Antibody therapeutics:

• REICHERT JM, ROSENDWEIG CJ, FADEN LB et al.: Monoclonal antibody successes in the clinic. Nat. Biotechnol. (2005) 23:1073-1078.
   PubMed Web of Science ®Google Scholar
• CARTER PJ: Potent antibody therapeutics by design. Nat. Rev. (2006) 6:343-357.
   Google Scholar
• SATOH M, IIDA S, SHITARA K: Non-fucosylated therapeutic antibodies as next-generation therapeutic antibodies. Expert Opin. Biol. Ther. (2006) 6:1161-1173.
   PubMed Web of Science ®Google Scholar
• BAKER M: Upping the ante on antibodies. Nat. Biotechnol. (2005) 23:1065-1072.
   PubMed Web of Science ®Google Scholar
• GLENNIE MJ, VAN DE WINKEL JG: Renaissance of cancer therapeutic antibodies. Drug Discov. Today (2003) 8:503-510.
   PubMed Web of Science ®Google Scholar
• MIRIK GR, BRADT BM, DENARDO SJ, DENARDO GL: A review of human anti-globulin antibody (HAGA, HAMA, HACA, HAHA) responses to monoclonal antibodies. Not four letter words. Q. J. Nucl. Med. Mol. Imaging (2004) 48:251-257.
   PubMed Web of Science ®Google Scholar
• KLITGAARD JL, COLJEE VJ, ANDERSEN PS et al.: Reduced susceptibility of recombinant polyclonal antibodies to inhibitory anti-variable domain antibody responses. J. Immunol. (2006) 177:3782-3790.
   PubMed Web of Science ®Google Scholar
• DEISENHOFER J: Crystallographic refinement and atomic models of a human Fc fragment and its complex with fragment B of protein A from Staphylococcus aureus at 2.9- and 2.8-Å resolution. Biochemistry (1981) 20:2361-2370.
   PubMed Web of Science ®Google Scholar
• WOOF JM, Burton DR: Human antibody-Fc receptor interactions illuminated by crystal structures. Nat. Rev. Immunol. (2004) 4:89-99.
   PubMed Web of Science ®Google Scholar
• NEZLIN R, Ghetie V: Interactions of immunoglobulins outside the antigen-combining site. Adv. Immunol. (2004) 82:155-215.
   PubMed Web of Science ®Google Scholar
• van SORGE NM, van der POL WL, van de WINKEL JG: FcγR polymorphisms: implications for function, disease susceptibility and immunotherapy. Tissue Antigens (2003) 61:189-202.
   PubMed Web of Science ®Google Scholar
• NIMMERJAHN F, RAVETCH JV: Fcγ receptors: old friends and new family members. Immunity (2006) 24:19-28.
   PubMed Web of Science ®Google Scholar
• JEFFERIS R: Glycosylation of recombinant antibody therapeutics. Biotechnol. Progress (2005) 21:11-16.
   PubMed Web of Science ®Google Scholar
• SINCLAIR AM, ELLIOTT S: Glycoengineering: the effect of glycosylation on the properties of therapeutic proteins. J. Pharm. Sci. (2005) 94:1626-1635.
   PubMed Web of Science ®Google Scholar
• SHIELDS RL, LAI J, KECK, R et al.: Lack of fucose on human IgG1 N-linked oligosaccharide improves binding to human FcγRIII and antibody-dependent cellular toxicity. J. Biol. Chem. (2002) 277:26733-26740.
   PubMed Web of Science ®Google Scholar
• SHINKAWA T, NAKAMURA K, YAMANE N et al.: The absence of fucose but not the presence of galactose or bisecting N-acetylglucosamine of human IgG1 complex-type oligosaccharides shows the critical role of enhancing antibody-dependent cellular cytotoxicity. J. Biol. Chem. (2003) 278:3466-3473.
   PubMed Web of Science ®Google Scholar
• NIWA R, NATSUME A, UEHARA A et al.: IgG subclass-independent improvement of antibody-dependent cellular cytotoxicity by fucose removal from Asn297-linked oligosaccharides. J. Immunol. Methods (2005) 306:151-160.
   PubMed Web of Science ®Google Scholar
• FERRARA C, BRUNKER P, MOSER S et al.: Modulation of therapeutic antibody effector functions by glycosylation engineering: influence of Golgi enzyme localization domain and co-expression of heterologous b1, 4-N-acetylglucosaminyltransferase III and Golgi α-mannosidase II. Biotechnol. Bioeng. (2006) 93:851-861.
