ArticleNature structural & molecular biology2024
Visualizing chaperone-mediated multistep assembly of the human 20S proteasome.
Article in Nature structural & molecular biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 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
24 citing papers in PubMed, 28 citations in OpenAlex.
- Molecular architecture and spatial organization of proteasomes in the human sperm nucleus.Nature structural & molecular biology · 2026Article
- Monoallelic PSMB8 variants cause PRAAS with immunodeficiency through impaired immunoproteasome assembly.American journal of human genetics · 2026Article
- Structural basis for regulation of the proteasome 20S core particle by the Parkinsonism-associated proteins FBXO7 and PI31.bioRxiv : the preprint server for biology · 2026Article
- Analysis of GRK2 aggregation in the pathology of Alzheimer disease in animal models.Cell reports. Medicine · 2026Article
- Plasticity in the structure and assembly of proteasomes.The Journal of biological chemistry · 2026Review
- Magical moments in protease biology: proteasome autocatalytic activation and PI31-mediated inhibition.Trends in biochemical sciences · 2026Review
- Deep homology and design of proteasome chaperone proteins in Candidozyma auris.Nature communications · 2026Article
- Structural transitions in the stepwise assembly of proteasome core particles.Nature communications · 2026Article
- TOGR3, a Proteasome β4 Subunit, Orchestrates Sugar Homeostasis to Trade Off Growth and Thermotolerance in Rice.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Molecular mechanisms in rare proteasomopathies.EULAR rheumatology open · 2026Review
- ZOMES: expanding roles of the PCI complexes from protein metabolism to drug discovery.npj metabolic health and disease · 2026Article
- A multivalent adaptor mechanism drives the nuclear import of proteasomes.Nature communications · 2026Article
- Within and beyond the boundaries of proteasomal assembly: PSMD9 chaperone as a multifunctional protein.Essays in biochemistry · 2025Review
- Bi-handed assembly chaperones regulate protein complex assembly through an intramolecular handover mechanism.Science advances · 2025Article
- A recombinant expression system for thebioRxiv : the preprint server for biology · 2025Article
- [Research and Therapeutic Advances of 26S Proteasome Subunit in Non-small Cell Lung Cancer].Zhongguo fei ai za zhi = Chinese journal of lung cancer · 2025Review
- PI31 is a positive regulator of 20S immunoproteasome assembly.Journal of cell science · 2025Article
- Evidence supporting a catalytic pentad mechanism for the proteasome and other N-terminal nucleophile enzymes.Nature communications · 2025Article
- Molecular basis for the stepwise and faithful maturation of the 20Science advances · 2025Article
- Stepwise order in protein complex assembly: approaches and emerging themes.Open biology · 2025Review
Corrections and comments
- Update of
Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
Dedicated assembly factors orchestrate the stepwise production of many molecular machines, including the 28-subunit proteasome core particle (CP) that mediates protein degradation. Here we report cryo-electron microscopy reconstructions of seven recombinant human subcomplexes that visualize all five chaperones and the three active site propeptides across a wide swath of the assembly pathway. Comparison of these chaperone-bound intermediates and a matching mature CP reveals molecular mechanisms determining the order of successive subunit additions, as well as how proteasome subcomplexes and assembly factors structurally adapt upon progressive subunit incorporation to stabilize intermediates, facilitate the formation of subsequent intermediates and ultimately rearrange to coordinate proteolytic activation with gated access to active sites. This work establishes a methodologic approach for structural analysis of multiprotein complex assembly intermediates, illuminates specific functions of assembly factors and reveals conceptual principles underlying human proteasome biogenesis, thus providing an explanation for many previous biochemical and genetic observations.
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.