ArticleProceedings of the National Academy of Sciences of the United States of America2014
Differential global structural changes in the core particle of yeast and mouse proteasome induced by ligand binding.
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 15 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
15 citing papers in PubMed, 32 citations in OpenAlex.
- Structural basis for allosteric modulation of M. tuberculosis proteasome core particle.Nature communications · 2025Article
- Mechanistic diversity in MHC class I antigen recognition.The Biochemical journal · 2021Review
- Conformational maps of human 20S proteasomes reveal PA28- and immuno-dependent inter-ring crosstalks.Nature communications · 2020Article
- Article
- Structure of human immunoproteasome with a reversible and noncompetitive inhibitor that selectively inhibits activated lymphocytes.Nature communications · 2017Article
- Article
- Extracellular proteasome-osteopontin circuit regulates cell migration with implications in multiple sclerosis.Scientific reports · 2017Article
- Understanding the molecular mechanism for the differential inhibitory activities of compounds against MTH1.Scientific reports · 2017Article
- Structure of the unliganded form of the proprotein convertase furin suggests activation by a substrate-induced mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Inhibition of Proteasome Activity Induces Formation of Alternative Proteasome Complexes.The Journal of biological chemistry · 2016Article
- Proteasomes generate spliced epitopes by two different mechanisms and as efficiently as non-spliced epitopes.Scientific reports · 2016Article
- Article
- Cryo-EM reveals the conformation of a substrate analogue in the human 20S proteasome core.Nature communications · 2015Article
- Proteasome inhibition by bortezomib: A left hook and a right punch.EBioMedicine · 2015Article
- Maturation of the proteasome core particle induces an affinity switch that controls regulatory particle association.Nature communications · 2015Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two clusters of configurations of the main proteolytic subunit β5 were identified by principal component analysis of crystal structures of the yeast proteasome core particle (yCP). The apo-cluster encompasses unliganded species and complexes with nonpeptidic ligands, and the pep-cluster comprises complexes with peptidic ligands. The murine constitutive CP structures conform to the yeast system, with the apo-form settled in the apo-cluster and the PR-957 (a peptidic ligand) complex in the pep-cluster. In striking contrast, the murine immune CP classifies into the pep-cluster in both the apo and the PR-957-liganded species. The two clusters differ essentially by multiple small structural changes and a domain motion enabling enclosure of the peptidic ligand and formation of specific hydrogen bonds in the pep-cluster. The immune CP species is in optimal peptide binding configuration also in its apo form. This favors productive ligand binding and may help to explain the generally increased functional activity of the immunoproteasome. Molecular dynamics simulations of the representative murine species are consistent with the experimentally observed configurations. A comparison of all 28 subunits of the unliganded species with the peptidic liganded forms demonstrates a greatly enhanced plasticity of β5 and suggests specific signaling pathways to other subunits.
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.