Demo Data from VLDB 2026 / reviewers in the wild / expert
Richard L. Colton
dblp:317/5203
· DBLP profile ↗
1ranked-venue papers
0as first author
0since 2021 · last 1997
—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 |
Medical and health informatics · 77% Bioinformatics and computational biology · 23% | |
| Computer architecture, parallel and distributed computing, and storage systems
1 paper |
Integrated circuit design · 100% |
Topics — the 2 heaviest of 3, each with the papers that count most for it
| Topic | Weight | Papers | Last | Evidence papers |
|---|---|---|---|---|
Medical and health informatics
biosensor |
0.0 | 1 | 1997 | A high-sensitivity micromachined biosensor · Proc. IEEE 1997 |
Integrated circuit design
microelectromechanical systems |
0.0 | 1 | 1997 | A high-sensitivity micromachined biosensor · Proc. IEEE 1997 |
Methods — techniques the papers use, named apart from their topics
microfabrication · 0.0
| Year | Publication | Venue | Position |
|---|---|---|---|
| 1997 | A high-sensitivity micromachined biosensorabstractThe Force Amplified Biological Sensor (FABS) is a desktop or portable instrument currently under development at the Naval Research Laboratory. FABS will use a rapid, automated immunoassay to detect analytes such as proteins, viruses, and bacteria. The assay uses forces produced by micron-sized magnetic particles to pull on antibody-antigen bonds. Microfabricated piezoresistive cantilevers measure the resulting piconewton-level forces with sufficient sensitivity to detect single antibody-antigen bonds. These forces also serve to characterize the bonds, allowing FABS to distinguish specific antibody-antigen bonds from nonspecific interactions. David R. Baselt, Gil U. Lee, Karolyn M. Hansen, Linda A. Chrisey, Richard L. Colton |
Proc. IEEE | 5 |