Relevant bibliographies by topics / Antibody Effector Function

Contents

  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers

Academic literature on the topic 'Antibody Effector Function'

Author: Grafiati
Published: 4 June 2021
Last updated: 12 February 2022

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Journal articles on the topic "Antibody Effector Function"

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Desjarlais, John R., and Greg A. Lazar. "Modulation of antibody effector function." Experimental Cell Research 317, no. 9 (May 2011): 1278–85. http://dx.doi.org/10.1016/j.yexcr.2011.03.018.

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BURTON, DENNIS R. "Molecular basis of antibody effector function." Biochemical Society Transactions 16, no. 6 (December 1, 1988): 953–56. http://dx.doi.org/10.1042/bst0160953.

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Lazar, G. A., W. Dang, S. Karki, O. Vafa, J. S. Peng, L. Hyun, C. Chan, et al. "Engineered antibody Fc variants with enhanced effector function." Proceedings of the National Academy of Sciences 103, no. 11 (March 6, 2006): 4005–10. http://dx.doi.org/10.1073/pnas.0508123103.

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Uccellini, Melissa B., Sadaf Aslam, Sean T. H. Liu, Fahmida Alam, and Adolfo García-Sastre. "Development of a Macrophage-Based ADCC Assay." Vaccines 9, no. 6 (June 17, 2021): 660. http://dx.doi.org/10.3390/vaccines9060660.

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Fc-dependent effector functions are an important determinant of the in vivo potency of therapeutic antibodies. Effector function is determined by the combination of FcRs bound by the antibody and the cell expressing the relevant FcRs, leading to antibody-dependent cellular cytotoxicity (ADCC). A number of ADCC assays have been developed; however, they suffer from limitations in terms of throughput, reproducibility, and in vivo relevance. Existing assays measure NK cell-mediated ADCC activity; however, studies suggest that macrophages mediate the effector function of many antibodies in vivo. Here, we report the development of a macrophage-based ADCC assay that relies on luciferase expression in target cells as a measure of live cell number. In the presence of primary mouse macrophages and specific antibodies, loss of luciferase signal serves as a surrogate for ADCC-dependent killing. We show that the assay functions for a variety of mouse and human isotypes with a model antigen/antibody complex in agreement with the known effector function of the isotypes. We also use this assay to measure the activity of a number of influenza-specific antibodies and show that the assay correlates well with the known in vivo effector functions of these antibodies.
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Chung, Amy W., Max Crispin, Laura Pritchard, Hannah Robinson, Miroslaw K. Gorny, Xiaojie Yu, Chris Bailey-Kellogg, et al. "Identification of antibody glycosylation structures that predict monoclonal antibody Fc-effector function." AIDS 28, no. 17 (November 2014): 2523–30. http://dx.doi.org/10.1097/qad.0000000000000444.

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Zhou, Qun, Julie Jaworski, Yanfeng Zhou, Delphine Valente, Joanne Cotton, Denise Honey, Ekaterina Boudanova, et al. "Engineered Fc-glycosylation switch to eliminate antibody effector function." mAbs 12, no. 1 (January 1, 2020): 1814583. http://dx.doi.org/10.1080/19420862.2020.1814583.

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Gao, Rongyuan, Zizhang Sheng, Chithra C. Sreenivasan, Dan Wang, and Feng Li. "Influenza A Virus Antibodies with Antibody-Dependent Cellular Cytotoxicity Function." Viruses 12, no. 3 (March 1, 2020): 276. http://dx.doi.org/10.3390/v12030276.

