ArticleBioinformatics (Oxford, England)2011
MAISTAS: a tool for automatic structural evaluation of alternative splicing products.
Article in Bioinformatics (Oxford, England), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Exploring the functional impact of alternative splicing on human protein isoforms using available annotation sources.Briefings in bioinformatics · 2019Review
- The hydrophobic temperature dependence of amino acids directly calculated from protein structures.PLoS computational biology · 2015Article
- Genome-wide Membrane Protein Structure Prediction.Current genomics · 2013Article
- DBATE: database of alternative transcripts expression.Database : the journal of biological databases and curation · 2013Article
- Characterization of ABL exon 7 deletion by molecular genetic and bioinformatic methods reveals no association with imatinib resistance in chronic myeloid leukemia.Medical oncology (Northwood, London, England) · 2012Article
- AS-EAST: a functional annotation tool for putative proteins encoded by alternatively spliced transcripts.Bioinformatics (Oxford, England) · 2012Article
- SpliceDisease database: linking RNA splicing and disease.Nucleic acids research · 2012Article
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Authors and funding
6 authors.
Funding
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Abstract
motivationAnalysis of the human genome revealed that the amount of transcribed sequence is an order of magnitude greater than the number of predicted and well-characterized genes. A sizeable fraction of these transcripts is related to alternatively spliced forms of known protein coding genes. Inspection of the alternatively spliced transcripts identified in the pilot phase of the ENCODE project has clearly shown that often their structure might substantially differ from that of other isoforms of the same gene, and therefore that they might perform unrelated functions, or that they might even not correspond to a functional protein. Identifying these cases is obviously relevant for the functional assignment of gene products and for the interpretation of the effect of variations in the corresponding proteins.
resultsHere we describe a publicly available tool that, given a gene or a protein, retrieves and analyses all its annotated isoforms, provides users with three-dimensional models of the isoform(s) of his/her interest whenever possible and automatically assesses whether homology derived structural models correspond to plausible structures. This information is clearly relevant. When the homology model of some isoforms of a gene does not seem structurally plausible, the implications are that either they assume a structure unrelated to that of the other isoforms of the same gene with presumably significant functional differences, or do not correspond to functional products. We provide indications that the second hypothesis is likely to be true for a substantial fraction of the cases. AVAILABILITY: http://maistas.bioinformatica.crs4.it/.
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