   PubMed Web of Science ®Google Scholar
• MIMURA Y, SONDERMANN P, GHIRLANDO R et al.: The role of oligosaccharide residues of IgG1-Fc in FcγIIb binding. J. Biol. Chem. (2001) 276:45539-45547.
   PubMed Web of Science ®Google Scholar
• KRAPP S, MIMURA Y, JEFFERIS R et al.: Structural analysis of human IgG glycoforms reveals a correlation between oligosaccharide content, structural integrity and Fcγ-receptor affinity. J. Mol. Biol. (2003) 325:979-989.
   PubMed Web of Science ®Google Scholar
• JONES AJ, PAPAC DI, CHIN EH et al.: Selective clearance of glycoforms of a complex glycoprotein pharmaceutical caused by terminal N-acetylglucosamine is similar in humans and cynomolgus monkeys. Glycobiology (2007) 17:529-540.
   PubMed Web of Science ®Google Scholar
• ALETE DE, RACHER AJ, BIRCH JR et al.: Proteomic analysis of enriched microsomal fractions from GS-NS0 murine myeloma cells with varying secreted recombinant monoclonal antibody productivities. Proteomics (2005) 18:4689-4704.
   Google Scholar
• QIAN J, LIU T, YANG L et al.: Structural characterization of N-linked oligosaccharides on monoclonal antibody cetuximab by the combination of orthogonal matrix-assisted laser desorption/ionization hybrid quadrupole-quadrupole time-of-flight tandem mass spectrometry and sequential enzymatic digestion. Anal. Biochem. (2007) 364:8-18.
   PubMed Web of Science ®Google Scholar
• GARRED P, MICHAELSEN TE, AASE A: The IgG subclass pattern of complement activation depends on epitope density and antibody and complement concentration. Scand. J. Immunol. (1989) 30:379-382.
   PubMed Web of Science ®Google Scholar
• MICHAELSEN TE, GARRED P, AASE A: Human IgG subclass pattern of inducing complement-mediated cytolysis depends on antigen concentration and to a lesser extent on epitope patchiness, antibody affinity and complement concentration. Eur. J. Immunol. (1991) 21:11-16.
   PubMed Web of Science ®Google Scholar
• LUCISANO VALIM YM, LACHMANN PJ: The effect of antibody isotype and antigenic epitope density on the complement-fixing activity of immune complexes: a systematic study using chimaeric anti-NIP antibodies with human Fc regions. Clin. Exp. Immunol. (1991) 84:1-8.
   PubMed Web of Science ®Google Scholar
• VOICE JK, LACHMANN PJ: Neutrophil Fc γ and complement receptors involved in binding soluble IgG immune complexes and in specific granule release induced by soluble IgG immune complexes. Eur. J. Immunol. (1997) 27:2514-2523.
   PubMed Web of Science ®Google Scholar
• WATIER H: Variability factors in the clinical response to recombinant antibodies and IgG Fc-containing fusion proteins. Expert Opin. Biol. Ther. (2005) 5(Suppl. 1):S1-S8.
   PubMed Web of Science ®Google Scholar
• MARCUS R, HAGENBEEK A: The therapeutic use of rituximab in non-Hodgkin's lymphoma. Eur. J. Haematol. Suppl. (2007) 67:5-14.
   PubMedGoogle Scholar
• LIFELY MR, HALE G, BOYSE S: Glycosylation and biological activity of CAMPATH-1H expressed in different cell lines and grown under different culture conditions. Glycobiology (1995) 5:813-822.
   PubMed Web of Science ®Google Scholar
• UMANA P, JEAN-MAIRET J, MOUDRY R et al.: Engineered glycoforms of an anti-neuroblastoma. IgG1 with optimized antibody-dependent cellular cytotoxic activity. Nat. Biotechnol. (1999) 17:176-180.
   PubMed Web of Science ®Google Scholar
• DAVIES J, JIANG L, LABARRE MJ et al.: Expression of GTIII in a recombinant anti-CD20 CHO production cell line: expression of antibodies of altered glycoforms leads to an increase in ADCC thro' higher affinity for FcRIII. Biotech. Bioeng. (2001) 74:288-294.
   PubMed Web of Science ®Google Scholar
• YMANE-OHUKI N, KINOSHITA S, INOUE-URAKUBO M et al.: Establishment of FUT8 knockout Chinese hamster ovary cells: an ideal host cell line for producing completely defucosylated antibodies with enhanced antibody-dependent cellular cytotoxicity. Biotechnol. Bioeng. (2004) 87:614-622.
