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A possible non-proteolytic role of ubiquitin conjugation in alleviating the pathology of Huntingtin’s aggregation

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Fig. 1: Site specific ubiquitination of Huntingtin on lysine residues 6 and 9 results in the formation of fewer but larger, probably multi-adduct aggregates.

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Acknowledgements

NEZ and AC were supported during the study on ubiquitination of Huntingtin by grants from the European Community’s Seventh Framework Programme FP7/2012 (TreatPolyQ, Grant Agreement No. 264508), the German-Israeli Foundation for Scientific Research and Development (GIF; I-1437-418.13/2017), the Rappaport Family Institute for Biomedical Research at the Technion-Israel Institute of Technology, and the Allen and Jewel Prince Center for Neurodegenerative Disorders of the Brain. AC is supported by grants from the Adelson Medical Research Foundation (AMRF), the Israel Science Foundation (ISF), the Technion-University of Michigan at Ann Arbor Collaborative Program and by an Israel Cancer Research Fund (ICRF) Professorship.

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Correspondence to Noam E. Ziv or Aaron Ciechanover.

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Ziv, N.E., Ciechanover, A. A possible non-proteolytic role of ubiquitin conjugation in alleviating the pathology of Huntingtin’s aggregation. Cell Death Differ 28, 814–817 (2021). https://doi.org/10.1038/s41418-020-00617-7

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