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OpenAlex Citation Counts

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OpenAlex is a bibliographic catalogue of scientific papers, authors and institutions accessible in open access mode, named after the Library of Alexandria. It's citation coverage is excellent and I hope you will find utility in this listing of citing articles!

If you click the article title, you'll navigate to the article, as listed in CrossRef. If you click the Open Access links, you'll navigate to the "best Open Access location". Clicking the citation count will open this listing for that article. Lastly at the bottom of the page, you'll find basic pagination options.

Requested Article:

Role of Fc Core Fucosylation in the Effector Function of IgG1 Antibodies
Josée Golay, Alain E. Andrea, Irene Cattaneo
Frontiers in Immunology (2022) Vol. 13
Open Access | Times Cited: 50

Showing 1-25 of 50 citing articles:

B cells in the tumor microenvironment: Multi-faceted organizers, regulators, and effectors of anti-tumor immunity
Céline M. Laumont, Brad H. Nelson
Cancer Cell (2023) Vol. 41, Iss. 3, pp. 466-489
Open Access | Times Cited: 77
IgG glycans in health and disease: Prediction, intervention, prognosis, and therapy
Sofia Shkunnikova, Anika Mijakovac, Lucija Sironić, et al.
Biotechnology Advances (2023) Vol. 67, pp. 108169-108169
Open Access | Times Cited: 38
Therapeutic antibodies for the prevention and treatment of cancer
Mukesh Kumar, Akansha Jalota, Ashutosh Kumar, et al.
Journal of Biomedical Science (2024) Vol. 31, Iss. 1
Open Access | Times Cited: 13
Genetics of glycosylation in mammalian development and disease
Pamela Stanley
Nature Reviews Genetics (2024)
Closed Access | Times Cited: 13
Antibody-Drug Conjugates: A promising breakthrough in cancer therapy
Swapnali Parit, Ajit Manchare, Amol D. Gholap, et al.
International Journal of Pharmaceutics (2024) Vol. 659, pp. 124211-124211
Closed Access | Times Cited: 13
Glycan Shape, Motions, and Interactions Explored by NMR Spectroscopy
Göran Widmalm
JACS Au (2024) Vol. 4, Iss. 1, pp. 20-39
Open Access | Times Cited: 8
Sequential immunotherapy: towards cures for autoimmunity
Francisco Ramírez‐Valle, Joseph Maranville, Sophie Roy, et al.
Nature Reviews Drug Discovery (2024) Vol. 23, Iss. 7, pp. 501-524
Closed Access | Times Cited: 7
Glycosylation shapes the efficacy and safety of diverse protein, gene and cell therapies
Frances Rocamora, Angelo G. Peralta, Seunghyeon Shin, et al.
Biotechnology Advances (2023) Vol. 67, pp. 108206-108206
Open Access | Times Cited: 20
The role of antibody glycosylation in autoimmune and alloimmune kidney diseases
Anaïs Beyze, Christian Larroque, Moglie Le Quintrec
Nature Reviews Nephrology (2024) Vol. 20, Iss. 10, pp. 672-689
Closed Access | Times Cited: 6
N-Glycosylation modulators for targeted manipulation of glycosylation for monoclonal antibodies
Neelesh Gangwar, Neha Dixit, Anurag S. Rathore
Applied Microbiology and Biotechnology (2025) Vol. 109, Iss. 1
Open Access
Improving the N-glycosylation occupancy of plant-produced IgG1 by engineering the amino acid environment at Asn297
Kathrin Göritzer, Valentina Ruocco, Ulrike Vavra, et al.
Frontiers in Plant Science (2025) Vol. 15
Open Access
Bisecting N-Acetylglucosamine of the N-Glycan of Immunoglobulin G Does Not Affect Binding to Fc Gamma Receptors
Gerlof P. Bosman, Inèz D. Stoof, Hans P. Bastiaansen, et al.
ACS Chemical Biology (2025)
Open Access
Uses and Challenges of Antiviral Polyclonal and Monoclonal Antibody Therapies
Evi Struble, Jonathan Rawson, Tzanko S. Stantchev, et al.
Pharmaceutics (2023) Vol. 15, Iss. 5, pp. 1538-1538
Open Access | Times Cited: 13
Modulating antibody effector functions by Fc glycoengineering
Mikel García-Alija, Berre Van Moer, Diego E. Sastre, et al.
Biotechnology Advances (2023) Vol. 67, pp. 108201-108201
Open Access | Times Cited: 12
Rhamnose modified antibodies show improved immune killing towards EGFR-positive solid tumor cells
Haofei Hong, Jie Zhao, Kun Zhou, et al.
Carbohydrate Research (2024) Vol. 536, pp. 109038-109038
Closed Access | Times Cited: 4
A Defucosylated Anti-EpCAM Monoclonal Antibody (EpMab-37-mG2a-f) Exerts Antitumor Activity in Xenograft Model
Teizo Asano, Tomohiro Tanaka, Hiroyuki Suzuki, et al.
Antibodies (2022) Vol. 11, Iss. 4, pp. 74-74
Open Access | Times Cited: 18
Inhibiting N‐glycan processing increases the antibody binding affinity and effector function of human natural killer cells
María C. Rodríguez, Harrison B. Hughes, Paul G Kremer, et al.
Immunology (2023) Vol. 170, Iss. 2, pp. 202-213
Open Access | Times Cited: 10
IgG1 glycosylation highlights premature aging in Down syndrome
Bianca M. M. Streng, Julie Van Coillie, Joanne Wildenbeest, et al.
Aging Cell (2024) Vol. 23, Iss. 7
Open Access | Times Cited: 3
Accelerated generation of gene‐engineered monoclonal CHO cell lines using FluidFM nanoinjection and CRISPR/Cas9
Justin S. Antony, Anabel Migenda Herranz, Tahereh Mohammadian, et al.
Biotechnology Journal (2024) Vol. 19, Iss. 4
Open Access | Times Cited: 3
Mature tertiary lymphoid structures: important contributors to anti-tumor immune efficacy
Xinyu Bao, Xuwen Lin, Mei Xie, et al.
Frontiers in Immunology (2024) Vol. 15
Open Access | Times Cited: 3
Study on antibody Fc-glycosylation for optimal effector functions
Vidya S. Shivatare, Po‐Kai Chuang, Tzu‐Hao Tseng, et al.
Chemical Communications (2023) Vol. 59, Iss. 37, pp. 5555-5558
Closed Access | Times Cited: 8
Immunoglobulin G genetic variation can confound assessment of antibody levels via altered binding to detection reagents
Ruth A Purcell, L Carissa Aurelia, Robyn Esterbauer, et al.
Clinical & Translational Immunology (2024) Vol. 13, Iss. 3
Open Access | Times Cited: 2
Revisiting the immunopathology of congenital disorders of glycosylation: an updated review
Carlota Pascoal, Rita Francisco, Patrícia Mexia, et al.
Frontiers in Immunology (2024) Vol. 15
Open Access | Times Cited: 2
The association between plasma IgG N-glycosylation and neonatal hypoxic–ischemic encephalopathy: a case-control study
Liangao Wang, Xinxia Lu, Meng Wang, et al.
Frontiers in Cellular Neuroscience (2024) Vol. 18
Open Access | Times Cited: 2
A metabolic inhibitor blocks cellular fucosylation and enables production of afucosylated antibodies
Pierre‐André Gilormini, V. Narasimharao Thota, Anthony Fers-Lidou, et al.
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 27
Closed Access | Times Cited: 2
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