ArticleBMC structural biology2007
Protein homologous cores and loops: important clues to evolutionary relationships between structurally similar proteins.
Article in BMC structural biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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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.
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Who cites it
3 citing papers in PubMed.
- Molecular docking of Glycine max and Medicago truncatula ureases with urea; bioinformatics approaches.Molecular biology reports · 2016Article
- Functional states of homooligomers: insights from the evolution of glycosyltransferases.Journal of molecular biology · 2010Article
- Analysis of loop boundaries using different local structure assignment methods.Protein science : a publication of the Protein Society · 2009Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
backgroundTo discover remote evolutionary relationships and functional similarities between proteins, biologists rely on comparative sequence analysis, and when structures are available, on structural alignments and various measures of structural similarity. The measures/scores that have most commonly been used for this purpose include: alignment length, percent sequence identity, superposition RMSD and their different combinations. More recently, we have introduced the "Homologous core structure overlap score" (HCS) and the "Loop Hausdorff Measure" (LHM). Along with these we also consider the "gapped structural alignment score" (GSAS), which was introduced earlier by other researchers.
resultsWe analyze the performance of these and other conventional measures at the task of ranking structure neighbors by homology, and we show that the HCS, LHM, and GSAS scores display considerably improved performance over the conventional measures of sequence or structural similarity.
conclusionThe HCS, LHM, and GSAS scores are easily computable quantities that allow users of structure-neighbor databases to more easily identify interesting structural similarities between proteins.
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