Evidence map›Paper›PMID 25261734›Full record

ReviewFree radical biology & medicine2015

Mass spectrometry in studies of protein thiol chemistry and signaling: opportunities and caveats.

Nelmi O Devarie Baez, Julie A Reisz, Cristina M Furdui

Abstract readReview
In one paragraph

Review in Free radical biology & medicine, 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
–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

27 citing papers in PubMed.

  1. Article
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  3. Review
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  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Review
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  13. The role of thiols in antioxidant systems.Free radical biology & medicine · 2019
    Review
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
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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

3 authors.

Nelmi O Devarie BaezDepartment of Internal Medicine, Section on Molecular Medicine, Wake Forest School of Medicine, Winston-Salem, NC 27157, USA.
Julie A ReiszDepartment of Internal Medicine, Section on Molecular Medicine, Wake Forest School of Medicine, Winston-Salem, NC 27157, USA.
Cristina M FurduiDepartment of Internal Medicine, Section on Molecular Medicine, Wake Forest School of Medicine, Winston-Salem, NC 27157, USA. Electronic address: cfurdui@wakehealth.edu.

Funding

Training Program in Translational Radiation OncologyT32CA113267 · NCI · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI BLACKSTOCK, ARTHUR W · 2005 to 2014
$2.6M
Analysis of Redox Modulated Signaling Networks in Response to Ionizing RadiationR01CA136810 · NCI · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI FURDUI, CRISTINA MARIA · 2009 to 2013
$1.5M
New Reagents for Tracking Protein Oxidation in Cells by MS and Imaging MethodsR33CA177461 · NCI · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI FURDUI, CRISTINA MARIA, POOLE, LESLIE B · 2013 to 2015
$1.0M
NCI NIH HHS R01 CA136810NCI NIH HHS R33 CA177461NCI NIH HHS R33CA177461NCI NIH HHS T32 CA113267
6 · The paper itself

Abstract

Mass spectrometry (MS) has become a powerful and widely utilized tool in the investigation of protein thiol chemistry, biochemistry, and biology. Very early biochemical studies of metabolic enzymes have brought to light the broad spectrum of reactivity profiles that distinguish cysteine thiols with functions in catalysis and protein stability from other cysteine residues in proteins. The development of MS methods for the analysis of proteins using electrospray ionization (ESI) or matrix-assisted laser desorption/ionization (MALDI) coupled with the emergence of high-resolution mass analyzers has been instrumental in advancing studies of thiol modifications, both in single proteins and within the cellular context. This article reviews MS instrumentation and methods of analysis employed in investigations of thiols and their reactivity toward a range of small biomolecules. A selected number of studies are detailed to highlight the advantages brought about by the MS technologies along with the caveats associated with these analyses.

Indexed as

AnimalsBiocatalysisCysteineHumansKineticsMolecular ProbesOxidation-ReductionPeptide FragmentsPeptide MappingProteinsProtein StabilitySpectrometry, Mass, Electrospray IonizationSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationSulfhydryl CompoundsCysteineMolecular ProbesPeptide FragmentsProteinsSulfhydryl CompoundsCysteineKineticsMass spectrometryModificationsPeptidesProteinsThiol

Identifiers

PMID25261734
PMCPMC4355329

What OpenQuestion holds

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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.