ArticleThe Journal of biological chemistry2017
An engineered transforming growth factor β (TGF-β) monomer that functions as a dominant negative to block TGF-β signaling.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
What it found
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Who cites it
29 citing papers in PubMed, 40 citations in OpenAlex.
- Intravenously deliverable oncolytic virus VET3-TGI favorably alters the tumor microenvironment.Journal for immunotherapy of cancer · 2026Article
- Cytokine multimerization: when more is more and sometimes less.Nature reviews. Immunology · 2026Review
- Recent advances in TGF-β signaling: insights into regulation, pathophysiological function, and clinical translation.Cell regeneration (London, England) · 2026Article
- Design of high-affinity binders to immune modulating receptors for cancer immunotherapy.Nature communications · 2025Article
- Structures of TGF-β with betaglycan and signaling receptors reveal mechanisms of complex assembly and signaling.Nature communications · 2025Article
- TGM6 is a helminth secretory product that mimics TGF-β binding to TGFBR2 to antagonize signaling in fibroblasts.Nature communications · 2025Article
- Multi-armored allogeneic MUC1 CAR T cells enhance efficacy and safety in triple-negative breast cancer.Science advances · 2024Article
- Design of High Affinity Binders to Convex Protein Target Sites.bioRxiv : the preprint server for biology · 2024Article
- An oncolytic virus-delivered TGFβ inhibitor overcomes the immunosuppressive tumor microenvironment.The Journal of experimental medicine · 2023Article
- TGFβJournal of extracellular vesicles · 2022Article
- Structure and Enzymatic Activity of an Intellectual Disability-Associated Ornithine Decarboxylase Variant, G84R.ACS omega · 2022Article
- Convergent evolution of a parasite-encoded complement control protein-scaffold to mimic binding of mammalian TGF-β to its receptors, TβRI and TβRII.The Journal of biological chemistry · 2022Article
- Emulsion-free chitosan-genipin microgels for growth plate cartilage regeneration.Journal of biomaterials applications · 2021Article
- Structure of AMH bound to AMHR2 provides insight into a unique signaling pair in the TGF-β family.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Novel TGFβ Inhibitors Ameliorate Oral Squamous Cell Carcinoma Progression and Improve the Antitumor Immune Response of Anti-PD-L1 Immunotherapy.Molecular cancer therapeutics · 2021Article
- TGF-β isoforms inhibit hepatitis C virus propagation in transforming growth factor beta/SMAD protein signalling pathway dependent and independent manners.Journal of cellular and molecular medicine · 2021Article
- TGFβ signaling networks in ovarian cancer progression and plasticity.Clinical & experimental metastasis · 2021Review
- TGFβ biology in cancer progression and immunotherapy.Nature reviews. Clinical oncology · 2021Review
- Reprogramming of Mesothelial-Mesenchymal Transition in Chronic Peritoneal Diseases by Estrogen Receptor Modulation and TGF-β1 Inhibition.International journal of molecular sciences · 2020Review
- Article
Corrections and comments
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Authors and funding
21 authors at 3 institutions in 2 countries.
Funding
Abstract
The transforming growth factor β isoforms, TGF-β1, -β2, and -β3, are small secreted homodimeric signaling proteins with essential roles in regulating the adaptive immune system and maintaining the extracellular matrix. However, dysregulation of the TGF-β pathway is responsible for promoting the progression of several human diseases, including cancer and fibrosis. Despite the known importance of TGF-βs in promoting disease progression, no inhibitors have been approved for use in humans. Herein, we describe an engineered TGF-β monomer, lacking the heel helix, a structural motif essential for binding the TGF-β type I receptor (TβRI) but dispensable for binding the other receptor required for TGF-β signaling, the TGF-β type II receptor (TβRII), as an alternative therapeutic modality for blocking TGF-β signaling in humans. As shown through binding studies and crystallography, the engineered monomer retained the same overall structure of native TGF-β monomers and bound TβRII in an identical manner. Cell-based luciferase assays showed that the engineered monomer functioned as a dominant negative to inhibit TGF-β signaling with a
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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.