Zanamivir: an influenza virus neuraminidase inhibitor

References

• Reid AH, Fanning TG, Hultin JV, Taubenberger JK. Origin and evolution of the 1918 ‘Spanish’ influenza virus hemagglutinin gene. Proc. Natl Acad. Sci. USA 96, 1651–1656 (1999).
   PubMed Web of Science ®Google Scholar
• Gamblin SJ, Haire LF, Russell RJ et al. The structure and receptor binding properties of the 1918 influenza hemagglutinin. Science 303, 1838–1842 (2004).
   PubMed Web of Science ®Google Scholar
• Kobasa D, Takada A, Shinya K et al. Enhanced virulence of influenza A viruses with the hemagglutinin of the 1918 pandemic virus. Nature 431, 703–707 (2004).
   PubMed Web of Science ®Google Scholar
• Peiris JS, Guan Y, Yuen KY. Severe acute respiratory syndrome. Nature Med. 10, S88–S97 (2004).
   PubMed Web of Science ®Google Scholar
• Abbott A, Pearson H. Fear of human pandemic grows as bird flu sweeps through Asia. Nature 427, 472–473 (2004).
   PubMed Web of Science ®Google Scholar
• Kuiken T, Rimmelzwaan G, van Riel D et al. Avian H5N1 influenza in cats. Science 306, 241 (2004).
   PubMed Web of Science ®Google Scholar
• Oxford JS, Mann A, Lambkin R. A designer drug against influenza: the NA inhibitor oseltamivir (Tamiflu®). Expert Rev. Anti Infect. Ther. 1(2), 337–342 (2003).
   PubMedGoogle Scholar
• Colman PM. Influenza virus neuraminidase: structure, antibodies, and inhibitors. Protein Sci. 3, 1687–1696 (1994).
   PubMed Web of Science ®Google Scholar
• Colman PM, Varghese JN, Laver WG. Structure of the catalytic and antigenic sites in influenza virus neuraminidase. Nature 303, 41–44 (1983).
   PubMed Web of Science ®Google Scholar
• Tulip WR, Varghese JN, Baker AT et al. Refined atomic structures of N9 subtype influenza virus neuraminidase and escape mutants. J. Mol. Biol. 221, 487–497 (1991).
   PubMed Web of Science ®Google Scholar
• Varghese JN, McKimm-Breschkin JL, Caldwell JB, Kortt AA, Colman PM. The structure of the complex between influenza virus neuraminidase and sialic acid, the viral receptor. Proteins 14, 327–332 (1992).
   PubMed Web of Science ®Google Scholar
• Meindl P, Tuppy H. 2-deoxy-2,3-dehydrosialic acids. II. Competitive inhibition of Vibrio cholerae neuraminidase by 2-deoxy-2,3-dehydro-N-acylneuraminic acids. Hoppe Seylers Z. Physiol. Chem. 350, 1088–1092 (1969).
   PubMedGoogle Scholar
• von Itzstein M, Wu WY, Kok GB et al. Rational design of potent sialidase-based inhibitors of influenza virus replication. Nature 363, 418–423 (1993).
   PubMed Web of Science ®Google Scholar
• Varghese JN, Epa VC, Colman PM. Three-dimensional structure of the complex of 4-guanidino-Neu5Ac2en and influenza virus neuraminidase. Protein Sci. 4, 1081–1087 (1995).
   PubMed Web of Science ®Google Scholar
• Kim CU, Lew W, Williams MA et al. Influenza neuraminidase inhibitors possessing a novel hydrophobic interaction in the enzyme active site: design, synthesis, and structural analysis of carbocyclic sialic acid analogs with potent anti-influenza activity. J. Am. Chem. Soc. 119, 681–690 (1997).
   PubMed Web of Science ®Google Scholar
• Woods JM, Bethell RC, Coates JA et al. 4 guanidino-2,4-dideoxy-2,3-dehydro-N-acetylneuraminic acid is a highly effective inhibitor both of the sialidase (neuraminidase) and of growth of a wide range of influenza A and B viruses in vitro. Antimicrob. Agents Chemother. 37, 1473–1479 (1993).
   PubMed Web of Science ®Google Scholar
• Smith PW, Sollis SL, Howes PD et al. Dihydropyrancarboxamides related to zanamivir: a new series of inhibitors of influenza virus sialidases. 1. Discovery, synthesis, biological activity, and structure-activity relationships of 4-guanidino- and 4-amino-4H-pyran-6-carboxamides. J. Med. Chem. 41, 787–797 (1998).