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Influenza causes millions of cases of hospitalizations annually and remains a public health concern on a global scale. Vaccines are developed and have proven to be the most effective countermeasures against influenza infection. Their efficacy has been largely evaluated by hemagglutinin inhibition (HI) titers exhibited by vaccine-induced neutralizing antibodies, which correlate fairly well with vaccine-conferred protection. Contrarily, non-neutralizing antibodies and their therapeutic potential are less well defined, yet, recent advances in anti-influenza antibody research indicate that non-neutralizing Fc-effector activities, especially antibody-dependent cellular cytotoxicity (ADCC), also serve as a critical mechanism in antibody-mediated anti-influenza host response. Monoclonal antibodies (mAbs) with Fc-effector activities have the potential for prophylactic and therapeutic treatment of influenza infection. Inducing mAbs mediated Fc-effector functions could be a complementary or alternative approach to the existing neutralizing antibody-based prevention and therapy. This review mainly discusses recent advances in Fc-effector functions, especially ADCC and their potential role in influenza countermeasures. Considering the complexity of anti-influenza approaches, future vaccines may need a cocktail of immunogens in order to elicit antibodies with broad-spectrum protection via multiple protective mechanisms.
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Li, Tiezheng, David J. DiLillo, Stylianos Bournazos, John P. Giddens, Jeffrey V. Ravetch, and Lai-Xi Wang. "Modulating IgG effector function by Fc glycan engineering." Proceedings of the National Academy of Sciences 114, no. 13 (March 13, 2017): 3485–90. http://dx.doi.org/10.1073/pnas.1702173114.

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IgG antibodies contain a conserved N-glycosylation site on the Fc domain to which a complex, biantennary glycan is attached. The fine structures of this glycan modulate antibody effector functions by affecting the binding affinity of the Fc to diverse Fc receptor family members. For example, core fucosylation significantly decreases antibody-dependent cellular cytotoxicity (ADCC), whereas terminal α2,6-sialylation plays a critical role in the anti-inflammatory activity of human i.v. immunoglobulin therapy. The effect of specific combinations of sugars in the glycan on ADCC remains to be further addressed, however. Therefore, we synthesized structurally well-defined homogeneous glycoforms of antibodies with different combinations of fucosylation and sialylation and performed side-by-side in vitro FcγR-binding analyses, cell-based ADCC assays, and in vivo IgG-mediated cellular depletion studies. We found that core fucosylation exerted a significant adverse effect on FcγRIIIA binding, in vitro ADCC, and in vivo IgG-mediated cellular depletion, regardless of sialylation status. In contrast, the effect of sialylation on ADCC was dependent on the status of core fucosylation. Sialylation in the context of core fucosylation significantly decreased ADCC in a cell-based assay and suppressed antibody-mediated cell killing in vivo. In contrast, in the absence of fucosylation, sialylation did not adversely impact ADCC.
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Wieland, Andreas, Alice O. Kamphorst, Rajesh M. Valanparambil, Jin-Hwan Han, Xiaojin Xu, Biswa P. Choudhury, and Rafi Ahmed. "Enhancing FcγR-mediated antibody effector function during persistent viral infection." Science Immunology 3, no. 27 (September 21, 2018): eaao3125. http://dx.doi.org/10.1126/sciimmunol.aao3125.

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Persistent viral infections can interfere with FcγR-mediated antibody effector functions by excessive immune complex (IC) formation, resulting in resistance to therapeutic FcγR-dependent antibodies. We and others have previously demonstrated that mice persistently infected with lymphocytic choriomeningitis virus (LCMV) are resistant to a wide range of depleting antibodies due to excessive IC formation. Here, we dissect the mechanisms by which two depleting antibodies overcome the obstacle of endogenous ICs and achieve efficient target cell depletion in persistently infected mice. Efficient antibody-mediated depletion during persistent LCMV infection required increased levels of antibody bound to target cells or use of afucosylated antibodies with increased affinity for FcγRs. Antibodies targeting the highly expressed CD90 antigen or overexpressed human CD20 efficiently depleted their target cells in naïve and persistently infected mice, whereas antibodies directed against less abundant antigens failed to deplete their target cells during persistent LCMV infection. In addition, we demonstrate the superior activity of afucosylated antibodies in the presence of endogenous ICs. We generated afucosylated antibodies directed against CD4 and CD8α, which, in contrast to their parental fucosylated versions, efficiently depleted their respective target cells in persistently infected mice. Efficient antibody-mediated depletion can thus be achieved if therapeutic antibodies can outcompete endogenous ICs for access to FcγRs either by targeting highly expressed antigens or by increased affinity for FcγRs. Our findings have implications for the optimization of therapeutic antibodies and provide strategies to allow efficient FcγR engagement in the presence of competing endogenous ICs in persistent viral infections, autoimmune diseases, and cancer.
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DORAI, HAIMANTI, BARBARA M. MUELLER, RALPH A. REISFELD, and STEPHEN D. GILLIES. "Aglycosylated Chimeric Mouse/Human IgG1 Antibody Retains Some Effector Function." Hybridoma 10, no. 2 (April 1991): 211–17. http://dx.doi.org/10.1089/hyb.1991.10.211.

