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Volumn 57, Issue 10, 2014, Pages 4337-4350

Optimization of small-molecule inhibitors of influenza virus polymerase: From thiophene-3-carboxamide to polyamido scaffolds

Author keywords

[No Author keywords available]

Indexed keywords

2 [[[5 (4 METHOXYPHENYL) 7 (TRIFLUOROMETHYL)PYRAZOLO[1,5 A]PYRIMIDIN 3 YL]CARBONYL]AMINO] 4,5,6,7 TETRAHYDROBENZO[B]THIOPHENE 3 CARBOXAMIDE; 2 [[[5 (4 TOLYL) 7 (DIFLUOROMETHYL)PYRAZOLO[1,5 A]PYRIMIDIN 3 YL]CARBONYL]AMINO] 4,5,6,7 TETRAHYDROBENZO[B]THIOPHENE 3 CARBOXAMIDE; 2 [[[5 PHENYL 7 (DIFLUOROMETHYL)PYRAZOLO[1,5 A]PYRIMIDIN 3 YL]CARBONYL]AMINO] 4,5,6,7 TETRAHYDROBENZO[B]THIOPHENE 3 CARBOXAMIDE; 2 [[[5 PHENYL 7 (TRIFLUOROMETHYL) [1,2,4]TRIAZOLO[1,5 A]PYRIMIDIN 3 YL]CARBONYL]AMINO] 4,5,6,7 TETRAHYDROBENZO[B]THIOPHENE 3 CARBOXAMIDE; 2 [[[5 PHENYL 7 (TRIFLUOROMETHYL)PYRAZOLO[1,5 A]PYRIMIDIN 3 YL]CARBONYL]AMINO] 4,5,6,7 TETRAHYDROBENZO[B]THIOPHENE 3 CARBOXAMIDE; 3 [2 (SEC BUTYLCARBAMOYL)PHENYLCARBAMOYL] 2 METHYL N (2,5 DIMETHYLPHENYL)BENZENESULFONAMIDE; 3 [2 (SEC BUTYLCARBAMOYL)PHENYLCARBAMOYL] N (4 HYDROXYPHENYL)BENZENESULFONAMIDE; 3 [2 (SEC BUTYLCARBAMOYL)PHENYLCARBAMOYL] N PHENYLBENZENESULFONAMIDE; 3 [N (2,5 DIMETHYLPHENYL)SULFAMOYL] 4 METHYL N [2 (PHENYLCARBAMOYL)PHENYL]BENZAMIDE; 5 [2 (SEC BUTYLCARBAMOYL)PHENYLCARBAMOYL] 2 METHYL N [(3 BENZAMIDO) PHENYLBENZENESULFONAMIDE; ANTIVIRUS AGENT; N (3 CARBOMOYL 5,6 DIHYDRO 4H CYCLOPENTA[B]THIOPHEN 2 YL) 5 PHENYL 7 (TRIFLUOROMETHYL)PYRAZOLO[1,5 A]PYRIMIDINE 3 CARBOXAMIDE; N (3 CARBOMOYL 5,6 DIHYDRO 4H CYCLOPENTA[B]THIOPHEN 2 YL) 7 (DIFLUOROMETHYL) 5 PHENYLPYRAZOLO[1,5 A]PYRIMIDINE 3 CARBOXAMIDE; RIBAVIRIN; RNA DIRECTED RNA POLYMERASE INHIBITOR; THIOPHENE 3 CARBOXAMIDE DERIVATIVE; UNCLASSIFIED DRUG;

EID: 84901255328     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm500300r     Document Type: Article
Times cited : (61)

References (62)
  • 1
    • 63649087759 scopus 로고    scopus 로고
    • Seasonal influenza in adults and children - Diagnosis, treatment, chemoprophylaxis, and institutional outbreak management: Clinical practice guidelines of the Infectious Diseases Society of America
    • Harper, S. A.; Bradley, J. S.; Englund, J. A.; File, T. M.; Gravenstein, S.; Hayden, F. G.; McGeer, A. J.; Neuzil, K. M.; Pavia, A. T.; Tapper, M. L.; Uyeki, T. M.; Zimmerman, R. K. Seasonal influenza in adults and children - diagnosis, treatment, chemoprophylaxis, and institutional outbreak management: clinical practice guidelines of the Infectious Diseases Society of America Clin. Infect. Dis. 2009, 48, 1003-1032
    • (2009) Clin. Infect. Dis. , vol.48 , pp. 1003-1032
    • Harper, S.A.1    Bradley, J.S.2    Englund, J.A.3    File, T.M.4    Gravenstein, S.5    Hayden, F.G.6    McGeer, A.J.7    Neuzil, K.M.8    Pavia, A.T.9    Tapper, M.L.10    Uyeki, T.M.11    Zimmerman, R.K.12
  • 2
    • 84864228530 scopus 로고    scopus 로고
    • Antivirals targeting influenza A virus
    • Das, K. Antivirals targeting influenza A virus J. Med. Chem. 2012, 55, 6263-6277
    • (2012) J. Med. Chem. , vol.55 , pp. 6263-6277
    • Das, K.1
  • 4
    • 77953517101 scopus 로고    scopus 로고
    • Targeting pandemic influenza: A primer on influenza antivirals and drug resistance
    • Moss, R. B.; Davey, R. T.; Steigbigel, R. T.; Fang, F. Targeting pandemic influenza: a primer on influenza antivirals and drug resistance J. Antimicrob. Chemother. 2010, 65, 1086-1093