   PubMed Web of Science ®Google Scholar
• Taylor NR, Cleasby A, Singh O et al. Dihydropyrancarboxamides related to zanamivir: a new series of inhibitors of influenza virus sialidases. 2. Crystallographic and molecular modeling study of complexes of 4-amino-4H-pyran-6-carboxamides and sialidase from influenza virus types A and B. J. Med. Chem. 41, 798–807 (1998).
   PubMed Web of Science ®Google Scholar
• Hurt AC, Barr IG, Komadina N, Hampson AW. A novel means of identifying the neuraminidase type of currently circulating human A(H1) influenza viruses. Virus Res. 103, 79–83 (2004).
   PubMedGoogle Scholar
• Mungall BA, Xu X, Klimov A. Surveillance of influenza isolates for susceptibility to neuraminidase inhibitors during the 2000–2002 influenza seasons. Virus Res. 103, 195–197 (2004).
   PubMedGoogle Scholar
• Tumpey TM, Garcia-Sastre A, Mikulasova A et al. Existing antivirals are effective against influenza viruses with genes from the 1918 pandemic virus. Proc. Natl Acad. Sci. USA 99, 13849–13854 (2002).
   PubMed Web of Science ®Google Scholar
• Palese P, Compans RW. Inhibition of influenza virus replication in tissue culture by 2-deoxy-2,3-dehydro-N-trifluoroacetylneuraminic acid (FANA): mechanism of action. J. Gen. Virol. 33, 159–163 (1976).
   PubMedGoogle Scholar
• Burnet FM. Mucins and mucoids in relation to influenza virus action. IV. Inhibition by purified mucoid of infection and hemagglutinin with the virus strain WSE. Aust. J. Exp. Biol. Med. Sci. 26, 381–387 (1948).
   PubMedGoogle Scholar
• Burnet FM, McCrea JF, Anderson SG. Mucin as a substrate of enzyme action by viruses of the mumps influenza group. Nature (London) 160, 404–405 (1947).
   PubMedGoogle Scholar
• Colman PM. In: The Influenza Viruses. Krug RM (Ed.). Plenum Press, NY, USA, 175–218 (1989).
   Google Scholar
• Matrosovich MN, Matrosovich TY, Gray T, Roberts NA, Klenk HD. Neuraminidase is important for the initiation of influenza virus infection in human airway epithelium. J. Virol. 78, 12665–12667 (2004).
   PubMed Web of Science ®Google Scholar
• McCullers JA, Bartmess KC. Role of neuraminidase in lethal synergism between influenza virus and Streptococcus pneumoniae. J. Infect. Dis. 187, 1000–1009 (2003).
   PubMed Web of Science ®Google Scholar
• Lawrence MC, Borg NA, Streltsov VA et al. Structure of the hemagglutinin-neuraminidase from human parainfluenza virus Type III. J. Mol. Biol. 335, 1343–1357 (2004).
   PubMedGoogle Scholar
• Chavas LM, Tringali C, Fusi P et al. Crystal structure of the human cytosolic sialidase Neu2: evidence for the dynamic nature of substrate recognition. J. Biol. Chem. 280, 469–475 (2004).
   PubMedGoogle Scholar
• Cheer SM, Wagstaff AJ. Zanamivir: an update of its use in influenza. Drugs 62, 71–106 (2002).
   PubMed Web of Science ®Google Scholar
• Dunn CJ, Goa KL. Zanamivir: a review of its use in influenza. Drugs 58, 761–784 (1999).
   PubMed Web of Science ®Google Scholar
• Hayden FG, Rollins BS, Madren LK. Anti-influenza virus activity of the neuraminidase inhibitor 4-guanidino-Neu5Ac2en in cell culture and in human respiratory epithelium. Antiviral Res. 25, 123–131 (1994).
   PubMed Web of Science ®Google Scholar
• Ryan DM, Ticehurst J, Dempsey MH. GG167 (4-guanidino-2,4-dideoxy-2,3-dehydro-N-acetylneuraminic acid) is a potent inhibitor of influenza virus in ferrets. Antimicrob. Agents Chemother. 39, 2583–2584 (1995).
   PubMed Web of Science ®Google Scholar
• Hayden FG, Treanor JJ, Betts RF, Lobo M, Esinhart JD, Hussey EK. Safety and efficacy of the neuraminidase inhibitor GG167 in experimental human influenza. J. Am. Med. Assoc. 275, 295–299 (1996).