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Dissertations / Theses on the topic "Antibody Effector Function"

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Mahan, Alison Emilia. "Regulation and Programming of Antibody Effector Function through IgG Glycosylation." Thesis, Harvard University, 2014. http://nrs.harvard.edu/urn-3:HUL.InstRepos:13070040.

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Antibodies are the defining characteristic of the humoral immune response. Their functions are diverse, including direct neutralization of pathogens and recruitment of other immune molecules or cells. While most successful vaccines induce protective neutralizing antibody responses, effective vaccine-elicited neutralizing antibodies against some pathogens, including HIV, HCV, malaria, and TB, remain elusive. Thus, researchers have begun to focus on how vaccines can elicit strong non-neutralizing antibody functions, including recruitment of innate immune factors for antibody-dependent cellular cytotoxicity, complement deposition, and anti\-body-dependent phagocytosis. The antibody's constant region (Fc) mediates most effector functions through isotype and subclass selection or alteration of the structure of the Fc-attached N-glycan, which controls function with exquisite specificity. Glycan modifications are naturally induced during inflammatory conditions such as autoimmune disease and natural infection however, the specific signals that regulate Fc-glycosylation remain unknown. This dissertation sought to understand how antibody glycosylation is regulated and how it can be programmed through vaccination. To do this, we first developed a technique to analyze antibody glycan structures both of bulk Fc and antigen-specific antibodies. Using this technique, we observed significant modulation of antibody glycans during viral infection as well as in vaccine-elicited antibodies. To identify specific signals important for altering the antibody glycan, we transcriptionally profiled stimulated B cells and identified a set of innate and adaptive stimuli that regulate the genes responsible for antibody glycosylation. The results described in this dissertation begin to define the specific mechanism(s) by which infection and vaccination modulate antibody glycosylation to elicit functional antibodies that can ultimately provide effective and sustained protection from infection.
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Barbarino, Verena [Verfasser], Christian [Gutachter] Pallasch, and Marcus [Gutachter] Krüger. "Macrophage-mediated antibody dependent effector function in aggressive B cell lymphoma treatment / Verena Barbarino ; Gutachter: Christian Pallasch, Marcus Krüger." Köln : Universitäts- und Stadtbibliothek Köln, 2021. http://nbn-resolving.de/urn:nbn:de:hbz:38-531485.

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Horne, Phillip Howard. "Activation and effector function of unconventional acute rejection pathways studied in a hepatocellular allograft model." Columbus, Ohio : Ohio State University, 2007. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1188397900.

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Sazinsky, Stephen L. (Stephen Lael). "Engineering aglycosylated antibody variants with immune effector functions." Thesis, Massachusetts Institute of Technology, 2009. http://hdl.handle.net/1721.1/61232.

