Demo Data from VLDB 2026 / reviewers in the wild / expert
Kirill Degtyarenko
dblp:27/4224
· DBLP profile ↗
2ranked-venue papers
2as first author
0since 2021 · last 2000
0009-0005-7896-7806ORCID · verified
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 2 heaviest of 3, each with the papers that count most for it
| Topic | Weight | Papers | Last | Evidence papers |
|---|---|---|---|---|
Bioinformatics and computational biology › structural bioinformatics
protein structure classification |
0.0 | 1 | 2000 | Bioinorganic motifs: towards functional classification of metalloproteins · Bioinform. 2000 |
Bioinformatics and computational biology
cytochrome p450 |
0.0 | 1 | 1996 | The directory of P450-containing systems on WorldWide Web · Comput. Appl. Biosci. 1996 |
Methods — techniques the papers use, named apart from their topics
database integration · 0.0database curation · 0.0
| Year | Publication | Venue | Position |
|---|---|---|---|
| 2000 | Bioinorganic motifs: towards functional classification of metalloproteinsabstractUNLABELLED: The habitat of bioinorganic motifs (BIMs) is at the interface of biological inorganic chemistry and bioinformatics. BIM is defined as a common structural feature shared by functionally related, but not necessarily homologous, proteins, and consisting of the metal atom(s) and first coordination shell ligands. BIMs appear to be suitable for classification of metal centres at any level, from groups of unrelated proteins with similar function to different functional states of the same protein, and for description of possible evolutionary relationships of metalloproteins. However, they have not attracted wide attention from the bioinformatics community. Although their presence is appreciated, they are difficult to predict-therefore the current 'high-throughput' initiatives are likely to miss or ignore them altogether. The protein sequence databases do not distinguish between proteins containing different prosthetic groups (unless they have different sequences) or between apo- and holoprotein. On the other hand, the protein structure databases include data on 'hetero compounds' of various origin but these data are often inconsistent. A number of specialized databases dealing with BIMs and attempts to classify them are reviewed. SUPPLEMENTARY INFORMATION: The additional bibliography and list of Internet resources on bioinorganic chemistry are available at http://www.ebi.ac.uk/ approximately kirill/biometal/ Kirill Degtyarenko |
Bioinform. | 1 |
| 1996 | The directory of P450-containing systems on WorldWide WebabstractTo facilitate access to electronic resources for all researchers working in the field of P450 proteins and P450-containing systems, a WorldWide Web server has been established called The Directory of P450-containing Systems at < http://www.icgeb.trieste.it/p450/ >. Currently it contains the most up-to-date list of sequences of both the P450 superfamily and proteins mediating electron transfer to P450, i.e. NADPH:P450 reductases, specific NAD(P)H:ferredoxin reductases, cytochrome b5 reductases, ferredoxins and cytochromes b5, and their homologues from different enzyme systems. All the referenced sequences are provided with accession numbers and cross-links to major sequence databanks: PIR, SWISS-PROT, EMBL/GenBank and PRF. Kirill Degtyarenko, Péter Fábián |
Comput. Appl. Biosci. | 1 |