   PubMed Web of Science ®Google Scholar
• Hayden F, Lobo M, Hussey EK, Eason CU. In: Options for the Control of Influenza III. Brown LE, Hampson AW, Webster RG (Eds). Elsevier, Amsterdam, 718–725 (1996).
   Google Scholar
• Cass LM, Efthymiopoulos C, Bye A. Pharmacokinetics of zanamivir after intravenous, oral, inhaled or intranasal administration to healthy volunteers. Clin. Pharmacokinet. 36(Suppl. 1), 1–11 (1999).
   PubMed Web of Science ®Google Scholar
• Peng AW, Hussey EK, Moore KH. A population pharmacokinetic analysis of zanamivir in subjects with experimental and naturally occurring influenza: effects of formulation and route of administration. J. Clin. Pharmacol. 40, 242–249 (2000).
   PubMed Web of Science ®Google Scholar
• Cass LM, Brown J, Pickford M et al. Pharmacoscintigraphic evaluation of lung deposition of inhaled zanamivir in healthy volunteers. Clin. Pharmacokinet. 36(Suppl. 1), 21–31 (1999).
   PubMed Web of Science ®Google Scholar
• Peng AW, Milleri S, Stein DS. Direct measurement of the anti-influenza agent zanamivir in the respiratory tract following inhalation. Antimicrob. Agents Chemother. 44, 1974–1976 (2000).
   PubMed Web of Science ®Google Scholar
• Makela MJ, Pauksens K, Rostila T et al. Clinical efficacy and safety of the orally inhaled neuraminidase inhibitor zanamivir in the treatment of influenza: a randomized, double-blind, placebo-controlled European study. J. Infect. 40, 42–48 (2000).
   PubMed Web of Science ®Google Scholar
• Fleming DM. Zanamivir in the treatment of influenza. Expert Opin. Pharmacother. 4(5), 799–805 (2003).
   PubMed Web of Science ®Google Scholar
• Hayden FG, Osterhaus AD, Treanor JJ et al. Efficacy and safety of the neuraminidase inhibitor zanamivir in the treatment of influenzavirus infections. GG167 Influenza Study Group. N. Engl. J. Med. 337, 874–880 (1997).
   PubMed Web of Science ®Google Scholar
• Boivin G, Goyette N, Hardy I, Aoki F, Wagner A, Trottier S. Rapid antiviral effect of inhaled zanamivir in the treatment of naturally occurring influenza in otherwise healthy adults. J. Infect. Dis. 181, 1471–1474 (2000).
   PubMed Web of Science ®Google Scholar
• Monto AS, Fleming DM, Henry D et al. Efficacy and safety of the neuraminidase inhibitor zanamivirin the treatment of influenza A and B virus infections. J. Infect. Dis. 180, 254–261 (1999).
   PubMed Web of Science ®Google Scholar
• Matsumoto K, Ogawa N, Nerome K et al. Safety and efficacy of the neuraminidase inhibitor zanamivir in treating influenza virus infection in adults: results from Japan. GG167 Group. Antiviral Ther. 4, 61–68 (1999).
   PubMed Web of Science ®Google Scholar
• Lalezari J, Klein T, Stapleton J et al. The efficacy and safety of inhaled zanamivir in the treatment of influenza in otherwise healthy and high-risk individuals in North America. J. Antimicrob. Chemother. 44(Suppl. A), 42 (1999).
   Google Scholar
• The MIST study group. Randomized trial of efficacy and safety of inhaled zanamivir in treatment of influenza A and B virus infections. The MIST (Management of Influenza in the Southern Hemisphere Trialists) Study Group. Lancet 352, 1877–1881 (1998).
   PubMedGoogle Scholar
• Osterhaus A, Hedrick J, Henrickson K et al. Clinical efficacy of inhaled zanamivir for the treatment of patients with influenza B virus infection: a pooled analysis of randomized, placebo-controlled studies. Clin. Drug Invest. 20, 223–228 (2000).
   Google Scholar
• Murphy KR, Eivindson A, Pauksens K et al. Efficacy and safety of inhaled zanamivir for the treatment of influenza in patients with asthma or chronic obstructive pulmonary disease: a double-blind, randomized, placebo-controlled, multicenter study. Clin. Drug Invest. 20, 337–349 (2000).