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Thesis (Ph. D.)--Massachusetts Institute of Technology, Dept. of Biological Engineering, February 2009.
"February 2008." Cataloged from PDF version of thesis.
Includes bibliographical references (p. 110-114).
Monoclonal antibodies have emerged as a promising class of therapeutics for the treatment of human disease, and in particular human cancer. While multiple mechanisms contribute to antibody efficacy, the engagement and activation of immune effector cells - mediated by the interaction of the conserved Fc regions of the antibody with the Fc gamma receptors (Fc[gamma]Rs) on immune cells - is critical to the efficacy of several. This thesis describes the engineering of antibody Fc domain interactions with Fc[gamma]Rs, using the' yeast S. cerevisiae. In an initial step, a microbial system for the production of full-length antibodies in S. cerevisiae in milligram per liter titers has been developed, which serves as a platform for the engineering of antibody Fc domains with defined properties. The presence of a single N-linked glycan on each chain of the antibody Fc, as well as the specific composition of the glycoforms comprising it, are critical to the binding of the Fc to Fc[gamma]Rs, and have largely limited the production of therapeutic antibodies to mammalian expression systems. Using a display system that tethers full-length antibodies on the surface of yeast, we identify and characterize aglycosylated antibody variants that bind a subset of the human low-affinity Fc[gamma]Rs, Fc[gamma]RIIA and Fc'yRIIB, with approximately wildtype binding affinity and activate immune effector functions in vivo. In a separate approach, we identify aglycosylated variants that weakly bind a third low-affinity receptor, Fc[gamma]RIIIA, and through subsequent engineering generate variants that bind all of the low-affinity Fc[gamma]Rs with approximately wild-type binding affinity. By decoupling the function of the antibody from its post-translational processing, these variants have the potential to open up therapeutic antibody production to a far wider array of expression systems than currently available. Finally, in parallel work, we use a similar system to screen for glycosylated Fc variants with improved affinity and specificity for the activating receptor Fc[gamma]RIIIA compared to the inhibitory receptor Fc[gamma]RIIB, properties which have been hypothesized to lead to more potent antibody therapeutics.
by Stephen L. Sazinsky.
Ph.D.
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Kennedy, David M. "The effect of glycation on antibody function." Thesis, University of Newcastle Upon Tyne, 1994. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.262111.

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Fatehchand, Kavin Fatehchand. "Enhancing monocyte effector functions in antibody therapy against cancer." The Ohio State University, 2018. http://rave.ohiolink.edu/etdc/view?acc_num=osu152267295564631.

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Püntener, Ursula. "The role of antibody-dependent cellular effector functions in CNS tumour immunotherapy /." Zürich : ETH, 2008. http://e-collection.ethbib.ethz.ch/show?type=diss&nr=17789.

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Martí, Fernández Iris [Verfasser], and Wolfang [Akademischer Betreuer] Enard. "Antibodies to myelin oligodendrocyte glycoprotein (MOG): Analysis of the impact of the glycosylation site of MOG for recognition of human autoantibodies and dissection of effector functions of the anti-MOG monoclonal antibody 8-18C5 / Iris Martí Fernández ; Betreuer: Wolfang Enard." München : Universitätsbibliothek der Ludwig-Maximilians-Universität, 2020. http://d-nb.info/1227840047/34.

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"Development of N-glycan Specific Plant Produced Antibody Therapeutics for a Fine-tuned Immune Response." Doctoral diss., 2019. http://hdl.handle.net/2286/R.I.53585.

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abstract: Antibodies are naturally occurring proteins that protect a host during infection through direct neutralization and/or recruitment of the innate immune system. Unfortunately, in some infections, antibodies present unique hurdles that must be overcome for a safer and more efficacious antibody-based therapeutic (e.g., antibody dependent viral enhancement (ADE) and inflammatory pathology). This dissertation describes the utilization of plant expression systems to produce N-glycan specific antibody-based therapeutics for Dengue Virus (DENV) and Chikungunya Virus (CHIKV). The Fc region of an antibody interacts with Fcγ Receptors (FcγRs) on immune cells and components of the innate immune system. Each class of immune cells has a distinct action of neutralization (e.g., antibody dependent cell-mediated cytotoxicity (ADCC) and antibody dependent cell-mediated phagocytosis (ADCP)). Therefore, structural alteration of the Fc region results in novel immune pathways of protection. One approach is to modulate the N-glycosylation in the Fc region of the antibody. Of scientific significance, is the plant’s capacity to express human antibodies with homogenous plant and humanized N-glycosylation (WT and GnGn, respectively). This allows to study how specific glycovariants interact with other components of the immune system to clear an infection, producing a tailor-made antibody for distinct diseases. In the first section, plant-produced glycovariants were explored for reduced interactions with specific FcγRs for the overall reduction in ADE for DENV infections. The results demonstrate a reduction in ADE of our plant-produced monoclonal antibodies in in vitro experiments, which led to a greater survival in vivo of immunodeficient mice challenged with lethal doses of DENV and a sub-lethal dose of DENV in ADE conditions. In the second section, plant-produced glycovariants were explored for increased interaction with specific FcγRs to improve ADCC in the treatment of the highly inflammatory CHIKV. The results demonstrate an increase ADCC activity in in vitro experiments and a reduction in CHIKV-associated inflammation in in vivo mouse models. Overall, the significance of this dissertation is that it can provide a treatment for DENV and CHIKV; but equally importantly, give insight to the role of N-glycosylation in antibody effector functions, which has a broader implication for therapeutic development for other viral infections.
Dissertation/Thesis
Doctoral Dissertation Molecular and Cellular Biology 2019
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Jung, Sang Taek. "Engineering of aglycosylated antibody Fc for effector functions." Thesis, 2009. http://hdl.handle.net/2152/23494.

