ArticleThe Journal of biological chemistry2010
The structure of the trimer of human 4-1BB ligand is unique among members of the tumor necrosis factor superfamily.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
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Who cites it
35 citing papers in PubMed, 51 citations in OpenAlex.
- Development of bicistronic plasmids and fusion proteins for clinical translation of tumor immune reprogramming.Molecular therapy. Advances · 2026Article
- MD Simulation Reveals a Trimerization-Enhanced Interaction of CD137L with CD137.International journal of molecular sciences · 2025Article
- ATOR-1017 (evunzekibart), an Fc-gamma receptor conditional 4-1BB agonist designed for optimal safety and efficacy, activates exhausted T cells in combination with anti-PD-1.Cancer immunology, immunotherapy : CII · 2023Article
- Engineered soluble, trimerized 4-1BBL variants as potent immunomodulatory agents.Cancer immunology, immunotherapy : CII · 2023Article
- Inherited TNFSF9 deficiency causes broad Epstein-Barr virus infection with EBV+ smooth muscle tumors.The Journal of experimental medicine · 2022Article
- Agonistic CD27 antibody potency is determined by epitope-dependent receptor clustering augmented through Fc-engineering.Communications biology · 2022Article
- 4-1BB: A promising target for cancer immunotherapy.Frontiers in oncology · 2022Review
- Novel anti-4-1BB×PD-L1 bispecific antibody augments anti-tumor immunity through tumor-directed T-cell activation and checkpoint blockade.Journal for immunotherapy of cancer · 2021Article
- Optimization of T Cell Redirecting Strategies: Obtaining Inspirations From Natural Process of T Cell Activation.Frontiers in immunology · 2021Review
- GMP-Compliant Universal Antigen Presenting Cells (uAPC) Promote the Metabolic Fitness and Antitumor Activity of Armored Cord Blood CAR-NK Cells.Frontiers in immunology · 2021Article
- Tumor necrosis family receptor superfamily member 9/tumor necrosis factor receptor-associated factor 1 pathway on hepatitis C viral persistence and natural history.World journal of hepatology · 2020Review
- 4-1BB costimulation promotes CAR T cell survival through noncanonical NF-κB signaling.Science signaling · 2020Article
- Crystal structure of the m4-1BB/4-1BBL complex reveals an unusual dimeric ligand that undergoes structural changes upon 4-1BB receptor binding.The Journal of biological chemistry · 2019Article
- Article
- Structure of the 4-1BB/4-1BBL complex and distinct binding and functional properties of utomilumab and urelumab.Nature communications · 2018Article
- The promise and challenges of immune agonist antibody development in cancer.Nature reviews. Drug discovery · 2018Review
- Crystal structures of the human 4-1BB receptor bound to its ligand 4-1BBL reveal covalent receptor dimerization as a potential signaling amplifier.The Journal of biological chemistry · 2018Article
- Crystal structure of the human 4-1BB/4-1BBL complex.The Journal of biological chemistry · 2018Article
- Crystal structure of murine 4-1BB and its interaction with 4-1BBL support a role for galectin-9 in 4-1BB signaling.The Journal of biological chemistry · 2018Article
- CD137 (4-1BB) Signalosome: Complexity Is a Matter of TRAFs.Frontiers in immunology · 2018Review
Corrections and comments
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Authors and funding
11 authors at 6 institutions in 2 countries.
Funding
Abstract
Binding of the 4-1BB ligand (4-1BBL) to its receptor, 4-1BB, provides the T lymphocyte with co-stimulatory signals for survival, proliferation, and differentiation. Importantly, the 4-1BB-4-1BBL pathway is a well known target for anti-cancer immunotherapy. Here we present the 2.3-A crystal structure of the extracellular domain of human 4-1BBL. The ectodomain forms a homotrimer with an extended, three-bladed propeller structure that differs from trimers formed by other members of the tumor necrosis factor (TNF) superfamily. Based on the 4-1BBL structure, we modeled its complex with 4-1BB, which was consistent with images obtained by electron microscopy, and verified the binding site by site-directed mutagenesis. This structural information will facilitate the development of immunotherapeutics targeting 4-1BB.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.