Evidence map›Paper›PMID 30862160›Full record

ArticleJournal of the American Chemical Society2019

Monitoring the Immunoproteasome in Live Cells Using an Activity-Based Peptide-Peptoid Hybrid Probe.

Breanna L Zerfas, Darci J Trader

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.7field-weighted citation impact, top 15% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. ACS chemical neuroscience · 2026
    Article
  3. Synthesis and Application of a Versatile Immunoproteasome Activity Probe.Chembiochem : a European journal of chemical biology · 2024
    Article
  4. Article
  5. Article
  6. Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Immunoproteasome in IgA Nephropathy: State-of-Art and Future Perspectives.International journal of biological sciences · 2020
    Review
  14. Article
  15. Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Breanna L ZerfasDepartment of Medicinal Chemistry and Molecular Pharmacology , Purdue University , 575 West Stadium Avenue , West Lafayette , Indiana 47907 , United States.
Darci J TraderDepartment of Medicinal Chemistry and Molecular Pharmacology , Purdue University , 575 West Stadium Avenue , West Lafayette , Indiana 47907 , United States.ORCID 0000-0002-0607-1243
Purdue University West Lafayette · US

Funding

Transgenic Mouse Core Facility Shared Resource (TMCF-SR)P30CA023168 · NCI · PURDUE UNIVERSITY WEST LAFAYETTE · PI Andrea L Kasinski · 1985 to 2026
$43.4M
Development of Activity-Based Chemical Reporters to Differentiate Proteasome Isoforms in CellsR21GM131206 · NIGMS · PURDUE UNIVERSITY · PI TRADER, DARCI J · 2019 to 2020
$426k
NCI NIH HHS P30 CA023168NIGMS NIH HHS R21 GM131206
6 · The paper itself

Abstract

Activity-based probes have greatly improved our understanding of the intrinsic roles and expression levels of various proteins within cells. To be useful in live cells, probes must be cell permeable and provide a read-out that can be measured without disrupting the cells or the activity of the target. Unfortunately, probes for the various forms of the proteasome that can be utilized in intact cells are limited; commercially available probes are most effectively used with purified protein or cell lysate. The proteasome, both the 26S and various isoforms of the 20S CP, is an important target with reported roles in cancer, autoimmune disorders, and neurodegenerative diseases. Here, we present the development of a selective probe for the immunoproteasome, a specialized isoform of the 20S proteasome, that becomes expressed in cells that encounter an inflammatory signal. Using a one-bead, one-compound library of small peptides, we discovered a trimer sequence efficiently cleaved by the immunoproteasome with significant selectivity over the standard proteasome. Upon conjugating this sequence to rhodamine 110 and a peptoid, we generated a probe with a considerable improvement in sensitivity compared to that of current aminomethylcoumarin-based proteasome probes. Importantly, our probe was capable of labeling immunoproteasome-expressing cells while maintaining its selectivity over other cellular proteases in live cell cultures. We anticipate this probe to find wide utility for those that wish to study the immunoproteasome's activity in a variety of cell lines and to be used as a reporter to discover small molecules that can perturb the activity of this proteasome isoform.

Indexed as

A549 CellsHumansMolecular ProbesMolecular StructurePeptidesPeptoidsProteasome Endopeptidase ComplexTumor Cells, CulturedMolecular ProbesPeptidesPeptoidsProteasome Endopeptidase Complex

Identifiers

PMID30862160
PMCPMC7389183
OpenAlexW2921237383

What OpenQuestion holds

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Registered trials

None linked

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.