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The antibody Fc region is critical for the therapeutic potency by virtue of its role in recruiting and activating the cytotoxic pathways of immune cells, complement activation and its role in antibody homeostasis (a process mediated by the pH dependent binding to the neonatal receptor FcRn). Bacterially produced antibodies lack of glycosylation at Asn297 and therefore do not bind to the surface Fc[gamma]Rs on effector innate immune cells, nor can they activate complement. This dissertation describes the engineering of aglycosylated bacterially expressed antibodies for binding to a specific Fc[gamma]R and therefore eliciting therapeutically relevant effector functions. Aglycosylated Fc mutants that bind to desired Fc binding ligands were isolated by a new E. coli homodimeric Fc display system coupled with high throughput flow cytometry. Two amino acids mutation in the CH3 domain (Fc5) conferred selectively high binding affinity of aglycosylated Fc domains to the Fc[gamma]RI receptor. Flow cytometry screening from a randomized Fc5 library resulted in the isolation of Fc mutants exhibiting higher affinity binding to Fc[gamma]RI receptor than the Fc5. Aglycosylated Fc[gamma]RI specific IgG containing the variable regions of the clinically important anti-Her2 antibody trastuzumab elicited dendritic cell-mediated ADCC in sharp contrast to the clinical grade trastuzumab (Herceptin) or the glycosylated coutreparts of the engineered antibodies, neither of which could potentiate target cell lysis with dendritic cells as effectors. In separate studies, a system was developed for the screening of periplasmically anchored E. coli libraries and the isolation of clones expressing antibodies that are specific to insoluble antigens or to cell surface markers. Following three rounds of flow cytometric screening, spheroplasts expressing specific scFvs were enriched 950-fold from a large excess (1,000x) of spheroplasts expressing nonspecific antibodies.
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Books on the topic "Antibody Effector Function"

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Josephs, Debra H., Heather J. Bax, Giulia Pellizzari, James F. Spicer, Ana Montes, and Sophia N. Karagiannis. Antibody Therapeutics for Ovarian Carcinoma and Translation to the Clinic. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780190248208.003.0001.

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Despite improvements over the past decade in the treatment of ovarian cancer, many patients are at risk of recurrent disease and emerging drug resistance. The increased selectivity and reduced toxicity of molecularly targeted anti-cancer agents renders them attractive for development in ovarian cancer, and monoclonal antibodies targeting ovarian cancer-specific tumor antigens represent the largest such group investigated in this clinical setting. This chapter describes examples of monoclonal antibodies clinically evaluated for efficacy in ovarian cancer. These agents recognize molecular targets expressed on tumors or within tumor microenvironments that may be essential for tumor cell survival and proliferation. Recently, antibodies targeting checkpoint molecules on immune cells have shown efficacy in modulating anti-tumor immunity, and applications in ovarian carcinomas are evaluated. The chapter focuses on therapeutic agents’ attributes on targeting key cancer growth and progression pathways, and propensity to engender effector functions by activating immune effector cells in tumors and the circulation.
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Isaacs, John D., and Philip M. Brown. Rituximab and abatacept. Oxford University Press, 2013. http://dx.doi.org/10.1093/med/9780199642489.003.0083.

