An uncharacterized FMAG_01619 protein from Fusobacterium mortiferum ATCC 9817 demonstrates that some bacterial macrodomains can also act as poly-ADP-ribosylhydrolases-Reference-Cited by-同舟云学术

An uncharacterized FMAG_01619 protein from Fusobacterium mortiferum ATCC 9817 demonstrates that some bacterial macrodomains can also act as poly-ADP-ribosylhydrolases

Published:2019-03-01 Issue:1 Volume:9 Page:
ISSN:2045-2322
Container-title:Scientific Reports
language:en
Short-container-title:Sci Rep

Author:

García-Saura Antonio Ginés,Zapata-Pérez Rubén,Hidalgo José Francisco,Cabanes Juana,Gil-Ortiz Fernando,Sánchez-Ferrer Álvaro^ORCID

Publisher

Springer Science and Business Media LLC

Subject

Multidisciplinary

Link

http://www.nature.com/articles/s41598-019-39691-4.pdf

Reference62 articles.

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2. Perina, D. et al. Distribution of protein poly(ADP-ribosyl)ation systems across all domains of life. DNA Repair (Amst) 23, 4–16, https://doi.org/10.1016/j.dnarep.2014.05.003 (2014).

3. Verheugd, P., Butepage, M., Eckei, L. & Luscher, B. Players in ADP-ribosylation: Readers and Erasers. Curr Protein Pept Sci 17, 654–667 (2016).

4. Moeller, G. K. & Timinszky, G. Reversing ADP-ribosylation. Elife 6, e29942, https://doi.org/10.7554/eLife.29942 (2017).

5. Palazzo, L., Mikoc, A. & Ahel, I. ADP-ribosylation: new facets of an ancient modification. The FEBS journal 284, 2932–2946, https://doi.org/10.1111/febs.14078 (2017).

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