{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Sun R"],"funding":["Purdue Center for Cancer Research","Susan G. Komen Breast Cancer Foundation","Purdue Institute for Drug Discovery (PIDD) Programmatic Area grant","Ralph W. and Grace M. Showalter Research Trust grant","NIGMS NIH HHS"],"pagination":["162"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8750214"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["11(1)"],"pubmed_abstract":["Leveraging the T cell immunity against tumors represents a revolutionary type of cancer therapy. 4-1BB is a well-characterized costimulatory immune receptor existing on activated T cells and mediating their proliferation and cytotoxicity under infectious diseases and cancers. Despite the accumulating interest in implementing 4-1BB as a therapeutic target for immune-related disorders, less is known about the pattern of its intracellular behaviors and regulations. It has been previously demonstrated that 4-1BB is heavily modified by <i>N</i>-glycosylation; however, the biological importance of this modification lacks detailed elucidation. Through biochemical, biophysical, and cell-biological approaches, we systematically evaluated the impact of <i>N</i>-glycosylation on the ligand interactio"],"journal":["Cells"],"pubmed_title":["<i>N</i>-Glycosylation Facilitates 4-1BB Membrane Localization by Avoiding Its Multimerization."],"pmcid":["PMC8750214"],"funding_grant_id":["N/A","R24 GM137782","CCR17488088"],"pubmed_authors":["Kim AMJ","Sun R","Lim SO","Murray AA"],"additional_accession":[]},"is_claimable":false,"name":"<i>N</i>-Glycosylation Facilitates 4-1BB Membrane Localization by Avoiding Its Multimerization.","description":"Leveraging the T cell immunity against tumors represents a revolutionary type of cancer therapy. 4-1BB is a well-characterized costimulatory immune receptor existing on activated T cells and mediating their proliferation and cytotoxicity under infectious diseases and cancers. Despite the accumulating interest in implementing 4-1BB as a therapeutic target for immune-related disorders, less is known about the pattern of its intracellular behaviors and regulations. It has been previously demonstrated that 4-1BB is heavily modified by <i>N</i>-glycosylation; however, the biological importance of this modification lacks detailed elucidation. Through biochemical, biophysical, and cell-biological approaches, we systematically evaluated the impact of <i>N</i>-glycosylation on the ligand interactio","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Jan","modification":"2026-04-08T06:49:28.557Z","creation":"2022-02-11T16:16:58.905Z"},"accession":"S-EPMC8750214","cross_references":{"pubmed":["35011724"],"doi":["10.3390/cells11010162"]}}