Editorial: Beyond protein degradation and lysine modification: novel insights into non-canonical ubiquitination

Aysegul Sapmaz; Jin Gan; Darragh P O'Brien; Adán Pinto-Fernández

doi:10.3389/fmolb.2024.1461356

Editorial: Beyond protein degradation and lysine modification: novel insights into non-canonical ubiquitination

Front Mol Biosci. 2024 Jul 30:11:1461356. doi: 10.3389/fmolb.2024.1461356. eCollection 2024.

Authors

Aysegul Sapmaz¹, Jin Gan², Darragh P O'Brien³, Adán Pinto-Fernández⁴

Affiliations

¹ Chemical Biology and Drug Discovery Laboratory, Department of Cell and Chemical Biology, Leiden University Medical Center, Leiden, Netherlands.
² Program in Cellular and Molecular Medicine, Boston Children's Hospital and Harvard Medical School, Boston, MA, United States.
³ Structural and Mechanistic Proteomics Laboratory, Nuffield Department of Medicine, Centre for Medicines Discovery, University of Oxford, Oxford, United Kingdom.
⁴ Translational Ubiquitomics Laboratory, Nuffield Department of Medicine, CAMS Oxford Institute and Centre for Medicines Discovery, University of Oxford, Oxford, United Kingdom.

No abstract available

Keywords: activity-based probes; chemical biology; non-canonical ubiquitination; post-translational modifications; ubiquitin; ubiquitin-like modifiers; ubiquitomics.

Publication types

Editorial

Grants and funding

The author(s) declare that financial support was received for the research, authorship, and/or publication of this article. AS work supported by the Innovative Medicines Initiative 2 (IMI2) Joint Undertaking under grant agreement no. 875510 (EUbOPEN project). Work in the AP-F lab is funded by Pfizer Inc., Ono Pharma UK Ltd., and the Chinese Academy of Medical Sciences (CAMS) Innovation Fund for Medical Science (CIFMS), China (grant number: 2018-I2M-2-002). The funders were not involved in the study design, collection, analysis, interpretation of data, the writing of this article, or the decision to submit it for publication.