IgG Fc engineering to modulate antibody effector functions

Fcγ receptors as regulators of immune responses

Nimmerjahn, F., & Ravetch, J. V. (2008) · Nature Reviews Immunology · doi:10.1038/nri2206 · Cited by 2,947

FcRn: the neonatal Fc receptor comes of age

Roopenian, D. C., & Akilesh, S. (2007) · Nature Reviews Immunology · doi:10.1038/nri2155 · Cited by 2,346

Therapeutic activity of humanized anti-CD20 monoclonal antibody and polymorphism in IgG Fc receptor FcγRIIIa gene

Cartron, G., Dacheux, L., Salles, G. A., Solal‐Céligny, P., BARDOS, P., Colombat, P., & Watier, H. (2002) · Blood · doi:10.1182/blood.v99.3.754 · Cited by 1,954

Lack of Fucose on Human IgG1 N-Linked Oligosaccharide Improves Binding to Human FcγRIII and Antibody-dependent Cellular Toxicity

Shields, R. L., Lai, J., Keck, R., O'Connell, L. Y., Hong, K., Meng, Y. G., Weikert, S. H. A., & Presta, L. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202069200 · Cited by 1,835

The Absence of Fucose but Not the Presence of Galactose or Bisecting N-Acetylglucosamine of Human IgG1 Complex-type Oligosaccharides Shows the Critical Role of Enhancing Antibody-dependent Cellular Cytotoxicity

Shinkawa, T., Nakamura, K., Yamane, N., Shoji-Hosaka, E., Kanda, Y., Sakurada, M., Uchida, K., Anazawa, H., Satoh, M., Yamasaki, M., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210665200 · Cited by 1,413

The therapeutic monoclonal antibody market

Ecker, D. M., Jones, S. D., & Levine, H. L. (2014) · mAbs · doi:10.4161/19420862.2015.989042 · Cited by 1,369

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

Shields, R. L., Namenuk, A. K., Hong, K., Meng, Y. G., Rae, J., Briggs, J. B., Xie, D., Lai, J., Stadlen, A., Li, B., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009483200 · Cited by 1,172

Potent antibody therapeutics by design

Carter, P. J. (2006) · Nature reviews. Immunology · doi:10.1038/nri1837 · Cited by 1,124

THE COVALENT STRUCTURE OF AN ENTIRE γG IMMUNOGLOBULIN MOLECULE

Edelman, G. M., Cunningham, B. A., Gall, W. E., Gottlieb, P. D., Rutishauser, U. S., & Waxdal, M. J. (1969) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.63.1.78 · Cited by 903

Engineered antibody Fc variants with enhanced effector function

Lazar, G. A., Dang, W., Karki, S., Vafa, O., Peng, J. S., Hyun, L., Chan, C. S. C., Chung, H. S., Eivazi, A., Yoder, S. C., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508123103 · Cited by 824

Cadonilimab plus chemotherapy as first-line treatment for persistent, recurrent, or metastatic cervical cancer: a cost-effectiveness analysis

Xiang, Z., Li, Z., Chen, X., & Fu, Y. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1562875 · Cited by 8

Development of a novel reporter gene assay to evaluate antibody-dependent cellular phagocytosis for anti-CD20 therapeutic antibodies

Liu, C., Yu, C., Yang, Y., Huang, J., Yu, X., Duan, M., Wang, L., & Wang, J. (2021) · International Immunopharmacology · doi:10.1016/j.intimp.2021.108112 · Cited by 8

Vaccinal antibodies: Fc antibody engineering to improve the antiviral antibody response and induce vaccine-like effects

Nawab, D. H. (2021) · Human Vaccines & Immunotherapeutics · doi:10.1080/21645515.2021.1985891 · Cited by 9

Research Progress of Antibody–Drug Conjugate Therapy for Advanced Gastric Cancer

Wang, N., Mei, Q., Wang, Z., Zhao, L., Zhang, D., Liao, D., Zuo, J., Xie, H., Jia, Y., & Kong, F. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.889017 · Cited by 9

