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Extraction, integration and analysis of alternative splicing and protein structure distributed information

BACKGROUND: Alternative splicing has been demonstrated to affect most of human genes; different isoforms from the same gene encode for proteins which differ for a limited number of residues, thus yielding similar structures. This suggests possible correlations between alternative splicing and protei...

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Detalles Bibliográficos
Autores principales: D'Antonio, Matteo, Masseroli, Marco
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2762064/
https://www.ncbi.nlm.nih.gov/pubmed/19828075
http://dx.doi.org/10.1186/1471-2105-10-S12-S15
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author D'Antonio, Matteo
Masseroli, Marco
author_facet D'Antonio, Matteo
Masseroli, Marco
author_sort D'Antonio, Matteo
collection PubMed
description BACKGROUND: Alternative splicing has been demonstrated to affect most of human genes; different isoforms from the same gene encode for proteins which differ for a limited number of residues, thus yielding similar structures. This suggests possible correlations between alternative splicing and protein structure. In order to support the investigation of such relationships, we have developed the Alternative Splicing and Protein Structure Scrutinizer (PASS), a Web application to automatically extract, integrate and analyze human alternative splicing and protein structure data sparsely available in the Alternative Splicing Database, Ensembl databank and Protein Data Bank. Primary data from these databases have been integrated and analyzed using the Protein Identifier Cross-Reference, BLAST, CLUSTALW and FeatureMap3D software tools. RESULTS: A database has been developed to store the considered primary data and the results from their analysis; a system of Perl scripts has been implemented to automatically create and update the database and analyze the integrated data; a Web interface has been implemented to make the analyses easily accessible; a database has been created to manage user accesses to the PASS Web application and store user's data and searches. CONCLUSION: PASS automatically integrates data from the Alternative Splicing Database with protein structure data from the Protein Data Bank. Additionally, it comprehensively analyzes the integrated data with publicly available well-known bioinformatics tools in order to generate structural information of isoform pairs. Further analysis of such valuable information might reveal interesting relationships between alternative splicing and protein structure differences, which may be significantly associated with different functions.
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spelling pubmed-27620642009-10-15 Extraction, integration and analysis of alternative splicing and protein structure distributed information D'Antonio, Matteo Masseroli, Marco BMC Bioinformatics Research BACKGROUND: Alternative splicing has been demonstrated to affect most of human genes; different isoforms from the same gene encode for proteins which differ for a limited number of residues, thus yielding similar structures. This suggests possible correlations between alternative splicing and protein structure. In order to support the investigation of such relationships, we have developed the Alternative Splicing and Protein Structure Scrutinizer (PASS), a Web application to automatically extract, integrate and analyze human alternative splicing and protein structure data sparsely available in the Alternative Splicing Database, Ensembl databank and Protein Data Bank. Primary data from these databases have been integrated and analyzed using the Protein Identifier Cross-Reference, BLAST, CLUSTALW and FeatureMap3D software tools. RESULTS: A database has been developed to store the considered primary data and the results from their analysis; a system of Perl scripts has been implemented to automatically create and update the database and analyze the integrated data; a Web interface has been implemented to make the analyses easily accessible; a database has been created to manage user accesses to the PASS Web application and store user's data and searches. CONCLUSION: PASS automatically integrates data from the Alternative Splicing Database with protein structure data from the Protein Data Bank. Additionally, it comprehensively analyzes the integrated data with publicly available well-known bioinformatics tools in order to generate structural information of isoform pairs. Further analysis of such valuable information might reveal interesting relationships between alternative splicing and protein structure differences, which may be significantly associated with different functions. BioMed Central 2009-10-15 /pmc/articles/PMC2762064/ /pubmed/19828075 http://dx.doi.org/10.1186/1471-2105-10-S12-S15 Text en Copyright © 2009 D'Antonio and Masseroli; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an open access article distributed under the terms of the Creative Commons Attribution License ( (http://creativecommons.org/licenses/by/2.0) ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research
D'Antonio, Matteo
Masseroli, Marco
Extraction, integration and analysis of alternative splicing and protein structure distributed information
title Extraction, integration and analysis of alternative splicing and protein structure distributed information
title_full Extraction, integration and analysis of alternative splicing and protein structure distributed information
title_fullStr Extraction, integration and analysis of alternative splicing and protein structure distributed information
title_full_unstemmed Extraction, integration and analysis of alternative splicing and protein structure distributed information
title_short Extraction, integration and analysis of alternative splicing and protein structure distributed information
title_sort extraction, integration and analysis of alternative splicing and protein structure distributed information
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2762064/
https://www.ncbi.nlm.nih.gov/pubmed/19828075
http://dx.doi.org/10.1186/1471-2105-10-S12-S15
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