Evidence map›Paper›PMID 22248862›Full record

ArticleFree radical biology & medicine2012

Inactivation of thiol-dependent enzymes by hypothiocyanous acid: role of sulfenyl thiocyanate and sulfenic acid intermediates.

Tessa J Barrett, David I Pattison, Stephen E Leonard, Kate S Carroll, Michael J Davies, Clare L Hawkins

Abstract read
In one paragraph

Article in Free radical biology & medicine, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed, 1 pooled it
2.2field-weighted citation impact, top 13% 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

23 citing papers in PubMed, 1 synthesis or guideline pooled it, 57 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Factors governing the response ofFrontiers in cellular and infection microbiology · 2026
    Review
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  8. Review
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  15. Diverse Redoxome Reactivity Profiles of Carbon Nucleophiles.Journal of the American Chemical Society · 2017
    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

6 authors at 3 institutions in 2 countries.

Tessa J BarrettThe Heart Research Institute, Newtown, NSW 2042, Australia.
David I Pattison
Stephen E Leonard
Kate S Carroll
Michael J Davies
Clare L Hawkins
University of Sydney · AUScripps Research Institute · USUniversity of Michigan–Ann Arbor · US

Funding

Probing the role of cysteine sulfenylation in cell signalingR01GM102187 · NIGMS · UNIVERSITY OF FLORIDA · PI Kate Suzanne Carroll · 2012 to 2026
$4.6M
NIGMS NIH HHS R01 GM102187
6 · The paper itself

Abstract

Myeloperoxidase (MPO) forms reactive oxidants including hypochlorous and hypothiocyanous acids (HOCl and HOSCN) under inflammatory conditions. HOCl causes extensive tissue damage and plays a role in the progression of many inflammatory-based diseases. Although HOSCN is a major MPO oxidant, particularly in smokers, who have elevated plasma thiocyanate, the role of this oxidant in disease is poorly characterized. HOSCN induces cellular damage by targeting thiols. However, the specific targets and mechanisms involved in this process are not well defined. We show that exposure of macrophages to HOSCN results in the inactivation of intracellular enzymes, including creatine kinase (CK) and glyceraldehyde-3-phosphate dehydrogenase (GAPDH). In each case, the active-site thiol residue is particularly sensitive to oxidation, with evidence for reversible inactivation and the formation of sulfenyl thiocyanate and sulfenic acid intermediates, on treatment with HOSCN (less than fivefold molar excess). Experiments with DAz-2, a cell-permeable chemical trap for sulfenic acids, demonstrate that these intermediates are formed on many cellular proteins, including GAPDH and CK, in macrophages exposed to HOSCN. This is the first direct evidence for the formation of protein sulfenic acids in HOSCN-treated cells and highlights the potential of this oxidant to perturb redox signaling processes.

Indexed as

AnimalsCatalytic DomainCell LineCreatine KinaseEnzyme ActivationGlyceraldehyde 3-Phosphate Dehydrogenase (NADP+)MacrophagesMiceOxidative StressPeroxidaseSulfenic AcidsSulfhydryl CompoundsThiocyanatesCreatine KinaseGlyceraldehyde 3-Phosphate Dehydrogenase (NADP+)hypothiocyanous acidPeroxidaseSulfenic AcidsSulfhydryl CompoundsThiocyanates

Identifiers

PMID22248862
PMCPMC3523338
OpenAlexW2036099283

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.