ArticleNature communications2016
A unified mechanism for proteolysis and autocatalytic activation in the 20S proteasome.
Article in Nature communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 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
65 citing papers in PubMed, 1 synthesis or guideline pooled it, 125 citations in OpenAlex.
- The proteasome as a druggable target with multiple therapeutic potentialities: Cutting and non-cutting edges.Pharmacology & therapeutics · 2020Pooled it
- Coordinated control of proteasome subunit gene expression promotes stress resistance, proteostasis, and longevity.GeroScience · 2026Article
- Molecular architecture and spatial organization of proteasomes in the human sperm nucleus.Nature structural & molecular biology · 2026Article
- The pivotal role of β-lactone stereochemistry in the development of SARS-CoV-2 MProtein science : a publication of the Protein Society · 2026Article
- Magical moments in protease biology: proteasome autocatalytic activation and PI31-mediated inhibition.Trends in biochemical sciences · 2026Review
- Structural transitions in the stepwise assembly of proteasome core particles.Nature communications · 2026Article
- Molecular mechanisms in rare proteasomopathies.EULAR rheumatology open · 2026Review
- Substrate secondary structure is associated with proteasomal cleavage propensity.Frontiers in bioinformatics · 2026Article
- Reevaluating Gold(I) Thiophilicity in Reduced Dielectric Environments: IRMPD Spectroscopy and Theoretical Investigation of Auranofin-Glutathione Complexes.Bioinorganic chemistry and applications · 2026Article
- Proteasome-derived peptides: separating the trash from the recycling.Trends in biochemical sciences · 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
- Anthricin-induced hyperactive proteasome and its molecular mechanism.Biochemistry and biophysics reports · 2024Article
- Structural roles of Ump1 and β-subunit propeptides in proteasome biogenesis.Life science alliance · 2024Article
- Functional 20S Proteasomes in Retroviruses: Evidence in Favor.International journal of molecular sciences · 2024Article
- Electrostatic Preorganization in Three Distinct Heterogeneous Proteasome β-Subunits.ACS catalysis · 2024Article
- Structural elucidation of recombinant Trichomonas vaginalis 20S proteasome bound to covalent inhibitors.Nature communications · 2024Article
- Dataset from a human-in-the-loop approach to identify functionally important protein residues from literature.Scientific data · 2024Article
- Mechanism of autocatalytic activation during proteasome assembly.Nature structural & molecular biology · 2024Article
5 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 5 institutions in 2 countries.
Funding
Abstract
Biogenesis of the 20S proteasome is tightly regulated. The N-terminal propeptides protecting the active-site threonines are autocatalytically released only on completion of assembly. However, the trigger for the self-activation and the reason for the strict conservation of threonine as the active site nucleophile remain enigmatic. Here we use mutagenesis, X-ray crystallography and biochemical assays to suggest that Lys33 initiates nucleophilic attack of the propeptide by deprotonating the Thr1 hydroxyl group and that both residues together with Asp17 are part of a catalytic triad. Substitution of Thr1 by Cys disrupts the interaction with Lys33 and inactivates the proteasome. Although a Thr1Ser mutant is active, it is less efficient compared with wild type because of the unfavourable orientation of Ser1 towards incoming substrates. This work provides insights into the basic mechanism of proteolysis and propeptide autolysis, as well as the evolutionary pressures that drove the proteasome to become a threonine protease.
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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.