Kendall G. Byler

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BACKGROUND Protein-protein interactions mediate a wide range of cellular functions and responses and have been studied rigorously through recent large-scale proteomics experiments and bioinformatics analyses. One of the most important findings of those endeavours was the observation that 'hub' proteins participate in significant numbers of protein(More)
We report consensus Structure-Activity Similarity (SAS) maps that address the dependence of activity landscapes on molecular representation. As a case study, we characterized the activity landscape of 54 compounds with activities against human cathepsin B (hCatB), human cathepsin L (hCatL), and Trypanosoma brucei cathepsin B (TbCatB). Starting from an(More)
UNLABELLED Hub proteins (those engaged in most physical interactions in a protein interaction network (PIN) have recently gained much research interest due to their essential role in mediating cellular processes and their potential therapeutic value. It is straightforward to identify hubs if the underlying PIN is experimentally determined; however,(More)
Proteins that are most essential for functioning and viability of bacterial cell have been shown to exhibit larger number of interactions with other cell components. Thus, by identifying the most connected proteins (or hubs) in protein interaction networks (PINs), one may discover prospective drug targets that can be utilized to combat emergent and(More)
Small molecules which alter biological processes or disease states are of significant interest. In-silico drug discovery commonly uses measures of structural similarity for identifying the " right " small molecule for a given task. Because explicit structure similarity determination is a very difficult task, modern chemoinformatics solutions typically use "(More)
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