Protein function is often modulated by protein-protein interactions (PPIs) and therefore defining the partners of a protein helps to understand its activity. PPIs can be detected through different experimental approaches and are collected in several expert curated databases. These databases are used by researchers interested in examining detailed information on particular proteins. In many anal...

MOTIVATION Protein-protein interactions (PPIs), though extremely valuable towards a better understanding of protein functions and cellular processes, do not provide any direct information about the regions/domains within the proteins that mediate the interaction. Most often, it is only a fraction of a protein that directly interacts with its biological partners. Thus, understanding interaction ...

Protein–protein interactions (PPIs) are involved in an extensive variety of biological procedures, including cell-to-cell interactions, and metabolic developmental control. PPIs becoming one the most important aims system biology. act as a fundamental part predicting protein function target drug ability molecules. An abundance work has been performed to develop methods computationally predict t...

Protein-protein interactions (PPIs) are intrinsic to almost all cellular processes. Different computational methods offer new chances to study PPIs. To predict PPIs, while the integrative methods use multiple data sources instead of a single source, the domain-based methods often use only protein domain features. Integration of both protein domain features and genomic/proteomic features from mu...

Wnt signalling is a critical developmental pathway and associated aberrant signaling drives oncogenesis including colorectal bone cancer. β-catenin, central protein forms range of protein-protein interactions(PPIs), fundamental to driving the transcription oncogenes inducing proliferation tumour formation. To further elucidate these interactions, we have sought i) identify inhibitors β-catenin ...

Protein phosphorylation is a reversible post-translational modification where a protein kinase adds a phosphate group to a protein, potentially regulating its function, localization and/or activity. Phosphorylation can affect protein-protein interactions (PPIs), abolishing interaction with previous binding partners or enabling new interactions. Extracting phosphorylation information coupled wit...

BACKGROUND In the last decade, the inhibition of protein-protein interactions (PPIs) has emerged from both academic and private research as a new way to modulate the activity of proteins. Inhibitors of these original interactions are certainly the next generation of highly innovative drugs that will reach the market in the next decade. However, in silico design of such compounds still remains c...

Direct interactions between proteins are essential for the regulation of their functions in biological pathways. Targeting the complex network of protein-protein interactions (PPIs) has now been widely recognized as an attractive means to therapeutically intervene in disease states. Even though this is a challenging endeavor and PPIs have long been regarded as "undruggable" targets, the last tw...

The majority of gene products that crowd a living cell interact, at least transiently, with other protein molecules. Concordantly, virtually all cellular events are mediated by protein-protein interactions (PPIs). The same applies to host-pathogen systems, where PPIs are essential in host colonization and infection. Some authors believe that the understanding of the human interactome will provi...

Protein-protein interactions (PPIs) are central to most biological processes. Although efforts have been devoted to the development of methodology for predicting PPIs and protein interaction networks, the application of most existing methods is limited because they need information about protein homology or the interaction marks of the protein partners. In the present work, we propose a method ...