Evidence map›Paper›PMID 38949857›Full record

ReviewFuture medicinal chemistry2024

Regulation of post-translational modification of PD-L1 and associated opportunities for novel small-molecule therapeutics.

Jinglin Tang, Han Liu, Jinze Li, Yibo Zhang, Suyang Yao, Kan Yang, Zhihao You, Xiaoqiang Qiao, Yali Song

Abstract readReview
In one paragraph

Review in Future medicinal chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed.

  1. Article
  2. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors.

Jinglin TangKey Laboratory of Pharmaceutical Quality Control of Hebei Province, College of Pharmaceutical Sciences, Hebei University, Baoding, Hebei 071002, China.
Han LiuKey Laboratory of Pharmaceutical Quality Control of Hebei Province, College of Pharmaceutical Sciences, Hebei University, Baoding, Hebei 071002, China.
Jinze LiKey Laboratory of Pharmaceutical Quality Control of Hebei Province, College of Pharmaceutical Sciences, Hebei University, Baoding, Hebei 071002, China.
Yibo ZhangKey Laboratory of Pharmaceutical Quality Control of Hebei Province, College of Pharmaceutical Sciences, Hebei University, Baoding, Hebei 071002, China.
Suyang YaoKey Laboratory of Pharmaceutical Quality Control of Hebei Province, College of Pharmaceutical Sciences, Hebei University, Baoding, Hebei 071002, China.
Kan YangKey Laboratory of Pharmaceutical Quality Control of Hebei Province, College of Pharmaceutical Sciences, Hebei University, Baoding, Hebei 071002, China.
Zhihao YouKey Laboratory of Pharmaceutical Quality Control of Hebei Province, College of Pharmaceutical Sciences, Hebei University, Baoding, Hebei 071002, China.
Xiaoqiang QiaoKey Laboratory of Pharmaceutical Quality Control of Hebei Province, College of Pharmaceutical Sciences, Hebei University, Baoding, Hebei 071002, China.
Yali SongKey Laboratory of Pharmaceutical Quality Control of Hebei Province, College of Pharmaceutical Sciences, Hebei University, Baoding, Hebei 071002, China.ORCID 0000-0002-7011-6741

Funding

Innovation Team Project of Hebei University IT2023C01National Natural Science Foundation of China 82273792, 82003597Natural Science Foundation of Hebei Province B2022201092, B2021201026Natural Science Foundation of Science and Technology Project of Hebei Education Department QN2022057Natural Science Interdisciplinary Research Program of Hebei University DXK202215Undergraduate Innovation and Entrepreneurship Training Program of Hebei Province S202310075048
6 · The paper itself

Abstract

PD-L1 is overexpressed on the surface of tumor cells and binds to PD-1, resulting in tumor immune escape. Therapeutic strategies to target the PD-1/PD-L1 pathway involve blocking the binding. Immune checkpoint inhibitors have limited efficacy against tumors because PD-L1 is also present in the cytoplasm. PD-L1 of post-translational modifications (PTMs) have uncovered numerous mechanisms contributing to carcinogenesis and have identified potential therapeutic targets. Therefore, small molecule inhibitors can block crucial carcinogenic signaling pathways, making them a potential therapeutic option. To better develop small molecule inhibitors, we have summarized the PTMs of PD-L1. This review discusses the regulatory mechanisms of small molecule inhibitors in carcinogenesis and explore their potential applications, proposing a novel approach for tumor immunotherapy based on PD-L1 PTM.

Indexed as

B7-H1 AntigenNeoplasmsProtein Processing, Post-TranslationalSmall Molecule LibrariesAntineoplastic AgentsHumansAntineoplastic AgentsB7-H1 AntigenCD274 protein, humanSmall Molecule LibrariesacetylationmethylationN-linked glycosylationpalmitoylationPD-L1phosphorylationPTMsubiquitination

Identifiers

PMID38949857
PMCPMC11370925

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.