It can be estimated that most membrane proteins function in complexes (Fig. 1) (Daley 2008). Protein-protein interactions (PPIs) within these complexes can either be direct (primary interaction) or indirect (secondary interaction). Direct interactions occur either by homooligomerisation as determined for bacterial two-component systems (Gao and Stock 2009) (Fig. 1A) or by hetero-oligomerisation...

The intricate molecular details of protein-protein interactions (PPIs) are crucial for function. Therefore, measuring the same interacting protein pair again, we expect the same result. This work measured the similarity in the molecular details of interaction for the same and for homologous protein pairs between different experiments. All scores analyzed suggested that different experiments oft...

BACKGROUND Regulated protein-protein interactions (PPIs) are pivotal molecular switches that are important for the regulation of signaling processes within eukaryotic cells. Cellular signaling is altered in various disease conditions and offers interesting options for pharmacological interventions. Constitutive PPIs are usually mediated by large interaction domains. In contrast, stimulus-regula...

Prediction of protein–protein interactions (PPIs) helps to grasp molecular roots disease. However, web-lab experiments predict PPIs are limited and costly. Using machine-learning-based frameworks can not only automatically identify PPIs, but also provide new ideas for drug research development from a promising alternative. We present novel deep-forest-based method prediction. Firstly, pseudo am...

A reversible green fluorogenic protein-fragment complementation assay was developed based on the crystal structure of UnaG, a recently discovered fluorescent protein. In living mammalian cells, the nonfluorescent fragments complemented and rapidly became fluorescent upon rapamycin-induced FKBP and Frb protein interaction, and lost fluorescence when the protein interaction was inhibited. This re...

Bimolecular fluorescence complementation (BiFC) has been widely used to visualize protein-protein interactions (PPIs) in cells. Until now, however, the resolution of BiFC has been limited by the diffraction of light to ∼250 nm, much larger than the nanometer scale at which PPIs occur or are regulated. Cellular imaging at the nanometer scale has recently been realized with single molecule superr...

Tens of thousands protein-protein interactions (PPIs) have been found in human cells and many these macromolecular partnerships could determine the cell growth death. Thus there is a need to develop methods catalogue macromolecules by detecting their interactions, modifications, cellular locations. It will be helpful for scientists compare difference between diseased state its normal find poten...

In protein-protein interaction (PPI) networks certain topological properties appear to be recurrent: network maps are considered scale-free. It is possible that this topology is reflected in the protein structure. In this paper, we investigate the role of protein disorder in the network topology. We find that the disorder of a protein (or of its neighbors) is independent of its number of PPIs. ...

Mapping and understanding of the protein interaction networks with their key modules and hubs can provide deeper insights into the molecular machinery underlying complex phenotypes. In this article, we present the basic characteristics and definitions of protein networks, starting with a distinction of the different types of associations between proteins. We focus the review on protein-protein ...

BACKGROUND One of the crucial steps toward understanding the biological functions of a cellular system is to investigate protein-protein interaction (PPI) networks. As an increasing number of reliable PPIs become available, there is a growing need for discovering PPIs to reconstruct PPI networks of interesting organisms. Some interolog-based methods and homologous PPI families have been propose...