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Protein kinase (CK2) has emerged as an attractive cancer therapeutic target and recent efforts have been made to develop its inhibitors. However, the development of selective inhibitors remains challenging because of the highly conserved ATP-binding pocket (orthosteric site) of kinase family. As an alternative strategy, allosteric inhibitors, by targeting the much more diversified allosteric site relative to the conserved ATP-binding site, achieve better pharmacological advantages than orthosteric inhibitors. Traditional serendipitous screening and structure-based design are robust tools for the discovery of CK2 allosteric inhibitors. In this review, we summarize the recent advances in the identification of CK2 allosteric inhibitors. Firstly, we briefly present the CK2 allosteric sites. Then, the allosteric inhibitors targeting the well-elucidated allosteric sites (α/β interface, αD pocket and interface between the Glycine-rich loop and αC-helix) are highlighted in the discovery process and possible binding modes with the allosteric sites are described. This study is expected to provide valuable clues for the design of CK2 allosteric inhibitors.

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Abstract. In recent years, superconducting fault current limiter (SFCL) has become one of the forefront topics of current-limiting technology in the world. In this paper, the structure and working principle of several SFCLs which perform high in the actual power grid, such as resistance type, reaction type, hybrid type, magnetic shielding type, saturated iron core type, bridge type, active type and three-phase circuit reactance type. Through the analysis of the advantages and disadvantages of the SFCLs, the reference for further study of the SFCLs is provided.

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