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Two biologics that target cells have been licensed to treat rheumatoid arthritis (RA). Rituximab is a chimeric monoclonal antibody (mAb) against CD20 that depletes B cells; abatacept is a soluble form of CTLA-4 that blocks costimulation and interferes with T-cell function. Both drugs alleviate signs and symptoms of RA and have been shown to retard radiographic progression. Rituximab is licensed for use following failure of tumour necrosis factor (TNF) blockade whereas abatacept's licence permits it use as a first-line biologic. In the United Kingdom, however, the National Institute for Health and Clinical Excellence (NICE) restricts the use of abatacept to patients who develop adverse effects with rituximab or in whom rituximab is contraindicated. As with other biologics, the use of either drug is associated with an enhanced risk of serious infections; additionally, rituximab in particular can cause infusion reactions, requiring prophylaxis. By targeting cells that are central to RA pathogenesis, these drugs provide important additional therapeutic options for patients with RA.
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Book chapters on the topic "Antibody Effector Function"

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Derer, Stefanie, Christian Kellner, Sven Berger, Thomas Valerius, and Matthias Peipp. "Fc Engineering: Design, Expression, and Functional Characterization of Antibody Variants with Improved Effector Function." In Antibody Engineering, 519–36. Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-61779-974-7_30.

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Ratner, Anna, and William R. Clark. "Derivatization of Cells with Antibody." In Cytotoxic Cells: Recognition, Effector Function, Generation, and Methods, 487. Boston, MA: Birkhäuser Boston, 1993. http://dx.doi.org/10.1007/978-1-4684-6814-4_51.

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Ratner, Anna, and William R. Clark. "Stimulation of CTL on Antibody-Coated Plates." In Cytotoxic Cells: Recognition, Effector Function, Generation, and Methods, 497. Boston, MA: Birkhäuser Boston, 1993. http://dx.doi.org/10.1007/978-1-4684-6814-4_56.

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Shinohara, Nobukata. "Antigen-Specific Suppression of Antibody Responses by Class II MHC-Restricted CTL." In Cytotoxic Cells: Recognition, Effector Function, Generation, and Methods, 378–83. Boston, MA: Birkhäuser Boston, 1993. http://dx.doi.org/10.1007/978-1-4684-6814-4_37.

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Vazquez-Lombardi, Rodrigo, Damien Nevoltris, Romain Rouet, and Daniel Christ. "Expression of IgG Monoclonals with Engineered Immune Effector Functions." In Antibody Engineering, 313–34. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-8648-4_16.

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Otz, Tina. "Determination of Fc-Mediated Antibody-Effector Functions by Chromium Release Assay." In Antibody Engineering, 749–63. Berlin, Heidelberg: Springer Berlin Heidelberg, 2010. http://dx.doi.org/10.1007/978-3-642-01144-3_49.

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Li, Chao, Tiezheng Li, and Lai-Xi Wang. "Chemoenzymatic Defucosylation of Therapeutic Antibodies for Enhanced Effector Functions Using Bacterial α-Fucosidases." In Antibody Engineering, 367–80. New York, NY: Springer New York, 2018. http://dx.doi.org/10.1007/978-1-4939-8648-4_19.

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Raju, T. Shantha. "Impact of Fc Glycosylation on Monoclonal Antibody Effector Functions and Degradation by Proteases." In Current Trends in Monoclonal Antibody Development and Manufacturing, 249–69. New York, NY: Springer New York, 2009. http://dx.doi.org/10.1007/978-0-387-76643-0_15.

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Akers, Donald L., David J. Lefer, I. Li Chen, Robert G. Wilkens, Janet Rice, Harmeet Aurora, Thomas A. Osgood, et al. "Effect of short-term treatment with a monoclonal antibody to P-selectin on balloon catheter-induced: Intimal hyperplasia, re-endothelialization, and attenuation of endothelial-dependent relaxation." In The Cellular Basis of Cardiovascular Function in Health and Disease, 13–20. Boston, MA: Springer US, 1997. http://dx.doi.org/10.1007/978-1-4615-5765-4_2.

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Burton, Dennis R., and Jenny M. Woof. "Human Antibody Effector Function." In Advances in Immunology Volume 51, 1–84. Elsevier, 1992. http://dx.doi.org/10.1016/s0065-2776(08)60486-1.

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Conference papers on the topic "Antibody Effector Function"

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Klein, Christian. "Abstract IA07: Enhancing immune effector function via antibody engineering." In Abstracts: AACR Special Conference: Tumor Immunology and Immunotherapy: A New Chapter; December 1-4, 2014; Orlando, FL. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/2326-6074.tumimm14-ia07.

