ArticleOpen biology2017
Phosphatase UBLCP1 controls proteasome assembly.
Article in Open biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 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
22 citing papers in PubMed, 26 citations in OpenAlex.
- PSMC2 drives tumor progression in nasopharyngeal carcinoma by inhibiting ferroptosis through STAT3.Discover oncology · 2026Article
- PSMC2 serves as a potential regulatory target of EZH2 in promoting glioma progression via epithelial-mesenchymal transition.Scientific reports · 2026Article
- A multi-omics target study for glioblastoma multiforme (GBM) based on Mendelian randomization analysis.IBRO neuroscience reports · 2025Article
- [Research and Therapeutic Advances of 26S Proteasome Subunit in Non-small Cell Lung Cancer].Zhongguo fei ai za zhi = Chinese journal of lung cancer · 2025Review
- Phosphatase UBLCP1 is required for the growth, virulence and mitochondrial integrity of Toxoplasma gondii.Parasites & vectors · 2025Article
- Exploring new drug treatment targets for immune related bone diseases using a multi omics joint analysis strategy.Scientific reports · 2025Article
- Promoting proteostasis by cAMP/PKA and cGMP/PKG.Trends in molecular medicine · 2025Review
- Mechanisms and regulation of substrate degradation by the 26S proteasome.Nature reviews. Molecular cell biology · 2025Review
- Identification of molecular signatures defines the differential proteostasis response in induced spinal and cranial motor neurons.Cell reports · 2024Article
- A novel autism-associated UBLCP1 mutation impacts proteasome regulation/activity.Translational psychiatry · 2023Article
- Research Trends in C-Terminal Domain Nuclear Envelope Phosphatase 1.Life (Basel, Switzerland) · 2023Review
- Transcriptomic underpinnings of high and low mirror aggression zebrafish behaviours.BMC biology · 2022Article
- Oxidative and salt stresses alter the 26S proteasome holoenzyme and associated protein profiles in Arabidopsis thaliana.BMC plant biology · 2021Article
- Diverse Functions of Tim50, a Component of the Mitochondrial Inner Membrane Protein Translocase.International journal of molecular sciences · 2021Review
- Proteins containing ubiquitin-like (Ubl) domains not only bind to 26S proteasomes but also induce their activation.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Reversible phosphorylation of Rpn1 regulates 26S proteasome assembly and function.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Article
- The Role and Regulation of Autophagy and the Proteasome During Aging and Senescence in Plants.Genes · 2019Review
- Regulation of Proteasome Activity by (Post-)transcriptional Mechanisms.Frontiers in molecular biosciences · 2019Review
- Dynamic Regulation of the 26S Proteasome: From Synthesis to Degradation.Frontiers in molecular biosciences · 2019Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Ubiquitin-like domain-containing C-terminal domain phosphatase 1 (UBLCP1), an FCP/SCP phosphatase family member, was identified as the first proteasome phosphatase. UBLCP1 binds to proteasome subunit Rpn1 and dephosphorylates the proteasome
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.