Complement Activation by an Anti-Dengue/Zika Antibody with Impaired Fcγ Receptor Binding Provides Strong Efficacy and Abrogates Risk of Antibody-Dependent Enhancement

Sampei, Z., Koo, C. X., Teo, F. J., Toh, Y. X., Fukuzawa, T., Gan, S. W., Nambu, T., Ho, A. W. S., Honda, K., Igawa, T., et al. (2023) · Antibodies · doi:10.3390/antib12020036 · Cited by 7

An intravenous DNA-binding priming agent protects cell-free DNA and improves the sensitivity of liquid biopsiesPreprint

Tabrizi, S., Martin-Alonso, C., Xiong, K., Blewett, T., Sridhar, S., An, Z., Patel, S., Rodriguez‐Aponte, S. A., Naranjo, C. A., Wang, S., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.01.13.523947 · Cited by 6

Precision engineering of antibodies: A review of modification and design in the Fab region

Wang, S. A., Li, Y., Mei, J., Wu, S., Ying, G., & Yi, Y. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.133730 · Cited by 7

CD22 modulation alleviates amyloid β-induced neuroinflammation

Mai, Y. D., Zhang, Q., Fung, C. L., Leung, S. O., & Chong, C. H. (2025) · Journal of Neuroinflammation · doi:10.1186/s12974-025-03361-2 · Cited by 7

Cetuximab increases LGR5 expression and augments LGR5-targeting antibody-drug conjugate efficacy in patient-derived colorectal cancer models

High, P. C., Liang, Z., Guernsey-Biddle, C., Subramanian, S., Shyu, Y.-M., Aldana, A. M., Toh, Y., & Carmon, K. S. (2025) · Cell Reports Medicine · doi:10.1016/j.xcrm.2025.102363 · Cited by 10

Selective decoupling of IgG1 binding to viral Fc receptors restores antibody-mediated NK cell activation against HCMV

Qerqez, A. N., Hoffmann, K., Lee, A. G., Pareek, S., Hager, K., Mishra, A. K., Delidakis, G., Bentley, K., Kerr-Jones, L. E., Cabrera, M., et al. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.116593 · Cited by 7

Computation-Aided Design of Albumin Affibody-Inserted Antibody Fragment for the Prolonged Serum Half-Life

Kwon, N. H., Lee, J. H., & Kwon, I. (2022) · Pharmaceutics · doi:10.3390/pharmaceutics14091769 · Cited by 7

High-fidelity large-diversity monoclonal mammalian cell libraries by cell cycle arrested recombinase-mediated cassette exchange

Chen, C., Wang, Z., Kang, M., Lee, K. B., & Ge, X. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad1001 · Cited by 7

Using IMGT unique numbering for IG allotypes and Fc‐engineered variants of effector properties and half‐life of therapeutic antibodies

Lefranc, M., & Lefranc, G. (2024) · Immunological Reviews · doi:10.1111/imr.13399 · Cited by 7

Screening Strategies for the Discovery of Ion Channel Monoclonal Antibodies

Colley, C. S., England, E., Linley, J. E., & Wilkinson, T. C. I. (2018) · Current Protocols in Pharmacology · doi:10.1002/cpph.44 · Cited by 8

Binding affinities of human IgG1 and chimerized pig and rabbit derivatives to human, pig and rabbit Fc gamma receptor IIIA

Bhatti, M. M., Cai, A. G., & Theunissen, J.-W. F. (2019) · PLoS ONE · doi:10.1371/journal.pone.0219999 · Cited by 7

Communication pathways bridge local and global conformations in an IgG4 antibody

Tarenzi, T., Rigoli, M., & Potestio, R. (2021) · Scientific Reports · doi:10.1038/s41598-021-02323-x · Cited by 6

Introduction of a Capillary Gel Electrophoresis-Based Workflow for Biotherapeutics Characterization: Size, Charge, and N-Glycosylation Variant Analysis of Bamlanivimab, an Anti-SARS-CoV-2 Product

