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Enes K. Ergin

dblp:340/3356 · DBLP profile ↗
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1ranked-venue papers
1as first author
1since 2021 · last 2022
0000-0001-9810-7399ORCID · reported

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

Applied, interdisciplinary, general and emerging computing · 1 · 1 first-author · 1 since 2021

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 3 heaviest of 3, each with the papers that count most for it

TopicWeightPapersLastEvidence papers
Bioinformatics and computational biology › proteomics › post-translational modification
post-translational modification analysis
0.612022
SQuAPP - simple quantitative analysis of proteins and PTMs · Bioinform. 2022
Bioinformatics and computational biology
proteomics
0.612022
SQuAPP - simple quantitative analysis of proteins and PTMs · Bioinform. 2022
Bioinformatics and computational biology › proteomics
quantitative proteomics
0.612022
SQuAPP - simple quantitative analysis of proteins and PTMs · Bioinform. 2022

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

statistical analysis · 0.6r shiny · 0.6
YearPublicationVenuePosition
2022 SQuAPP - simple quantitative analysis of proteins and PTMs
abstract
SUMMARY: The comprehensive analysis of the proteome and its modulation by post-translational modification (PTM) is increasingly used in biological and biomedical studies. As a result, proteomics data analysis is ever more carried out by scientists with limited expertise in this type of data. While excellent software solutions for comprehensive and rigorous analysis of quantitative proteomic data exist, most are complex and not well suited for non-proteomics scientists. Integrative analysis of multi-level proteomics data on protein and diverse PTMs, like phosphorylation or proteolytic processing, remains particularly challenging and inaccessible to most biologists. To fill this void, we developed SQuAPP, an R-Shiny web-based analysis pipeline for the quantitative analysis of proteomic data. SQuAPP uses a streamlined workflow model to guide expert and novice users through quality control, data pre-processing, statistical analysis and visualization steps. Processing the protein, peptide and PTM datasets in parallel and their quantitative integration enable rapid identification of protein-level-independent modulation of protein modifications and intuitive interpretation of dynamic dependencies between different protein modifications. AVAILABILITY AND IMPLEMENTATION: SQuAPP is available at http://squapp.langelab.org/. The source code and local setup instructions can be accessed from https://github.com/LangeLab/SQuAPP.
Enes K. Ergin, Anuli C. Uzozie, Philipp F. Lange
Bioinform.1