ReviewJournal of molecular biology2013
Design principles of a universal protein degradation machine.
Review in Journal of molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 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
38 citing papers in PubMed, 60 citations in OpenAlex.
- Substrate-interacting pore loops of two ATPase subunits determine the degradation efficiency of the 26S proteasome.Nature communications · 2026Article
- Desmosome and Hemidesmosome Release via Exosomes from Retinal Pigmented Epithelium - A Precursor to Epithelial-Mesenchymal Transition in Early AMD?Current eye research · 2025Review
- Structural landscape of the degrading 26S proteasome reveals conformation-specific binding of TXNL1.Nature structural & molecular biology · 2025Article
- Structural landscape of AAA+ ATPase motor states in the substrate-degrading human 26S proteasome reveals conformation-specific binding of TXNL1.bioRxiv : the preprint server for biology · 2024Article
- Article
- Ubiquitin modulates 26Science advances · 2022Article
- Functions and Molecular Mechanisms of Deltex Family Ubiquitin E3 Ligases in Development and Disease.Frontiers in cell and developmental biology · 2021Review
- Cooperative Binding of the Cationic Porphyrin Tris-T4 Enhances Catalytic Activity of 20S Proteasome Unveiling a Complex Distribution of Functional States.International journal of molecular sciences · 2020Article
- Cracking the Monoubiquitin Code of Genetic Diseases.International journal of molecular sciences · 2020Review
- Examination of the nucleotide-linked assembly mechanism of E. coli ClpA.Protein science : a publication of the Protein Society · 2019Article
- ClpP Protease, a Promising Antimicrobial Target.International journal of molecular sciences · 2019Review
- Small molecule inhibitors reveal allosteric regulation of USP14 via steric blockade.Cell research · 2018Article
- POH1 Knockdown Induces Cancer Cell Apoptosis via p53 and Bim.Neoplasia (New York, N.Y.) · 2018Article
- An inhibitor of the proteasomal deubiquitinating enzyme USP14 induces tau elimination in cultured neurons.The Journal of biological chemistry · 2017Article
- Regulating protein breakdown through proteasome phosphorylation.The Biochemical journal · 2017Review
- Induction of proteotoxic stress by the mycotoxin patulin.Toxicology letters · 2017Article
- Functional Diversity of AAA+ Protease Complexes inFrontiers in molecular biosciences · 2017Review
- AAA-ATPases in Protein Degradation.Frontiers in molecular biosciences · 2017Review
- Ligand-induced and small-molecule control of substrate loading in a hexameric helicase.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Endoplasmic Reticulum-Associated Degradation and Lipid Homeostasis.Annual review of nutrition · 2016Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 2 institutions in 1 country.
Funding
Abstract
The 26S proteasome is a 2.5-MDa, 32-subunit ATP-dependent protease that is responsible for the degradation of ubiquitinated protein targets in all eukaryotic cells. This proteolytic machine consists of a barrel-shaped peptidase capped by a large regulatory particle, which contains a heterohexameric AAA+ unfoldase as well as several structural modules of previously unknown function. Recent electron microscopy (EM) studies have allowed major breakthroughs in understanding the architecture of the regulatory particle, revealing that the additional modules provide a structural framework to position critical, ubiquitin-interacting subunits and thus allow the 26S proteasome to function as a universal degradation machine for a wide variety of protein substrates. The EM studies have also uncovered surprising asymmetries in the spatial arrangement of proteasome subunits, yet the functional significance of these architectural features remains unclear. This review will summarize the recent findings on 26S proteasome structure and discuss the mechanistic implications for substrate binding, deubiquitination, unfolding, and degradation.
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.