Szabo, M., Sárközy, D., Szigeti, M., Farsang, R., Kardos, Z., Kozma, Á., Csánky, E., Chung, D. S., Szekanecz, Z., & Guttman, A. (2022) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2022.839374 · Cited by 7

Rhamnose modified antibodies show improved immune killing towards EGFR-positive solid tumor cells

Hong, H., Zhao, J. J., Zhou, K., Li, Y., Li, D., & Wu, Z. (2024) · Carbohydrate Research · doi:10.1016/j.carres.2024.109038 · Cited by 7

Removal of Fc Glycans from [89Zr]Zr-DFO-Anti-CD8 Prevents Peripheral Depletion of CD8+ T Cells

White, J. M., Keinänen, O. M., Cook, B. E., Zeglis, B. M., Gibson, H. M., & Viola, N. T. (2020) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.0c00270 · Cited by 7

Taking the Hinge off: An Approach to Effector-Less Monoclonal Antibodies

Valeich, J. E., Boyd, D., Kanwar, M., Stenzel, D., Ghosh, D. D., Ebrahimi, A., Woo, J., Wang, J., & Ambrogelly, A. (2020) · Antibodies · doi:10.3390/antib9040050 · Cited by 7

Generation and characterization of iPSC‐derived microglia for in vitro modeling of stimuli‐specific neuroimmune responses

Haskell, A. K., Kulas, J. A., Carter, W., Javens‐Wolfe, J., Hinkel, R. D., Moussaif, M., Smiley, J. S., Lazaro, O., Robertson, S., Palkowitz, A. D., et al. (2026) · Alzheimer s & Dementia · doi:10.1002/alz.71117 · Cited by 6

Receptor transfer between immune cells by autoantibody-enhanced, CD32-driven trogocytosis is hijacked by HIV-1 to infect resting CD4 T cells

Albanese, M., Chen, H., Gapp, M., Muenchhoff, M., Yang, H.-H., Peterhoff, D., Hoffmann, K., Xiao, Q., Ruhle, A., Ambiel, I., et al. (2024) · Cell Reports Medicine · doi:10.1016/j.xcrm.2024.101483 · Cited by 7

Whole-canine neutralizing antibodies generated by single B cell antibody technology elicit therapeutic protection against canine distemper virus infection

Shi, P., Wang, Z., Sheng, W., Wang, Z., Wang, S., Zhang, C., Zhao, L., Zou, J., & Zhou, H. (2025) · Veterinary Microbiology · doi:10.1016/j.vetmic.2025.110412 · Cited by 6

The Epitope-Specific Anti-human CD4 Antibody MAX.16H5 and Its Role in Immune Tolerance

Stahl, L., Dünkel, A., Hilger, N., Tretbar, S., & Fricke, S. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01035 · Cited by 6

Utilizing PK and PD Biomarkers to Guide the First-in-Human Starting Dose Selection of MTBT1466A: A Novel Humanized Monoclonal Anti-TGFβ3 Antibody for the Treatment of Fibrotic Diseases

Yadav, R., Sukumaran, S., Lutman, J., Mitra, M. S., Halpern, W., Sun, T., Setiadi, A., Neighbors, M., Sheng, X. R., Yip, V., et al. (2023) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2023.07.005 · Cited by 6

Virus-Like Particle-Mediated Vaccination against Interleukin-13 May Harbour General Anti-Allergic Potential beyond Atopic Dermatitis

Foerster, J., & Molęda, A. (2020) · Viruses · doi:10.3390/v12040438 · Cited by 6

Innovative Preparation of Biopharmaceuticals Using Transglycosylation Activity of Microbial Endoglycosidases

Katoh, T., & Yamamoto, K. (2021) · Journal of Applied Glycoscience · doi:10.5458/jag.jag.jag-2020_0013 · Cited by 6

Structural Study on the Impact of S239D/I332E Mutations in the Binding of Fc and FcγRIIIa

