Demo Data from EDBT 2026 / reviewers in the wild / expert
Ahmed Arslan
dblp:197/8396
· DBLP profile ↗
2ranked-venue papers
2as first author
0since 2021 · last 2017
0000-0002-5325-6558ORCID · corroborated
Domains — the database's venue-derived domains; a paper can count in several
Applied, interdisciplinary, general and emerging computing · 2 · 2 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
2 papers |
Bioinformatics and computational biology · 100% |
Topics — the 6 heaviest of 7, each with the papers that count most for it
| Topic | Weight | Papers | Last | Evidence papers |
|---|---|---|---|---|
Bioinformatics and computational biology
protein function prediction |
0.3 | 1 | 2017 | Evolutionary conservation of Ebola virus proteins predicts important functions at residue level · Bioinform. 2017 |
Bioinformatics and computational biology › genomics
variant annotation |
0.3 | 1 | 2017 | yMap: an automated method to map yeast variants to protein modifications and functional regions · Bioinform. 2017 |
Bioinformatics and computational biology › proteomics › post-translational modification
post-translational modification analysis |
0.1 | 1 | 2017 | yMap: an automated method to map yeast variants to protein modifications and functional regions · Bioinform. 2017 |
Bioinformatics and computational biology › protein analysis › protein-protein interaction
protein-protein interaction analysis |
0.1 | 1 | 2017 | Evolutionary conservation of Ebola virus proteins predicts important functions at residue level · Bioinform. 2017 |
Bioinformatics and computational biology
protein structure analysis |
0.1 | 1 | 2017 | Evolutionary conservation of Ebola virus proteins predicts important functions at residue level · Bioinform. 2017 |
Bioinformatics and computational biology › molecular informatics › molecular modeling
structural modeling |
0.1 | 1 | 2017 | Evolutionary conservation of Ebola virus proteins predicts important functions at residue level · Bioinform. 2017 |
Methods — techniques the papers use, named apart from their topics
statistical testing · 0.3sequence conservation analysis · 0.3kinase prediction · 0.3homology modeling · 0.3
| Year | Publication | Venue | Position |
|---|---|---|---|
| 2017 | Evolutionary conservation of Ebola virus proteins predicts important functions at residue levelabstractMOTIVATION: The recent outbreak of Ebola virus disease (EVD) resulted in a large number of human deaths. Due to this devastation, the Ebola virus has attracted renewed interest as model for virus evolution. Recent literature on Ebola virus (EBOV) has contributed substantially to our understanding of the underlying genetics and its scope with reference to the 2014 outbreak. But no study yet, has focused on the conservation patterns of EBOV proteins. RESULTS: We analyzed the evolution of functional regions of EBOV and highlight the function of conserved residues in protein activities. We apply an array of computational tools to dissect the functions of EBOV proteins in detail: (i) protein sequence conservation, (ii) protein-protein interactome analysis, (iii) structural modeling and (iv) kinase prediction. Our results suggest the presence of novel post-translational modifications in EBOV proteins and their role in the modulation of protein functions and protein interactions. Moreover, on the basis of the presence of ATM recognition motifs in all EBOV proteins we postulate a role of DNA damage response pathways and ATM kinase in EVD. The ATM kinase is put forward, for further evaluation, as novel potential therapeutic target. AVAILABILITY AND IMPLEMENTATION: http://www.biw.kuleuven.be/CSB/EBOV-PTMs CONTACT: [email protected] information: Supplementary data are available at Bioinformatics online. Ahmed Arslan, Vera van Noort |
Bioinform. | 1 |
| 2017 | yMap: an automated method to map yeast variants to protein modifications and functional regionsabstractSummary: Recent advances in sequence technology result in large datasets of sequence variants. For the human genome, several tools are available to predict the impact of these variants on gene and protein functions. However, for model organisms such as yeast such tools are lacking, specifically to predict the effect of protein sequence altering variants on the protein level. We present a python framework that enables users to map in a fully automated fashion large set of variants to protein functional regions and post-translationally modified residues. Furthermore, we provide the user with the possibility to retrieve predicted functional information on modified residues from other resources for example that are predicted to play a role in protein-protein interactions. The results are complemented by statistical tests to highlight the significance of underlying functions and pathways affected by mutations. We show the application of this package on a yeast dataset derived from a recent evolutionary experiment on adaptation to ethanol. Availability and Implementation: The package is available from https://github.com/CSB-KUL/yMap and is implemented in Python. Contact: [email protected]. Supplementary information: Supplementary data are available at Bioinformatics online. Ahmed Arslan, Vera van Noort |
Bioinform. | 1 |