   Web of Science ®Google Scholar
• Hedrick JA, Barzilai A, Behre U et al. Zanamivir for treatment of symptomatic influenza A and B infection in children five to twelve years of age: a randomized controlled trial. Pediatr. Infect. Dis. J. 19, 410–417 (2000).
   PubMed Web of Science ®Google Scholar
• Cooper NJ, Sutton AJ, Abrams KR, Wailoo A, Turner D, Nicholson KG. Effectiveness of neuraminidase inhibitors in treatment and prevention of influenza A and B: systematic review and meta-analyses of randomized controlled trials. Br. Med. J. 326, 1235 (2003).
   PubMed Web of Science ®Google Scholar
• Wutzler P, Kossow KD, Lode H et al. Antiviral treatment and prophylaxis of influenza in primary care: German recommendations. J. Clin. Virol. 31, 84–91 (2004).
   PubMedGoogle Scholar
• Schilling M, Povinelli L, Krause P et al. Efficacy of zanamivir for chemoprophylaxis of nursing home influenza outbreaks. Vaccine 16, 1771–1774 (1998).
   PubMedGoogle Scholar
• Monto AS, Robinson DP, Herlocher ML, Hinson JM Jr, Elliott MJ, Crisp A. Zanamivir in the prevention of influenza among healthy adults: a randomized controlled trial. J. Am. Med. Assoc. 282, 31–35 (1999).
   PubMedGoogle Scholar
• Hayden FG, Gubareva LV, Monto AS et al. Inhaled zanamivir for the prevention of influenza in families. Zanamivir Family Study Group. N. Engl. J. Med. 343, 1282–1289 (2000).
   PubMed Web of Science ®Google Scholar
• Monto AS, Pichichero ME, Blanckenberg SJ et al. Zanamivir prophylaxis: an effective strategy for the prevention of influenza types A and B within households. J. Infect. Dis. 186, 1582–1588 (2002).
   PubMed Web of Science ®Google Scholar
• Hayden FG, Belshe RB, Clover RD, Hay AJ, Oakes MG, Soo W. Emergence and apparent transmission of rimantadine-resistant influenza A virus in families. N. Engl. J. Med. 321, 1696–1702 (1989).
   PubMed Web of Science ®Google Scholar
• Hayden FG, Hay AJ. Emergence and transmission of influenza A viruses resistant to amantadine and rimantadine. Curr. Topics Microbiol. Immunol. 176, 119–130 (1992).
   PubMed Web of Science ®Google Scholar
• Langley JM, Faughnan ME. Prevention of influenza in the general population. Can. Med. Assoc. J. 171, 1213–1222 (2004).
   PubMed Web of Science ®Google Scholar
• Langley JM, Faughnan ME. Prevention of influenza in the general population: recommendation statement from the Canadian Task Force on Preventive Healthcare. Can. Med. Assoc. J. 171, 1169–1170 (2004).
   Google Scholar
• Balicer RD, Huerta M, Grotto I. Tackling the next influenza pandemic. Br. Med. J. 328, 1391–1392 (2004).
   PubMed Web of Science ®Google Scholar
• Longini IM Jr, Halloran ME, Nizam A, Yang Y. Containing pandemic influenza with antiviral agents. Am. J. Epidemiol. 159, 623–633 (2004).
   PubMed Web of Science ®Google Scholar
• Freund B, Gravenstein S, Elliott M, Miller I. Zanamivir: a review of clinical safety. Drug Saf. 21, 267–281 (1999).
   PubMed Web of Science ®Google Scholar
• Gravenstein S, Johnston SL, Loeschel E, Webster A. Zanamivir: a review of clinical safety in individuals at high risk of developing influenza-related complications. Drug Saf. 24, 1113–1125 (2001).
   PubMed Web of Science ®Google Scholar
• Blick TJ, Tiong T, Sahasrabudhe A et al. Generation and characterization of an influenza virus neuraminidase variant with decreased sensitivity to the neuraminidase-specific inhibitor 4 guanidino-Neu5Ac2en. Virology 214, 475–484 (1995).
   PubMed Web of Science ®Google Scholar
• Staschke KA, Colacino JM, Baxter AJ et al. Molecular basis for the resistance of influenza viruses to 4-guanidino-Neu5Ac2en. Virology 214, 642–646 (1995).
   PubMed Web of Science ®Google Scholar
• McKimm-Breschkin JL, Blick TJ, Sahasrabudhe A et al. Generation and characterization of variants of NWS/G70C influenza virus after in vitro passage in 4 amino-Neu5Ac2en and 4-guanidino-Neu5Ac2en. Antimicrob. Agents Chemother. 40, 40–46 (1996).