Jebamani, P., Sriramulu, D. K., Jung, S. T., & Lee, S. (2021) · Biotechnology and Bioprocess Engineering · doi:10.1007/s12257-021-0024-2 · Cited by 6

Perspectives of the Danger/Injury Model of Immunology as Applied to Antigen-Related Human Disorders

Land, W. G. (2023) · Springer eBooks · doi:10.1007/978-3-031-21776-0_1 · Cited by 7

A structural perspective on the design of decoy immune modulators

Lankipalli, S., & Ramagopal, U. A. (2021) · Pharmacological Research · doi:10.1016/j.phrs.2021.105735 · Cited by 6

A Perspective on the CD47-SIRPA Axis in High-Risk Neuroblastoma

Tang, X. X., Shimada, H., & Ikegaki, N. (2024) · Current Oncology · doi:10.3390/curroncol31060243 · Cited by 5

Growth Factors and Cytokines for Regenerative Medicine: Translational Challenges and Emerging Engineering Solutions

Mohammadi, A., Heydari, M. A., & Jamalpoor, Z. (2025) · Regenerative Engineering and Translational Medicine · doi:10.1007/s40883-025-00458-1 · Cited by 5

Systematic Analysis of the Expression and Prognosis of Fcγ Receptors in Clear Cell Renal Cell Carcinoma

Nie, W., Yao, Y., Luo, B., Zhu, J., Li, S., Yang, X., Luo, T., Liu, W., & Shibing, Y. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.755936 · Cited by 5

Chemoenzymatic Synthesis of a Rhamnose‐Functionalized Bispecific Nanobody as a Bispecific Antibody Mimic for Cancer Immunotherapy

Hong, H., Han, L., Li, D., Gong, L., Zhou, K., Li, Y., Yu, H., Zhao, K., Shi, J., Zhou, Z., et al. (2022) · Angewandte Chemie · doi:10.1002/ange.202208773 · Cited by 5

Matrixed CDR grafting: A neoclassical framework for antibody humanization and developability

Gupta, P., Horspool, A. M., Trivedi, G., Moretti, G., Datar, A., Huang, Z.-F., Chiecko, J., Kenny, C. H., & Marlow, M. S. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.105555 · Cited by 6

FcγRIIB (CD32B) antibodies enhance immune responses through activating FcγRs

Simpson, A. P., Oldham, R. J., Cox, K. L., Taylor, M. C., James, S., White, A. L., Bogdanov, Y. D., Glennie, M. J., Frendéus, B., Cragg, M. S., et al. (2025) · Clinical & Experimental Immunology · doi:10.1093/cei/uxaf015 · Cited by 5

Human IgG1 Fc pH-dependent optimization from a constant pH molecular dynamics simulation analysis

Lim, Y. Y., Lim, T. S., & Choong, Y. S. (2020) · RSC Advances · doi:10.1039/c9ra10712f · Cited by 5

Identification, Efficacy, and Stability Evaluation of Succinimide Modification With a High Abundance in the Framework Region of Golimumab

Liu, T., Xu, J., Guo, Q., Zhang, D., Li, J., Qian, W., Guo, H., Zhou, X., & Hou, S. (2022) · Frontiers in Chemistry · doi:10.3389/fchem.2022.826923 · Cited by 7

The application of antibody-based agents in cancer therapy based on their mechanisms of action

Qian, K., Li, G., Zhang, S., Zou, Y., Ai, H., Zheng, X., Fu, W., Lei, C., & Hu, S. (2024) · Fundamental Research · doi:10.1016/j.fmre.2024.02.021 · Cited by 6

Mapping affinity and allostery in human IgG antibody Fc region-Fc γ receptor interactionsPreprint

Keith, A. D., Xu, T., Chernova, T. A., Keen, M. M., Bogacz, M., Nedeljković, M., Flowers, M. W., Brown, T. J., Frank, F., Ortlund, E. A., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.03.28.645945 · Cited by 5

