ArticleMolecular biotechnology2015
Simultaneous EGFP and tag labeling of the β7 subunit for live imaging and affinity purification of functional human proteasomes.
Article in Molecular biotechnology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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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.
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Who cites it
9 citing papers in PubMed.
- A novel autism-associated UBLCP1 mutation impacts proteasome regulation/activity.Translational psychiatry · 2023Article
- Myelin Basic Protein Fragmentation by Engineered Human Proteasomes with Different Catalytic Phenotypes Revealed Direct Peptide Ligands of MS-Associated and Protective HLA Class I Molecules.International journal of molecular sciences · 2023Article
- Article
- Post-Translational Modifications of Extracellular Proteasome.Molecules (Basel, Switzerland) · 2020Article
- Proteomic analysis of affinity-purified extracellular proteasomes reveals exclusively 20S complexes.Oncotarget · 2017Article
- Catalytically Active Proteasomes Function Predominantly in the Cytosol.The Journal of biological chemistry · 2016Article
- Nuclear Import of Yeast Proteasomes.Cells · 2015Review
- Intracellular Dynamics of the Ubiquitin-Proteasome-System.F1000Research · 2015Review
- Article
Corrections and comments
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The proteasome is a multi-subunit protein complex that serves as a major pathway for intracellular protein degradation, playing important functions in various biological processes. The C-terminus of the β7 (PSMB4) proteasome subunit was tagged with EGFP and with a composite element for affinity purification and TEV cleavage elution (HTBH). When the construct was retrovirally delivered into HeLa cells, virtually all of the β7-EGFP-HTBH fusion protein was found to be incorporated into fully functional proteasomes. This ensured that subcellular localization of the EGFP signal in living HeLa cells could be attributed to β7-EGFP-HTBH within the proteasome complex rather than to free protein. The β7-EGFP-HTBH fusion can, therefore, serve as a valuable tool for in vivo imaging of proteasomes as well as for high-affinity purification of these complexes and associated molecules for subsequent analyses.
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Registered trials
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