Indexing a protein-protein interaction network expedites network alignment
نویسندگان
چکیده
منابع مشابه
Protein-Protein Interaction Network Alignment
Proteins are some of the building blocks of organisms. They usually perform their functions by interacting with each other and forming protein complexes. A protein-protein interaction network is a graph that consists of proteins as vertices and their interactions as edges. Protein-protein interaction network alignment is very important in identifying protein complexes and predicting protein fun...
متن کاملSPINAL: scalable protein interaction network alignment
MOTIVATION Given protein-protein interaction (PPI) networks of a pair of species, a pairwise global alignment corresponds to a one-to-one mapping between their proteins. Based on the presupposition that such a mapping provides pairs of functionally orthologous proteins accurately, the results of the alignment may then be used in comparative systems biology problems such as function prediction/v...
متن کاملAlignment-free protein interaction network comparison
MOTIVATION Biological network comparison software largely relies on the concept of alignment where close matches between the nodes of two or more networks are sought. These node matches are based on sequence similarity and/or interaction patterns. However, because of the incomplete and error-prone datasets currently available, such methods have had limited success. Moreover, the results of netw...
متن کاملUsing the Protein-protein Interaction Network to Identifying the Biomarkers in Evolution of the Oocyte
Background Oocyte maturity includes nuclear and cytoplasmic maturity, both of which are important for embryo fertilization. The development of oocyte is not limited to the period of follicular growth, and starts from the embryonic period and continues throughout life. In this study, for the purpose of evaluating the effect of the FSH hormone on the expression of genes, GEO access codes for this...
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ژورنال
عنوان ژورنال: BMC Bioinformatics
سال: 2015
ISSN: 1471-2105
DOI: 10.1186/s12859-015-0756-0