Evidence map›Paper›PMID 20961958›Full record

ArticleNucleic acids research2011

Identification of new homologs of PD-(D/E)XK nucleases by support vector machines trained on data derived from profile-profile alignments.

Mindaugas Laganeckas, Mindaugas Margelevicius, Ceslovas Venclovas

Abstract read
In one paragraph

Article in Nucleic acids research, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. Two D-loop resolution systems enable natural genetic transformation in bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  5. Review
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  8. Type II Restriction-Modification System fromPathogens (Basel, Switzerland) · 2020
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Mitochondrial Mechanisms of Neuronal Cell Death: Potential Therapeutics.Annual review of pharmacology and toxicology · 2017
    Review
  15. 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.

Mindaugas LaganeckasInstitute of Biotechnology, Graičiūno 8, LT-02241 Vilnius, Lithuania.
Mindaugas Margelevicius
Ceslovas Venclovas

Funding

Howard Hughes Medical Institute 55005627
6 · The paper itself

Abstract

PD-(D/E)XK nucleases, initially represented by only Type II restriction enzymes, now comprise a large and extremely diverse superfamily of proteins. They participate in many different nucleic acids transactions including DNA degradation, recombination, repair and RNA processing. Different PD-(D/E)XK families, although sharing a structurally conserved core, typically display little or no detectable sequence similarity except for the active site motifs. This makes the identification of new superfamily members using standard homology search techniques challenging. To tackle this problem, we developed a method for the detection of PD-(D/E)XK families based on the binary classification of profile-profile alignments using support vector machines (SVMs). Using a number of both superfamily-specific and general features, SVMs were trained to identify true positive alignments of PD-(D/E)XK representatives. With this method we identified several PFAM families of uncharacterized proteins as putative new members of the PD-(D/E)XK superfamily. In addition, we assigned several unclassified restriction enzymes to the PD-(D/E)XK type. Results show that the new method is able to make confident assignments even for alignments that have statistically insignificant scores. We also implemented the method as a freely accessible web server at http://www.ibt.lt/bioinformatics/software/pdexk/.

Indexed as

Artificial IntelligenceAmino Acid SequenceCatalytic DomainConserved SequenceDNA Restriction EnzymesEndonucleasesExonucleasesHolliday Junction ResolvasesMolecular Sequence DataProtein Structure, TertiarySequence AlignmentSequence Homology, Amino AcidSoftwareDNA Restriction EnzymesEndonucleasesExonucleasesHolliday Junction Resolvases

Identifiers

PMID20961958
PMCPMC3045609

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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.