VLDB 2026 Research / reviewers in the wild / expert
Bong Hyun Sung
dblp:176/9846
· DBLP profile ↗
1ranked-venue papers
0as first author
0since 2021 · last 2016
0000-0002-8992-1118ORCID · 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 1 heaviest of 1, each with the papers that count most for it
| Topic | Weight | Papers | Last | Evidence papers |
|---|---|---|---|---|
Bioinformatics and computational biology › structural bioinformatics
protein structure determination |
0.2 | 1 | 2016 | NMRe: a web server for NMR protein structure refinement with high-quality structure validation scores · Bioinform. 2016 |
Methods — techniques the papers use, named apart from their topics
statistical torsion angle potential · 0.2NOE distance restraints · 0.2
| Year | Publication | Venue | Position |
|---|---|---|---|
| 2016 | NMRe: a web server for NMR protein structure refinement with high-quality structure validation scoresabstractUNLABELLED: Protein structure refinement is a necessary step for the study of protein function. In particular, some nuclear magnetic resonance (NMR) structures are of lower quality than X-ray crystallographic structures. Here, we present NMRe, a web-based server for NMR structure refinement. The previously developed knowledge-based energy function STAP (Statistical Torsion Angle Potential) was used for NMRe refinement. With STAP, NMRe provides two refinement protocols using two types of distance restraints. If a user provides NOE (Nuclear Overhauser Effect) data, the refinement is performed with the NOE distance restraints as a conventional NMR structure refinement. Additionally, NMRe generates NOE-like distance restraints based on the inter-hydrogen distances derived from the input structure. The efficiency of NMRe refinement was validated on 20 NMR structures. Most of the quality assessment scores of the refined NMR structures were better than those of the original structures. The refinement results are provided as a three-dimensional structure view, a secondary structure scheme, and numerical and graphical structure validation scores. AVAILABILITY AND IMPLEMENTATION: NMRe is available at http://psb.kobic.re.kr/nmre/. Hyojung Ryu, Gyutae Lim, Bong Hyun Sung, Jinhyuk Lee |
Bioinform. | 3 |