A New Nanobody-Based Biosensor to Study Endogenous PARP1 In Vitro and in Live Human Cells

Author:

Buchfellner Andrea,Yurlova Larisa,Nüske Stefan,Scholz Armin M.,Bogner Jacqueline,Ruf Benjamin,Zolghadr Kourosh,Drexler Sophie E.,Drexler Guido A.,Girst Stefanie,Greubel Christoph,Reindl Judith,Siebenwirth Christian,Romer Tina,Friedl Anna A.,Rothbauer Ulrich

Publisher

Public Library of Science (PLoS)

Subject

Multidisciplinary

Reference67 articles.

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2. Domain C of human poly(ADP-ribose) polymerase-1 is important for enzyme activity and contains a novel zinc-ribbon motif;Z Tao;Biochemistry,2008

3. Poly (ADP-Ribose) synthetase. Separation and identification of three proteolytic fragments as the substrate-binding domain, the DNA-binding domain, and the automodification domain;I Kameshita;The Journal of biological chemistry,1984

4. Poly(ADP-ribose) polymerase: a molecular nick-sensor;G de Murcia;Trends in biochemical sciences,1994

5. PARP1-dependent kinetics of recruitment of MRE11 and NBS1 proteins to multiple DNA damage sites;JF Haince;The Journal of biological chemistry,2008

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