DIP, the Database of Interacting Proteins: a research tool for studying cellular networks of protein interactions
Top Cited Papers
Open Access
- 1 January 2002
- journal article
- research article
- Published by Oxford University Press (OUP) in Nucleic Acids Research
- Vol. 30 (1) , 303-305
- https://doi.org/10.1093/nar/30.1.303
Abstract
The Database of Interacting Proteins (DIP: http://dip.doe-mbi.ucla.edu) is a database that documents experimentally determined protein–protein interactions. It provides the scientific community with an integrated set of tools for browsing and extracting information about protein interaction networks. As of September 2001, the DIP catalogs ∼11 000 unique interactions among 5900 proteins from >80 organisms; the vast majority from yeast, Helicobacter pylori and human. Tools have been developed that allow users to analyze, visualize and integrate their own experimental data with the information about protein–protein interactions available in the DIP database.Keywords
This publication has 16 references indexed in Scilit:
- DIP: The Database of Interacting Proteins: 2001 updateNucleic Acids Research, 2001
- YPDTM, PombePDTM and WormPDTM: model organism volumes of the BioKnowledgeTM Library, an integrated resource for protein informationNucleic Acids Research, 2001
- BIND--The Biomolecular Interaction Network DatabaseNucleic Acids Research, 2001
- Genomic Expression Programs in the Response of Yeast Cells to Environmental ChangesMolecular Biology of the Cell, 2000
- A computationally directed screen identifying interacting coiled coils from Saccharomyces cerevisiaeProceedings of the National Academy of Sciences, 2000
- Zip3 Provides a Link between Recombination Enzymes and Synaptonemal Complex ProteinsCell, 2000
- A comprehensive analysis of protein–protein interactions in Saccharomyces cerevisiaeNature, 2000
- Toward a protein–protein interaction map of the budding yeast: A comprehensive system to examine two-hybrid interactions in all possible combinations between the yeast proteinsProceedings of the National Academy of Sciences, 2000
- DIP: the Database of Interacting ProteinsNucleic Acids Research, 2000
- The Saccharomyces cerevisiae Start-Specific Transcription Factor Swi4 Interacts through the Ankyrin Repeats with the Mitotic Clb2/Cdc28 Kinase and through Its Conserved Carboxy Terminus with Swi6Molecular and Cellular Biology, 1996