Demo Data from EDBT 2026 / reviewers in the wild / expert
Richard J. Roberts
dblp:76/1661
· DBLP profile ↗
5ranked-venue papers
3as first author
0since 2021 · last 2015
0000-0002-4348-0169ORCID · verified
Domains — the database's venue-derived domains; a paper can count in several
Applied, interdisciplinary, general and emerging computing · 5 · 3 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 5 heaviest of 5, each with the papers that count most for it
| Topic | Weight | Papers | Last | Evidence papers |
|---|---|---|---|---|
Bioinformatics and computational biology › genomics › genomic data management
genome database |
0.0 | 1 | 1997 | Hunting for new restriction enzymes in GenBank (abstract) · RECOMB 1997 |
Bioinformatics and computational biology
sequence analysis |
0.0 | 1 | 1997 | Hunting for new restriction enzymes in GenBank (abstract) · RECOMB 1997 |
Bioinformatics and computational biology
multiple sequence comparison |
0.0 | 1 | 1994 | VISA: Visual Sequence Analysis for the comparison of multiple amino acid sequences · Comput. Appl. Biosci. 1994 |
Bioinformatics and computational biology
protein sequence analysis |
0.0 | 1 | 1994 | VISA: Visual Sequence Analysis for the comparison of multiple amino acid sequences · Comput. Appl. Biosci. 1994 |
Bioinformatics and computational biology › protein analysis › protein bioinformatics
protein family |
0.0 | 1 | 1994 | VISA: Visual Sequence Analysis for the comparison of multiple amino acid sequences · Comput. Appl. Biosci. 1994 |
Methods — techniques the papers use, named apart from their topics
database search · 0.0
| Year | Publication | Venue | Position |
|---|---|---|---|
| 2015 | Ten Simple Rules to Win a Nobel PrizeabstractIt is remarkable how many students, young faculty, and even senior faculty hanker after a Nobel Prize. Somehow, they think that it is possible to structure their scientific careers so that the culmination will bring this much sought-after honor. Some even think that as a Nobel laureate myself, I may have the key to success—some secrets that I can share and so greatly improve their odds of success. Unfortunately, I must begin by disappointing everyone. There is only one path that should be followed. It is summed up in Rule 1, but some of the other Rules may prove helpful—or if not helpful, then at least amusing.
1. Never Start Your Career by Aiming for a Nobel Prize
Don’t even hope for it or think about it. Just focus on doing the very best science that you can. Ask good questions, use innovative methods to answer them, and look for those unexpected results that may reveal some unexpected aspect of nature. If you are successful in your research career, then you will make lots of discoveries and have a very happy life. If you are lucky, you will make a big discovery that may even bag you a prize or two. But only if you are extraordinarily lucky will you stand any chance of winning a Nobel Prize. They are very elusive. Richard J. Roberts |
PLoS Comput. Biol. | 1 |
| 2005 | Phylogenetic detection of conserved gene clusters in microbial genomesabstractBACKGROUND: Microbial genomes contain an abundance of genes with conserved proximity forming clusters on the chromosome. However, the conservation can be a result of many factors such as vertical inheritance, or functional selection. Thus, identification of conserved gene clusters that are under functional selection provides an effective channel for gene annotation, microarray screening, and pathway reconstruction. The problem of devising a robust method to identify these conserved gene clusters and to evaluate the significance of the conservation in multiple genomes has a number of implications for comparative, evolutionary and functional genomics as well as synthetic biology. RESULTS: In this paper we describe a new method for detecting conserved gene clusters that incorporates the information captured by a genome phylogenetic tree. We show that our method can overcome the common problem of overestimation of significance due to the bias in the genome database and thereby achieve better accuracy when detecting functionally connected gene clusters. Our results can be accessed at database GeneChords http://genomics10.bu.edu/GeneChords. CONCLUSION: The methodology described in this paper gives a scalable framework for discovering conserved gene clusters in microbial genomes. It serves as a platform for many other functional genomic analyses in microorganisms, such as operon prediction, regulatory site prediction, functional annotation of genes, evolutionary origin and development of gene clusters. Yu Zheng 0019, Brian P. Anton, Richard J. Roberts, Simon Kasif |
BMC Bioinform. | 3 |
| 2000 | The early days of bioinformatics publishingabstractAbstract A brief history of the early days of publishing in the bioinformatics field is presented. Contact: [email protected] Richard J. Roberts |
Bioinform. | 1 |
| 1997 | Hunting for new restriction enzymes in GenBank (abstract)abstractNo abstract available. Richard J. Roberts |
RECOMB | 1 |
| 1994 | VISA: Visual Sequence Analysis for the comparison of multiple amino acid sequencesabstractVISA (VIsual Sequence Analysis) is a software package that displays global similarities within a set of related protein sequences. The program identifies amino acid patterns that are common to many members of the set of sequences and displays them as a series of histograms. Individual peaks on the display can be assigned a color and analogous peaks in the other sequences are then automatically marked in the same color. This can be repeated for each significant peak and leads to a display in which major matching segments of multiple amino acid sequences appear as dominant peaks of the histograms with matching colors. These peaks usually correspond to the conserved sequence motifs that are characteristic of particular proteins. An extensive set of software tools is included to help the localization, visualization and analysis of the global similarities displayed. VISA provides a graphic overview of the sequence similarity that can help to understand the architecture of the protein family and can be helpful while designing experiments to probe function. Janos Posfai, Z. Szaraz, Richard J. Roberts |
Comput. Appl. Biosci. | 3 |