{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["14(2)"],"submitter":["Anany MA"],"pubmed_abstract":["<b>Background:</b> Selective TNFR2 activation can be used to treat immune pathologies by activating and expanding regulatory T-cells (Tregs) but may also restore anti-tumour immunity by co-stimulating CD8<sup>+</sup> T-cells. Oligomerized TNFR2-specific TNF mutants or anti-TNFR2 antibodies can activate TNFR2 but suffer either from poor production and pharmacokinetics or in the case of anti-TNFR2 antibodies typically from the need of FcγR binding to elicit maximal agonistic activity. <b>Methods:</b> To identify the major factor(s) determining FcγR-independent agonism of anti-TNFR2 antibodies, we systematically investigated a comprehensive panel of anti-TNFR2 antibodies and antibody-based constructs differing in the characteristics of their TNFR2 binding domains but also in the number and po"],"journal":["Theranostics"],"pagination":["496-509"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10758050"],"repository":["biostudies-literature"],"pubmed_title":["Generic design principles for antibody-based tumour necrosis factor (TNF) receptor 2 (TNFR2) agonists with FcγR-independent agonism."],"pmcid":["PMC10758050"],"pubmed_authors":["Beilhack A","Wajant H","Medler J","Packert L","Kucka K","van Rompaey L","Steinfatt T","Lang I","Haack S","Vargas JG","Zaitseva O","Anany MA","Zhang T","Van Belle T","Dahlhoff J","Weisenberger D"],"additional_accession":[]},"is_claimable":false,"name":"Generic design principles for antibody-based tumour necrosis factor (TNF) receptor 2 (TNFR2) agonists with FcγR-independent agonism.","description":"<b>Background:</b> Selective TNFR2 activation can be used to treat immune pathologies by activating and expanding regulatory T-cells (Tregs) but may also restore anti-tumour immunity by co-stimulating CD8<sup>+</sup> T-cells. Oligomerized TNFR2-specific TNF mutants or anti-TNFR2 antibodies can activate TNFR2 but suffer either from poor production and pharmacokinetics or in the case of anti-TNFR2 antibodies typically from the need of FcγR binding to elicit maximal agonistic activity. <b>Methods:</b> To identify the major factor(s) determining FcγR-independent agonism of anti-TNFR2 antibodies, we systematically investigated a comprehensive panel of anti-TNFR2 antibodies and antibody-based constructs differing in the characteristics of their TNFR2 binding domains but also in the number and po","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024","modification":"2025-05-29T16:36:37.639Z","creation":"2025-05-29T16:36:37.639Z"},"accession":"S-EPMC10758050","cross_references":{"pubmed":["38169605"],"doi":["10.7150/thno.84404"]}}