ReviewThe FEBS journal2021
Proteasome interaction with ubiquitinated substrates: from mechanisms to therapies.
Review in The FEBS journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 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
41 citing papers in PubMed, 62 citations in OpenAlex.
- PROTACs in personalized and precision medicine: transforming targeted therapy with advances in selectivity and patient stratification.Cancer chemotherapy and pharmacology · 2026Review
- Structures of dynamic interactors at native proteasomes by PhIX-MS and cryo-electron microscopy.Molecular cell · 2026Article
- Reprogramming the lipid peroxidation product 4-ONE as a chemoselective cleavable crosslinker.Nature communications · 2026Article
- Identification of novel ubiquitin receptors on the 26S proteasome by photo-crosslinking mass spectrometry.The Journal of biological chemistry · 2026Article
- Identification of Genes Associated with Seed Weight and Development of Functional Markers forBiology · 2026Article
- The Art of Domesticating Proteins: How Cancer Cells Adapt to Therapeutic and Environmental Stressors.International journal of molecular sciences · 2026Review
- Proteasome activity maintains cell-type-specific gene expression.Cell reports · 2026Article
- Identification of novel ubiquitin receptors on the 26S proteasome by photo-crosslinking mass spectrometry.bioRxiv : the preprint server for biology · 2025Article
- Bidirectional crosstalk between ER stress and lipid metabolism: From proteostasis to tumor adaptation.Cell death discovery · 2025Review
- Review
- Degradation of nNOS in the PVN of Rats With Heart Failure: Role of CHIP.Hypertension (Dallas, Tex. : 1979) · 2025Article
- FTO-associated osteoclastogenesis promotes alveolar bone resorption in apical periodontitis male rat via the HK1/USP14/RANK pathway.Nature communications · 2025Article
- Stress sensing and response through biomolecular condensates in plants.Plant communications · 2025Review
- Mechanisms and regulation of substrate degradation by the 26S proteasome.Nature reviews. Molecular cell biology · 2025Review
- N-degron pathways.Proceedings of the National Academy of Sciences of the United States of America · 2024Review
- Visualizing chaperone-mediated multistep assembly of the human 20S proteasome.Nature structural & molecular biology · 2024Article
- A structure-based designed small molecule depletes hRpn13Nature communications · 2024Article
- WSB1, as an E3 ligase, restrains myocardial ischemia-reperfusion injury by activating β-catenin signaling via promoting GSK3β ubiquitination.Molecular medicine (Cambridge, Mass.) · 2024Article
- Visualizing chaperone-mediated multistep assembly of the human 20S proteasome.bioRxiv : the preprint server for biology · 2024Article
- The E3 ubiquitin ligase TRIM39 modulates renal fibrosis induced by unilateral ureteral obstruction through regulating proteasomal degradation of PRDX3.Cell death discovery · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The 26S proteasome is responsible for regulated proteolysis in eukaryotic cells. Its substrates are diverse in structure, function, sequence length, and amino acid composition, and are targeted to the proteasome by post-translational modification with ubiquitin. Ubiquitination occurs through a complex enzymatic cascade and can also signal for other cellular events, unrelated to proteasome-catalyzed degradation. Like other post-translational protein modifications, ubiquitination is reversible, with ubiquitin chain hydrolysis catalyzed by the action of deubiquitinating enzymes (DUBs), ~ 90 of which exist in humans and allow for temporal events and dynamic ubiquitin-chain remodeling. DUBs have been known for decades to be an integral part of the proteasome, as deubiquitination is coupled to substrate unfolding and translocation into the internal degradation chamber. Moreover, the proteasome also binds several ubiquitinating enzymes and shuttle factors that recruit ubiquitinated substrates. The role of this intricate machinery and how ubiquitinated substrates interact with proteasomes remains an area of active investigation. Here, we review what has been learned about the mechanisms used by the proteasome to bind ubiquitinated substrates, substrate shuttle factors, ubiquitination machinery, and DUBs. We also discuss many open questions that require further study or the development of innovative approaches to be answered. Finally, we address the promise of expanded therapeutic targeting that could benefit from such new discoveries.
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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.