Second messenger function and the structure–activity relationship of cyclic adenosine diphosphoribose (cADPR)

@article{Guse2005SecondMF,
  title={Second messenger function and the structure–activity relationship of cyclic adenosine diphosphoribose (cADPR)},
  author={Andreas H. Guse},
  journal={The FEBS Journal},
  year={2005},
  volume={272}
}
  • A. Guse
  • Published 1 September 2005
  • Biology, Chemistry
  • The FEBS Journal
Cyclic ADP‐ribose (cADPR) is a Ca2+ mobilizing second messenger found in various cell types, tissues and organisms. Receptor‐mediated formation of cADPR may proceed via transmembrane shuttling of the substrate NAD and involvement of the ectoenzyme CD38, or via so far unidentified ADP‐ribosyl cyclases located within the cytosol or in internal membranes. cADPR activates intracellular Ca2+ release via type 2 and 3 ryanodine receptors. The exact molecular mechanism, however, remains to be… 

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TLDR
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TLDR
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Second messenger analogues highlight unexpected substrate sensitivity of CD38: total synthesis of the hybrid “L-cyclic inosine 5′-diphosphate ribose”

TLDR
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cADPR Does Not Activate TRPM2

TLDR
It is shown that the N-terminal MHR1/2 domain and the C-terminals NUDT9H domain are required for activation of human TRPM2 by ADPR and 2′-deoxy-ADPR (2dADPR), and that pure cADPR does not activate TR PM2 under a variety of conditions that have previously been shown to result in channel activation.

New Molecular Mechanisms on the Activation of TRPM2 Channels by Oxidative Stress and ADP-Ribose

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The effects of various inhibitors such as flufenamic acid and PARP inhibitors on ADPR, NAD+ and H2O2-induced TRPM2 currents are reviewed, and inhibitor roles of antioxidants are summarized.
...

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