    • (2010) J. Antimicrob. Chemother. , vol.65 , pp. 1086-1093
    • Moss, R.B.1    Davey, R.T.2    Steigbigel, R.T.3    Fang, F.4
  • 5
    • 0020633096 scopus 로고
    • Structure of the catalytic and antigenic sites in influenza virus neuraminidase
    • Colman, P. M.; Varghese, J. N.; Laver, W. G. Structure of the catalytic and antigenic sites in influenza virus neuraminidase Nature 1983, 303, 41-44
    • (1983) Nature , vol.303 , pp. 41-44
    • Colman, P.M.1    Varghese, J.N.2    Laver, W.G.3
  • 8
    • 0021871375 scopus 로고
    • A computational procedure for determining energetically favorable binding sites on biologically important macromolecules
    • Goodford, P. J. A computational procedure for determining energetically favorable binding sites on biologically important macromolecules J. Med. Chem. 1985, 28, 849-857
    • (1985) J. Med. Chem. , vol.28 , pp. 849-857
    • Goodford, P.J.1
  • 9
    • 84876003028 scopus 로고    scopus 로고
    • Influenza virus resistance to neuraminidase inhibitors
    • Samson, M.; Pizzorno, A.; Abed, Y.; Boivin, G. Influenza virus resistance to neuraminidase inhibitors Antiviral Res. 2013, 98, 174-185
    • (2013) Antiviral Res. , vol.98 , pp. 174-185
    • Samson, M.1    Pizzorno, A.2    Abed, Y.3    Boivin, G.4
  • 10
    • 84908642098 scopus 로고    scopus 로고
    • Antiviral strategies against influenza virus: Towards new therapeutic approaches
    • [Online early access]. DOI 10.1007/s00018-014-1615-2.
    • Loregian, A.; Mercorelli, B.; Nannetti, G.; Compagnin, G.; Palù, G. Antiviral strategies against influenza virus: towards new therapeutic approaches. Cell. Mol. Life Sci. 2014, [Online early access]. DOI 10.1007/s00018-014-1615-2.
    • (2014) Cell. Mol. Life Sci.
    • Loregian, A.1    Mercorelli, B.2    Nannetti, G.3    Compagnin, G.4    Palù, G.5
  • 11
    • 80555130981 scopus 로고    scopus 로고
    • A novel function of the N-terminal domain of PA in assembly of influenza A virus RNA polymerase
    • Suzuki, T.; Ainai, A.; Nagata, N.; Sata, T.; Sawa, H.; Hasegawa, H. A novel function of the N-terminal domain of PA in assembly of influenza A virus RNA polymerase Biochem. Biophys. Res. Commun. 2011, 414, 719-726
    • (2011) Biochem. Biophys. Res. Commun. , vol.414 , pp. 719-726
    • Suzuki, T.1    Ainai, A.2    Nagata, N.3    Sata, T.4    Sawa, H.5    Hasegawa, H.6
  • 18
    • 84891492237 scopus 로고    scopus 로고
    • High-throughput docking for the identification of new influenza A virus polymerase inhibitors targeting the PA-PB1 protein-protein interaction
    • Tintori, C.; Laurenzana, I.; Fallacara, A. L.; Kessler, U.; Pilger, B.; Stergiou, L.; Botta, M. High-throughput docking for the identification of new influenza A virus polymerase inhibitors targeting the PA-PB1 protein-protein interaction Bioorg. Med. Chem. Lett. 2014, 24, 280-282
    • (2014) Bioorg. Med. Chem. Lett. , vol.24 , pp. 280-282
    • Tintori, C.1    Laurenzana, I.2    Fallacara, A.L.3    Kessler, U.4    Pilger, B.5    Stergiou, L.6    Botta, M.7
  • 19
    • 34447299235 scopus 로고    scopus 로고
    • Orthomyxoviridae: The viruses and their replication
    • 5 th ed. Knipe, D. M. Howley, P. M. Lippencott Williams and Wilkins: Philadelphia, PA
    • Palese, P.; Shaw, M. L. Orthomyxoviridae: The viruses and their replication. In Fields Virology, 5 th ed.; Knipe, D. M.; Howley, P. M., Eds.; Lippencott Williams and Wilkins: Philadelphia, PA, 2007; Vol. 2, pp 1647-1689.