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Alley, Stephen C., Django R. Sussman, Scott C. Jeffrey, Lindsay Torrey, Patrick J. Burke, Jocelyn Setter, Brian Gfeller, et al. "Abstract 4395: SEA technology: A novel strategy for enhancing antibody effector function." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-4395.

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Alley, Stephen C., Django R. Sussman, Scott C. Jeffrey, Lindsay Torrey, Patrick J. Burke, Kerry Klussman, Nicole M. Okeley, Peter D. Senter, and Dennis R. Benjamin. "Abstract B133: SEA technology: A novel strategy for enhancing antibody effector function." In Abstracts: AACR-NCI-EORTC International Conference: Molecular Targets and Cancer Therapeutics--Nov 15-19, 2009; Boston, MA. American Association for Cancer Research, 2009. http://dx.doi.org/10.1158/1535-7163.targ-09-b133.

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Smith, Alyson, Weiping Zeng, Bryan Grogan, Jane Haass, Amber Blackmarr, Scott Peterson, and Shyra J. Gardai. "Abstract 4986: TIGIT directed human antibody modulates T-regulatory and effector cell function." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-4986.

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Smith, Alyson, Weiping Zeng, Bryan Grogan, Jane Haass, Amber Blackmarr, Scott Peterson, and Shyra J. Gardai. "Abstract 4986: TIGIT directed human antibody modulates T-regulatory and effector cell function." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-4986.

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Hwang, Mun Kyung, Anlai Wang, Zhili Song, Shujia Dai, Bailin Zhang, Joachim Theilhaber, Lily Pao, Dmitri Wiederschain, and Chen Zhu. "Abstract 1632: Antibody mediated crosslinking of CD38 triggers costimulatory signaling and promotes T cell effector function." In Proceedings: AACR Annual Meeting 2021; April 10-15, 2021 and May 17-21, 2021; Philadelphia, PA. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1538-7445.am2021-1632.

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Cheng, Zhi-Jie Jey, Denise Garvin, Rich Moravec, Aileen Paguio, Frank Fan, and Teresa Surowy. "Abstract 5523: Measuring the Fc effector function of therapeutic antibody in antibody-dependent cell-mediated cytotoxicity using a bioluminescent cell-based reporter bioassay." In Proceedings: AACR 104th Annual Meeting 2013; Apr 6-10, 2013; Washington, DC. American Association for Cancer Research, 2013. http://dx.doi.org/10.1158/1538-7445.am2013-5523.

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Ritthipichai, Krit, Marcus Machin, Maria Fardis, and Cecile Chartier. "Abstract LB-110: Anti-OX40 agonistic antibody enhancesex vivoCD8+TIL expansion with increased T-cell effector function." In Proceedings: AACR Annual Meeting 2018; April 14-18, 2018; Chicago, IL. American Association for Cancer Research, 2018. http://dx.doi.org/10.1158/1538-7445.am2018-lb-110.

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Pernasetti, Flavia, Shu-Hui Liu, Gu Yin, Bernadette Pascual, Zhengming Yan, Max Hallin, Rolla Yafawi, et al. "Abstract 2649: Fc-effector function activity of the CXCR4 IgG1 antibody PF-06747143: a novel clinical candidate for the treatment of hematologic malignancies." In Proceedings: AACR Annual Meeting 2017; April 1-5, 2017; Washington, DC. American Association for Cancer Research, 2017. http://dx.doi.org/10.1158/1538-7445.am2017-2649.

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Bougherara, Houcine, Fariba Némati, Christophe De Romeuf, Jean-Marc Barret, Gérald Massonnet, Marie-Aude Le Frère-Belda, Jean-François Prost, Didier Decaudin, and Emmanuel Donnadieu. "Abstract A01: Ex vivo evaluation of an anti-Müllerian hormone type II receptor humanized antibody with optimized Fc effector function in ovarian cancer." In Abstracts: AACR Special Conference: Tumor Immunology and Immunotherapy: A New Chapter; December 1-4, 2014; Orlando, FL. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/2326-6074.tumimm14-a01.

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