ArticleInternational journal of molecular sciences2025
Shortened PGLYRP1 Peptides Regulate Antitumor Activity of Cytotoxic Lymphocytes via TREM-1 Receptor: From Biology to Bioinformatics.
Article in International journal of molecular sciences, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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
1 citing paper in PubMed.
- Triggering receptor expressed on myeloid cell family in atherosclerosis: from mechanisms to intervention strategies.Cell communication and signaling : CCS · 2026Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
Abstract
The pro-inflammatory immune response plays an important role in protecting the body from pathogens and tumors. In this study, we were able to identify three peptides of the innate immunity protein PGLYRP1 (Tag7) that could regulate the activity of the TREM-1 receptor. TREM-1 receptor activation on monocytes triggers the appearance of antitumor lymphocytes. All three peptides studied (17.0, N9, and N15) bind with the TREM-1 receptor with the Kds 1.32 ± 0.2 nM, 9.66 ± 0.5 nM, and 7.43 ± 0.4 nM, respectively. An N9 peptide inhibiting the activity of the receptor was identified in addition to two peptides (N9 and N15) that jointly trigger the activation of the receptor. The conducted molecular docking study revealed amino acid residues (Ile57, Ile58, Glu106, Ser108, Leu110, Tyr116, Pro118, Pro119, Arg130, and Val 132), necessary for various functions of peptides, providing important knowledge for understanding the mechanism of activation of this receptor that can also serve as a basis for the development of therapeutic drugs to regulate its activity in the treatment of autoimmune diseases and tumors.
Indexed as
Identifiers
What Socratic 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 Socratic graph.