Evidence map›Paper›PMID 16260744›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2005

Diversity and functional plasticity of eukaryotic selenoproteins: identification and characterization of the SelJ family.

Sergi Castellano, Alexey V Lobanov, Charles Chapple, Sergey V Novoselov, Mario Albrecht, Deame Hua, Alain Lescure, Thomas Lengauer, Alain Krol, Vadim N Gladyshev and 1 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
6.6field-weighted citation impact, top 3% 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

37 citing papers in PubMed, 117 citations in OpenAlex.

  1. Trial
  2. Article
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  4. Review
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  6. Article
  7. Review
  8. Intracellular mono-ADP-ribosyltransferases at the host-virus interphase.Cellular and molecular life sciences : CMLS · 2022
    Review
  9. The algal selenoproteomes.BMC genomics · 2020
    Article
  10. Bioinformatics of Selenoproteins.Antioxidants & redox signaling · 2020
    Review
  11. Bioinformatics of Metalloproteins and Metalloproteomes.Molecules (Basel, Switzerland) · 2020
    Review
  12. Article
  13. Review
  14. Article
  15. Selenoprotein Gene Nomenclature.The Journal of biological chemistry · 2016
    Article
  16. Knockdown of 15-kDa selenoprotein (Sep15) increases hLE cells' susceptibility to tunicamycin-induced apoptosis.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2015
    Article
  17. Effects of acclimation salinity on the expression of selenoproteins in the tilapia, Oreochromis mossambicus.Journal of trace elements in medicine and biology : organ of the Society for Minerals and Trace Elements (GMS) · 2014
    Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 4 institutions in 4 countries.

Sergi CastellanoGrup de Recerca en Informàtica Biomèdica, Institut Municipal d'Investigació Mèdica, Universitat Pompeu Fabra and Centre de Regulació Genòmica, Carrer del Doctor Aiguader 80, 08003 Barcelona, Spain. sc464@cornell.edu
Alexey V Lobanov
Charles Chapple
Sergey V Novoselov
Mario Albrecht
Deame Hua
Alain Lescure
Thomas Lengauer
Alain Krol
Vadim N Gladyshev
Roderic Guigó
Pompeu Fabra University · ESMax Planck Institute for Informatics · DEUniversity of Nebraska–Lincoln · USInstitut de Biologie Moléculaire et Cellulaire · FR

Funding

IDENTITY OF TERMINATOR AND SELENOCYSTEINE UGA CODONSR01GM061603 · NIGMS · UNIVERSITY OF NEBRASKA LINCOLN · PI GLADYSHEV, VADIM N. · 2000 to 2016
$4.0M
NIGMS NIH HHS GM061603NIGMS NIH HHS R01 GM061603
6 · The paper itself

Abstract

Selenoproteins are a diverse group of proteins that contain selenocysteine (Sec), the 21st amino acid. In the genetic code, UGA serves as a termination signal and a Sec codon. This dual role has precluded the automatic annotation of selenoproteins. Recent advances in the computational identification of selenoprotein genes have provided a first glimpse of the size, functions, and phylogenetic diversity of eukaryotic selenoproteomes. Here, we describe the identification of a selenoprotein family named SelJ. In contrast to known selenoproteins, SelJ appears to be restricted to actinopterygian fishes and sea urchin, with Cys homologues only found in cnidarians. SelJ shows significant similarity to the jellyfish J1-crystallins and with them constitutes a distinct subfamily within the large family of ADP-ribosylation enzymes. Consistent with its potential role as a structural crystallin, SelJ has preferential and homogeneous expression in the eye lens in early stages of zebrafish development. A structural role for SelJ would be in contrast to the majority of known selenoenzymes. The unusually highly restricted phylogenetic distribution of SelJ, its specialization, and the comparative analysis of eukaryotic selenoproteomes reveal the diversity and functional plasticity of selenoproteins and point to a mosaic evolution of the use of Sec in proteins.

Indexed as

Adenosine Diphosphate RiboseAnimalsFish ProteinsGenomeMiceNIH 3T3 CellsPhylogenyPromoter Regions, GeneticProteomeSelenoproteinsTetraodontiformesAdenosine Diphosphate RiboseFish ProteinsProteomeSelenoproteins

Identifiers

PMID16260744
PMCPMC1283428
OpenAlexW1969459260

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.