ArticleMolecular cell2009
Structure and activity of the N-terminal substrate recognition domains in proteasomal ATPases.
Article in Molecular cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers, 1 of them a synthesis that pooled it.
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
71 citing papers in PubMed, 1 synthesis or guideline pooled it, 119 citations in OpenAlex.
- The proteasome as a druggable target with multiple therapeutic potentialities: Cutting and non-cutting edges.Pharmacology & therapeutics · 2020Pooled it
- "Pupdates" on proteasomal degradation in bacteria.Journal of bacteriology · 2025Review
- Flotillin-mediated stabilization of unfolded proteins in bacterial membrane microdomains.Nature communications · 2024Article
- To Kill or to Be Killed: How Does the Battle between the UPS and Autophagy Maintain the Intracellular Homeostasis in Eukaryotes?International journal of molecular sciences · 2023Review
- Stoichiometry of Nucleotide Binding to Proteasome AAA+ ATPase Hexamer Established by Native Mass Spectrometry.Molecular & cellular proteomics : MCP · 2020Article
- The molecular principles governing the activity and functional diversity of AAA+ proteins.Nature reviews. Molecular cell biology · 2020Review
- N domain of the Lon AAA+ protease controls assembly and substrate choice.Protein science : a publication of the Protein Society · 2019Article
- Stepping up protein degradation.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Cryo-EM structures of the archaeal PAN-proteasome reveal an around-the-ring ATPase cycle.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Biology and Biochemistry of Bacterial Proteasomes.Sub-cellular biochemistry · 2019Review
- The Bacterial Proteasome at the Core of Diverse Degradation Pathways.Frontiers in molecular biosciences · 2019Review
- Proteolytic systems of archaea: slicing, dicing, and mincing in the extreme.Emerging topics in life sciences · 2018Article
- Conformational switching in the coiled-coil domains of a proteasomal ATPase regulates substrate processing.Nature communications · 2018Article
- Cellular origin of the viral capsid-like bacterial microcompartments.Biology direct · 2017Article
- Proteasome Structure and Assembly.Journal of molecular biology · 2017Review
- Mycobacterium tuberculosis proteasomal ATPase Mpa has a β-grasp domain that hinders docking with the proteasome core protease.Molecular microbiology · 2017Article
- Reversible phosphorylation of the 26S proteasome.Protein & cell · 2017Review
- Bacterial Proteasomes: Mechanistic and Functional Insights.Microbiology and molecular biology reviews : MMBR · 2017Review
- High-resolution cryo-EM structure of the proteasome in complex with ADP-AlFx.Cell research · 2017Article
- Time-resolved neutron scattering provides new insight into protein substrate processing by a AAA+ unfoldase.Scientific reports · 2017Article
11 more citing papers are in PubMed but not listed here.
Corrections and comments
- Commented on by
Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The proteasome forms the core of the protein quality control system in archaea and eukaryotes and also occurs in one bacterial lineage, the Actinobacteria. Access to its proteolytic compartment is controlled by AAA ATPases, whose N-terminal domains (N domains) are thought to mediate substrate recognition. The N domains of an archaeal proteasomal ATPase, Archaeoglobus fulgidus PAN, and of its actinobacterial homolog, Rhodococcus erythropolis ARC, form hexameric rings, whose subunits consist of an N-terminal coiled coil and a C-terminal OB domain. In ARC-N, the OB domains are duplicated and form separate rings. PAN-N and ARC-N can act as chaperones, preventing the aggregation of heterologous proteins in vitro, and this activity is preserved in various chimeras, even when these include coiled coils and OB domains from unrelated proteins. The structures suggest a molecular mechanism for substrate processing based on concerted radial motions of the coiled coils relative to the OB rings.
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.