Patents by Inventor Myriam Banville
Myriam Banville has filed for patents to protect the following inventions. This listing includes patent applications that are pending as well as patents that have already been granted by the United States Patent and Trademark Office (USPTO).
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Publication number: 20200325243Abstract: Herein described are antibodies to epidermal growth factor receptor (EGFR) having an EGFR binding affinity that is sufficient to kill disease cells presenting EGFR at high density, but is insufficient for binding to normal cells. A therapeutic effect is thus achieved while avoiding adverse events that result from unintended binding to normal cells.Type: ApplicationFiled: February 21, 2020Publication date: October 15, 2020Inventors: Ilia Alexandre TIKHOMIROV, Maria L. JARAMILLO, Maureen D. O'CONNOR-MCCOURT, Traian SULEA, Renald GILBERT, Bruno GAILLET, Jason BAARDSNES, Myriam BANVILLE, Suzanne GROTHE
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Patent number: 10570211Abstract: Herein described are antibodies to epidermal growth factor receptor (EGFR) having an EGFR binding affinity that is sufficient to kill disease cells presenting EGFR at high density, but is insufficient for binding to normal cells. A therapeutic effect is thus achieved while avoiding adverse events that result from unintended binding to normal cells.Type: GrantFiled: January 20, 2012Date of Patent: February 25, 2020Assignees: GILEAD SCIENCES, INC., NATIONAL RESEARCH COUNCIL OF CANADAInventors: Ilia Alexandre Tikhomirov, Maria L. Jaramillo, Maureen D. O'Connor-McCourt, Traian Sulea, Renald Gilbert, Bruno Gaillet, Jason Baardsnes, Myriam Banville, Suzanne Grothe
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Publication number: 20190194349Abstract: An erbB2 antibody is provided that binds preferentially to disease cells having an erbB2 density greater than a normal erbB2 density. The erbB2 antibody comprises a heavy chain and a light chain. Each chain has a constant region and a variable region. Each variable region comprises framework regions and complementarity determining regions (CDRs), wherein the CDRs have an amino acid sequence set forth below: For the heavy chain: CDR1 GFNIKDTYIH (SEQ ID No. 1) CDR2 RIYPTNGY57TR59YADSVKG (SEQ ID No. 2) CDR3 WGGDGFYAMDY (SEQ ID No. 3). For the light chain: CDR1 RASQDVN30TAVA (SEQ ID No. 4) CDR2 SASF53LYS (SEQ ID No. 5) CDR3 QQHY92TTPPT (SEQ ID NO. 6). At least one of Y57, R59, N30, F53, and Y92 is substituted by an amino acid that confers on said antibody a reduced erbB2 binding affinity (Kd) that is in the range from 0.1 nM to 100 nM. The substitution is other than N30A, F53N, Y92A and Y92F when there is a single substitution in the antibody light chain.Type: ApplicationFiled: December 31, 2018Publication date: June 27, 2019Inventors: Ilia Alexandre Tikhomirov, Maria L. Jaramillo, Maureen D. O'Connor-McCourt, Traian Sulea, Renald Gilbert, Bruno Gaillet, Jason Baardsnes, Myriam Banville
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Patent number: 8987417Abstract: The present invention addresses limitations of prior art receptor-based traps through a methodology called the clamp/click/cleave (CCC) approach. Two fusion proteins each comprising a binding domain fused to a coiled-coil are non-covalently dimerized through the coiled-coil (clamp), and the dimer so formed is stabilized by a covalent disulphide bond (click) between cysteine residues located on the fusion proteins between the binding domains and coiled-coils. Once the disulphide bond has formed, the coiled-coils are subsequently removed (cleave) by cleaving the fusions proteins at cleavage sites located between the cysteine residues and the coiled-coils to provide the covalently dimerized bivalent binding agent of the present invention. Such binding agents are useful in the treatment and diagnosis of disease states characterized by production and/or overexpression of a ligand to which the binding domains bind.Type: GrantFiled: November 28, 2011Date of Patent: March 24, 2015Assignee: National Research Council of CanadaInventors: John C. Zwaagstra, Maureen D. O'Connor-McCourt, Traian Sulea, Catherine Collins, Myriam Banville, Maria L. Jaramillo
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Publication number: 20130295086Abstract: Herein described are antibodies to epidermal growth factor receptor (EGFR) having an EGFR binding affinity that is sufficient to kill disease cells presenting EGFR at high density, but is insufficient for binding to normal cells. A therapeutic effect is thus achieved while avoiding adverse events that result from unintended binding to normal cells.Type: ApplicationFiled: January 20, 2012Publication date: November 7, 2013Applicants: NATIONAL RESEARCH COUNCIL OF CANADA, YM BIOSCIENCES INC.Inventors: Ilia Alexandre Tikhomirov, Maria L. Jaramillo, Maureen D. O'Connor-McCourt, Traian Sulea, Renald Gilbert, Bruno Gaillet, Jason Baardsnes, Myriam Banville, Suzanne Grothe
