ArticleMedChemComm2019
Structural insights and binding analysis for determining the molecular bases for programmed cell death protein ligand-1 inhibition.
Article in MedChemComm, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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
5 citing papers in PubMed, 12 citations in OpenAlex.
- Therapeutic potential inhibitor for dipeptidyl peptidase IV in diabetic type 2: in silico approaches.3 Biotech · 2025Article
- Progress in small-molecule inhibitors targeting PD-L1.RSC medicinal chemistry · 2024Review
- An in silico investigation on the binding site preference of PD-1 and PD-L1 for designing antibodies for targeted cancer therapy.PloS one · 2024Article
- Therapeutic targeting of PD-1/PD-L1 blockade by novel small-molecule inhibitors recruits cytotoxic T cells into solid tumor microenvironment.Journal for immunotherapy of cancer · 2022Article
- A Potential Off-Target Effect of the Wnt/β-Catenin Inhibitor KYA1797K: PD-L1 Binding and Checkpoint Inhibition.Biomedicine hubArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Programmed cell death protein 1 (PD-1) and PD-ligand 1 (PD-L1) interaction plays an important role in cancer immunotherapy. Several PD-1/PD-L1 inhibitors have been approved with remarkable impact on overall patient survival rates. Inhibitors in clinical practice are presently limited to monoclonal antibodies. However, their severe shortcomings expose the need for a new generation of PD-L1 inhibitors. Understanding the tumor microenvironment, identifying specific biomarkers and X-ray crystalline structures of PD-1/PD-L1 complexes, including molecular and genomic signature studies are essential to determine the success for the development of PD-1/PD-L1 inhibitors into safer and efficient cancer immunotherapeutics. Currently, the development of immune-modulatory small molecules is being explored due to their benefits over recombinant protein approaches. Nevertheless, their development is hampered in part due to lack of structural information. The current study builds on PD-L1 small-molecule inhibitor structural information and provides insights into the design of new inhibitors. To this end, a comprehensive analysis of crystallographic structures and benchmarking studies were performed, showing the specific structure model and software best suited to study PD-L1. The use of
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.