ArticleNature communications2020
Allosteric coupling between α-rings of the 20S proteasome.
Article in Nature communications, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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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.
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Who cites it
16 citing papers in PubMed, 27 citations in OpenAlex.
- A cost-effective 200 kV cryo-EM core facility for high resolution single particle analysis.Methods in microscopy · 2026Article
- Integrative analysis of the PSMA family identifies PSMA6 as an adverse prognostic biomarker promoting bladder cancer cell proliferation.International journal of medical sciences · 2026Article
- Not Just PA28γ: What We Know About the Role of PA28αβ in Carcinogenesis.Biomolecules · 2025Review
- Structural basis for allosteric modulation of M. tuberculosis proteasome core particle.Nature communications · 2025Article
- Scanning Tunneling Microscope Measurement of Proteasome Conductance.Biomolecules · 2025Article
- Modeling liquid-liquid phase separation and its impact on proteasomal substrate degradation.Computational and structural biotechnology journal · 2025Article
- Analysis of 26S Proteasome Activity across Arabidopsis Tissues.Plants (Basel, Switzerland) · 2024Article
- Stability of 20S Proteasome Configurations: Preopening the Axial Gate.The journal of physical chemistry letters · 2023Article
- Allosteric regulation of the 20S proteasome by the Catalytic Core Regulators (CCRs) family.Nature communications · 2023Article
- Matrix-Landing Mass Spectrometry for Electron Microscopy Imaging of Native Protein Complexes.Analytical chemistry · 2022Article
- Allostery Modulates Interactions between Proteasome Core Particles and Regulatory Particles.Biomolecules · 2022Review
- Cooperative allostery and structural dynamics of streptavidin at cryogenic- and ambient-temperature.Communications biology · 2022Article
- PA28γ-20S proteasome is a proteolytic complex committed to degrade unfolded proteins.Cellular and molecular life sciences : CMLS · 2021Article
- High-power near-concentric Fabry-Perot cavity for phase contrast electron microscopy.The Review of scientific instruments · 2021Article
- Structural Fluctuations of the Human Proteasome α7 Homo-Tetradecamer Double Ring Imply the Proteasomal α-Ring Assembly Mechanism.International journal of molecular sciences · 2021Article
- Review
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
Abstract
Proteasomal machinery performs essential regulated protein degradation in eukaryotes. Classic proteasomes are symmetric, with a regulatory ATPase docked at each end of the cylindrical 20S. Asymmetric complexes are also present in cells, either with a single ATPase or with an ATPase and non-ATPase at two opposite ends. The mechanism that populates these different proteasomal complexes is unknown. Using archaea homologs, we construct asymmetric forms of proteasomes. We demonstrate that the gate conformation of the two opposite ends of 20S are coupled: binding one ATPase opens a gate locally, and also opens the opposite gate allosterically. Such allosteric coupling leads to cooperative binding of proteasomal ATPases to 20S and promotes formation of proteasomes symmetrically configured with two identical ATPases. It may also promote formation of asymmetric complexes with an ATPase and a non-ATPase at opposite ends. We propose that in eukaryotes a similar mechanism regulates the composition of the proteasomal population.
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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.