Genetically engineered IgG1 and nanobody oligomers acquire strong intrinsic CD40 agonism

Hesen, N. A., Anany, M. A., Freidel, A., Baker, M., Siegmund, D., Zaitseva, O., Wajant, H., & Lang, I. (2024) · Bioengineered · doi:10.1080/21655979.2024.2302246 · Cited by 4

Adebrelimab in Small Cell Lung Cancer: From Current Advances to Emerging Combination Strategy and Challenge

Yang, H., Yang, L., Liu, Y., & Wang, L. (2025) · Biologics · doi:10.2147/btt.s500470 · Cited by 4

Cytokine Engineering Approaches for Regenerative Medicine

Li, S., You, W., & Martino, M. M. (2025) · Advanced Therapeutics · doi:10.1002/adtp.202500103 · Cited by 5

Engineering strategies of Anti-HIV antibody therapeutics in clinical development

Pihlstrom, N. L., & Bournazos, S. (2023) · Current Opinion in HIV and AIDS · doi:10.1097/coh.0000000000000796 · Cited by 4

Fc engineering by monoclonal mammalian cell display for improved affinity and selectivity towards FcγRs

Wang, Z., Kang, M., Ebrahimpour, A., Chen, C., & Ge, X. (2024) · Antibody Therapeutics · doi:10.1093/abt/tbae017 · Cited by 4

In Situ Self‐Assembly of Antibody‐Rhamnose Complex as a Pre‐Targeting Strategy for Enhanced Cancer Immunotherapy

Hong, H., Zhou, K., Han, L. G., Li, Y., & Wu, Z. (2024) · Chemistry - A European Journal · doi:10.1002/chem.202403539 · Cited by 4

Chapter 1: Monoclonal Antibodies: Structure, Physicochemical Stability, and Protein Engineering

Mills, B. J., Moussa, E. M., & Jameel, F. (2020) · AAPS advances in the pharmaceutical sciences series · doi:10.1007/978-3-030-31415-6_1 · Cited by 4

Introduction to Antibody–Drug Conjugates

Lambert, J. M., & van Delft, F. L. (2021) · Royal Society of Chemistry eBooks · doi:10.1039/9781839165153-00001 · Cited by 4

A Novel Fc-Engineered Anti-HER2 Bispecific Antibody With Enhanced Antitumor Activity

Mohammadi, M., Jeddi‐Tehrani, M., Golsaz‐Shirazi, F., Arjmand, M., Torkashvand, F., Bahadori, T., Judaki, M. A., Shiravi, F., Zare, H. A., Haghighat, F. N., et al. (2023) · Journal of Immunotherapy · doi:10.1097/cji.0000000000000464 · Cited by 4

Stellabody: A novel hexamer‐promoting mutation for improved IgG potency

Whitehead, C. A., Wines, B. D., Davies, A. M., McDonnell, J. M., Trist, H. M., Esparon, S. E., & Hogarth, P. M. (2024) · Immunological Reviews · doi:10.1111/imr.13400 · Cited by 4

Factor VIII-Fc Activates Natural Killer Cells via Fc-Mediated Interactions With CD16

Lagassé, H. A. D., Hopkins, L., Jankowski, W., Jacquemin, M. G., Sauna, Z. E., & Golding, B. (2021) · Frontiers in Immunology · doi:10.3389/fimmu.2021.692157 · Cited by 4

Tuning antibody stability and function by rational designs of framework mutations

Ng, J. C.-F., Chenoweth, A. M., Sciscio, M. L. D., Grandits, M., Cheung, A., Chu, T., McCraw, A. J., Chauhan, J., Liu, Y., Guo, D., et al. (2025) · mAbs · doi:10.1080/19420862.2025.2532117 · Cited by 5

Enhancement of Protein–Protein Interactions by Destabilizing Mutations Revealed by HDX-MS

Hamuro, Y., Armstrong, A., Branson, J. D., Wu, S., Huang, R. Y. ‐., & Jacobs, S. (2025) · Biomolecules · doi:10.3390/biom15081201 · Cited by 3

