ReviewBiological chemistry2008
Some assembly required: dedicated chaperones in eukaryotic proteasome biogenesis.
Review in Biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 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
29 citing papers in PubMed, 43 citations in OpenAlex.
- MSTO1 functions as a TRiC assembly factor linking cytosolic proteostasis to mitochondrial function.bioRxiv : the preprint server for biology · 2026Article
- The α5-α6-α7-Pba3-Pba4 Complex: A Starting Unit in Proteasome Core Particle Assembly.Biomolecules · 2025Article
- Retinal Pigment Epithelium Under Oxidative Stress: Chaperoning Autophagy and Beyond.International journal of molecular sciences · 2025Review
- Assembly chaperone Nas6 selectively destabilizes 26S proteasomes with defective regulatory particle-core particle interfaces.The Journal of biological chemistry · 2023Article
- Chaperone-mediated assembly of the proteasome core particle - recent developments and structural insights.Journal of cell science · 2022Review
- Structure, Dynamics and Function of the 26S Proteasome.Sub-cellular biochemistry · 2021Review
- Regulation of proteasome assembly and activity in health and disease.Nature reviews. Molecular cell biology · 2018Review
- Distinct Elements in the Proteasomal β5 Subunit Propeptide Required for Autocatalytic Processing and Proteasome Assembly.The Journal of biological chemistry · 2016Article
- Maturation of the proteasome core particle induces an affinity switch that controls regulatory particle association.Nature communications · 2015Article
- N-terminal α7 deletion of the proteasome 20S core particle substitutes for yeast PI31 function.Molecular and cellular biology · 2015Article
- Assembly of the 20S proteasome.Biochimica et biophysica acta · 2014Review
- Mouse zygote-specific proteasome assembly chaperone important for maternal-to-zygotic transition.Biology open · 2013Article
- Molecular architecture and assembly of the eukaryotic proteasome.Annual review of biochemistry · 2013Review
- The ubiquitin-proteasome system of Saccharomyces cerevisiae.Genetics · 2012Review
- Stable incorporation of ATPase subunits into 19 S regulatory particle of human proteasome requires nucleotide binding and C-terminal tails.The Journal of biological chemistry · 2012Article
- Vid30 is required for the association of Vid vesicles and actin patches in the vacuole import and degradation pathway.Autophagy · 2012Article
- Incorporation of the Rpn12 subunit couples completion of proteasome regulatory particle lid assembly to lid-base joining.Molecular cell · 2011Article
- Novel interactions between actin and the proteasome revealed by complex haploinsufficiency.PLoS genetics · 2011Article
- C termini of proteasomal ATPases play nonequivalent roles in cellular assembly of mammalian 26 S proteasome.The Journal of biological chemistry · 2011Article
- A conserved 20S proteasome assembly factor requires a C-terminal HbYX motif for proteasomal precursor binding.Nature structural & molecular biology · 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
Abstract
The 26S proteasome is the key eukaryotic protease responsible for the degradation of intracellular proteins. Protein degradation by the 26S proteasome plays important roles in numerous cellular processes, including the cell cycle, differentiation, apoptosis, and the removal of damaged or misfolded proteins. How this 2.5-MDa complex, composed of at least 32 different polypeptides, is assembled in the first place is not well understood. However, it has become evident that this complicated task is facilitated by a framework of protein factors that chaperone the nascent proteasome through its various stages of assembly. We review here the known proteasome-specific assembly factors, most only recently discovered, and describe their potential roles in proteasome assembly, with an emphasis on the many remaining unanswered questions about this intricate process of assisted self-assembly.
Indexed as
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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.