ReviewAnnual review of biochemistry2018
Structure and Function of the 26S Proteasome.
Review in Annual review of biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 498 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
498 citing papers in PubMed, 817 citations in OpenAlex.
- PSMA1, PSMA5, and PSMB2 serve as prognostic biomarkers and are correlated with tumor-infiltrating leukocytes in HCC.Epigenetics · 2026Article
- Pulling and gripping: Proteasomal translocation pathway elements differentially contribute to substrate unfolding.Protein science : a publication of the Protein Society · 2026Article
- Allantopyrone A promotes cross-linking of ubiquitin-specific protease 5 (USP5) and inhibits its deubiquitinase activity by targeting distinct domains.The Journal of antibiotics · 2026Article
- Proteasomal surveillance of exposed cysteines.bioRxiv : the preprint server for biology · 2026Article
- "MIDA masking" of boronic acid therapeutics for enhanced stability and economy.RSC chemical biology · 2026Article
- Nanotechnology-Enabled Targeted Protein Degradation: Strategies, Opportunities, and Challenges.Small methods · 2026Review
- Assessing the Stability of Molecular Glues with Weighted Ensemble Simulations.Journal of chemical theory and computation · 2026Article
- PA200 modulates immunoproteasome structure and activity.Nature communications · 2026Article
- Structures of dynamic interactors at native proteasomes by PhIX-MS and cryo-electron microscopy.Molecular cell · 2026Article
- FaCPK19-FaTT1 axis decodes heat-induced CaThe New phytologist · 2026Article
- Review
- Identifying endogenous substrates of the 26S proteasome through site-specific photocrosslinking.bioRxiv : the preprint server for biology · 2026Article
- Molecular basis of ubiquitin-independent recognition and degradation of ODC/Antizyme by the 26S proteasome.bioRxiv : the preprint server for biology · 2026Article
- FOXA2 suppresses ESCC proliferation and metastasis by inhibiting PSMB9 expression, thereby attenuating proteasome activity.Cancer cell international · 2026Article
- Chemical Induction of MYC Protein Degradation via MYC-MAX Disruption and 20S Proteasome Activation.ACS chemical biology · 2026Article
- The Nematicide Tioxazafen Disrupts Proteasome Function via Cytochrome P450 Bioactivation.bioRxiv : the preprint server for biology · 2026Article
- P-glycoprotein-mediated efflux of rapaprotin-L dictates sensitivity of cancer cells to the inducer of 26S proteasome disassembly.European journal of pharmacology · 2026Article
- Anticancer proteasome inhibitors are detrimental to the growth of Toxoplasma gondii in vitro.BMC research notes · 2026Article
- PSMD8 promotes breast cancer progression and attenuates paclitaxel sensitivity by stabilizing KIF10.Cancer cell international · 2026Article
- Small bites for big problems: stepwise aggregate degradation by autophagy.Biochemical Society transactions · 2026Review
438 more citing papers are in PubMed but not listed here.
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 at 3 institutions in 1 country.
Funding
Abstract
As the endpoint for the ubiquitin-proteasome system, the 26S proteasome is the principal proteolytic machine responsible for regulated protein degradation in eukaryotic cells. The proteasome's cellular functions range from general protein homeostasis and stress response to the control of vital processes such as cell division and signal transduction. To reliably process all the proteins presented to it in the complex cellular environment, the proteasome must combine high promiscuity with exceptional substrate selectivity. Recent structural and biochemical studies have shed new light on the many steps involved in proteasomal substrate processing, including recognition, deubiquitination, and ATP-driven translocation and unfolding. In addition, these studies revealed a complex conformational landscape that ensures proper substrate selection before the proteasome commits to processive degradation. These advances in our understanding of the proteasome's intricate machinery set the stage for future studies on how the proteasome functions as a major regulator of the eukaryotic proteome.
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.