ArticleAdvanced science (Weinheim, Baden-Wurttemberg, Germany)2026
DLST Succinylation-Mediated Mitochondrial Metabolic Remodeling and Cuproptosis Resistance Promote Malignant Progression of Lung Adenocarcinoma.
Article in Advanced science (Weinheim, Baden-Wurttemberg, Germany), 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors.
Funding
Abstract
Metabolic remodeling is one of the hallmarks of malignant tumors, and post-translational modifications of proteins, such as succinylation, play an important role in the process of metabolic remodeling by regulating the function of metabolic enzymes. However, the role of succinylation modifications of key mitochondrial metabolic enzymes in lung adenocarcinoma (LUAD) remains unclear. Here, using succinylation proteomics, it is demonstrated that the succinylation level of lysine 409 (K409) on dihydrolipoamide S-succinyltransferase (DLST) is significantly increased in LUAD. Further, DLST K409 succinylation (K409succ), which is catalyzed by carnitine palmitoyltransferase 1A (CPT1A), can affect oxidative phosphorylation (OXPHOS) and redox homeostasis by regulating enzyme activity, thereby promoting the malignant progression of LUAD. Notably, the succinylation of DLST can enhance the cuproptosis resistance by inhibiting its lipoylation. Subsequently, a small-molecule inhibitor SI409-1 that can specifically target DLST K409 has been developed. In vitro and in vivo experiments show that SI409-1 can inhibit the LUAD growth and enhance the sensitivity to cuproptosis inducers. Collectively, these findings provide a novel predictive target and intervention strategy for the clinical diagnosis and treatment of LUAD.
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.