   PubMed Web of Science ®Google Scholar
• PREITHNER S, ELM S, LEPPOLD S et al.: High concentrations of therapeutic IgG1 antibodies are needed to compensate for the inhibition of ADCC by excess endogenous immunoglobulin G. Mol. Immunol. (2006) 43:1183-1193.
   PubMed Web of Science ®Google Scholar
• NECHANSKY A, SCHUSTER M, JOST W et al.: Compensation of endogenous IgG mediated inhibition of antibody-dependent cellular cytotoxicity by glyco-engineering of therapeutic antibodies. Mol. Immunol. (2007) 44:1815-1817.
   PubMed Web of Science ®Google Scholar
• IIDA S, MISAKA H, INOUE M et al.: Non-fucosylated therapeutic IgG antibody can evade the inhibitory effect of serum IgG on antibody-dependent cellular cytotoxicity through its binding to FcγRIIIa. Clin. Cancer Res. (2006) 12:2879-2887.
   PubMed Web of Science ®Google Scholar
• SUZUKI E, NIWA R, SAJI SA et al.: Nonfucosylated anti-HER2 antibody augments antibody-dependent cellular cytotoxicity in breast cancer patients. Clin. Cancer Res. (2007) 13:1875-1882.
   PubMed Web of Science ®Google Scholar
• ANDERSON CL: Human IgG Fc receptors. Clin. Immunol. Immunopathol. (1989) 53:S63-S71.
   PubMedGoogle Scholar
• KOENE HR, KLEIJER M, ALGRA J et al.: FcγRIIIa-158V/F polymorphism influences the binding of IgG by natural killer cell FcγRIIIa, independently of the Fcγ RIIIa-48L/R/H phenotype. Blood (1997) 90:1109-1114.
   PubMed Web of Science ®Google Scholar
• CARTRON G, DACHEUX L, SALLES G et al.: Therapeutic activity of humanized anti-CD20 monoclonal antibody and polymorphism in IgG Fc receptor FcγRIIIa gene. Blood (2002) 99:754-758.
   PubMed Web of Science ®Google Scholar
• ANOLIK JH, CAMPBELL D, FELGAR RE et al.: The relationship of FcγRIIIa genotype to degree of B cell depletion by Rituximab in the treatment of systemic lupus erythematosus. Arthritis Rheum. (2003) 48:455-459.
   PubMed Web of Science ®Google Scholar
• LOUIS E, EL GHOUL Z, VERMEIRE S et al.: Association between polymorphism in IgG FcγIIIa coding gene and biological response to Infliximab in Crohn's disease. Aliment. Pharmacol. Ther. (2004) 19:511-519.
   PubMed Web of Science ®Google Scholar
• MIESCHER S, SPYCHER MO, AMSTUTZ H et al.: A single recombinant anti-RhD IgG prevents RhD immunization: association of RhD-positive red blood cell clearance rate with polymorphisms in the FcγRIIA and FcγIIIA genes. Blood (2004) 103:4028-4035.
   PubMed Web of Science ®Google Scholar
• LIN TS, FLINN IW, MODALI R et al.: FCGR3A and FCGR2A polymorphisms may not correlate with response to Alemtuzumab in chronic lymphocytic leukemia. Blood (2005) 105:289-291.
   PubMed Web of Science ®Google Scholar
• TEELING JL, FRENCH RR, CRAGG MS et al.: Characterization of new human CD20 monoclonal antibodies with potent cytolytic activity against non-Hodgkin lymphomas. Blood (2004) 104:1793-1800.
   PubMed Web of Science ®Google Scholar
• CRAGGS MS, WALSHE CA, IVANOV AO et al.: The biology of CD20 and its potential as a target for mAb therapy. Curr. Dir. Autoimmun. (2005) 8:140-174.
   PubMedGoogle Scholar
• TEELING JL, MACKUS WJ, WIEGMAN LJ et al.: The biological activity of human CD20 monoclonal antibodies is linked to unique epitopes on CD20. J. Immunol. (2006) 177:362-371.