   PubMed Web of Science ®Google Scholar
• Gubareva LV, Bethell R, Hart GJ, Murti KG, Penn CR, Webster RG. Characterization of mutants of influenza A virus selected with the neuraminidase inhibitor 4-guanidino-Neu5Ac2en. J. Virol. 70, 1818–1827 (1996).
   PubMed Web of Science ®Google Scholar
• Gubareva LV, Robinson MJ, Bethell RC, Webster RG. Catalytic and framework mutations in the neuraminidase active site of influenza viruses that are resistant to 4 guanidino-Neu5Ac2en. J. Virol. 71, 3385–3390 (1997).
   PubMed Web of Science ®Google Scholar
• Goto H, Bethell RC, Kawaoka Y. Mutations affecting the sensitivity of the influenza virus neuraminidase to 4-guanidino-2,4-dideoxy-2,3-dehydro-N-acetylneuraminic acid. Virology 238, 265–272 (1997).
   PubMed Web of Science ®Google Scholar
• McKimm-Breschkin JL, Sahasrabudhe A, Blick TJ et al. Mutations in a conserved residue in the influenza virus neuraminidase active site decreases sensitivity to Neu5Ac2en-derived inhibitors. J. Virol. 72, 2456–2462 (1998).
   PubMedGoogle Scholar
• Tai CY, Escarpe PA, Sidwell RW et al. Characterization of human influenza virus variants selected in vitro in the presence of the neuraminidase inhibitor GS 4071. Antimicrob. Agents Chemother. 42, 3234–3241 (1998).
   PubMed Web of Science ®Google Scholar
• Varghese JN, Smith PW, Sollis SL et al. Drug design against a shifting target: a structural basis for resistance to inhibitors in a variant of influenza virus neuraminidase. Structure 6, 735–746 (1998).
   PubMed Web of Science ®Google Scholar
• Kiso M, Mitamura K, Sakai-Tagawa Y et al. Resistant influenza A viruses in children treated with oseltamivir: descriptive study. Lancet 364, 759–765 (2004).
   PubMed Web of Science ®Google Scholar
• Gubareva LV. Molecular mechanisms of influenza virus resistance to neuraminidase inhibitors. Virus Res. 103, 199–203 (2004).
   PubMed Web of Science ®Google Scholar
• McKimm-Breschkin JL, McDonald M, Blick TJ, Colman PM. Mutation in the influenza virus neuraminidase gene resulting in decreased sensitivity to the neuraminidase inhibitor 4-guanidino-Neu5Ac2en leads to instability of the enzyme. Virology 225, 240–242 (1996).
   PubMed Web of Science ®Google Scholar
• McKimm-Breschkin JL. Resistance of influenza viruses to neuraminidase inhibitors – a review. Antiviral Res. 47, 1–17 (2000).
   PubMed Web of Science ®Google Scholar
• Abed Y, Goyette N, Boivin G. A reverse-genetics study of resistance to neuraminidase inhibitors in an influenza A/H1N1 virus. Antiviral Ther. 9, 577–581 (2004).
   PubMedGoogle Scholar
• Barnett JM, Cadman A, Gor D et al. Zanamivir susceptibility monitoring and characterization of influenza virus clinical isolates obtained during Phase II clinical efficacy studies. Antimicrob. Agents Chemother. 44, 78–87 (2000).
   PubMed Web of Science ®Google Scholar
• Gubareva LV, Matrosovich MN, Brenner MK, Bethell RC, Webster RG. Evidence for zanamivir resistance in an immunocompromised child infected with influenza B virus. J. Infect. Dis. 178, 1257–1262 (1998).
   PubMed Web of Science ®Google Scholar
• Weinstock DM, Gubareva LV, Zuccotti G. Prolonged shedding of multi-drug resistant influenza A virus in an immunocompromised patient. N. Engl. J. Med. 348, 867–868 (2003).
   PubMed Web of Science ®Google Scholar
• Ives JA, Carr JA, Mendel DB et al. The H274Y mutation in the influenza A/H1N1 neuraminidase active site following oseltamivir phosphate treatment leave virus severely compromised both in vitro and in vivo. Antiviral Res. 55, 307–317 (2002).
