Demo Data from VLDB 2026 / reviewers in the wild / expert
Marc S. Cortese
dblp:91/4631
· DBLP profile ↗
1ranked-venue papers
0as first author
0since 2021 · last 2005
0000-0002-5903-0525ORCID · reported
Domains — the database's venue-derived domains; a paper can count in several
Applied, interdisciplinary, general and emerging computing · 1
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 2 heaviest of 2, each with the papers that count most for it
| Topic | Weight | Papers | Last | Evidence papers |
|---|---|---|---|---|
Bioinformatics and computational biology › protein structure analysis › intrinsically disordered protein
intrinsically disordered protein database |
0.1 | 1 | 2005 | DisProt: a database of protein disorder · Bioinform. 2005 |
Bioinformatics and computational biology
protein structure analysis |
0.1 | 1 | 2005 | DisProt: a database of protein disorder · Bioinform. 2005 |
Methods — techniques the papers use, named apart from their topics
manual curation · 0.1
| Year | Publication | Venue | Position |
|---|---|---|---|
| 2005 | DisProt: a database of protein disorderabstractUNLABELLED: The Database of Protein Disorder (DisProt) is a curated database that provides structure and function information about proteins that lack a fixed three-dimensional (3D) structure under putatively native conditions, either in their entirety or in part. Starting from the central premise that intrinsic disorder is an important structural class of protein and in order to meet the increasing interest thereof, DisProt is aimed at becoming a central repository of disorder-related information. For each disordered protein, the database includes the name of the protein, various aliases, accession codes, amino acid sequence, location of the disordered region(s), and methods used for structural (disorder) characterization. If applicable, most entries also list the biological function(s) of each disordered region, how each region of disorder is used for function, as well as provide links to PubMed abstracts and major protein databases. AVAILABILITY: www.disprot.org Slobodan Vucetic, Zoran Obradovic, Vladimir Vacic, Predrag Radivojac, Kang Peng, Lilia M. Iakoucheva, Marc S. Cortese, J. David Lawson, Celeste J. Brown, Jason G. Sikes, Crystal D. Newton, A. Keith Dunker |
Bioinform. | 7 |