cells and their potential role in messenger RNA processing: a review
    • Jacob S.T., Terns M.P., and Maguire K.A. Polyadenylate polymerases from normal and cancer cells and their potential role in messenger RNA processing: a review. Cancer Res. 49 (1989) 2827-2833
    • (1989) Cancer Res. , vol.49 , pp. 2827-2833
    • Jacob, S.T.1    Terns, M.P.2    Maguire, K.A.3
  • 54
    • 0034935020 scopus 로고    scopus 로고
    • Identification and functional characterization of neo-poly(A) polymerase, an RNA processing enzyme overexpressed in human tumors
    • Topalian S.L., Kaneko S., Gonzales M.I., Bond G.L., Ward Y., and Manley J.L. Identification and functional characterization of neo-poly(A) polymerase, an RNA processing enzyme overexpressed in human tumors. Mol. Cell Biol. 21 (2001) 5614-5623
    • (2001) Mol. Cell Biol. , vol.21 , pp. 5614-5623
    • Topalian, S.L.1    Kaneko, S.2    Gonzales, M.I.3    Bond, G.L.4    Ward, Y.5    Manley, J.L.6
  • 55
    • 0034306990 scopus 로고    scopus 로고
    • Polyadenylate polymerase enzymatic activity in mammary tumor cytosols: a new independent prognostic marker in primary breast cancer
    • Scorilas A., Talieri M., Ardavanis A., Courtis N., Dimitriadis E., Yotis J., Tsiapalis C.M., and Trangas T. Polyadenylate polymerase enzymatic activity in mammary tumor cytosols: a new independent prognostic marker in primary breast cancer. Cancer Res. 60 (2000) 5427-5433
    • (2000) Cancer Res. , vol.60 , pp. 5427-5433
    • Scorilas, A.1    Talieri, M.2    Ardavanis, A.3    Courtis, N.4    Dimitriadis, E.5    Yotis, J.6    Tsiapalis, C.M.7    Trangas, T.8


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