Abstract The SARS-CoV-2 main protease (M pro ) is a key antiviral target that equilibrates between an active dimer and inactive monomer, making the dimerization interface a promising therapeutic vu...
<p><strong>Tác giả:</strong> Chengxi Liu, Qinyu Jia, Chang Zhao, Zhong‐Ping Yao</p>
<p>Abstract The SARS-CoV-2 main protease (M pro ) is a key antiviral target that equilibrates between an active dimer and inactive monomer, making the dimerization interface a promising therapeutic vulnerability. This study investigates M pro monomer-dimer equilibrium and conformational changes induced by inhibitor binding using 13 C labeling with native mass spectrometry and hydrogen/deuterium exchange mass spectrometry (HDX-MS). We evaluated how peptidomimetic inhibitors (PF-07321332, PF-00835...</p>
<p>📄 DOI: <a href="https://doi.org/https://doi.org/10.7554/elife.109956.4" target="_blank" rel="noopener">https://doi.org/10.7554/elife.109956.4</a></p>
<p>📖 <a href="https://doi.org/https://doi.org/10.7554/elife.109956.4" target="_blank" rel="noopener">Xem bài báo đầy đủ</a></p>
Bài viết được biên soạn lại bởi LIFVietnam. Nguồn tham khảo: OpenAlex