Simple endoglycosidase-assisted peptide mapping workflow for characterizing non-consensus n-glycosylation in therapeutic monoclonal antibodies

Zhong, J., Huang, M., Qiu, H., Seol, H., Yan, Y., Wang, S., & Li, N. (2024) · Journal of Pharmaceutical Sciences · doi:10.1016/j.xphs.2024.11.024 · Cited by 3

Resistance to Antibody-Drug Conjugate

Hochberg, J. C., & Alexander, S. W. (2019) · Resistance to targeted anti-cancer therapeutics · doi:10.1007/978-3-030-24424-8_3 · Cited by 3

Strategies to evaluate potential effector function of glycan variants: A case study of ordesekimab (AMG 714 or PRV-015)

Wei, Y.-L., Wegesser, T. C., Kuhns, S. T., Werner, J. A., Lebrec, H. N., & Wang, X. (2022) · Journal of Immunotoxicology · doi:10.1080/1547691x.2022.2113841 · Cited by 3

High-Throughput Glycan Profiling of Human Serum IgG Subclasses Using Parallel Reaction Monitoring Peptide Bond Fragmentation of Glycopeptides and Microflow LC-MS

Zhao, Y., Raidas, S., Mao, Y., & Li, N. (2024) · Journal of Proteome Research · doi:10.1021/acs.jproteome.3c00311 · Cited by 3

Development and characterization of DIA 12.3, a fully human intact anti-CEACAM1 monoclonal antibody

Centonze, M., Fiori, V., Kujawski, M., Li, L., Wong, P. W., Williams, L., Mambro, T. D., Dominici, S., Sparti, A., Shively, J. E., et al. (2024) · PLoS ONE · doi:10.1371/journal.pone.0295345 · Cited by 3

Striking the Balance with a PD-L1×4–1BB Bispecific Antibody

Ha, J., Grippin, A., Kim, B. Y. S., & Jiang, W. (2024) · Cancer Research · doi:10.1158/0008-5472.can-24-0566 · Cited by 3

Viral Vectors for Treatment of Human Disease: Therapeutic and Manufacturing Challenges

Diallo, J. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-814470-1.00007-1 · Cited by 3

Synthetically Useful Glycosyltransferases for the Access of Mammalian Glycomes

Guan, W., Edmunds, G. A., Wu, Z., & Li, L. (2019) · Royal Society of Chemistry eBooks · doi:10.1039/9781788016575-00046 · Cited by 3

Coronavirus Pandemic: Treatment and Future Prevention

Lundstrom, K. H. (2020) · Future Microbiology · doi:10.2217/fmb-2020-0174 · Cited by 4

BMFPs, a versatile therapeutic tool for redirecting a preexisting Epstein-Barr virus antibody response toward defined target cells

Gamain, B., Brousse, C., Rainey, N. E., Diallo, B., Paquereau, C.-E., Desrames, A., Ceputyte, J., Semblat, J., Bertrand, O., Gangnard, S., et al. (2022) · Science Advances · doi:10.1126/sciadv.abl4363 · Cited by 3

NHDL, a recombinant V L /V H hybrid antibody control for IgG2/4 antibodies

Lau, C., McAdam, M. B., Bergseth, G., Grevys, A., Bruun, J., Ludviksen, J. K., Fure, H., Espevik, T., Moen, A. R., Andersen, J. T., et al. (2019) · mAbs · doi:10.1080/19420862.2019.1686319 · Cited by 3

Engineering Antibody‐Based Therapeutics: Progress and Opportunities

Nguyen, A. W., & Maynard, J. A. (2021) · Wiley eBooks · doi:10.1002/9783527815128.ch13 · Cited by 4

Human anti-ACE2 monoclonal antibodies as pan-sarbecovirus prophylactic agentsPreprint

