122970-38-1Relevant articles and documents
Chain-terminating and clickable NAD+ analogues for labeling the target proteins of ADP-ribosyltransferases
Wang, Yan,Roesner, Daniel,Grzywa, Magdalena,Marx, Andreas
, p. 8159 - 8162 (2014/08/18)
ADP-ribosyltransferases (ARTs) use NAD+ as a substrate and play important roles in numerous biological processes, such as the DNA damage response and cell cycle regulation, by transferring multiple ADP-ribose units onto target proteins to form poly(ADP-ribose) (PAR) chains of variable sizes. Efforts to identify direct targets of PARylation, as well as the specific ADP-ribose acceptor sites, must all tackle the complexity of PAR. Herein, we report new NAD+ analogues that are efficiently processed by wild-type ARTs and lead to chain termination owing to a lack of the required hydroxy group, thereby significantly reducing the complexity of the protein modification. Due to the presence of an alkyne group, these NAD+ analogues allow subsequent manipulations by click chemistry for labeling with dyes or affinity markers. This study provides insight into the substrate scope of ARTs and might pave the way for the further developments of chemical tools for investigating PAR metabolism.
Novel, Stable Congeners of the Antiretroviral Compound 2',3'-Dideoxyadenosine
Nair, Vasu,Buenger, Greg S.
, p. 8502 - 8504 (2007/10/02)
Novel congeners of the antiretroviral compound 2',3'-dideoxyadenosine (ddA) have been synthesized through metal-mediated and photochemical conversions as the key steps.These compounds are inherently more stable than ddA with respect to both glycosidic bond cleavage and deamination by adenosine deaminase.