    • (2007) Fields Virology , vol.2 , pp. 1647-1689
    • Palese, P.1    Shaw, M.L.2
  • 20
    • 0019140033 scopus 로고
    • The large P proteins of influenza A viruses are composed of one acidic and two basic polypeptides
    • Horisberger, M. A. The large P proteins of influenza A viruses are composed of one acidic and two basic polypeptides Virology 1980, 107, 302-305
    • (1980) Virology , vol.107 , pp. 302-305
    • Horisberger, M.A.1
  • 21
    • 47649116956 scopus 로고    scopus 로고
    • Host factors for replication and transcription of the influenza virus genome
    • Nagata, K.; Kawaguchi, A.; Naito, T. Host factors for replication and transcription of the influenza virus genome Rev. Med. Virol. 2008, 18, 247-260
    • (2008) Rev. Med. Virol. , vol.18 , pp. 247-260
    • Nagata, K.1    Kawaguchi, A.2    Naito, T.3
  • 22
    • 84884562233 scopus 로고    scopus 로고
    • Inhibition of herpesvirus and influenza virus replication by blocking polymerase subunit interactions
    • Palù, G.; Loregian, A. Inhibition of herpesvirus and influenza virus replication by blocking polymerase subunit interactions Antiviral Res. 2013, 99, 318-327
    • (2013) Antiviral Res. , vol.99 , pp. 318-327
    • Palù, G.1    Loregian, A.2
  • 25
    • 67649552964 scopus 로고    scopus 로고
    • Structural insight into the essential PB1-PB2 subunit contact of the influenza virus RNA polymerase
    • Sugiyama, K.; Obayashi, E.; Kawaguchi, A.; Suzuki, Y.; Tame, J. R.; Nagata, K.; Park, S. Y. Structural insight into the essential PB1-PB2 subunit contact of the influenza virus RNA polymerase EMBO J. 2009, 28, 1803-1811
    • (2009) EMBO J. , vol.28 , pp. 1803-1811
    • Sugiyama, K.1    Obayashi, E.2    Kawaguchi, A.3    Suzuki, Y.4    Tame, J.R.5    Nagata, K.6    Park, S.Y.7
  • 26
    • 84855838185 scopus 로고    scopus 로고
    • Targeting of the influenza A virus polymerase PB1-PB2 interface indicates strain-specific assembly differences
    • Reuther, P.; Mänz, B.; Brunotte, L.; Schwemmle, M.; Wunderlich, K. Targeting of the influenza A virus polymerase PB1-PB2 interface indicates strain-specific assembly differences J. Virol. 2011, 85, 13298-13309
    • (2011) J. Virol. , vol.85 , pp. 13298-13309
    • Reuther, P.1    Mänz, B.2    Brunotte, L.3    Schwemmle, M.4    Wunderlich, K.5
  • 29
    • 84887918731 scopus 로고    scopus 로고
    • From peptides to small molecules: An intriguing but intricated way to new drugs
    • Scognamiglio, P. L.; Di Natale, C.; Perretta, G.; Marasco, D. From peptides to small molecules: an intriguing but intricated way to new drugs Curr. Med. Chem. 2013, 20, 3803-3817
    • (2013) Curr. Med. Chem. , vol.20 , pp. 3803-3817
    • Scognamiglio, P.L.1    Di Natale, C.2    Perretta, G.3    Marasco, D.4
  • 30
    • 49449097238 scopus 로고    scopus 로고
    • The many roles for fluorine in medicinal chemistry
    • Hagmann, W. K. The many roles for fluorine in medicinal chemistry J. Med. Chem. 2008, 51, 4359-4369
    • (2008) J. Med. Chem. , vol.51 , pp. 4359-4369
    • Hagmann, W.K.1
  • 31
    • 72049096999 scopus 로고    scopus 로고
    • Fluorine in medicinal chemistry: A century of progress and a 60-year retrospective of selected highlights
    • Filler, R.; Saha, R. Fluorine in medicinal chemistry: a century of progress and a 60-year retrospective of selected highlights Future Med. Chem. 2009, 1, 777-791
