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Novel 8-substituted base and sugar-modified analogues of the Ca(2+) mobilizing second messenger cyclic adenosine 5'-diphosphate ribose (cADPR) were synthesized using a chemoenzymatic approach and evaluated for activity in sea urchin egg homogenate (SUH) and in Jurkat T-lymphocytes; conformational analysis investigated by (1)H NMR spectroscopy revealed that a C2'endo/syn conformation of the "southern" ribose is crucial for agonist or antagonist activity at the SUH-, but not at the T cell-cADPR receptor.

Original publication

DOI

10.1039/c0ob00396d

Type

Journal

Org Biomol Chem

Publication Date

07/01/2011

Volume

9

Pages

278 - 290

Keywords

Animals, Aplysia, Calcium, Cyclic ADP-Ribose, Models, Molecular, Molecular Conformation, Receptors, Purinergic P1, Ribose, Sea Urchins