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Veronika Suni

dblp:223/8363 · DBLP profile ↗
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1ranked-venue papers
1as first author
0since 2021 · last 2018
0000-0001-8269-7291ORCID · reported

Domains — the database's venue-derived domains; a paper can count in several

Applied, interdisciplinary, general and emerging computing · 1 · 1 first-author

Expertise — from the expertise taxonomy: the topics of the expert's papers under the CCF categories. A weight counts papers with recency: 1 for a paper about the topic, 0.3 when the topic is its context, halved every five years.

Interdisciplinary, comprehensive, and emerging computing
1 paper
Bioinformatics and computational biology · 100%

Topics — the 4 heaviest of 4, each with the papers that count most for it

TopicWeightPapersLastEvidence papers
Bioinformatics and computational biology › proteomics
mass spectrometry data analysis
0.312018
SimPhospho: a software tool enabling confident phosphosite assignment · Bioinform. 2018
Bioinformatics and computational biology › proteomics
phosphoproteomics
0.312018
SimPhospho: a software tool enabling confident phosphosite assignment · Bioinform. 2018
Bioinformatics and computational biology
proteomics
0.312018
SimPhospho: a software tool enabling confident phosphosite assignment · Bioinform. 2018
Bioinformatics and computational biology › proteomics › phosphoproteomics
phosphoproteomics analysis
0.112018
SimPhospho: a software tool enabling confident phosphosite assignment · Bioinform. 2018

Methods — techniques the papers use, named apart from their topics

simulated phosphopeptide spectral library · 0.3
YearPublicationVenuePosition
2018 SimPhospho: a software tool enabling confident phosphosite assignment
abstract
Motivation: Mass spectrometry combined with enrichment strategies for phosphorylated peptides has been successfully employed for two decades to identify sites of phosphorylation. However, unambiguous phosphosite assignment is considered challenging. Given that site-specific phosphorylation events function as different molecular switches, validation of phosphorylation sites is of utmost importance. In our earlier study we developed a method based on simulated phosphopeptide spectral libraries, which enables highly sensitive and accurate phosphosite assignments. To promote more widespread use of this method, we here introduce a software implementation with improved usability and performance. Results: We present SimPhospho, a fast and user-friendly tool for accurate simulation of phosphopeptide tandem mass spectra. Simulated phosphopeptide spectral libraries are used to validate and supplement database search results, with a goal to improve reliable phosphoproteome identification and reporting. The presented program can be easily used together with the Trans-Proteomic Pipeline and integrated in a phosphoproteomics data analysis workflow. Availability and implementation: SimPhospho is open source and it is available for Windows, Linux and Mac operating systems. The software and its user's manual with detailed description of data analysis as well as test data can be found at https://sourceforge.net/projects/simphospho/. Supplementary information: Supplementary data are available at Bioinformatics online.
Veronika Suni, Tomi Suomi, Tomoya Tsubosaka, Susumu Y. Imanishi, Laura Elo, Garry L. Corthals
Bioinform.1