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Publication number: 20130266564Abstract: An erbB2 antibody is provided that binds preferentially to disease cells having an erbB2 density greater than a normal erbB2 density. The erbB2 antibody comprises a heavy chain and a light chain. Each chain has a constant region and a variable region. Each variable region comprises framework regions and complementarity determining regions (CDRs), wherein the CDRs have an amino acid sequence set forth below: For the heavy chain: CDR1 GFNIKDTYIH (SEQ ID No. 1) CDR2 RIYPTNGY57TR59 YADSVKG (SEQ ID No. 2) CDR3 WGGDGFYAMDY (SEQ ID No. 3) For the light chain: CDR1 RASQDVN30TAVA (SEQ ID No. 4) CDR2 SASF53LYS (SEQ ID No. 5) CDR3 QQHY92TTPPT (SEQ ID No. 6). At least one of Y57, R59, N30, F53, and Y92 is substituted by an amino acid that confers on said antibody a reduced erbB2 binding affinity (Kd) that is in the range from 0.1 nM to 100 nM. The substitution is other than N30A, F53N, Y92A and Y92F when there is a single substitution in the antibody light chain.Type: ApplicationFiled: December 2, 2011Publication date: October 10, 2013Applicant: National Research Council of CanadaInventors: Maria L. Jaramillo, Maureen D. O'Connor-McCourt, Traian Sulea, Ronald Gilbert, Bruno Gaillet, Jason Baardsnes, Myriam Banville, Ilia Tikhomirov
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Publication number: 20130251712Abstract: The present invention addresses limitations of prior art receptor-based traps through a methodology called the clamp/click/cleave (CCC) approach. Two fusion proteins each comprising a binding domain fused to a coiled-coil are non-covalently dimerized through the coiled-coil (clamp), and the dimer so formed is stabilized by a covalent disulphide bond (click) between cysteine residues located on the fusion proteins between the binding domains and coiled-coils. Once the disulphide bond has formed, the coiled-coils are subsequently removed (cleave) by cleaving the fusions proteins at cleavage sites located between the cysteine residues and the coiled-coils to provide the covalently dimerized bivalent binding agent of the present invention. Such binding agents are useful in the treatment and diagnosis of disease states characterized by production and/or overexpression of a ligand to which the binding domains bind.Type: ApplicationFiled: November 28, 2011Publication date: September 26, 2013Applicant: National Research Council of CanadaInventors: John C. Zwaagstra, Maureen D. O'Connor-McCourt, Traian Sulea, Catherine Collins, Myriam Banville, Maria L. Jaramillo
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Patent number: 7786261Abstract: Fusion proteins and coiled-coil induced dimers prepared from both the ectodomains and the kinase domains are disclosed. The receptor domains when presented in the form of a homodimer or heterodimer by virtue of the coiled-coil tag have enhanced ligand binding activity or enhanced kinase activity. The kinetics of binding and the antagonistic potencies of the ectodomain dimers, and their use to alter or inhibit signaling is described. Application of the ectodomain and kinase domain dimers in assays for selecting compounds capable of inhibiting ligand binding and kinase activity, respectively, is described.Type: GrantFiled: September 2, 2004Date of Patent: August 31, 2010Assignee: National Research Council of CanadaInventors: Gregory De Crescenzo, Maureen D. O'Conner, Beatrice Paul-Roc, John Zwaagstra, Myriam Banville, Maria Jaramillo
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Publication number: 20070154994Abstract: Fusion proteins and coiled-coil induced dimers prepared from both the ectodomains and the kinase domains are disclosed. The receptor domains when presented in the form of a homodimer or heterodimer by virtue of the coiled-coil tag have enhanced ligand binding activity or enhanced kinase activity. The kinetics of binding and the antagonistic potencies of the ectodomain dimers, and their use to alter or inhibit signaling is described. Application of the ectodomain and kinase domain dimers in assays for selecting compounds capable of inhibiting ligand binding and kinase activity, respectively, is described.Type: ApplicationFiled: September 2, 2004Publication date: July 5, 2007Applicant: National Research Council of CanadaInventors: Gregory De Crescenzo, Maureen O'Conner, Beatrice Paul-Roc, John Zwaagstra, Myriam Banville, Maria Jaramillo