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Jongkeun Park

As seen in: Nature, MDPI, BioRxiv
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Articles

N-MIX: an in silico framework for predicting ADAM10-mediated substrate cleavage sites through structural and spatial analysis of protease–substrate interactions

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By Dae Sun Chung, Jongkeun Park, Won Choi, Dongwan Hong
| Nature Verified
Abstract ADAM10 is a membrane-anchored metalloprotease that mediates ectodomain shedding of diverse substrates implicated in cancer, inflammation, and neurodegeneration. Despite its biological significance, ADAM10 substrate specificity remains poorly understood, as conventional sequence-based analyses have proven insufficient to identify conserved cleavage motifs.
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Deciphering Features of Metalloprotease Cleavage Targets Using Protein Structure Prediction

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By Jongkeun Park, WonJong Choi, Young Jin Seong, Dae Sun Chung
| BioRxiv
Abstract Metalloproteases are a class of enzymes that utilize metal ions within their active sites to catalyze the hydrolysis of peptide bonds in proteins. Among these, ADAM10 (A Disintegrin and Metalloproteinase 10), a member of the ADAM family, plays a crucial role in mediating intracellular signaling by cleaving specific substrates, thereby influencing a variety of physiological and pathological processes.
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AIVE: accurate predictions of SARS-CoV-2 infectivity from comprehensive analysis

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By Jongkeun Park, WonJong Choi, Young Jin Seong, Seungpil Jeong
| BioRxiv
Abstract An unprecedented amount of SARS-CoV-2 data has been accumulated compared with previous infectious diseases, enabling insights into its evolutionary process and more thorough analyses. This study investigates SARS-CoV-2 features as it evolved to evaluate its infectivity. We examined viral sequences and identified the polarity of amino acids in the Receptor Binding Motif (RBM) region.
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