Evidence map›Paper›PMID 23686610›Full record

ReviewCell biochemistry and biophysics2013

Measuring activity in the ubiquitin-proteasome system: from large scale discoveries to single cells analysis.

Adam T Melvin, Gregery S Woss, Jessica H Park, Marcey L Waters, Nancy L Allbritton

Abstract readReview
In one paragraph

Review in Cell biochemistry and biophysics, 2013. 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
1.0field-weighted citation impact, top 24% 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, 27 citations in OpenAlex.

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  5. Targeted protein degradation in mammalian cells: A promising avenue toward future.Computational and structural biotechnology journal · 2022
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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

5 authors at 2 institutions in 1 country.

Adam T MelvinDepartment of Chemistry, University of North Carolina, Chapel Hill, NC 27599, USA.
Gregery S Woss
Jessica H Park
Marcey L Waters
Nancy L Allbritton
University of North Carolina at Chapel Hill · USNorth Carolina State University · US

Funding

Protectides: A tool for drug target assays in myelomaR01EB011763 · NIBIB · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ALLBRITTON, NANCY L. · 2010 to 2013
$2.2M
Design of Degron-based Substrates Capable of E3 Ligase-mediated UbiquitinationF32CA162574 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI MELVIN, ADAM THOMAS · 2011 to 2013
$110k
NCI NIH HHS F32 CA162574NCI NIH HHS F32CA162574NIBIB NIH HHS R01 EB011763NIBIB NIH HHS R01EB011763
6 · The paper itself

Abstract

The ubiquitin-proteasome system (UPS) is the primary pathway responsible for the recognition and degradation of misfolded, damaged, or tightly regulated proteins in addition to performing essential roles in DNA repair, cell cycle regulation, cell migration, and the immune response. While traditional biochemical techniques have proven useful in the identification of key proteins involved in this pathway, the implementation of novel reporters responsible for measuring enzymatic activity of the UPS has provided valuable insight into the effectiveness of therapeutics and role of the UPS in various human diseases such as multiple myeloma and Huntington's disease. These reporters, usually consisting of a recognition sequence fused to an analytical handle, are designed to specifically evaluate enzymatic activity of certain members of the UPS including the proteasome, E3 ubiquitin ligases, and deubiquitinating enzymes. This review highlights the more commonly used reporters employed in a variety of scenarios ranging from high-throughput screening of novel inhibitors to single cell microscopy techniques measuring E3 ligase or proteasome activity. Finally, a recent study is presented highlighting the development of a novel degron-based substrate designed to overcome the limitations of current reporting techniques in measuring E3 ligase and proteasome activity in patient samples.

Indexed as

beta CateninFluorescence Resonance Energy TransferGreen Fluorescent ProteinsHumansMicroscopy, ConfocalProteasome Endopeptidase ComplexSingle-Cell AnalysisSubstrate SpecificityUbiquitinUbiquitinationUbiquitin-Protein Ligasesbeta CateninGreen Fluorescent ProteinsProteasome Endopeptidase ComplexUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID23686610
PMCPMC3758771
OpenAlexW2049910024

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

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.