   PubMed Web of Science ®Google Scholar
• CARDELLI PM, QUIN M, BUCKMAN D et al.: Binding to CD20 by anti-B1 antibody or F(ab´)(2) is sufficient for induction of apoptosis in B-cell lines. Cancer Immunol. Immunother. (2002) 51:15-24
   PubMed Web of Science ®Google Scholar
• LIU Y, ZHENG M, LAI Z et al.: Inhibition of human B-cell lymphoma by an anti-CD20 antibody and its chimeric F(ab´)2 fragment via induction of apoptosis. Cancer Lett. (2004) 205:143-153
   PubMed Web of Science ®Google Scholar
• LUND J, TAKAHASHI N, POUND J et al.: Multiple interactions of IgG with its core oligosaccharide can modulate recognition by complement and human FcγRI and influence the synthesis of its oligosaccharide chains. J. Immunol. (1996) 157:4963-4969.
   PubMed Web of Science ®Google Scholar
• SHIELDS RL, NAMENUK AK, HONG K et al.: High resolution mapping of the binding site on human IgG1 for FcγRI, FcγRII, FcγRIII, and FcRn and design of IgG1 variants with improved binding to the FcγR. J. Biol. Chem. (2001) 276:6591-6604.
   PubMed Web of Science ®Google Scholar
• LAZAR GA, DANG W, KARKI S et al.: Engineered antibody Fc variants with enhanced effector function. Proc. Natl. Acad. Sci. USA (2006) 103:4005.
   PubMed Web of Science ®Google Scholar
• DALL'ACQUA WF, COOK KE, DAMSCHRODER MM: Modulation of the effector functions of a human IgG1 through engineering of its hinge region. J. Immunol. (2006) 177:1129-1138.
   PubMed Web of Science ®Google Scholar
• VERI MC, GORLATOV S, LI H et al.: Monoclonal antibodies capable of discriminating the human inhibitory Fcγ-receptor IIB (CD32B) from the activating Fcγ-receptor IIA (CD32A): biochemical, biological and functional characterization. Immunology (2007).
   PubMedGoogle Scholar
• SARVAS H, RAUTONEN H, KAYHTY M et al.: Effect of Gm allotypes on IgG2 antibody responses and IgG2 concentrations in children and adults. Int. Immunol. (1990) 2:317-322.
   PubMed Web of Science ®Google Scholar
• PAN Q, HAMMARSTROM L: Molecular basis of IgG subclass deficiency. Immunol. Rev. (2000) 178:99-110.
   PubMed Web of Science ®Google Scholar
• JONSSON G, OXELIUS VA, TRUEDSSON L et al.: Homozygosity for the IgG2 subclass allotype G2M(n) protects against severe infection in hereditary C2 deficiency. J. Immunol. (2006) 77:722-728.
   Google Scholar
• SALTZ L, EASTLEY C, KIRKPATRICK P: Panitumumab. Nat. Rev. Drug Discov. (2006) 5:987-988.
   PubMed Web of Science ®Google Scholar
• PARREN PW, WARMERDAM PA, BOEIJE LC et al.: On the interaction of IgG subclasses with the low affinity FcγRIIa (CD32) on human monocytes, neutrophils, and platelets. Analysis of a functional polymorphism to human IgG2. J. Clin. Invest. (1992) 90:1537-1546.
   PubMed Web of Science ®Google Scholar
• RODRIGUEZ ME, VAN DER POL W-L, SANDERS LAM: Crucial role of FcγRIIa (CD32) in assessment of functional anti-Streptococcus pneumoniae antibody activity in human sera. J. Infect. Dis. (1999) 179:423-433.
   PubMed Web of Science ®Google Scholar
• LAI Z, KIMMEL R, PETERSEN S et al.: Multi-valent human monoclonal antibody preparation against Pseudomonas aeruginosa derived from transgenic mice containing human immunoglobulin loci is protective against fatal pseudomonas sepsis caused by multiple serotypes. Vaccine (2005) 23:3264-3271.
   PubMed Web of Science ®Google Scholar
• PENICHETT ML, DELA CRUZ JS, SHIN SU, MORRISON SL: A recombinant IgG3-(IL-2) fusion protein for the treatment of human HER2/neu expressing tumors. Hum. Antibodies (2001) 10:43-49.
   PubMedGoogle Scholar
• HELQUERA G, RODRIGUEZ JA, PENICHET ML: Cytokines fused to antibodies and their combinations as therapeutic agents against different peritoneal HER2/neu expressing tumors. Mol. Cancer Ther. (2006) 5:1029-1040.
   PubMed Web of Science ®Google Scholar
• MICHAESEN TE, BREKKE OH, AASE A et al.: One disulfide bond in front of the second heavy chain constant region is necessary and sufficient for effector functions of human IgG3 without a genetic hinge. Proc. Natl. Acad. Sci. USA (1994) 91:9243-9247.
