ReviewRSC advances2025
Breaking the oncogenic alliance: advances in disrupting the MTDH-SND1 complex for cancer therapy.
Review in RSC advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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
2 citing papers in PubMed.
- AEG-1/MTDH Enhances Hepatocellular Carcinoma Radioresistance by Recruiting PTBP1 Via SND1 To Stabilize ATG5 mRNA and Promote Protective Autophagy.Cell biochemistry and biophysics · 2026Article
- 1H-Indazole-3-Carboxylic Acid Derivatives as Disruptors of the Oncogenic MTDH-SND1 Protein-Protein Interaction: An In Silico-to-In Vitro Study.Cell biochemistry and biophysics · 2026Article
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.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Metadherin (MTDH/AEG-1/LYRIC) partners with Staphylococcal Nuclease Domain-Containing Protein 1 (SND1) to form an oncogenic hub that drives proliferation, survival and metastasis in many tumors. Interrupting this interaction dampens pivotal pathways-including NF-κB, PI3K/Akt and Wnt/β-catenin-and simultaneously promotes SND1 degradation, yielding broad antitumor effects. This review consolidates current knowledge of the MTDH-SND1 axis and highlights preclinical studies showing that genetic knock-out or pharmacologic blockade of the complex can sharply reduce primary growth and metastatic spread. We summarize structural studies that map the binding interface, emphasizing the essential MTDH tryptophan pair and the SN1/SN2 barrels of SND1, and we survey therapeutic approaches designed to exploit these determinants. Candidate disruptors range from phage-derived stapled peptides to small molecules unearthed by high-throughput and structure-guided screens; several demonstrate potent cytotoxicity in cell lines and xenografts, particularly when delivered through cell-penetrating motifs or nanoformulations. We also examine hurdles that protein-protein interaction inhibitors must overcome, such as off-target toxicity, metabolic instability and limited bioavailability, and discuss combination regimens that may amplify efficacy. Finally, we outline emerging avenues-PROTAC-mediated degraders, rational biomarker selection and advanced drug-delivery technologies-that could sharpen specificity and accelerate clinical translation. Together, these data validate MTDH-SND1 disruption as a versatile strategy against treatment-refractory cancers.
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.