ArticleInternational journal of molecular sciences2020
Disulfide-Linked Peptides for Blocking BTLA/HVEM Binding.
Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
12 citing papers in PubMed, 27 citations in OpenAlex.
- Role of BTLA in ovarian cancer and its clinical prognostic significance based on multi-omics analysis.Journal of ovarian research · 2026Article
- Determination of the Inhibitory Properties of Compounds Toward Immune Checkpoint Complex Formation Using ELISA.Methods in molecular biology (Clifton, N.J.) · 2026Article
- CD160-Derived Peptide as a Bidirectional Inhibitor Toward Immune Checkpoints BTLA/HVEM and HVEM/LIGHT.Journal of medicinal chemistry · 2025Article
- Negative Immune Checkpoint Inhibitors.Pharmaceutics · 2025Review
- Insights into therapeutic peptides in the cancer-immunity cycle: Update and challenges.Acta pharmaceutica Sinica. B · 2024Review
- Inhibitors of Immune Checkpoints: Small Molecule- and Peptide-Based Approaches.Journal of personalized medicine · 2024Review
- Highly potent multivalent VHH antibodies against Chikungunya isolated from an alpaca naïve phage display library.Journal of nanobiotechnology · 2022Article
- Multi-target combinatory strategy to overcome tumor immune escape.Frontiers of medicine · 2022Review
- Theory and Practice of Coarse-Grained Molecular Dynamics of Biologically Important Systems.Biomolecules · 2021Article
- Virtual Evolution of HVEM Segment for Checkpoint Inhibitor Discovery.International journal of molecular sciences · 2021Article
- The BTLA and PD-1 signaling pathways independently regulate the proliferation and cytotoxicity of human peripheral blood γδ T cells.Immunity, inflammation and disease · 2021Article
- Fragments of gD Protein as Inhibitors of BTLA/HVEM Complex Formation-Design, Synthesis, and Cellular Studies.International journal of molecular sciences · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
14 authors at 5 institutions in 2 countries.
Funding
Abstract
Immune checkpoints are crucial in the maintenance of antitumor immune responses. The activation or blockade of immune checkpoints is dependent on the interactions between receptors and ligands; such interactions can provide inhibitory or stimulatory signals, including the enhancement or suppression of T-cell proliferation, differentiation, and/or cytokine secretion. B-and T-lymphocyte attenuator (BTLA) is a lymphoid-specific cell surface receptor which is present on T-cells and interacts with herpes virus entry mediator (HVEM), which is present on tumor cells. The binding of HVEM to BTLA triggers an inhibitory signal which attenuates the immune response. This feature is interesting for studying the molecular interactions between HVEM and BTLA, as they may be targeted for novel immunotherapies. This work was based on the crystal structure of the BTLA/HVEM complex showing that BTLA binds the N-terminal cysteine-rich domain of HVEM. We investigated the amino acid sequence of HVEM and used molecular modeling methods to develop inhibitors of the BTLA/HVEM interaction. We synthesized novel compounds and determined their ability to interact with the BTLA protein and inhibit the formation of the BTLA/HVEM complex. Our results suggest that the HVEM (14-39) peptide is a potent inhibitor of the formation of the BTLA/HVEM protein complex.
Indexed as
Identifiers
What OpenQuestion holds
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.