   PubMed Web of Science ®Google Scholar
• Treanor JJ, Hayden FG, Vrooman PS et al. Efficacy and safety of the oral neuraminidase inhibitor oseltamivir in treating acute influenza: a randomized controlled trial. US Oral Neuraminidase Study Group. J. Am. Med. Assoc. 283, 1016–1024 (2000).
   PubMed Web of Science ®Google Scholar
• Hayden FG. Perspectives on antiviral use during pandemic influenza. Philos. Trans. R. Soc. Lond. B. Biol. Sci. 356, 1877–1884 (2001).
   PubMed Web of Science ®Google Scholar
• Whitley RJ, Hayden FG, Reisinger KS et al. Oral oseltamivir treatment of influenza in children. Pediatr. Infect. Dis. J. 20, 127–133 (2001).
   PubMed Web of Science ®Google Scholar
• Carr J, Ives J, Kelly L et al. Influenza virus carrying neuraminidase with reduced sensitivity to oseltamivir carboxylate has altered properties in vitro and is compromised for infectivity and replicative ability in vivo. Antiviral Res. 54, 79–88 (2002).
   PubMed Web of Science ®Google Scholar
• Moscona A. Oseltamivir-resistant influenza? Lancet 364, 733–734 (2004).
   PubMedGoogle Scholar
• Herlocher ML, Truscon R, Elias S et al. Influenza viruses resistant to the antiviral drug oseltamivir: transmission studies in ferrets. J. Infect. Dis. 190, 1627–1630 (2004).
   PubMed Web of Science ®Google Scholar
• Zambon M, Hayden FG. Position statement: global neuraminidase inhibitor susceptibility network. Antiviral Res. 49, 147–156 (2001).
   PubMed Web of Science ®Google Scholar
• McKimm-Breschkin J, Trivedi T, Hampson A et al. Neuraminidase sequence analysis and susceptibilities of influenza virus clinical isolates to zanamivir and oseltamivir. Antimicrob. Agents Chemother. 47, 2264–2272 (2003).
   PubMed Web of Science ®Google Scholar
• Hurt AC, Barr IG, Hartel G, Hampson AW. Susceptibility of human influenza viruses from Australasia and Southeast Asia to the neuraminidase inhibitors zanamivir and oseltamivir. Antiviral Res. 62, 37–45 (2004).
   PubMedGoogle Scholar
• Enserink M. Influenza: girding for disaster. Looking the pandemic in the eye. Science 306, 392–394 (2004).
   PubMedGoogle Scholar
• Kaiser J. Influenza: girding for disaster. Facing down pandemic flu, the world’s defenses are weak. Science 306, 394–397 (2004).
   PubMedGoogle Scholar
• Palese P. Influenza: old and new threats. Nature Med. 10, S82–S87 (2004).
   PubMed Web of Science ®Google Scholar
• Macdonald SJ, Watson KG, Cameron R et al. Potent and long-acting dimeric inhibitors of influenza virus neuraminidase are effective at a once-weekly dosing regimen. Antimicrob. Agents Chemother. 48, 4542–4549 (2004).
   PubMed Web of Science ®Google Scholar
• McKimm-Breschkin JL, Colman PM, Jin B et al. Tethered neuraminidase inhibitors that bind an influenza virus: a first step towards a diagnostic method for influenza. Angew. Chem. Int. Ed. Engl. 42, 3118–3121 (2003).
   PubMedGoogle Scholar
• Monti E, Bassi MT, Bresciani R et al. Molecular cloning and characterization of NEU4, the fourth member of the human sialidase gene family. Genomics 83, 445–453 (2004).
   PubMedGoogle Scholar
• Miyagi T, Wada T, Iwamatsu A et al. Molecular cloning and characterization of a plasma membrane-associated sialidase specific for gangliosides. J. Biol. Chem. 274, 5004–5011 (1999).
   PubMed Web of Science ®Google Scholar
• Kakugawa Y, Wada T, Yamaguchi K et al. Upregulation of plasma membrane-associated ganglioside sialidase (Neu3) in human colon cancer and its involvement in apoptosis suppression. Proc. Natl Acad. Sci. USA 99, 10718–10723 (2002).
   PubMedGoogle Scholar
• Crain SM, Shen KF. Neuraminidase inhibitor, oseltamivir blocks GM1 ganglioside-regulated excitatory opioid receptor-mediated hyperalgesia, enhances opioid analgesia and attenuates tolerance in mice. Brain Res. 995, 260–266 (2004).
   PubMed Web of Science ®Google Scholar