ArticleNature communications2015
Cryo-EM reveals the conformation of a substrate analogue in the human 20S proteasome core.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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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.
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Who cites it
29 citing papers in PubMed.
- Substrate secondary structure is associated with proteasomal cleavage propensity.Frontiers in bioinformatics · 2026Article
- Inhibitors of the 20S proteasome β5 subunit as potent and selective agents againstAntimicrobial agents and chemotherapy · 2025Article
- Optimization of Species-Selective Reversible Proteasome Inhibitors for the Treatment of Malaria.Journal of medicinal chemistry · 2025Article
- The Evolving Landscape of Protein Allostery: From Computational and Experimental Perspectives.Journal of molecular biology · 2025Review
- Foam film vitrification for cryo-EM.Nature communications · 2025Article
- RNA sample optimization for cryo-EM analysis.Nature protocols · 2025Review
- Identification of potent and reversible piperidine carboxamides that are species-selective orally active proteasome inhibitors to treat malaria.Cell chemical biology · 2024Article
- Characterization of Complexes and Supramolecular Structures by Electron Microscopy.Advances in experimental medicine and biology · 2024Article
- A guide to antigen processing and presentation.Nature reviews. Immunology · 2022Review
- Developing Graphene Grids for Cryoelectron Microscopy.Frontiers in molecular biosciences · 2022Review
- The Cryo-EM Effect: Structural Biology of Neurodegenerative Disease Proteostasis Factors.Journal of neuropathology and experimental neurology · 2021Review
- Association with proteasome determines pathogenic threshold of polyglutamine expansion diseases.Biochemical and biophysical research communications · 2021Article
- Characterization of Fully Recombinant Human 20S and 20S-PA200 Proteasome Complexes.Molecular cell · 2019Article
- Current outcomes when optimizing 'standard' sample preparation for single-particle cryo-EM.Journal of microscopy · 2019Article
- Microfluidic protein isolation and sample preparation for high-resolution cryo-EM.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- A Practical Review of Proteasome Pharmacology.Pharmacological reviews · 2019Review
- Classification of Single Particles from Human Cell Extract Reveals Distinct Structures.Cell reports · 2018Article
- Approaches to altering particle distributions in cryo-electron microscopy sample preparation.Acta crystallographica. Section D, Structural biology · 2018Review
- Structure of human immunoproteasome with a reversible and noncompetitive inhibitor that selectively inhibits activated lymphocytes.Nature communications · 2017Article
- Structure-based drug design: aiming for a perfect fit.Essays in biochemistry · 2017Review
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
The proteasome is a highly regulated protease complex fundamental for cell homeostasis and controlled cell cycle progression. It functions by removing a wide range of specifically tagged proteins, including key cellular regulators. Here we present the structure of the human 20S proteasome core bound to a substrate analogue inhibitor molecule, determined by electron cryo-microscopy (cryo-EM) and single-particle analysis at a resolution of around 3.5 Å. Our map allows the building of protein coordinates as well as defining the location and conformation of the inhibitor at the different active sites. These results open new prospects to tackle the proteasome functional mechanisms. Moreover, they also further demonstrate that cryo-EM is emerging as a realistic approach for general structural studies of protein-ligand interactions.
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Registered trials
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