Evidence map›Paper›PMID 31562246›Full record

ArticleThe Journal of biological chemistry2019

Proteomic analysis of affinity-purified 26S proteasomes identifies a suite of assembly chaperones in

David C Gemperline, Richard S Marshall, Kwang-Hee Lee, Qingzhen Zhao, Weiming Hu, Fionn McLoughlin, Mark Scalf, Lloyd M Smith, Richard D Vierstra

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

18 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. Article
  3. Genome-wide analysis of theFrontiers in plant science · 2026
    Article
  4. Review
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  6. Streamline Protocol forPlant direct · 2025
    Article
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  12. Review
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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

9 authors at 2 institutions in 1 country.

David C GemperlineDepartment of Genetics, University of Wisconsin, Madison, Wisconsin 53706.
Richard S MarshallDepartment of Genetics, University of Wisconsin, Madison, Wisconsin 53706.
Kwang-Hee LeeDepartment of Genetics, University of Wisconsin, Madison, Wisconsin 53706.
Qingzhen ZhaoDepartment of Biology, Washington University in St. Louis, St. Louis, Missouri 63130.
Weiming HuDepartment of Biology, Washington University in St. Louis, St. Louis, Missouri 63130.ORCID 0000-0002-0151-886X
Fionn McLoughlinDepartment of Biology, Washington University in St. Louis, St. Louis, Missouri 63130.
Mark ScalfDepartment of Chemistry, University of Wisconsin, Madison, Wisconsin 53706.
Lloyd M SmithDepartment of Chemistry, University of Wisconsin, Madison, Wisconsin 53706.
Richard D VierstraDepartment of Genetics, University of Wisconsin, Madison, Wisconsin 53706 rdvierstra@wustl.edu.
University of Wisconsin–Madison · USWashington University in St. Louis · US

Funding

PREDOCTORAL TRAINING PROGRAM IN GENETICST32GM007133 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI PERNA, NICOLE T · 1985 to 2023
$16.5M
Wisconsin Center of Excellence in Genomics ScienceP50HG004952 · NHGRI · TEXAS BIOMEDICAL RESEARCH INSTITUTE · PI OLIVIER, MICHAEL · 2009 to 2013
$13.0M
The Epigenotype of Human ES CellsP01GM081629 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI THOMSON, JAMES ALEXANDER · 2008 to 2012
$8.9M
Revealing Proteoforms: The Primary Effectors of Biological FunctionR35GM126914 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI Lloyd M Smith · 2018 to 2026
$6.2M
Autophagic Clearance of Proteasomes and CDC48 as Models for Amyloidogenic Protein Quality Control.R01GM124452 · NIGMS · WASHINGTON UNIVERSITY · PI JEZ, JOSEPH MARTIN · 2018 to 2025
$2.4M
Intact Proteoform Identification and QuantificationR01GM114292 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI GOULD, MICHAEL N, SMITH, LLOYD M · 2015 to 2018
$1.6M
NHGRI NIH HHS P50 HG004952NIGMS NIH HHS P01 GM081629NIGMS NIH HHS R01 GM114292NIGMS NIH HHS R01 GM124452NIGMS NIH HHS R35 GM126914NIGMS NIH HHS T32 GM007133
6 · The paper itself

Abstract

The 26S proteasome is an essential protease that selectively eliminates dysfunctional and short-lived regulatory proteins in eukaryotes. To define the composition of this proteolytic machine in plants, we tagged either the core protease (CP) or the regulatory particle (RP) sub-complexes in

Indexed as

ProteomicsArabidopsisArabidopsis ProteinsCysteine EndopeptidasesMass SpectrometryMolecular ChaperonesProteasome Endopeptidase ComplexProtein IsoformsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsArabidopsis ProteinsAT4G31300 protein, ArabidopsisATP dependent 26S proteaseCysteine EndopeptidasesEcm29 protein, S cerevisiaeHSM3 protein, S cerevisiaeMolecular ChaperonesNAS2 protein, S cerevisiaeNAS6 protein, S cerevisiaePba1 protein, S cerevisiaePba2 protein, S cerevisiaeProteasome Endopeptidase Complexproteasome maturation proteinProtein IsoformsSaccharomyces cerevisiae ProteinsArabidopsischaperonecore proteasemass spectrometry (MS)proteasomeprotein assemblyprotein degradationproteomicsregulatory particleubiquitin

Identifiers

PMID31562246
PMCPMC6873196
OpenAlexW2975347041

What OpenQuestion holds

Textmetadata
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.