    • (2009) Future Med. Chem. , vol.1 , pp. 777-791
    • Filler, R.1    Saha, R.2
  • 36
    • 0034926661 scopus 로고    scopus 로고
    • Fluorine substituent effects (on bioactivity)
    • Smart, B. E. Fluorine substituent effects (on bioactivity) J. Fluorine Chem. 2001, 109, 3-11
    • (2001) J. Fluorine Chem. , vol.109 , pp. 3-11
    • Smart, B.E.1
  • 39
    • 0043198517 scopus 로고    scopus 로고
    • Carbonic anhydrase inhibitors: X-ray crystallographic structure of the adduct of human isozyme II with the perfluorobenzoyl analogue of methazolamide. Implications for the drug design of fluorinated inhibitors
    • Abbate, F.; Casini, A.; Scozzafava, A.; Supuran, C. T. Carbonic anhydrase inhibitors: X-ray crystallographic structure of the adduct of human isozyme II with the perfluorobenzoyl analogue of methazolamide. Implications for the drug design of fluorinated inhibitors J. Enzyme Inhib. Med. Chem. 2003, 18, 303-308
    • (2003) J. Enzyme Inhib. Med. Chem. , vol.18 , pp. 303-308
    • Abbate, F.1    Casini, A.2    Scozzafava, A.3    Supuran, C.T.4
  • 40
    • 66149091492 scopus 로고    scopus 로고
    • N -tosyl- S -difluoromethyl- S -phenylsulfoximine: A new difluoromethylation reagent for S-, N-, and C-nucleophiles
    • Zhang, W.; Wang, F.; Hu, J. N -tosyl- S -difluoromethyl- S -phenylsulfoximine: a new difluoromethylation reagent for S-, N-, and C-nucleophiles Org. Lett. 2009, 11, 2109-2112
    • (2009) Org. Lett. , vol.11 , pp. 2109-2112
    • Zhang, W.1    Wang, F.2    Hu, J.3
  • 41
    • 34247263219 scopus 로고    scopus 로고
    • A common reference framework for analyzing/comparing proteins and ligands. Fingerprints for Ligands and Proteins (FLAP): Theory and application
    • Baroni, M.; Cruciani, G.; Sciabola, S.; Perruccio, F.; Mason, J. S. A common reference framework for analyzing/comparing proteins and ligands. Fingerprints for Ligands And Proteins (FLAP): theory and application J. Chem. Inf. Model 2007, 47, 279-294
    • (2007) J. Chem. Inf. Model , vol.47 , pp. 279-294
    • Baroni, M.1    Cruciani, G.2    Sciabola, S.3    Perruccio, F.4    Mason, J.S.5
  • 43
    • 84860875380 scopus 로고
    • Heterocyclen aus CH-aciden Nitrilen, VIII. 2-amino-thiophene aus methylenaktiven nitrilen, carbonylverbindungen und schwefel
    • Gewald, K.; Schinke, E.; Böttcher, H. Heterocyclen aus CH-aciden Nitrilen, VIII. 2-amino-thiophene aus methylenaktiven nitrilen, carbonylverbindungen und schwefel Chem. Ber. 1966, 99, 94-100
    • (1966) Chem. Ber. , vol.99 , pp. 94-100
    • Gewald, K.1    Schinke, E.2    Böttcher, H.3
  • 44
    • 78649449205 scopus 로고    scopus 로고
    • Synthesis and structure-activity relationship of tetrahydropyrazolopyrimidine derivatives-A novel structural class of potent calcium-sensing receptor antagonists
    • Yoshida, M.; Mori, A.; Inaba, A.; Oka, M.; Makino, H.; Yamaguchi, M.; Fujita, H.; Kawamoto, T.; Goto, M.; Kimura, H.; Baba, A.; Yasuma, T. Synthesis and structure-activity relationship of tetrahydropyrazolopyrimidine derivatives-A novel structural class of potent calcium-sensing receptor antagonists Bioorg. Med. Chem. 2010, 18, 8501-8511
    • (2010) Bioorg. Med. Chem. , vol.18 , pp. 8501-8511
    • Yoshida, M.1    Mori, A.2    Inaba, A.3    Oka, M.4    Makino, H.5    Yamaguchi, M.6    Fujita, H.7    Kawamoto, T.8    Goto, M.9    Kimura, H.10    Baba, A.11    Yasuma, T.12
