Engineering Af1521 improves ADP-ribose binding and identification of ADP-ribosylated proteins
ADP-ribose binding macro domains facilitate the enrichment and detection of cellular ADP-ribosylation. Here, the authors generate an engineered macro domain with increased ADP-ribose affinity, improving the identification of ADP-ribosylated proteins by proteomics, western blot and immunofluorescence...
Main Authors: | Kathrin Nowak, Florian Rosenthal, Tobias Karlberg, Mareike Bütepage, Ann-Gerd Thorsell, Birgit Dreier, Jonas Grossmann, Jens Sobek, Ralph Imhof, Bernhard Lüscher, Herwig Schüler, Andreas Plückthun, Deena M. Leslie Pedrioli, Michael O. Hottiger |
---|---|
Format: | Article |
Language: | English |
Published: |
Nature Publishing Group
2020-10-01
|
Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-020-18981-w |
Similar Items
-
Intracellular Mono-ADP-Ribosylation in Signaling and Disease
by: Mareike Bütepage, et al.
Published: (2015-09-01) -
Selective monitoring of the protein-free ADP-ribose released by ADP-ribosylation reversal enzymes.
by: Samuel Kasson, et al.
Published: (2021-01-01) -
Synthesis, purification and characterization of small mono(ADP-ribosyl)ated molecules in the ADP-ribose elongation reaction catalyzed by poly(ADP-ribose)polymerase
by: Pacheco-Rodriguez, Gustavo
Published: (1993) -
Uncovering the Invisible: Mono-ADP-ribosylation Moved into the Spotlight
by: Ann-Katrin Hopp, et al.
Published: (2021-03-01) -
Poly(ADP)-Ribose Polymerase Activity in the Eukaryotic Mono-ADP-Ribosyl Transferase, ART2: a Dissertation
by: Morrison, Alan R.
Published: (2003)