نتایج جستجو برای: protein protein interaction ppis
تعداد نتایج: 1703658 فیلتر نتایج به سال:
Proteins are macromolecules which hardly act alone; they need to make interactions with some other proteins to do so. Numerous factors are there which can regulate the interactions between proteins [4]. Here in this present study we aim to understand Protein -Protein Interactions (PPIs) of two proteins ABCB11 and ADA from quantitative point of view. One of our major aims also is to study the fa...
MOTIVATION Identification and characterization of protein-protein interactions (PPIs) is one of the key aims in biological research. While previous research in text mining has made substantial progress in automatic PPI detection from literature, the need to improve the precision and recall of the process remains. More accurate PPI detection will also improve the ability to extract experimental ...
Understanding the cell as a system has become one of the foremost challenges in the post-genomic era. As a result of advances in high-throughput (HTP) methodologies, we have seen a rapid growth in new types of data at the whole-genome scale. Over the last decade, HTP experimental techniques such as yeast two-hybrid assays and co-affinity purification couple with mass spectrometry have generated...
Protein-protein interactions (PPIs) perform important roles on biological functions. Researches of mutants on protein interactions can further understand PPIs. In the past, many researchers have developed databases that stored mutants on protein interactions, which are old and not updated till now. To address the issue, we developed a kinetic and thermodynamic database of mutant protein interac...
Advances in protein-protein interaction (PPI) detection technology and computational analysis methods have produced numerous PPI networks, whose completeness appears to depend on the extent of data derived from different PPI assay methods and the complexity of the studied organism. Despite the partial nature of human PPI networks, computational data integration and analyses helped to elucidate ...
Protein-protein interactions (PPIs) are important in all aspects of cellular function, and there is interest in finding inhibitors of these contacts. However, PPIs with weak affinities and/or large interfaces have traditionally been more resistant to the discovery of inhibitors, partly because it is more challenging to develop high-throughput screening (HTS) methods that permit direct measureme...
Analysis of protein-protein interaction networks has revealed the presence of proteins with multiple interaction ligand proteins, such as hub proteins. For such proteins, multiple ligands would be predicted as interacting partners when predicting all-to-all protein-protein interactions (PPIs). In this work, to obtain a better understanding of PPI mechanisms, we focused on protein interaction su...
Pattern discovery in protein interaction networks can reveal crucial biological knowledge on the inner workings of cellular machinery. Although far from complete, extracting meaningful patterns from proteomic networks is a nontrivial task due to their size-complexity. This paper proposes a computational framework to efficiently discover topologically-similar patterns from large proteomic networ...
Modification of protein-protein interactions (PPIs) holds promise for novel rational drug design. Disrupting or modifying protein interactions offers new challenges in terms of chemical compound libraries and techniques for compound validation. As proteins interact with several partners in different allosteric conformation in a pathological and tissue-specific fashion, it is difficult to predic...
Inhibition of protein-protein interactions (PPIs) is emerging as a promising therapeutic strategy despite the difficulty in targeting such interfaces with drug-like small molecules. PPIs generally feature large and flat binding surfaces as compared to typical drug targets. These features pose a challenge for structural characterization of the surface using geometry-based pocket-detection method...
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