  • 45
    • 2942521736 scopus 로고    scopus 로고
    • Benzamides and benzamidines as specific inhibitors of epidermal growth factor receptor and v-Src protein tyrosine kinases
    • Asano, T.; Yoshikawa, T.; Usui, T.; Yamamoto, H.; Yamamoto, Y.; Uehara, Y.; Nakamura, H. Benzamides and benzamidines as specific inhibitors of epidermal growth factor receptor and v-Src protein tyrosine kinases Bioorg. Med. Chem. 2004, 12, 3529-3542
    • (2004) Bioorg. Med. Chem. , vol.12 , pp. 3529-3542
    • Asano, T.1    Yoshikawa, T.2    Usui, T.3    Yamamoto, H.4    Yamamoto, Y.5    Uehara, Y.6    Nakamura, H.7
  • 46
    • 0344434802 scopus 로고
    • Kinetics of reactions of amines with isatoic anhydride
    • Bunnett, J. F.; Naff, M. B. Kinetics of reactions of amines with isatoic anhydride J. Am. Chem. Soc. 1966, 88, 4001-4008
    • (1966) J. Am. Chem. Soc. , vol.88 , pp. 4001-4008
    • Bunnett, J.F.1    Naff, M.B.2
  • 48
    • 0022998598 scopus 로고
    • The reaction of sulfinic acid salts with hydroxylamine- O -sulfonic acid. A useful synthesis of primary sulfonamides
    • Graham, S. L.; Scholz, T. H. The reaction of sulfinic acid salts with hydroxylamine- O -sulfonic acid. A useful synthesis of primary sulfonamides Synthesis 1986, 12, 1031-1032
    • (1986) Synthesis , vol.12 , pp. 1031-1032
    • Graham, S.L.1    Scholz, T.H.2
  • 49
    • 9944250866 scopus 로고    scopus 로고
    • Increased amounts of the influenza virus nucleoprotein do not promote higher levels of viral genome replication
    • Mullin, A. E.; Dalton, R. M.; Amorim, M. J.; Elton, D.; Digard, P. Increased amounts of the influenza virus nucleoprotein do not promote higher levels of viral genome replication J. Gen. Virol. 2004, 85, 3689-3698
    • (2004) J. Gen. Virol. , vol.85 , pp. 3689-3698
    • Mullin, A.E.1    Dalton, R.M.2    Amorim, M.J.3    Elton, D.4    Digard, P.5
  • 50
    • 0015523596 scopus 로고
    • Broad-spectrum antiviral activity of Virazole: 1-Beta-Dribofuranosyl-1,2, 4-triazole-3-carboxamide
    • Sidwell, R. W.; Huffman, J. H.; Khare, G. P.; Allen, L. B.; Witkowski, J. T.; Robins, R. K. Broad-spectrum antiviral activity of Virazole: 1-Beta-Dribofuranosyl-1,2,4-triazole-3-carboxamide Science 1972, 177, 705-706
    • (1972) Science , vol.177 , pp. 705-706
    • Sidwell, R.W.1    Huffman, J.H.2    Khare, G.P.3    Allen, L.B.4    Witkowski, J.T.5    Robins, R.K.6
  • 51
    • 76249105085 scopus 로고    scopus 로고
    • Molecular basis of the interaction for an essential subunit PA-PB1 in influenza virus RNA polymerase: Insights from molecular dynamics simulation and free energy calculation
    • Liu, H.; Yao, X. Molecular basis of the interaction for an essential subunit PA-PB1 in influenza virus RNA polymerase: Insights from molecular dynamics simulation and free energy calculation Mol. Pharmaceutics 2010, 7, 75-85
    • (2010) Mol. Pharmaceutics , vol.7 , pp. 75-85
    • Liu, H.1    Yao, X.2
  • 52
    • 0037770337 scopus 로고    scopus 로고
    • Inhibition of human cytomegalovirus DNA polymerase by C-terminal peptides from the UL54 subunit
    • Loregian, A.; Rigatti, R.; Murphy, M.; Schievano, E.; Palù, G.; Marsden, H. S. Inhibition of human cytomegalovirus DNA polymerase by C-terminal peptides from the UL54 subunit J. Virol. 2003, 77, 8336-8344
    • (2003) J. Virol. , vol.77 , pp. 8336-8344
