Essentially all biological processes depend on protein-protein interactions (PPIs). Timing of such interactions is crucial for regulatory function. Although circadian (~24-hour) clocks constitute fundamental cellular timing mechanisms regulating important physiological processes, PPI dynamics on this timescale are largely unknown. Here, we identified 109 novel PPIs among circadian clock protein...

Recent technical advances in identifying protein-protein interactions (PPIs) have generated the genomic-wide interaction data, collectively collectively referred to as the interactome. These interaction data give an insight into the underlying mechanisms of biological processes. However, the PPI data determined by experimental and computational methods include an extremely large number of false...

Objective(s): First, 10-bromodecanoic acid was covalently attached to all available surface primary amines of PPI G2 and G3 to increase their lipophilicity. In the subsequent step, PPIs were conjugated to the alkylcarboxylate groups of alkylcarboxylate-PPI derivatives to increase the number of surface primary amines. Physicochemical properties of modified PPIs were determined. Transfection expe...

The simplicity and sensitivity of the bimolecular fluorescence complementation (BiFC) assay make it a powerful tool to investigate protein-protein interactions (PPIs) in living cells. However, non-specific association of the fluorescent protein fragments in a BiFC system can complicate evaluation of PPIs. Here, we introduced a bicistronic expression vector, pBudCE4.1, into an mLumin-based BiFC ...

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...

In biomedical texts, contradictions about proteinprotein interactions (PPIs) occur when an author reports observing a given PPI whereas another author argues that very same interaction does not take place: e.g., when author X argues that “protein A interacts with protein B” whereas author Y claims that “protein A does not interact with B”. Of course, merely discovering a potential contradiction...

MOTIVATION Protein-protein interaction (PPI) extraction from published biological articles has attracted much attention because of the importance of protein interactions in biological processes. Despite significant progress, mining PPIs from literatures still rely heavily on time- and resource-consuming manual annotations. RESULTS In this study, we developed a novel methodology based on Bayes...

Protein-protein interactions (PPIs), involved in many biological processes such as cellular signaling, are ultimately encoded in the genome. Solving the problem of predicting protein interactions from the genome sequence will lead to increased understanding of complex networks, evolution and human disease. We can learn the relationship between genomes and networks by focusing on an easily appro...

objective(s): first, 10-bromodecanoic acid was covalently attached to all available surface primary amines of ppi g2 and g3 to increase their lipophilicity. in the subsequent step, ppis were conjugated to the alkylcarboxylate groups of alkylcarboxylate-ppi derivatives to increase the number of surface primary amines. physicochemical properties of modified ppis were determined. transfection expe...

Pathogens usually evade and manipulate host-immune pathways through pathogen-host protein-protein interactions (PPIs) to avoid being killed by the host immune system. Therefore, uncovering pathogen-host PPIs is critical for determining the mechanisms underlying pathogen infection and survival. In this study, we developed a computational method, which we named pairwise structure similarity (PSS)...