Evidence map›Paper›PMID 15382231›Full record

ArticleProteins2004

Analysis of protein homology by assessing the (dis)similarity in protein loop regions.

Anna R Panchenko, Thomas Madej

Abstract read
In one paragraph

Article in Proteins, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Analysis of loop boundaries using different local structure assignment methods.Protein science : a publication of the Protein Society · 2009
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. New metrics for comparative genomics.Current opinion in biotechnology · 2006
    Review
  14. Article
  15. 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

2 authors.

Anna R PanchenkoComputational Biology Branch, National Center for Biotechnology Information, National Institutes of Health, Bethesda, Maryland 20894, USA. panch@ncbi.nlm.nih.gov <panch@ncbi.nlm.nih.gov>
Thomas Madej

Funding

PROTEIN 3D STRUCTURE COMPARISONZ01LM000057 · NLM · NATIONAL LIBRARY OF MEDICINE · PI BRYANT, STEPHEN H. · 1994 to 2006
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NLM NIH HHS Z01 LM000057-12
6 · The paper itself

Abstract

Two proteins are considered to have a similar fold if sufficiently many of their secondary structure elements are positioned similarly in space and are connected in the same order. Such a common structural scaffold may arise due to either divergent or convergent evolution. The intervening unaligned regions ("loops") between the superimposable helices and strands can exhibit a wide range of similarity and may offer clues to the structural evolution of folds. One might argue that more closely related proteins differ less in their nonconserved loop regions than distantly related proteins and, at the same time, the degree of variability in the loop regions in structurally similar but unrelated proteins is higher than in homologs. Here we introduce a new measure for structural (dis)similarity in loop regions that is based on the concept of the Hausdorff metric. This measure is used to gauge protein relatedness and is tested on a benchmark of homologous and analogous protein structures. It has been shown that the new measure can distinguish homologous from analogous proteins with the same or higher accuracy than the conventional measures that are based on comparing proteins in structurally aligned regions. We argue that this result can be attributed to the higher sensitivity of the Hausdorff (dis)similarity measure in detecting particularly evident dissimilarities in structures and draw some conclusions about evolutionary relatedness of proteins in the most populated protein folds.

Indexed as

Structural Homology, ProteinComputational BiologyEvolution, MolecularMethyltransferasesModels, MolecularOxidoreductasesProtein FoldingProteinsProtein Structure, TertiaryS-AdenosylmethionineSensitivity and SpecificityMethyltransferasesOxidoreductasesProteinsS-Adenosylmethionine

Identifiers

PMID15382231
PMCPMC1994810

What OpenQuestion holds

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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.