ArticleProceedings of the National Academy of Sciences of the United States of America2014
Understanding the mechanism of proteasome 20S core particle gating.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
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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
23 citing papers in PubMed.
- Molecular architecture and spatial organization of proteasomes in the human sperm nucleus.Nature structural & molecular biology · 2026Article
- Article
- Allosteric regulation of proteolytic machines unveiled by the synergy between cryo-EM and solution NMR spectroscopy.The Biochemical journal · 2025Review
- Bortezomib Inhibits Open Configurations of the 20S Proteasome.Journal of the American Society for Mass Spectrometry · 2024Article
- In-silico identification and prioritization of therapeutic targets of asthma.Scientific reports · 2023Article
- Polymer/copper nanocomplex-induced lysosomal cell death promotes tumor lymphocyte infiltration and synergizes anti-PD-L1 immunotherapy for triple-negative breast cancer.Biomaterials science · 2023Article
- Article
- Article
- Insulin-Degrading Enzyme Is a Non Proteasomal Target of Carfilzomib and Affects the 20S Proteasome Inhibition by the Drug.Biomolecules · 2022Article
- The diversity of linkage-specific polyubiquitin chains and their role in synaptic plasticity and memory formation.Neurobiology of learning and memory · 2020Review
- The War against Tuberculosis: A Review of Natural Compounds and Their Derivatives.Molecules (Basel, Switzerland) · 2020Review
- Comparative Structural Analysis of 20S Proteasome Ortholog Protein Complexes by Native Mass Spectrometry.ACS central science · 2020Article
- Exploring long-range cooperativity in the 20S proteasome core particle fromProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Methyl-Based NMR Spectroscopy Methods for Uncovering Structural Dynamics in Large Proteins and Protein Complexes.Biochemistry · 2019Review
- Origin of Internal Friction in Disordered Proteins Depends on Solvent Quality.The journal of physical chemistry. B · 2018Article
- Insight into Inhibitor Binding in the Eukaryotic Proteasome: Computations of the 20S CP.International journal of molecular sciences · 2018Article
- Induction of gut proteasome activity in hemorrhagic shock and its recovery by treatment with diphenyldihaloketones CLEFMA and EF24.American journal of physiology. Gastrointestinal and liver physiology · 2018Article
- Small Molecule Modulation of Proteasome Assembly.Biochemistry · 2018Article
- Probing the cooperativity ofProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Precise assembly and regulation of 26S proteasome and correlation between proteasome dysfunction and neurodegenerative diseases.BMB reports · 2016Review
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The 20S core particle proteasome is a molecular machine playing an important role in cellular function by degrading protein substrates that no longer are required or that have become damaged. Regulation of proteasome activity occurs, in part, through a gating mechanism controlling the sizes of pores at the top and bottom ends of the symmetric proteasome barrel and restricting access to catalytic sites sequestered in the lumen of the structure. Although atomic resolution models of both open and closed states of the proteasome have been elucidated, the mechanism by which gates exchange between these states remains to be understood. Here, this is investigated by using magnetization transfer NMR spectroscopy focusing on the 20S proteasome core particle from Thermoplasma acidophilum. We show from viscosity-dependent proteasome gating kinetics that frictional forces originating from random solvent motions are critical for driving the gating process. Notably, a small effective hydrodynamic radius (EHR; <4Å) is obtained, providing a picture in which gate exchange proceeds through many steps involving only very small segment sizes. A small EHR further suggests that the kinetics of gate interconversion will not be affected appreciably by large viscogens, such as macromolecules found in the cell, so long as they are inert. Indeed, measurements in cell lysate reveal that the gate interconversion rate decreases only slightly, demonstrating that controlled studies in vitro provide an excellent starting point for understanding regulation of 20S core particle function in complex, biologically relevant environments.
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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.