Zhang, F., Jenkins, J., de Carvalho, R. A., Nakandakari-Higa, S., Chen, T., Abernathy, M. E., Nyakatura, E. K., Andrew, D. P., Lebedeva, I., Lorenz, I. C., et al. (2022) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2022.08.24.505169 · Cited by 3

Engineering an Fc-inert feline IgG1 by targeted mutations: Application to anti-PD-1 antibody development

Nishibori, S., Takeda, Y., Igase, M., & Mizuno, T. (2025) · Veterinary Immunology and Immunopathology · doi:10.1016/j.vetimm.2025.111000 · Cited by 2

Industry Perspective on Nonclinical Approaches for Hepatotoxicity Risk Assessment: Insights from Two Longitudinal Surveys Conducted in 2023 and 2017

Sakatis, M. Z., Norona, L. M., Karmel, J., Proctor, W. R., Sarr, F. H., Rana, P., Zane, D., Rae, J. M. C., Faber, S. C., Ravindra, K. C., et al. (2025) · Chemical Research in Toxicology · doi:10.1021/acs.chemrestox.5c00235 · Cited by 2

Fucosylation limits ADCC in clinically used anti‐ RhD monoclonal antibodies

Koike, G., Bondt, A., Schulte, D., Leuvenink, R. W., Mons, D. J., Ligthart, P. C., Verweij, E. J. T., Heck, A. J. R., van der Schoot, C. E., & Vidarsson, G. (2025) · Transfusion · doi:10.1111/trf.18449 · Cited by 2

AbDrop-a scalable microfluidics-enabled platform for rapid discovery and functional analysis of plasma cell-derived antibodies

Meng, Y., Wang, L., Yang, Y., Su, L., Ge, Y., Xi, H., Lin, S., Chen, Y., Liu, W., Wang, W., et al. (2025) · mAbs · doi:10.1080/19420862.2025.2597610 · Cited by 2

Evolution of Immune Checkpoint Blockade in Metastatic NSCLC: A Narrative Review of Emerging Bispecific Antibodies and the Practical Challenges of Clinical Integration

Kang, J. H. (2026) · Cancers · doi:10.3390/cancers18040709 · Cited by 2

Model acetylcholinesterase‐Fc fusion glycoprotein biotechnology system for the manufacture of an organophosphorus toxicant bioscavenging countermeasure

Biel, T. G., Faison, T., Matthews, A. M., Ortega‐Rodriguez, U., Falkowski, V. M., Meek, E. C., Bush, X., Flores, M. J., Johnson, S., Wu, W. W., et al. (2024) · Bioengineering & Translational Medicine · doi:10.1002/btm2.10666 · Cited by 2

A Novel Tetravalent CD95 /Fas Fusion Protein With Superior CD95L / FasL Antagonism

Lang, I., Paulus, O., Zaitseva, O., & Wajant, H. (2024) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26741 · Cited by 2

Integrating Biochemical and Computational Approaches Reveal Structural Insights in Trastuzumab scFv-Fc Antibody Engineering

Bednova, O., Ketchemen, J. P., Mslati, H., Barok, M., Joensuu, H., Zeytuni, N., Gentile, F., Sanche, L., Fonge, H., & Leyton, J. V. (2025) · Biomolecules · doi:10.3390/biom15050606 · Cited by 2

Mapping economic outcomes: how biosimilars enhance access to health systems in Latin America and the Caribbean

Herrán, M., & Anaya, J. (2025) · Current Opinion in Immunology · doi:10.1016/j.coi.2025.102606 · Cited by 2

Improvement of Key Characteristics of Antibodies

Brewis, N. (2020) · Learning materials in biosciences · doi:10.1007/978-3-030-54630-4_11 · Cited by 2

Novel immunotherapy strategies involving matrix metalloproteinase (MMP) family

Garay-Canales, C. A., Díaz-Alvarez, L., & López-Cortés, G. I. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-822028-3.00015-7 · Cited by 2

Discovery of conformation-sensitive anti-amyloid protofibril monoclonal antibodies using an engineered chaperone-like amyloid-binding proteinPreprint

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