Universität zu Köln

Ribeiro, Victoria Chaves, Wirtz, Jessica ORCID: 0009-0000-1994-1722 and Leidecker, Orsolya ORCID: 0000-0001-5315-014X (2025). The beauty of ADP-ribosylation: versatility in every link and organelle. BIOspektrum, 31 (3). pp. 258-261. Springer Nature. ISSN 0947-0867

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Abstract

ADPr is a crucial modification that regulates various cellular processes. Its complexity stems from the diverse chemical linkages it can form, including connections to various amino acids and nucleic acid components. ADPr can manifest as single ADP-ribose unit or as chains and can also form hybrid modifications. Here we focus on the remarkable versatility of ADPr and the distinct subcellular localization of its writers, which enable it to regulate essential processes in a spatiotemporal manner.

Item Type:	Article
Creators:	Creators Email ORCID ORCID Put Code Ribeiro, Victoria Chaves UNSPECIFIED UNSPECIFIED UNSPECIFIED Wirtz, Jessica UNSPECIFIED https://orcid.org/0009-0000-1994-1722 UNSPECIFIED Leidecker, Orsolya UNSPECIFIED https://orcid.org/0000-0001-5315-014X UNSPECIFIED
URN:	urn:nbn:de:hbz:38-801078
Identification Number:	10.1007/s12268-025-2460-6
Journal or Publication Title:	BIOspektrum
Volume:	31
Number:	3
Page Range:	pp. 258-261
Number of Pages:	4
Date:	8 May 2025
Publisher:	Springer Nature
ISSN:	0947-0867
Language:	English
Faculty:	Faculty of Mathematics and Natural Sciences
Divisions:	CECAD - Cluster of Excellence Cellular Stress Responses in Aging-Associated Diseases
Subjects:	Life sciences
['eprint_fieldname_oa_funders' not defined]:	Publikationsfonds UzK
Refereed:	Yes
URI:	http://kups.ub.uni-koeln.de/id/eprint/80107