   PubMed Web of Science ®Google Scholar
• BREKKE OH, MICHAELSEN TE, SANDLIE I: The structural requirements for complement activation by IgG: does it hinge on the hinge? Immunol. Today (1995) 16:85-90.
   PubMedGoogle Scholar
• JEFFERIS R: Immunoglobulins: Allotypes. In: Encyclopaedia of Immunology. 2nd Edition, Roitt IM, Delves PJ (Eds), Saunders, Florida, USA (1998).
   Google Scholar
• AALBERSE RC, SHCUUMANN J: IgG4 breaking the rules. Immunology (2002) 105:9-19.
   PubMed Web of Science ®Google Scholar
• SMALLING R, FOOT M, MOLINEUX G et al.: Drug-induced and antibody-mediated pure red cell aplasia: a review of literature and current knowledge. Biotechnol. Annu. Rev. (2004) 10:237-250.
   PubMedGoogle Scholar
• AMICO D, BARBUI AM, ERBA E et al.: Differential response of human acute myeloid leukemia cells to Gemtuzumab ozogamicin in vitro: role of Chk1 and Chk2 phosphorylation and caspase 3. Blood (2003) 101:4589-4597.
   PubMed Web of Science ®Google Scholar
• O'CONNOR P: Natalizumab and the role of α4-integrin antagonism in the treatment of multiple sclerosis. Expert Opin. Biol. Ther. (2007) 7:123-136.
   PubMed Web of Science ®Google Scholar
• BRUGGEMANN M, WILLIAMS GT, BINDON CL et al.: Comparison of the effector function of human immunoglobulins using a matched set of chimeric antibodies. J. Exp. Med. (1987) 166:1351-1361.
   PubMed Web of Science ®Google Scholar
• HOLLAND M, HEWINS P, GOODALL M et al.: Anti-neutrophil cytoplasmic antibody IgG subclasses in Wegener's granulomatosis: a possible pathogenic role for the IgG4 subclass. Clin. Exp. Immunol. (2004) 138:183-192.
   PubMed Web of Science ®Google Scholar
• EHLERS S: Tumor necrosis factor and its blockade in granulomatous infections: differential modes of action of infliximab and etanercept? Clin. Infect. Dis. (2005) 41 (Suppl. 3):S199-S203.
   PubMed Web of Science ®Google Scholar
• DUBCENCO E, OTTAWAY CA, CHEN DL, BAKER JP: Neurological symptoms suggestive of demyelisation in Crohn's disease after infliximab therapy. Eur. J. Gastroenterol. Hepatol. (2006) 18:565-566.
   PubMed Web of Science ®Google Scholar
• COLE MS, ANASETTI C, TSO JY: Human IgG2 variants of chimeric anti-CD3 are non-mitogenic to T cells. J. Immunol. (1997) 159:3613-3621.
   PubMed Web of Science ®Google Scholar
• SONDERMANN P, HUBER R, OOSTHUIZEN V, JACOB U: The 3.2-A crystal structure of the human IgG1 Fc -FcγRIII complex. Nature (2000) 406:267-273.
   PubMed Web of Science ®Google Scholar
• RADAEV S, MOTYKA S, FRIDMAN WH et al.: The structure of human type FcγIII receptor in complex with Fc. J. Biol. Chem. (2001) 276:16469-16477.
   PubMed Web of Science ®Google Scholar
• MARTIN WL, WEST AP, GAN L, BJORKMAN PJ: Crystal structure at 2.8 A of an FcRn/heterodimeric Fc complex: mechanism of pH-dependent binding. Mol. Cell (2001) 7:867-877.
   PubMed Web of Science ®Google Scholar
• HINTON PR, XIONG JM, JOHLFS MG et al.: An engineered human IgG1 antibody with longer serum half-life. J. Immunol. (2006) 176:346-356.
   PubMed Web of Science ®Google Scholar
• VACCARO C, ZHOU J, OBER RJ, WARD ES: Engineering the Fc region of immunoglobulin G to modulate in vivo antibody levels. Nat. Biotechnol. (2005) 23:1283-1288.
   PubMed Web of Science ®Google Scholar
• BITONTI AJ, DUMONT JA: Pulmonary administration of therapeutic proteins using an immunoglobulin transport pathway. Adv. Drug Deliv. Rev. (2006) 58:1106-1118.
