Demo Data from EDBT 2026 / reviewers in the wild / expert
Christopher Reynolds
dblp:73/7065
· DBLP profile ↗
1ranked-venue papers
1as first author
0since 2021 · last 2009
0000-0002-8219-7462ORCID · 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 3 heaviest of 3, each with the papers that count most for it
| Topic | Weight | Papers | Last | Evidence papers |
|---|---|---|---|---|
Bioinformatics and computational biology › protein analysis › protein-protein interaction
protein-protein interaction analysis |
0.1 | 1 | 2009 | ProtorP: a protein-protein interaction analysis server · Bioinform. 2009 |
Bioinformatics and computational biology › protein structure analysis › quaternary structure
protein-protein interface characterization |
0.1 | 1 | 2009 | ProtorP: a protein-protein interaction analysis server · Bioinform. 2009 |
Bioinformatics and computational biology
structural bioinformatics |
0.1 | 1 | 2009 | ProtorP: a protein-protein interaction analysis server · Bioinform. 2009 |
Methods — techniques the papers use, named apart from their topics
physicochemical parameter computation · 0.1
| Year | Publication | Venue | Position |
|---|---|---|---|
| 2009 | ProtorP: a protein-protein interaction analysis serverabstractSUMMARY: The PROTORP server analyses protein-protein associations in 3D structures. The server calculates a series of physical and chemical parameters of the protein interaction sites that contribute to the binding energy of the association. These parameters include, size and shape, intermolecular bonding, residue and atom composition and secondary structure contributions. The server is flexible, in that it allows users to analyse individual protein associations or large datasets of associations deposited in the PDB, or upload and analyse proprietary files. The properties calculated can be compared with parameter distributions for non-homologous datasets of different classes of protein associations provided on the server website. The server provides an efficient way of characterizing protein-protein associations of new or existing proteins, and a means of putting these values in the context of previously observed associations. AVAILABILITY: http://www.bioinformatics.sussex.ac.uk/protorp Christopher Reynolds, David Damerell, Susan Jones |
Bioinform. | 1 |