ArticleBioorganic & medicinal chemistry2015
A potent and selective inhibitor for the UBLCP1 proteasome phosphatase.
Article in Bioorganic & medicinal chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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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, 13 citations in OpenAlex.
- Immune Cell-Mediated Retinoblastoma Development: Genetic and Molecular Mechanisms.International journal of genomics · 2026Article
- 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
- Localized Proteasomal Degradation: From the Nucleus to Cell Periphery.Biomolecules · 2022Review
- Reversible phosphorylation of Rpn1 regulates 26S proteasome assembly and function.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Key Topics in Molecular Docking for Drug Design.International journal of molecular sciences · 2019Review
- Phosphatase UBLCP1 controls proteasome assembly.Open biology · 2017Article
- Reversible phosphorylation of the 26S proteasome.Protein & cell · 2017Review
- Dephosphorylating eukaryotic RNA polymerase II.Biochimica et biophysica acta · 2016Review
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
The ubiquitin-like domain-containing C-terminal domain phosphatase 1 (UBLCP1) has been implicated as a negative regulator of the proteasome, a key mediator in the ubiquitin-dependent protein degradation. Small molecule inhibitors that block UBLCP1 activity would be valuable as research tools and potential therapeutics for human diseases caused by the cellular accumulation of misfold/damaged proteins. We report a salicylic acid fragment-based library approach aimed at targeting both the phosphatase active site and its adjacent binding pocket for enhanced affinity and selectivity. Screening of the focused libraries led to the identification of the first potent and selective UBLCP1 inhibitor 13. Compound 13 exhibits an IC50 of 1.0μM for UBLCP1 and greater than 5-fold selectivity against a large panel of protein phosphatases from several distinct families. Importantly, the inhibitor possesses efficacious cellular activity and is capable of inhibiting UBLCP1 function in cells, which in turn up-regulates nuclear proteasome activity. These studies set the groundwork for further developing compound 13 into chemical probes or potential therapeutic agents targeting the UBLCP1 phosphatase.
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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.