Evidence map›Paper›PMID 23121622›Full record

ReviewAntioxidants & redox signaling2013

Selenocysteine in thiol/disulfide-like exchange reactions.

Robert J Hondal, Stefano M Marino, Vadim N Gladyshev

Abstract readReview
In one paragraph

Review in Antioxidants & redox signaling, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
8.0field-weighted citation impact, top 2% 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

76 citing papers in PubMed, 181 citations in OpenAlex.

  1. Review
  2. Article
  3. A Crystalline and Thermally Stable Selenocysteine Selenenic Acid.Angewandte Chemie (International ed. in English) · 2026
    Article
  4. Article
  5. Review
  6. Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
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  15. Review
  16. Review
  17. Review
  18. Review
  19. Article
  20. Article

16 more citing papers are in PubMed but not listed here.

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 2 institutions in 1 country.

Robert J HondalGiven Laboratory, Department of Biochemistry, University of Vermont, Burlington, VT 05405, USA. Robert.Hondal@uvm.edu
Stefano M Marino
Vadim N Gladyshev
Brigham and Women's Hospital · USUniversity of Vermont · US

Funding

IDENTITY OF TERMINATOR AND SELENOCYSTEINE UGA CODONSR01GM061603 · NIGMS · UNIVERSITY OF NEBRASKA LINCOLN · PI GLADYSHEV, VADIM N. · 2000 to 2016
$4.0M
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
The Biological and Chemical Function of Selenium in EnzymesR01GM094172 · NIGMS · UNIVERSITY OF VERMONT & ST AGRIC COLLEGE · PI HONDAL, ROBERT J · 2010 to 2013
$1.3M
NIGMS NIH HHS GM061603NIGMS NIH HHS GM065204NIGMS NIH HHS GM094172NIGMS NIH HHS R01 GM061603NIGMS NIH HHS R01 GM094172NIGMS NIH HHS R37 GM065204
6 · The paper itself

Abstract

significanceAmong trace elements used as cofactors in enzymes, selenium is unique in that it is incorporated into proteins co-translationally in the form of an amino acid, selenocysteine (Sec). Sec differs from cysteine (Cys) by only one atom (selenium versus sulfur), yet this switch dramatically influences important aspects of enzyme reactivity. RECENT ADVANCES: The main focus of this review is an updated and critical discussion on how Sec might be used to accelerate thiol/disulfide-like exchange reactions in natural selenoenzymes, compared with their Cys-containing homologs. CRITICAL ISSUES: We discuss in detail three major aspects associated with thiol/disulfide exchange reactions: (i) nucleophilicity of the attacking thiolate (or selenolate); (ii) electrophilicity of the center sulfur (or selenium) atom; and (iii) stability of the leaving group (sulfur or selenium). In all these cases, we analyze the benefits that selenium might provide in these types of reactions. FUTURE DIRECTIONS: It is the biological thiol oxidoreductase-like function that benefits from the use of Sec, since Sec functions to chemically accelerate the rate of these reactions. We review various hypotheses that could help explain why Sec is used in enzymes, particularly with regard to competitive chemical advantages provided by the presence of the selenium atom in enzymes. Ultimately, these chemical advantages must be connected to biological functions of Sec.

Indexed as

CatalysisDisulfidesGlutaredoxinsGlutathione PeroxidaseMethionine Sulfoxide ReductasesOxidation-ReductionPeroxidaseSeleniumSelenocysteineSulfhydryl CompoundsSulfurThioredoxin-Disulfide ReductaseDisulfidesGlutaredoxinsGlutathione Peroxidasemethionine sulfoxide reductaseMethionine Sulfoxide ReductasesPeroxidaseSeleniumSelenocysteineSulfhydryl CompoundsSulfurThioredoxin-Disulfide Reductase

Identifiers

PMID23121622
PMCPMC3613276
OpenAlexW1987802440

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.