ArticleBioorganic & medicinal chemistry2012
A bright approach to the immunoproteasome: development of LMP2/β1i-specific imaging probes.
Article in Bioorganic & medicinal chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 21 citations in OpenAlex.
- Solid tumor rejection using personalized incompatible human leukocyte antigen (HLA) and blood group ABH antigens.Exploration of medicine · 2025Article
- Imaging antigen processing and presentation in cancer.Immunotherapy advances · 2025Review
- Identification of a new class of proteasome inhibitors based on a naphthyl-azotricyclic-urea-phenyl scaffold.RSC medicinal chemistry · 2023Article
- Site-Specific Proteasome Inhibitors.Biomolecules · 2021Review
- Emerging role of immunoproteasomes in pathophysiology.Immunology and cell biology · 2016Review
- Elucidating the catalytic subunit composition of distinct proteasome subtypes: a crosslinking approach employing bifunctional activity-based probes.Chembiochem : a European journal of chemical biology · 2015Article
- A FRET-based approach for identification of proteasome catalytic subunit composition.Molecular bioSystems · 2014Article
- Activity-based imaging probes of the proteasome.Cell biochemistry and biophysics · 2013Review
- Inhibitors of the immunoproteasome: current status and future directions.Current pharmaceutical design · 2013Review
- Activity-based near-infrared fluorescent probe for LMP7: a chemical proteomics tool for the immunoproteasome in living cells.Chembiochem : a European journal of chemical biology · 2012Article
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
Abstract
While the constitutive, 26S proteasome plays an important role in regulating many important cellular processes, a variant form known as the immunoproteasome is thought to primarily function in adaptive immune responses. However, recent studies indicate an association of immunoproteasomes with many physiological disorders such as cancer, neurodegenerative, and inflammatory diseases. Despite this, the detailed functions of the immunoproteasome remain poorly understood. Immunoproteasome-specific probes are essential to gain insight into immunoproteasome function. Here, we describe for the first time the development of cell-permeable activity-based fluorescent probes, UK101-Fluor and UK101-B660, which selectively target the catalytically active LMP2/β1i subunit of the immunoproteasome. These probes facilitate rapid detection of the cellular localization of catalytically active immunoproteasomes in living cells, providing a valuable tool to analyze immunoproteasome functions. Additionally, as LMP2/β1i may serve as a potential tumor biomarker, an LMP2/β1i-targeting fluorescent imaging probe may be applicable to a rapid readout assay to determine tumor LMP2/β1i levels.
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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.