Motivation: Protein-ligand binding affinity prediction is a central task in drug design and development. Cross-modal attention mechanism has recently become a core component of many deep learning models due to its potential to improve model explainability. Non-covalent interactions (NCIs), one of the most critical domain knowledge in binding affinity prediction task, should be incorporated into protein-ligand attention mechanism for more explainable deep drug-target interaction models.
View Article and Find Full Text PDFAMoRE (Advanced Mo-based Rare process Experiment) is an international collaboration searching for the neutrinoless double-beta decay of the Mo isotope with cryogenic detectors using molybdate (MoO)-based scintillation crystals. The process requires that the detector apparatus and its components, including bolometric crystals and thus initial materials used for the crystal growth, be extremely low in radioactive isotopes having decays that may generate background noise signals in the region of interest. The present study summarizes an ICP-MS assay program conducted for the AMoRE experiment.
View Article and Find Full Text PDFMotivation: Recent advances in deep learning have offered solutions to many biomedical tasks. However, there remains a challenge in applying deep learning to survival analysis using human cancer transcriptome data. As the number of genes, the input variables of survival model, is larger than the amount of available cancer patient samples, deep-learning models are prone to overfitting.
View Article and Find Full Text PDFA procedure to locate the Pt nanostructure inside the hydrophilic channel of a Nafion membrane was developed in order to enhance Pt utilization in PEMFCs. Nanosize Pt-embedded MEA was constructed by Cu electroless plating and subsequent Pt electrodeposition inside the hydrophilic channels of the Nafion membrane. The metallic Pt nanostructure fabricated inside the membrane was employed as an oxygen reduction catalyst for a PEMFC and facilitated effective use of the hydrophilic channels inside the membrane.
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