Enhancing the potency of therapeutic monoclonal antibodies via Fc optimization.

[1]  D. Beckett,et al.  A minimal peptide substrate in biotin holoenzyme synthetase‐catalyzed biotinylation , 2008, Protein science : a publication of the Protein Society.

[2]  J. Stavenhagen,et al.  Fc optimization of therapeutic antibodies enhances their ability to kill tumor cells in vitro and controls tumor expansion in vivo via low-affinity activating Fcgamma receptors. , 2007, Cancer research.

[3]  J. Stavenhagen,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 , 2007, Immunology.

[4]  Steve Burke,et al.  CD32B, the human inhibitory Fc-gamma receptor IIB, as a target for monoclonal antibody therapy of B-cell lymphoma. , 2006, Blood.

[5]  P. Carter.  Potent antibody therapeutics by design , 2006, Nature Reviews Immunology.

[6]  Brian Mohan Gurbaxani,et al.  Development of new models for the analysis of Fc-FcRn interactions. , 2006, Molecular immunology.

[7]  E. Kimby,et al.  Polymorphisms in FcγRIIIA (CD16) receptor expression are associated with clinical response to rituximab in Waldenstrom's macroglobulinemia. , 2004, Journal of clinical oncology : official journal of the American Society of Clinical Oncology.

[8]  K. Haas,et al.  The Innate Mononuclear Phagocyte Network Depletes B Lymphocytes through Fc Receptor–dependent Mechanisms during Anti-CD20 Antibody Immunotherapy , 2004, The Journal of experimental medicine.

[9]  W. Weng,et al.  Two immunoglobulin G fragment C receptor polymorphisms independently predict response to rituximab in patients with follicular lymphoma. , 2003, Journal of clinical oncology : official journal of the American Society of Clinical Oncology.

[10]  R. Kerbel,et al.  Disruption of cell-cell adhesion enhances antibody-dependent cellular cytotoxicity: implications for antibody-based therapeutics of cancer. , 2002, Cancer research.

[11]  G. Salles,et al.  Therapeutic activity of humanized anti-CD20 monoclonal antibody and polymorphism in IgG Fc receptor FcgammaRIIIa gene. , 2002, Blood.

[12]  P. Carter,et al.  Improving the efficacy of antibody-based cancer therapies , 2001, Nature Reviews Cancer.

[13]  Leonard G. Presta,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* , 2001, The Journal of Biological Chemistry.

[14]  D. Scheinberg,et al.  Monoclonal antibody therapies–a ‘constant’ threat to cancer , 2000, Nature Medicine.

[15]  L. Presta,et al.  Inhibitory Fc receptors modulate in vivo cytoxicity against tumor targets , 2000, Nature Medicine.

[16]  G. Adams,et al.  Monoclonal antibody therapy of cancer , 1999, Nature Biotechnology.

[17]  K D Wittrup,et al.  Selection of functional T cell receptor mutants from a yeast surface-display library. , 1999, Proceedings of the National Academy of Sciences of the United States of America.

[18]  Eric T. Boder,et al.  Yeast surface display for screening combinatorial polypeptide libraries , 1997, Nature Biotechnology.

[19]  J. Isaacs,et al.  Therapy with monoclonal antibodies. An in vivo model for the assessment of therapeutic potential. , 1992, Journal of immunology.

[20]  L. Presta,et al.  Humanization of an anti-p185HER2 antibody for human cancer therapy. , 1992, Proceedings of the National Academy of Sciences of the United States of America.

[21]  M. Witmer,et al.  Blockade of clearance of immune complexes by an anti-F(cγ) receptor monoclonal antibody , 1986, The Journal of experimental medicine.

[22]  J. V. Ravetch,et al.  IgG Fc receptors. , 2001, Annual review of immunology.