Evidence map›Paper›PMID 26491016›Full record

ArticleThe Journal of biological chemistry2015

Proteomic Analysis Identifies Ribosome Reduction as an Effective Proteotoxic Stress Response.

Angel Guerra-Moreno, Marta Isasa, Meera K Bhanu, David P Waterman, Vinay V Eapen, Steven P Gygi, John Hanna

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing 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

40 citing papers in PubMed.

  1. Conserved Molecular Responses to Arsenite Exposure inbioRxiv : the preprint server for biology · 2026
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  18. Investigation of metabolic crosstalk between host and pathogenicFrontiers in bioengineering and biotechnology · 2022
    Article
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  20. 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

7 authors.

Angel Guerra-MorenoFrom the Department of Pathology, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts 02115.
Marta IsasaDepartment of Cell Biology, Harvard Medical School, Boston, Massachusetts, 02115, and.
Meera K BhanuFrom the Department of Pathology, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts 02115.
David P WatermanRosenstiel Basic Medical Sciences Research Center and the Department of Biology, Brandeis University, Waltham, Massachusetts 02254.
Vinay V EapenRosenstiel Basic Medical Sciences Research Center and the Department of Biology, Brandeis University, Waltham, Massachusetts 02254.
Steven P GygiDepartment of Cell Biology, Harvard Medical School, Boston, Massachusetts, 02115, and.
John HannaFrom the Department of Pathology, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts 02115, jwhanna@partners.org.

Funding

VASCULAR, PULMONARY AND RENAL INJURYT32HL007627 · NHLBI · BRIGHAM AND WOMEN'S HOSPITAL · PI GIMBRONE, MICHAEL A, MITCHELL, RICHARD N · 1985 to 2019
$12.7M
GENETIC AND BIOCHEMICAL MECHANISMS OF REGULATIONT32GM007122 · NIGMS · BRANDEIS UNIVERSITY · PI LOVETT, SUSAN THOMAS · 1985 to 2020
$7.5M
Arrest, Recovery, and Adaptation from DNA DamageR01GM061766 · NIGMS · BRANDEIS UNIVERSITY · PI HABER, JAMES E · 2001 to 2016
$4.6M
New Ubiquitin-Proteasome System Components that Protect against ProteotoxicityDP5OD019800 · OD · BRIGHAM AND WOMEN'S HOSPITAL · PI HANNA, JOHN W · 2014 to 2018
$2.2M
NHLBI NIH HHS T32 HL007627NHLBI NIH HHS T32HL007627-30NIGMS NIH HHS GM97645NIGMS NIH HHS R01-GM061766NIGMS NIH HHS T32 GM007122NIH HHS DP5 OD019800NIH HHS DP5-OD019800
6 · The paper itself

Abstract

Stress responses are adaptive cellular programs that identify and mitigate potentially dangerous threats. Misfolded proteins are a ubiquitous and clinically relevant stress. Trivalent metalloids, such as arsenic, have been proposed to cause protein misfolding. Using tandem mass tag-based mass spectrometry, we show that trivalent arsenic results in widespread reorganization of the cell from an anabolic to a catabolic state. Both major pathways of protein degradation, the proteasome and autophagy, show increased abundance of pathway components and increased functional output, and are required for survival. Remarkably, cells also showed a down-regulation of ribosomes at the protein level. That this represented an adaptive response and not an adverse toxic effect was indicated by enhanced survival of ribosome mutants after arsenic exposure. These results suggest that a major source of toxicity of trivalent arsenic derives from misfolding of newly synthesized proteins and identifies ribosome reduction as a rapid, effective, and reversible proteotoxic stress response.

Indexed as

ProteomicsStress, PhysiologicalArsenitesRibosomesSaccharomyces cerevisiaearseniteArsenitesautophagyproteasomeproteostasisribosomestress response

Identifiers

PMID26491016
PMCPMC4705986

What OpenQuestion holds

Textmetadata
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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.