ReviewCellular and molecular life sciences : CMLS2004
Keepers at the final gates: regulatory complexes and gating of the proteasome channel.
Review in Cellular and molecular life sciences : CMLS, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 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
28 citing papers in PubMed, 1 synthesis or guideline pooled it, 66 citations in OpenAlex.
- The proteasome as a druggable target with multiple therapeutic potentialities: Cutting and non-cutting edges.Pharmacology & therapeutics · 2020Pooled it
- Differential Activity and Expression of Proteasome in Seminiferous Epithelium During Mouse Spermatogenesis.International journal of molecular sciences · 2025Article
- Proteasome Activators and Ageing: Restoring Proteostasis Using Small Molecules.Sub-cellular biochemistry · 2024Review
- A Role for the Proteasome Alpha2 Subunit N-Tail in Substrate Processing.Biomolecules · 2023Article
- Modulation of the 20S Proteasome Activity by Porphyrin Derivatives Is Steered through Their Charge Distribution.Biomolecules · 2022Article
- Review
- Structural Insights into Substrate Recognition and Processing by the 20S Proteasome.Biomolecules · 2021Review
- Cryo-EM structures of the human PA200 and PA200-20S complex reveal regulation of proteasome gate opening and two PA200 apertures.PLoS biology · 2020Article
- Probing the cooperativity ofProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Protein Expression of Proteasome Subunits in Elderly Patients with Schizophrenia.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2016Article
- Uncommon functional properties of the first piscine 26S proteasome from the Antarctic notothenioid Trematomus bernacchii.Bioscience reports · 2016Article
- Nuclear transport of yeast proteasomes.Biomolecules · 2014Review
- Understanding the mechanism of proteasome 20S core particle gating.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Inhibition of human and yeast 20S proteasome by analogues of trypsin inhibitor SFTI-1.PloS one · 2014Article
- Redox regulation of the proteasome via S-glutathionylation.Redox biology · 2013Review
- Redox control of 20S proteasome gating.Antioxidants & redox signaling · 2012Article
- Article
- Dependence of proteasome processing rate on substrate unfolding.The Journal of biological chemistry · 2011Article
- Proteasome activator 200: the heat is on...Molecular & cellular proteomics : MCP · 2011Review
- Analysis of proteasomal proteolysis during the in vitro metacyclogenesis of Trypanosoma cruzi.PloS one · 2011Article
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 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The proteolytic active sites of the 26S proteasome are sequestered within the central chamber of its 20S catalytic core particle. Access to this chamber is through a narrow channel defined by the outer alpha subunits. Free proteasome 20S core particles are found in an autoinhibited state in which the N-termini of neighboring alpha subunits are anchored by an intricate lattice of interactions blocking access to the channel. Entry of substrates into proteasomes can be enhanced by attachment of activators or regulatory particles. An important part of this activation is channel gating; regulatory particles rearrange the blocking residues to form an open pore and promote substrate entry into the proteolytic chamber. Interestingly, some substrates can open the entrance themselves and thus facilitate their own destruction. In this review, we will discuss the mechanisms proposed for channel gating and the interactions required to maintain stable closed and open conformations.
Indexed as
Identifiers
What Socratic 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 Socratic graph.