PhosphoHunter: An Efficient Software Tool for Phosphopeptide Identification. (12th January 2015)
- Record Type:
- Journal Article
- Title:
- PhosphoHunter: An Efficient Software Tool for Phosphopeptide Identification. (12th January 2015)
- Main Title:
- PhosphoHunter: An Efficient Software Tool for Phosphopeptide Identification
- Authors:
- Tiengo, Alessandra
Pasotti, Lorenzo
Barbarini, Nicola
Magni, Paolo - Other Names:
- Chen Ming Academic Editor.
- Abstract:
- Abstract : Phosphorylation is a protein posttranslational modification. It is responsible of the activation/inactivation of disease-related pathways, thanks to its role of "molecular switch." The study of phosphorylated proteins becomes a key point for the proteomic analyses focused on the identification of diagnostic/therapeutic targets. Liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS) is the most widely used analytical approach. Although unmodified peptides are automatically identified by consolidated algorithms, phosphopeptides still require automated tools to avoid time-consuming manual interpretation. To improve phosphopeptide identification efficiency, a novel procedure was developed and implemented in a Perl/C tool called PhosphoHunter, here proposed and evaluated. It includes a preliminary heuristic step for filtering out the MS/MS spectra produced by nonphosphorylated peptides before sequence identification. A method to assess the statistical significance of identified phosphopeptides was also formulated. PhosphoHunter performance was tested on a dataset of 1500 MS/MS spectra and it was compared with two other tools: Mascot and Inspect. Comparisons demonstrated that a strong point of PhosphoHunter is sensitivity, suggesting that it is able to identify real phosphopeptides with superior performance. Performance indexes depend on a single parameter (intensity threshold) that users can tune according to the study aim. All the three tools localizedAbstract : Phosphorylation is a protein posttranslational modification. It is responsible of the activation/inactivation of disease-related pathways, thanks to its role of "molecular switch." The study of phosphorylated proteins becomes a key point for the proteomic analyses focused on the identification of diagnostic/therapeutic targets. Liquid chromatography coupled to tandem mass spectrometry (LC-MS/MS) is the most widely used analytical approach. Although unmodified peptides are automatically identified by consolidated algorithms, phosphopeptides still require automated tools to avoid time-consuming manual interpretation. To improve phosphopeptide identification efficiency, a novel procedure was developed and implemented in a Perl/C tool called PhosphoHunter, here proposed and evaluated. It includes a preliminary heuristic step for filtering out the MS/MS spectra produced by nonphosphorylated peptides before sequence identification. A method to assess the statistical significance of identified phosphopeptides was also formulated. PhosphoHunter performance was tested on a dataset of 1500 MS/MS spectra and it was compared with two other tools: Mascot and Inspect. Comparisons demonstrated that a strong point of PhosphoHunter is sensitivity, suggesting that it is able to identify real phosphopeptides with superior performance. Performance indexes depend on a single parameter (intensity threshold) that users can tune according to the study aim. All the three tools localized >90% of phosphosites. … (more)
- Is Part Of:
- Advances in bioinformatics. Volume 2015(2015)
- Journal:
- Advances in bioinformatics
- Issue:
- Volume 2015(2015)
- Issue Display:
- Volume 2015, Issue 2015 (2015)
- Year:
- 2015
- Volume:
- 2015
- Issue:
- 2015
- Issue Sort Value:
- 2015-2015-2015-0000
- Page Start:
- Page End:
- Publication Date:
- 2015-01-12
- Subjects:
- Bioinformatics -- Periodicals
Bioinformatics
Computational Biology -- Periodicals
Periodicals
570.285 - Journal URLs:
- http://bibpurl.oclc.org/web/52720 ↗
https://www.hindawi.com/journals/abi/ ↗
http://www.ncbi.nlm.nih.gov/pmc/journals/984/ ↗ - DOI:
- 10.1155/2015/382869 ↗
- Languages:
- English
- ISSNs:
- 1687-8027
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library HMNTS - ELD Digital store
- Ingest File:
- 10256.xml