25457-99-2Relevant academic research and scientific papers
Chemical Proteomics Approach for Profiling the NAD Interactome
?ileikyt?, Justina,Sundalam, Sunil,David, Larry L.,Cohen, Michael S.
supporting information, p. 6787 - 6791 (2021/05/29)
Nicotinamide adenine dinucleotide (NAD+) is a multifunctional molecule. Beyond redox metabolism, NAD+ has an equally important function as a substrate for post-translational modification enzymes, the largest family being the poly-ADP-ribose polymerases (PARPs, 17 family members in humans). The recent surprising discoveries of noncanonical NAD (NAD+/NADH)-binding proteins suggests that the NAD interactome is likely larger than previously thought; yet, broadly useful chemical tools for profiling and discovering NAD-binding proteins do not exist. Here, we describe the design, synthesis, and validation of clickable, photoaffinity labeling (PAL) probes, 2- and 6-ad-BAD, for interrogating the NAD interactome. We found that 2-ad-BAD efficiently labels PARPs in a UV-dependent manner. Chemical proteomics experiments with 2- and 6-ad-BAD identified known and unknown NAD+/NADH-binding proteins. Together, our study shows the utility of 2- and 6-ad-BAD as clickable PAL NAD probes.
HYDROXY SCHIFF BASE-OXAZOLIDINE TAUTOMERISM: APPARENT BREAKDOWN OF BALDWIN'S RULES
Astudillo, Mario E. Alva,Chokotho, Norris C. J.,Jarvis, Terence C.,Johnson, C. David,Lewis, Colin C.,McDonnell, Peter D.
, p. 5919 - 5928 (2007/10/02)
The tautomerism between hydroxy Schiff bases, X=C6H4CR=NCMe2CH2OH (R=H, Me, C6H5; X is a range of substituents) and X=C6H4CR=NC6H4(o-CH2OH), and the corresponding ring closed systems, oxazolidines and dihydrobenzoxazines, has been investigated.In all case
