Evidence map›Paper›PMID 26340608›Full record

ReviewFree radical research2016

Biological chemistry and functionality of protein sulfenic acids and related thiol modifications.

Nelmi O Devarie-Baez, Elsa I Silva Lopez, Cristina M Furdui

Open access · greenAbstract readReview
In one paragraph

Review in Free radical research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
3.9field-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

42 citing papers in PubMed, 80 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Electron transfer in biological systems.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2024
    Review
  6. Balanced Duality: HInternational journal of molecular sciences · 2024
    Review
  7. Article
  8. [Redox biology · 2022
    Article
  9. Review
  10. Review
  11. Review
  12. Article
  13. Review
  14. Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. 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

3 authors at 1 institution in 1 country.

Nelmi O Devarie-Baeza Department of Internal Medicine, Section on Molecular Medicine , Wake Forest School of Medicine , Winston-Salem , NC , USA.
Elsa I Silva Lopeza Department of Internal Medicine, Section on Molecular Medicine , Wake Forest School of Medicine , Winston-Salem , NC , USA.
Cristina M Furduia Department of Internal Medicine, Section on Molecular Medicine , Wake Forest School of Medicine , Winston-Salem , NC , USA.
Wake Forest University · US

Funding

Wake Forest Clinical and Translational Science AwardUL1TR001420 · NCATS · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI ARD, JAMY D, FOLEY, KRISTIE L · 2015 to 2023
$32.3M
Training Program in Translational Radiation OncologyT32CA113267 · NCI · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI BLACKSTOCK, ARTHUR W · 2005 to 2014
$2.6M
Postdoctoral Research, Instruction, and Mentoring Experience (PRIME)K12GM102773 · NIGMS · WAKE FOREST UNIVERSITY HEALTH SCIENCES · PI HOWLETT, ALLYN C · 2013 to 2018
$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
NCATS NIH HHS UL1 TR001420NCI NIH HHS R01 CA136810NCI NIH HHS R33 CA177461NCI NIH HHS T32 CA113267NIGMS NIH HHS K12 GM102773
6 · The paper itself

Abstract

Selective modification of proteins at cysteine residues by reactive oxygen, nitrogen or sulfur species formed under physiological and pathological states is emerging as a critical regulator of protein activity impacting cellular function. This review focuses primarily on protein sulfenylation (-SOH), a metastable reversible modification connecting reduced cysteine thiols to many products of cysteine oxidation. An overview is first provided on the chemistry principles underlining synthesis, stability and reactivity of sulfenic acids in model compounds and proteins, followed by a brief description of analytical methods currently employed to characterize these oxidative species. The following chapters present a selection of redox-regulated proteins for which the -SOH formation was experimentally confirmed and linked to protein function. These chapters are organized based on the participation of these proteins in the regulation of signaling, metabolism and epigenetics. The last chapter discusses the therapeutic implications of altered redox microenvironment and protein oxidation in disease.

Indexed as

AnimalsCysteineEpigenomicsHumansOxidation-ReductionProteinsSignal TransductionSulfenic AcidsSulfhydryl CompoundsCysteineProteinsSulfenic AcidsSulfhydryl CompoundsChemistryreactive oxygen speciesredox statussulfenic acidthiols

Identifiers

PMID26340608
PMCPMC5292231
OpenAlexW1719708418

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.