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. 2024 Sep 6;18:11782234241276310. doi: 10.1177/11782234241276310

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© The Author(s) 2024

This article is distributed under the terms of the Creative Commons Attribution-NonCommercial 4.0 License (https://creativecommons.org/licenses/by-nc/4.0/) which permits non-commercial use, reproduction and distribution of the work without further permission provided the original work is attributed as specified on the SAGE and Open Access pages (https://us.sagepub.com/en-us/nam/open-access-at-sage).

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Figure 3. — Three-dimensional (3D) structure of the MIF trimer (Protein Data Bank entry, https://www.rcsb.org/, selected for display: 1CA7) and the binding site of various classes of small molecule inhibitors of the MIF tautomerase, including (A) competitive inhibitors (namely, ISO-1, ISO-66, and CPSI-1306), (B) irreversible inhibitors (ie, 4-IPP and epicatechin), and (C) allosteric inhibitors (that is, ibudilast, ebselen, and P425). They can be therapeutic strategies to inhibit the MIF signaling and play a significant role in improving BC with effects, such as apoptosis and cell death, cell proliferation inhibition, angiogenesis, and metastasis.