    • Loregian, A.1    Rigatti, R.2    Murphy, M.3    Schievano, E.4    Palù, G.5    Marsden, H.S.6
  • 53
    • 32844463538 scopus 로고    scopus 로고
    • Selective anti-cytomegalovirus compounds discovered by screening for inhibitors of subunit interactions of the viral polymerase
    • Loregian, A.; Coen, D. M. Selective anti-cytomegalovirus compounds discovered by screening for inhibitors of subunit interactions of the viral polymerase Chem. Biol. 2006, 13, 191-200
    • (2006) Chem. Biol. , vol.13 , pp. 191-200
    • Loregian, A.1    Coen, D.M.2
  • 54
    • 60849095491 scopus 로고    scopus 로고
    • 1H NMR to facilitate solubility measurement for drug discovery compounds
    • 1H NMR to facilitate solubility measurement for drug discovery compounds Int. J. Pharm. 2009, 369, 47-52
    • (2009) Int. J. Pharm. , vol.369 , pp. 47-52
    • Lin, M.1    Tesconi, M.2    Tischler, M.3
  • 55
    • 0032568397 scopus 로고    scopus 로고
    • Physicochemical high throughput screening: Parallel artificial membrane permeation assay in the description of passive absorption processes
    • Kansy, M.; Senner, F.; Gubernator, K. Physicochemical high throughput screening: parallel artificial membrane permeation assay in the description of passive absorption processes J. Med. Chem. 1998, 41, 1007-1010
    • (1998) J. Med. Chem. , vol.41 , pp. 1007-1010
    • Kansy, M.1    Senner, F.2    Gubernator, K.3
  • 56
    • 84867763360 scopus 로고    scopus 로고
    • GRID-based three-dimensional pharmacophores I: FLAPpharm, a novel approach for pharmacophore elucidation
    • Cross, S.; Baroni, M.; Goracci, L.; Cruciani, G. GRID-based three-dimensional pharmacophores I: FLAPpharm, a novel approach for pharmacophore elucidation J. Chem. Inf. Model. 2012, 52, 2587-2598
    • (2012) J. Chem. Inf. Model. , vol.52 , pp. 2587-2598
    • Cross, S.1    Baroni, M.2    Goracci, L.3    Cruciani, G.4
  • 59
    • 0019412060 scopus 로고
    • Synthesis of bicyclic 1,2,6-thiadiazines
    • Offermann, W.; Eger, K.; Roth, H. J. Synthesis of bicyclic 1,2,6-thiadiazines Arch. Pharm. 1981, 314, 168-175
    • (1981) Arch. Pharm. , vol.314 , pp. 168-175
    • Offermann, W.1    Eger, K.2    Roth, H.J.3
  • 61
    • 0347626042 scopus 로고    scopus 로고
    • Residues of human cytomegalovirus DNA polymerase catalytic subunit UL54 that are necessary and sufficient for interaction with the accessory protein UL44
    • Loregian, A.; Appleton, B. A.; Hogle, J. M.; Coen, D. M. Residues of human cytomegalovirus DNA polymerase catalytic subunit UL54 that are necessary and sufficient for interaction with the accessory protein UL44 J. Virol. 2004, 78, 158-167
    • (2004) J. Virol. , vol.78 , pp. 158-167
    • Loregian, A.1    Appleton, B.A.2    Hogle, J.M.3    Coen, D.M.4
  • 62
    • 3242681272 scopus 로고    scopus 로고
    • Specific residues in the connector loop of the human cytomegalovirus DNA polymerase accessory protein, UL44, are crucial for interaction with the UL54 catalytic subunit
    • Loregian, A.; Appleton, B. A.; Hogle, J. M.; Coen, D. M. Specific residues in the connector loop of the human cytomegalovirus DNA polymerase accessory protein, UL44, are crucial for interaction with the UL54 catalytic subunit J. Virol. 2004, 78, 9084-9092
    • (2004) J. Virol. , vol.78 , pp. 9084-9092
    • Loregian, A.1    Appleton, B.A.2    Hogle, J.M.3    Coen, D.M.4


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