Evidence map›Paper›PMID 21976664›Full record

ArticleThe Journal of biological chemistry2011

Using quantitative redox proteomics to dissect the yeast redoxome.

Nicolas Brandes, Dana Reichmann, Heather Tienson, Lars I Leichert, Ursula Jakob

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

57 citing papers in PubMed, 121 citations in OpenAlex.

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  17. Sod1 integrates oxygen availability to redox regulate NADPH production and the thiol redoxome.Proceedings of the National Academy of Sciences of the United States of America · 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 1 institution in 1 country.

Nicolas BrandesDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109.
Dana ReichmannDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109.
Heather TiensonDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109.
Lars I LeichertDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109.
Ursula JakobDepartment of Molecular, Cellular, and Developmental Biology, University of Michigan, Ann Arbor, Michigan 48109. Electronic address: ujakob@umich.edu.
University of Michigan–Ann Arbor · US

Funding

Research Training in BiogerontologyT32AG000114 · NIA · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SCOTT PLETCHER · 1985 to 2026
$12.4M
Oxidative Thiol Modifications and AgingR01AG027349 · NIA · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI JAKOB, URSULA H. · 2007 to 2011
$1.4M
TUMOR INDUCED IMMUNOSUPPRESSIONZ01AG000114 · NIA · AGING · PI LONGO, DAN L. · 2000 to 2007
$241k
Intramural NIH HHS Z01 AG000114NIA NIH HHS AG027349NIA NIH HHS R01 AG027349NIA NIH HHS T32 AG000114
6 · The paper itself

Abstract

To understand and eventually predict the effects of changing redox conditions and oxidant levels on the physiology of an organism, it is essential to gain knowledge about its redoxome: the proteins whose activities are controlled by the oxidation status of their cysteine thiols. Here, we applied the quantitative redox proteomic method OxICAT to Saccharomyces cerevisiae and determined the in vivo thiol oxidation status of almost 300 different yeast proteins distributed among various cellular compartments. We found that a substantial number of cytosolic and mitochondrial proteins are partially oxidized during exponential growth. Our results suggest that prevailing redox conditions constantly control central cellular pathways by fine-tuning oxidation status and hence activity of these proteins. Treatment with sublethal H(2)O(2) concentrations caused a subset of 41 proteins to undergo substantial thiol modifications, thereby affecting a variety of different cellular pathways, many of which are directly or indirectly involved in increasing oxidative stress resistance. Classification of the identified protein thiols according to their steady-state oxidation levels and sensitivity to peroxide treatment revealed that redox sensitivity of protein thiols does not predict peroxide sensitivity. Our studies provide experimental evidence that the ability of protein thiols to react to changing peroxide levels is likely governed by both thermodynamic and kinetic parameters, making predicting thiol modifications challenging and de novo identification of peroxide sensitive protein thiols indispensable.

Indexed as

Hydrogen PeroxideOxidantsOxidation-ReductionProtein Processing, Post-TranslationalProteomicsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsHydrogen PeroxideOxidantsSaccharomyces cerevisiae Proteins

Identifiers

PMID21976664
PMCPMC3308895
OpenAlexW2045030736

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.