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The latest advances in the sequencing methods in head and neck squamous cell carcinoma (HNSCC) tissues have revolutionized our understanding of the disease by taking off the veil from the most frequent genetic alterations in the components of the oncogenic pathways. Among all the identified alterations, aberrancies in the genes attributed to the phosphoinositide 3‐kinases (PI3K) axis have attracted special attention as they were altered in more than 90% of the tissues isolated from HNSCC patients. In fact, the association between these aberrancies and the increased risk of cancer metastasis suggested this axis as an “Achilles Heel” of HNSCC, which may be therapeutically targeted. The results of the clinical trials investigating the therapeutic potential of the inhibitors targeting the components of the PI3K axis in the treatment of HNSCC patients, either alone or in a combined‐modal strategy, opened a new chapter in the treatment strategy of this malignancy. The present study aimed to review the importance of the PI3K axis in the pathogenesis of HNSCC and also provide a piece of information about the breakthroughs and challenges of PI3K inhibitors in the therapeutic strategies of the disease.
Mutations in the novel coronavirus SARS‐CoV2 are the major concern as they might lead to drug/vaccine resistance. In the host cell, the virus largely depends on the main protease (Mpro) to regulate infection hence it is one of the most attractive targets for inhibitor design. However, >19,000 mutations in the Mpro have already been reported. The mutations encompassing 282 amino acid positions and these “hotspots” might change the Mpro structure, activity and potentially delay therapeutic strategies targeting Mpro. Thus, here we identified 24 mutational “coldspots” where mutations have not been observed. We compared the structure‐function relationship of these coldspots with several SARS‐CoV2 Mpro X‐ray crystal structures. We found that three coldspot residues (Leu141, Phe185, and Gln192) help to form the active site, while seven (Gly2, Arg4, Tyr126, Lys137, Leu141, Leu286, and Leu287) contribute to dimer formation that is required for Mpro activity. The surface of the dimer interface is more resistant to mutations compared to the active site. Interestingly, most of the coldspots are found in three clusters and forms conserved patterns when compared with other coronaviruses. Importantly, several conserved coldspots are available on the surface of the active site and at the dimer interface for targeting. The identification and short list of these coldspots offers a new perspective to target the SARS‐CoV2 Mpro while avoiding mutationbased drug resistance.
SPECIAL ISSUE CALL FOR PAPERS
GUEST EDITORS: Yi-Ching Wang (National Cheng Kung University) and Chih-Peng Chang (National Cheng Kung University)
Manuscripts should be submitted by 31 May 2021
Expected issue publication will be October 2021
GUEST EDITORS: Nesrin Kartal Ozer (Marmara University), Jose Vina (University of Valencia), Gloria Olaso (University of Valencia), Erdi Sozen (Marmara University)
Manuscripts should be submitted by 31 May 2021
Expected issue publication will be November 2021
GUEST EDITOR: Ruey-Hwa Chen (Institute of Biological Chemistry, Academia Sinica, Taiwan)
Manuscripts should be submitted by 10 September 2021
Expected issue publication will be February 2022
GUEST EDITOR: Xiangya Ding, Nanjing Medical University
Manuscripts should be submitted by 30 September 2021
Expected issue publication will be early 2022
GUEST EDITORS: Nikos Karamanos (Univ. of Patras), Sylvie Ricard-Blum (Univ. of Lyon), Dimitris Kletsas (NCSR Demokritos, Athens)
Manuscripts should be submitted by 31 October 2021
Expected issue publication will be March 2022
NEW VIRTUAL ISSUES
Biotechnology and Applied Biochemistry
Biochemistry and Molecular Biology Education
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Molecular Aspects of Medicine
Volume 74 (2020) 100894
The Atlas of Inflammation Resolution (AIR)