L
Leonard G. Presta
Researcher at Genentech
Publications - 188
Citations - 24751
Leonard G. Presta is an academic researcher from Genentech. The author has contributed to research in topics: Antibody & Receptor. The author has an hindex of 53, co-authored 183 publications receiving 24145 citations. Previous affiliations of Leonard G. Presta include Seattle Genetics & Schering-Plough.
Papers
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Journal ArticleDOI
Inhibitory Fc receptors modulate in vivo cytotoxicity against tumor targets.
TL;DR: It is demonstrated that Fc-receptor-dependent mechanisms contribute substantially to the action of cytotoxic antibodies against tumors and indicate that an optimal antibody against tumors would bind preferentially to activation Fc receptors and minimally to the inhibitory partner FcγRIIB.
Journal ArticleDOI
Lack of Fucose on Human IgG1 N-Linked Oligosaccharide Improves Binding to Human FcγRIII and Antibody-dependent Cellular Toxicity
Robert L. Shields,Jadine Lai,Rodney G. Keck,Lori Y. O'Connell,Kyu Hong,Y. Gloria Meng,Stefanie Weikert,Leonard G. Presta +7 more
TL;DR: Antibody-dependent cellular cytot toxicity assays using purified peripheral blood monocytes or natural killer cells from several donors showed enhanced cytotoxicity, especially evident at lower antibody concentrations.
Journal ArticleDOI
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
Robert L. Shields,Angela K. Namenuk,Kyu Hong,Y. Gloria Meng,Julie Rae,Josephine P. Briggs,Dong Xie,Jadine Lai,Andrew Stadlen,Betty Li,Judith A. Fox,Leonard G. Presta +11 more
TL;DR: Select IgG1 variants with improved binding to FcγRIIIA exhibited up to 100% enhancement in antibody-dependent cell cytotoxicity using human effector cells; these variants included changes at residues not found at the binding interface in the IgG/Fcγ RIIIA co-crystal structure.
Patent
Polypeptide variants with altered effector function
TL;DR: In this article, the present invention concerns polypeptides comprising a variant of the Fc region, which have altered effector function as a consequence of one or more amino acid modifications in the region thereof.
Patent
Altered polypeptides with increased half-life
TL;DR: In this paper, the salvage receptor binding epitope of an Fc region of an IgG was altered so as to comprise a salvage receptor and thereby have increased circulatory half-life.