Evidence map›Paper›PMID 27043013›Full record

ArticlePloS one2016

An Inducible System for Rapid Degradation of Specific Cellular Proteins Using Proteasome Adaptors.

Shameika R Wilmington, Andreas Matouschek

Abstract read
In one paragraph

Article in PloS one, 2016. 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
–field-weighted citation impact
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.

  1. Article
  2. Ubiquitin-Independent Degradation: An Emerging PROTAC Approach?BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  3. Article
  4. Article
  5. Catalytic Protein Inhibitors.Angewandte Chemie (International ed. in English) · 2024
    Review
  6. Review
  7. Article
  8. Design principles that protect the proteasome from self-destruction.Protein science : a publication of the Protein Society · 2022
    Article
  9. Article
  10. Review
  11. Substrate selection by the proteasome through initiation regions.Protein science : a publication of the Protein Society · 2019
    Review
  12. Article
  13. Structure and Function of the 26S Proteasome.Annual review of biochemistry · 2018
    Review
  14. Article
  15. Article
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.

Shameika R WilmingtonDepartment of Molecular Biosciences, Northwestern University, Evanston, IL, United States of America.
Andreas MatouschekDepartment of Molecular Biosciences, Northwestern University, Evanston, IL, United States of America.

Funding

CELLULAR &MOLECULAR BASIS OF DISEASE TRAINING PROGRAMT32GM008061 · NIGMS · NORTHWESTERN UNIVERSITY · PI CARTHEW, RICHARD W. · 1985 to 2022
$17.1M
Protein unfolding in a physiological systemR01GM063004 · NIGMS · NORTHWESTERN UNIVERSITY · PI MATOUSCHEK, ANDREAS · 2001 to 2012
$2.7M
Development of proteasome adaptors to catalytically deplete specific proteins from cellsR21CA196456 · NCI · UNIVERSITY OF TEXAS AT AUSTIN · PI MATOUSCHEK, ANDREAS · 2016 to 2018
$597k
Cracking the Ubiquitination Code by Top Down Mass SpectrometryR21CA191664 · NCI · UNIVERSITY OF TEXAS AT AUSTIN · PI BRODBELT, JENNIFER S. · 2015 to 2016
$355k
NCI NIH HHS R21 CA191664NCI NIH HHS R21CA191664NCI NIH HHS R21 CA196456NIGMS NIH HHS R01 GM063004NIGMS NIH HHS R01GM63004NIGMS NIH HHS T32 GM008061NIGMS NIH HHS T32GM08061
6 · The paper itself

Abstract

A common way to study protein function is to deplete the protein of interest from cells and observe the response. Traditional methods involve disrupting gene expression but these techniques are only effective against newly synthesized proteins and leave previously existing and stable proteins untouched. Here, we introduce a technique that induces the rapid degradation of specific proteins in mammalian cells by shuttling the proteins to the proteasome for degradation in a ubiquitin-independent manner. We present two implementations of the system in human culture cells that can be used individually to control protein concentration. Our study presents a simple, robust, and flexible technology platform for manipulating intracellular protein levels.

Indexed as

Gene ExpressionProteolysisHEK293 CellsHumansProteasome Endopeptidase ComplexUbiquitinProteasome Endopeptidase ComplexUbiquitin

Identifiers

PMID27043013
PMCPMC4820223

What OpenQuestion holds

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LicenceCC BY
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.