ReviewFrontiers in oncology2026
The deubiquitinase USP35: from an oncogenic hub to a therapeutic target in human cancers.
Review in Frontiers in oncology, 2026. 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
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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.
- Regulatory roles of five key USP family deubiquitinases in cancer: from mechanisms to targeted therapy advances.Frontiers in pharmacology · 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
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ubiquitination is a critical post-translational modification in eukaryotic cells, mediated by a sequential enzymatic cascade involving E1 (activating), E2 (conjugating), and E3 (ligase) enzymes that catalyze the covalent conjugation of ubiquitin to substrate proteins. This modification precisely controls substrate stability, localization, and function, thereby governing fundamental cellular processes such as the cell cycle, DNA repair, and apoptosis. Deubiquitinating enzymes (DUBs) counteract ubiquitination by hydrolyzing ubiquitin chains, thereby maintaining cellular protein homeostasis. Ubiquitin-Specific Protease 35 (USP35), a core member of the USP family, relies on a conserved Cys-His-Asp catalytic triad and C-terminal domain (CTD)-dependent dimerization for its enzymatic activity to specifically remove ubiquitin modifications from diverse substrates. USP35 is frequently overexpressed in diverse malignancies, including clear cell renal cell carcinoma and breast cancer. By stabilizing key oncogenic factors-such as Aurora B (a proliferation regulator), NRF2 and BRD4 (inhibitors of ferroptosis), and Snail1 (a promoter of EMT)-USP35 acts as a central driver of core malignant phenotypes, including tumor cell proliferation, apoptotic evasion, metabolic reprogramming, epithelial-mesenchymal transition (EMT), and resistance to chemotherapy and immunotherapy. This review systematically summarizes the multi-dimensional regulatory mechanisms of USP35 in tumorigenesis and progression across various cancers, highlights its clinical significance as a pan-cancer prognostic biomarker and potential therapeutic target, and provides a forward-looking perspective on the development of USP35-targeted small-molecule inhibitors and combination therapies. We aim to establish a theoretical foundation and highlight translational directions for developing USP35-based precision oncology approaches.
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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.