ReviewAnnual review of biochemistry2009
Recognition and processing of ubiquitin-protein conjugates by the proteasome.
Review in Annual review of biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 994 papers, 1 of them a synthesis that pooled it.
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
994 citing papers in PubMed, 1 synthesis or guideline pooled it, 1,764 citations in OpenAlex.
- Meta-analysis fails to show any correlation between protein abundance and ubiquitination changes.FEBS open bio · 2026Pooled it
- From aggregate structure to disease trajectory: the role of the proteostasis network.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2026Review
- Ubiquitin receptor-mediated, ubiquitin-independent targeted protein degradation via 26Science advances · 2026Article
- RPT2a-mediated degradation of WDR5a regulates flowering time in Arabidopsis.Plant cell reports · 2026Article
- TRIM23 prevents adenovirus replication by p62-mediated selective autophagic degradation of viral E1A protein.PLoS pathogens · 2026Article
- Review
- FaCPK19-FaTT1 axis decodes heat-induced CaThe New phytologist · 2026Article
- Advancing Biochemical Molecule Registration, Representation and Search for New Drug Modalities.Journal of chemical information and modeling · 2026Article
- Molecular basis of ubiquitin-independent recognition and degradation of ODC/Antizyme by the 26S proteasome.bioRxiv : the preprint server for biology · 2026Article
- Review
- PROTAC-mediated regulation of programmed cell death: From molecular mechanisms to therapeutic breakthroughs.Innovation (Cambridge (Mass.)) · 2026Review
- Comparative analysis of Cdc48-dependent proteolysis at the ER, mitochondria and chloroplasts.Nature communications · 2026Review
- Integrative Pan-Cancer Mapping of Proteasome Dependency Prioritizes PSMB5 and PSMB6 as Context-Dependent Vulnerability Biomarkers Linked to Immune Context.Molecules (Basel, Switzerland) · 2026Article
- Cold-responsive interaction between MdRAD23D1 and MdMYB15 confers cold stress tolerance via the CBF pathway in apple (Malus domestica).PLoS genetics · 2026Article
- Spatial Single-Cell Proteomics Reveals Molecular Trajectories Of Tangle-Bearing Neurons In Alzheimer's Disease.bioRxiv : the preprint server for biology · 2026Article
- Mechanisms and Design Principles of Proteolysis-Targeting Chimeras and Their Emerging Applications.ACS pharmacology & translational science · 2026Review
- Rad23b exacerbates pathological aggregates through disrupting proteasome functions in Spinocerebellar ataxia type 3.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2026Article
- A Bacterial Effector Hijacks NBR1 to Modulate Both Autophagy and Ubiquitination-Mediated Degradation That Promotes Bacterial Infection.Plant biotechnology journal · 2026Article
- PSMD12 Overexpression Promotes Lung Adenocarcinoma Progression via Ubiquitin-Proteasome Pathway Dysregulation.Cancer science · 2026Article
- Association of circulating proteasome activity with Alzheimer's pathology and cognitive functions in APOE ε4 carriers.Alzheimer's research & therapy · 2026Observational
934 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
1 author at 1 institution in 1 country.
Funding
Abstract
The proteasome is an intricate molecular machine, which serves to degrade proteins following their conjugation to ubiquitin. Substrates dock onto the proteasome at its 19-subunit regulatory particle via a diverse set of ubiquitin receptors and are then translocated into an internal chamber within the 28-subunit proteolytic core particle (CP), where they are hydrolyzed. Substrate is threaded into the CP through a narrow gated channel, and thus translocation requires unfolding of the substrate. Six distinct ATPases in the regulatory particle appear to form a ring complex and to drive unfolding as well as translocation. ATP-dependent, degradation-coupled deubiquitination of the substrate is required both for efficient substrate degradation and for preventing the degradation of the ubiquitin tag. However, the proteasome also contains deubiquitinating enzymes (DUBs) that can remove ubiquitin before substrate degradation initiates, thus allowing some substrates to dissociate from the proteasome and escape degradation. Here we examine the key elements of this molecular machine and how they cooperate in the processing of proteolytic substrates.
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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.