   PubMed Web of Science ®Google Scholar
• YOUINGS A, CHANG SC, DWEK RA et al.: Site-specific glycosylation of human immunoglobulin G is altered in four rheumatoid arthritis patients. Biochem. J. (1996) 314:621-630.
   PubMed Web of Science ®Google Scholar
• HOLLAND M, YAGI H, TAKAHASHI N et al.: Differential glycosylation of polyclonal IgG, IgG-Fc and IgG-Fab isolated from the sera of patients with ANCA associated systemic vasculitis. Biochim Biophys. Acta (2006) 1760:669-677.
   PubMed Web of Science ®Google Scholar
• HUANG L, BIOLOSI S, BALES KR, KUCHIBHOTLA U: Impact of variable domain glycosylation on antibody clearance: an LC/MS characterization. Anal Biochem. (2006) 349:197-207.
   PubMed Web of Science ®Google Scholar
• ANDERSEN DC, REILLY DE: Production technologies for monoclonal antibodies and their fragments. Curr. Opin. Biotechnol. (2000) 15:456-462.
   Google Scholar
• GOMORD V, CHABERLAIN P, JEFFERIS R, FAYE L: Biopharmaceutical production in plants: problems, solutions and opportunities. Trends Biotechnol. (2005) 23:559-565.
   PubMed Web of Science ®Google Scholar
• FITCHETTE AC, DINH OT, FAYE L, BARDOR M: Plant proteomics and glycosylation. Methods Mol. Biol. (2007) 355:317-342.
   PubMedGoogle Scholar
• COX KM, STERLING JD, REGAN JT et al.: Glycan optimization of a human monoclonal antibody in the aquatic plant Lemna minor. Nat. Biotechnol. (2006) 24:1591-1597.
   PubMed Web of Science ®Google Scholar
• KAPRIVOVA A, STEMMER C, ALTMANN F et al.: Targeted knockouts of Physcomitrella lacking plant-specific immunogenic N-glycans. Plant. Biotechnol. J. (2004) 2:517-523.
   PubMed Web of Science ®Google Scholar
• STRASSER R, ALTMANN F, MACH L et al.: Generation of Arabidopsis thaliana plants with complex N-glycans lacking b1,2-linked xylose and core a1,3-linked fucose. FEBS Lett. (2004) 561:132-136.
   PubMed Web of Science ®Google Scholar
• HILL DR, AIMILLER JJ, SHI X, JARVIS DL: Isolation and analysis of a baculovirus vector that supports recombinant glycoprotein sialylation by SfSWT-1 cells cultured in serum-free medium. Biotechnol. Bioeng. (2006) 95:37-47.
   PubMed Web of Science ®Google Scholar
• HAMILTON SR, DAVIDSON RC, SETHURAMAN N et al.: Humanization of yeast to produce complex terminally sialylated glycoproteins. Science (2006) 313:1441-1443.
   PubMed Web of Science ®Google Scholar
• GEORGIOU G, SEGATORI L: Preparative expression of secreted proteins in bacteria: status report and future prospects. Curr. Opin. Biotechnol. (2005) 16:538-545.
   PubMed Web of Science ®Google Scholar
• WACKER M, FELDMAN MF, CALLWAERT N et al.: Substrate specificity of bacterial oligosaccharyltransferase suggests a common transfer mechanism for the bacterial and eukaryotic systems. Proc. Natl. Acad. Sci. USA (2006) 103:7088-7093.
   PubMed Web of Science ®Google Scholar
• WONG JB, SINGH G, KAVANAUGH A: Estimating the cost-effectiveness of 54 weeks of infliximab for rheumatoid arthritis. Am. J. Med. (2002) 113:400-408.
   PubMed Web of Science ®Google Scholar

Websites

• http://www.fda.gov/cder/biologics/review/ritugen112697-r2.pdf
   Google Scholar
• http://www.freepatentsonline.com/20060121028.html US Patent 20060121028.
   Google Scholar
• http://www.fda.gov/cder/drug/infopage/natalizumab
   Google Scholar
• http://www.dh.gov.uk/en/Publicationsandstatistics/Publications/PublicationsPolicyAndGuidance/DH_063117
   Google Scholar
• http://www.syntnx.com/home.php
   Google Scholar
• http://www.medicalnewstoday.com/medicalnews.php?newsid=31791
   Google Scholar
• http://www.brentpct.nhs.uk/BrentHerceptinPositionPaper0206.doc
   Google Scholar
• http://pymol.sourceforge.net
   Google Scholar