Describing biological protein interactions in terms of protein states and state transitions: the LiveDIP database.

Details

Serval ID
serval:BIB_283478F05AFB
Type
Article: article from journal or magazin.
Collection
Publications
Title
Describing biological protein interactions in terms of protein states and state transitions: the LiveDIP database.
Journal
Molecular and Cellular Proteomics
Author(s)
Duan X.J., Xenarios I., Eisenberg D.
ISSN
1535-9476 (Print)
ISSN-L
1535-9476
Publication state
Published
Issued date
2002
Volume
1
Number
2
Pages
104-116
Language
english
Abstract
Biological protein-protein interactions differ from the more general class of physical interactions; in a biological interaction, both proteins must be in their proper states (e.g. covalently modified state, conformational state, cellular location state, etc.). Also in every biological interaction, one or both interacting molecules undergo a transition to a new state. This regulation of protein states through protein-protein interactions underlies many dynamic biological processes inside cells. Therefore, understanding biological interactions requires information on protein states. Toward this goal, DIP (the Database of Interacting Proteins) has been expanded to LiveDIP, which describes protein interactions by protein states and state transitions. This additional level of characterization permits a more complete picture of the protein-protein interaction networks and is crucial to an integrated understanding of genome-scale biology. The search tools provided by LiveDIP, Pathfinder, and Batch Search allow users to assemble biological pathways from all the protein-protein interactions collated from the scientific literature in LiveDIP. Tools have also been developed to integrate the protein-protein interaction networks of LiveDIP with large scale genomic data such as microarray data. An example of these tools applied to analyzing the pheromone response pathway in yeast suggests that the pathway functions in the context of a complex protein-protein interaction network. Seven of the eleven proteins involved in signal transduction are under negative or positive regulation of up to five other proteins through biological protein-protein interactions. During pheromone response, the mRNA expression levels of these signaling proteins exhibit different time course profiles. There is no simple correlation between changes in transcription levels and the signal intensity. This points to the importance of proteomic studies to understand how cells modulate and integrate signals. Integrating large scale, yeast two-hybrid data with mRNA expression data suggests biological interactions that may participate in pheromone response. These examples illustrate how LiveDIP provides data and tools for biological pathway discovery and pathway analysis.
Keywords
Databases, Protein, Gene Expression Profiling/statistics & numerical data, Oligonucleotide Array Sequence Analysis/statistics & numerical data, Protein Binding, Proteins/chemistry, Proteins/genetics, Proteome/chemistry, Proteome/genetics, Two-Hybrid System Techniques
Pubmed
Create date
18/10/2012 10:07
Last modification date
20/08/2019 14:07
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