A ribose-functionalized NAD+ with unexpected high activity and selectivity for protein poly-ADP-ribosylation
The study of NAD+ dependent ADP-ribosylation can be challenging. Here the authors report on the development of NAD+ analogues, using chemo-enzymatic methods, which can be used as probes to label the substrate proteins of poly-ADP-ribose polymerase.
Saved in:
Main Authors: | Xiao-Nan Zhang, Qinqin Cheng, Jingwen Chen, Albert T. Lam, Yanran Lu, Zhefu Dai, Hua Pei, Nikolai M. Evdokimov, Stan G. Louie, Yong Zhang |
---|---|
Format: | article |
Language: | EN |
Published: |
Nature Portfolio
2019
|
Subjects: | |
Online Access: | https://doaj.org/article/99a2c69f536344e0816740d2ed77a8f6 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
Selective monitoring of the protein-free ADP-ribose released by ADP-ribosylation reversal enzymes.
by: Samuel Kasson, et al.
Published: (2021) -
Mechanistic insights into the three steps of poly(ADP-ribosylation) reversal
by: Johannes Gregor Matthias Rack, et al.
Published: (2021) -
PARP2 mediates branched poly ADP-ribosylation in response to DNA damage
by: Qian Chen, et al.
Published: (2018) -
Structural and biochemical evidence supporting poly ADP-ribosylation in the bacterium Deinococcus radiodurans
by: Chao-Cheng Cho, et al.
Published: (2019) -
Poly(ADP-ribose) polymerase 1 accelerates vascular calcification by upregulating Runx2
by: Cheng Wang, et al.
Published: (2019)