Evidence map›Paper›PMID 31113833›Full record

ArticlePlant physiology2019

HSP101 Interacts with the Proteasome and Promotes the Clearance of Ubiquitylated Protein Aggregates.

Fionn McLoughlin, Minsoo Kim, Richard S Marshall, Richard D Vierstra, Elizabeth Vierling

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

50 citing papers in PubMed, 103 citations in OpenAlex.

  1. Principles and mechanisms of plant acclimation to heat stress.Nature reviews. Molecular cell biology · 2026
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Fionn McLoughlinDepartment of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, Massachusetts 01009.ORCID 0000-0002-2430-5074
Minsoo KimDepartment of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, Massachusetts 01009.
Richard S MarshallDepartment of Biology, Washington University in St. Louis, St. Louis, Missouri 63130.ORCID 0000-0002-6844-1078
Richard D VierstraDepartment of Biology, Washington University in St. Louis, St. Louis, Missouri 63130.ORCID 0000-0003-0210-3516
Elizabeth VierlingDepartment of Biochemistry and Molecular Biology, University of Massachusetts, Amherst, Massachusetts 01009 vierling@biochem.umass.edu.ORCID 0000-0002-0066-4881
Washington University in St. Louis · USUniversity of Massachusetts Amherst · US

Funding

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
NIGMS NIH HHS R01 GM124452
6 · The paper itself

Abstract

Stressful environments often lead to protein unfolding and the formation of cytotoxic aggregates that can compromise cell survival. The molecular chaperone heat shock protein (HSP) 101 is a protein disaggregase that co-operates with the small HSP (sHSP) and HSP70 chaperones to facilitate removal of such aggregates and is essential for surviving severe heat stress. To better define how HSP101 protects plants, we investigated the localization and targets of this chaperone in Arabidopsis (

Indexed as

ArabidopsisArabidopsis ProteinsGene Expression Regulation, PlantHeat-Shock ResponseHot TemperaturePlant ProteinsProteasome Endopeptidase ComplexStress, PhysiologicalTranscription FactorsArabidopsis ProteinsHSP101 protein, plantPlant ProteinsProteasome Endopeptidase ComplexTranscription Factors

Identifiers

PMID31113833
PMCPMC6670096
OpenAlexW2946647912

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.