VLDB 2026 Research / reviewers in the wild / expert
Catherine M. Radcliffe
dblp:53/6848
· DBLP profile ↗
1ranked-venue papers
0as first author
0since 2021 · last 2008
—ORCID · none
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 › structural bioinformatics › macromolecular structure analysis
glycan structure analysis |
0.1 | 1 | 2008 | GlycoBase and autoGU: tools for HPLC-based glycan analysis · Bioinform. 2008 |
Bioinformatics and computational biology › structural bioinformatics › macromolecular structure analysis
glycan structure assignment |
0.1 | 1 | 2008 | GlycoBase and autoGU: tools for HPLC-based glycan analysis · Bioinform. 2008 |
Methods — techniques the papers use, named apart from their topics
relational database · 0.1footprint analysis · 0.1
| Year | Publication | Venue | Position |
|---|---|---|---|
| 2008 | GlycoBase and autoGU: tools for HPLC-based glycan analysisabstractSUMMARY: The development of robust high-performance liquid chromatography (HPLC) technologies continues to improve the detailed analysis and sequencing of glycan structures released from glycoproteins. Here, we present a database (GlycoBase) and analytical tool (autoGU) to assist the interpretation and assignment of HPLC-glycan profiles. GlycoBase is a relational database which contains the HPLC elution positions for over 350 2-AB labelled N-glycan structures together with predicted products of exoglycosidase digestions. AutoGU assigns provisional structures to each integrated HPLC peak and, when used in combination with exoglycosidase digestions, progressively assigns each structure automatically based on the footprint data. These tools are potentially very promising and facilitate basic research as well as the quantitative high-throughput analysis of low concentrations of glycans released from glycoproteins. AVAILABILITY: http://glycobase.ucd.ie Matthew P. Campbell, Louise Royle, Catherine M. Radcliffe, Raymond A. Dwek, Pauline M. Rudd |
Bioinform. | 3 |