Evidence map›Paper›PMID 25799144›Full record

ArticleNature chemical biology2015

Monitoring methionine sulfoxide with stereospecific mechanism-based fluorescent sensors.

Lionel Tarrago, Zalán Péterfi, Byung Cheon Lee, Thomas Michel, Vadim N Gladyshev

Open access · greenAbstract read
In one paragraph

Article in Nature chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
4.1field-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

27 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. In Vivo Imaging with Genetically Encoded Redox Biosensors.International journal of molecular sciences · 2020
    Review
  11. Article
  12. Review
  13. Article
  14. Emerging Omics Approaches in Aging Research.Antioxidants & redox signaling · 2018
    Review
  15. Review
  16. Review
  17. Article
  18. Article
  19. Regulated methionine oxidation by monooxygenases.Free radical biology & medicine · 2017
    Review
  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

5 authors at 1 institution in 3 countries.

Lionel TarragoDivision of Genetics, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts, USA.
Zalán PéterfiDivision of Genetics, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts, USA.
Byung Cheon Lee1] Division of Genetics, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts, USA. [2] College of Life Sciences and Biotechnology, Korea University, Seoul, South Korea.ORCID 0000000167888030
Thomas MichelCardiovascular Division, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts, USA.
Vadim N GladyshevDivision of Genetics, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts, USA.
Brigham and Women's Hospital · US

Funding

Tissue AnalysesP01HL048743 · NHLBI · BRIGHAM AND WOMEN'S HOSPITAL · PI GLADYSHEV, VADIM N. · 1992 to 2014
$26.3M
Methionine sulfoxide reduction, selenium and agingR01AG021518 · NIA · UNIVERSITY OF NEBRASKA LINCOLN · PI GLADYSHEV, VADIM N. · 2003 to 2018
$5.0M
ENDOTHELIAL NITRIC OXIDE SYNTHASER01HL046457 · NHLBI · BRIGHAM AND WOMEN'S HOSPITAL · PI MICHEL, THOMAS · 1996 to 2011
$4.7M
Protein interactions in cardiovascular signalingR01GM036259 · NIGMS · BRIGHAM AND WOMEN'S HOSPITAL · PI MICHEL, THOMAS · 1985 to 2009
$4.6M
Functions of thioredoxin reductases and their targetsR37GM065204 · NIGMS · BRIGHAM AND WOMEN'S HOSPITAL · PI GLADYSHEV, VADIM N. · 2011 to 2020
$4.0M
Functions of Mammalian Thioredoxin ReductasesR01GM065204 · NIGMS · UNIVERSITY OF NEBRASKA LINCOLN · PI GLADYSHEV, VADIM N. · 2002 to 2009
$2.2M
NHLBI NIH HHS HL48743NHLBI NIH HHS P01 HL048743NHLBI NIH HHS R01 HL046457NIA NIH HHS AG021518NIA NIH HHS R01 AG021518NIGMS NIH HHS GM065204NIGMS NIH HHS R01 GM036259NIGMS NIH HHS R01 GM065204NIGMS NIH HHS R37 GM065204
6 · The paper itself

Abstract

Methionine can be reversibly oxidized to methionine sulfoxide (MetO) under physiological and pathophysiological conditions, but its use as a redox marker suffers from the lack of tools to detect and quantify MetO within cells. In this work, we created a pair of complementary stereospecific genetically encoded mechanism-based ratiometric fluorescent sensors of MetO by inserting a circularly permuted yellow fluorescent protein between yeast methionine sulfoxide reductases and thioredoxins. The two sensors, respectively named MetSOx and MetROx for their ability to detect S and R forms of MetO, were used for targeted analysis of protein oxidation, regulation and repair as well as for monitoring MetO in bacterial and mammalian cells, analyzing compartment-specific changes in MetO and examining responses to physiological stimuli.

Indexed as

Escherichia coliFluorescenceHEK293 CellsHumansMethionineOxidantsOxidation-ReductionSodium HypochloriteStereoisomerismMethioninemethionine sulfoxideOxidantsSodium Hypochlorite

Identifiers

PMID25799144
PMCPMC4402147
OpenAlexW2056714200

What OpenQuestion holds

Textmetadata
LicenceTDM
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.