Demo Data from EDBT 2026 / reviewers in the wild / expert
Andrei Preoteasa
dblp:437/1464
· DBLP profile ↗
1ranked-venue papers
1as first author
1since 2021 · last 2026
—ORCID · none
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
| Topic | Weight | Papers | Last | Evidence papers |
|---|---|---|---|---|
Bioinformatics and computational biology
protein structure analysis |
1.0 | 1 | 2026 | EMERALD-UI: an interactive web application to unveil novel protein biology hidden in the alternative alignment space · Bioinform. 2026 |
Bioinformatics and computational biology › structural bioinformatics › protein structure representation
protein structure visualization |
1.0 | 1 | 2026 | EMERALD-UI: an interactive web application to unveil novel protein biology hidden in the alternative alignment space · Bioinform. 2026 |
Bioinformatics and computational biology
sequence alignment |
1.0 | 1 | 2026 | EMERALD-UI: an interactive web application to unveil novel protein biology hidden in the alternative alignment space · Bioinform. 2026 |
Methods — techniques the papers use, named apart from their topics
sequence alignment · 1.0protein structure prediction · 1.0
| Year | Publication | Venue | Position |
|---|---|---|---|
| 2026 | EMERALD-UI: an interactive web application to unveil novel protein biology hidden in the alternative alignment spaceabstractSUMMARY: Life over the past four billion years has been shaped by proteins and their capacity to assemble into three-dimensional conformations. Protein sequence alignments have been the enabling technology for exploring the evolution and functional adaptation of proteins across the tree of life. Recent advancements in scaling the prediction of three-dimensional protein structures from primary sequence alone, revealed that different modes of conservation and function operate on the sequence and structure level. This difference in protein conservation patterns and their underlying functional change that could emerge in suboptimal alignment configurations is often ignored in optimal protein alignment approaches. We introduce EMERALD-UI, an open-source interactive web application which is designed to reveal unexplored biology by visualising stable structural conformations or protein regions hidden in the alternative alignment space. AVAILABILITY: EMERALD-UI is available at https://algbio.github.io/emerald-ui/. The source code of the version described in this manuscript is available at https://github.com/algbio/emerald-ui and archived at Software Heritage: swh: 1: dir: 8b5a70160396d5e9a2e6d015c3b6f1426176d9a4. Andrei Preoteasa, Andreas Grigorjew, Alexandru I. Tomescu, Hajk-Georg Drost |
Bioinform. | 1 |