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Sherie L. Morrison

Researcher at University of California, Los Angeles

Publications -  187
Citations -  11206

Sherie L. Morrison is an academic researcher from University of California, Los Angeles. The author has contributed to research in topics: Antibody & Fusion protein. The author has an hindex of 61, co-authored 186 publications receiving 10841 citations. Previous affiliations of Sherie L. Morrison include University of Guelph & Hokkaido University.

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Effect of glycosylation on antibody function: implications for genetic engineering

TL;DR: Antibody glycosylation can be influenced by the cell in which it is produced, the conformation of the antibody and cell culture conditions, and the structure of the attached carbohydrate can also affect antibody activity.
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Immunoglobulin gene expression in transformed lymphoid cells.

TL;DR: The S107 light chain is synthesized and secreted as part of an intact antibody molecule by transformed hybridoma cells that normally secrete an IgGl (gamma, K) antibody molecule and is identical to the light chain synthesized by the S107 myeloma cell line, as judged by immunoprecipitation and two-dimensional gel electrophoresis.
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Structural features of human immunoglobulin G that determine isotype-specific differences in complement activation.

TL;DR: Using point mutants of chimeric antibodies, specific residues responsible for the differing ability of the IgG subclasses to fix complement are identified and it is shown that Ser at position 331 in gamma 4 is critical for determining the inability of that isotype to bind C1q and activate complement.
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Analysis of the pH Dependence of the Neonatal Fc Receptor/Immunoglobulin G Interaction Using Antibody and Receptor Variants

TL;DR: It is shown that the affinity of FcRn for IgG is reduced about 2 orders of magnitude as the pH is raised from 6.0 to 7.0, and it is demonstrated that IgG histidines located at the junction between the CH2 and CH3 domains contribute to the pH-dependent affinity transition.
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Design and production of novel tetravalent bispecific antibodies

TL;DR: Novel bispecific antibodies are produced by fusing the DNA encoding a single chain antibody after the C terminus (CH3-ScFv) or after the hinge (Hinge-Scfv) with an antibody of a different specificity.