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. 2024 Sep 19;15:7707. doi: 10.1038/s41467-024-51889-3

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© The Author(s) 2024

Open Access This article is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License, which permits any non-commercial use, sharing, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if you modified the licensed material. You do not have permission under this licence to share adapted material derived from this article or parts of it. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by-nc-nd/4.0/.

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Fig. 3 — a Changes in solvent exposure of the parkin complex upon addition of pUb at four time points (15 s, 1 min, 10 min, 60 min) and the sum of the four time points (gray bars). The largest changes occur in the Ubl domain, which is released by pUb binding, and RING1, which is the site of pUb binding. b Changes in solvent exposure upon addition of BIO-2007817 in the presence of pUb. The largest changes occur in the Rcat domain. c, d Addition of BIO-2007817 does not change solvent exposure in the absence of pUb or in the parkin K211N mutant. e HDX-MS analysis of individual peptides from the parkin Rcat domain show solvent exposure in the presence of BIO-2007817 but not the inactive diastereomer BIO-2007818. f Mapping of increased (red) and decreased (blue) exchange upon BIO-2007817 addition to parkin:pUb (b).