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FEBS Letters|December 10, 1990
Ca2(+)-mobilising properties of synthetic fluoro-analogues of myo-inositol 1,4,5-trisphosphate and their interaction with myo-inositol 1,4,5-trisphosphate 3-kinase and 5-phosphataseS T Safrany, D Sawyer, R J Wojcikiewicz, et al.
European Journal of Pharmacology|July 1, 1992
3-position modification of myo-inositol 1,4,5-trisphosphate: consequences for intracellular Ca2+ mobilisation and enzyme recognitionS T Safrany, R A Wilcox, C Liu, et al.
Progress in Neuro-Psychopharmacology & Biological Psychiatry|May 1, 1992
Muscarinic receptors, phosphoinositide metabolism and intracellular calcium in neuronal cellsD G Lambert, R J Wojcikiewicz, S T Safrany, et al.
Biochemical Society Transactions|October 26, 2005
The regulation of membrane to cytosol partitioning of signalling proteins by phosphoinositides and their soluble headgroupsC P Downes, A Gray, A Fairservice, et al.
Molecular Pharmacology|April 1, 1993
Identification of partial agonists with low intrinsic activity at the inositol-1,4,5-trisphosphate receptorS T Safrany, R A Wilcox, C Liu, et al.
European Journal of Biochemistry|July 1, 1994
Modification at C2 of myo-inositol 1,4,5-trisphosphate produces inositol trisphosphates and tetrakisphosphates with potent biological activitiesR A Wilcox, S T Safrany, D Lampe, et al.
Molecular Pharmacology|June 1, 1991
Synthetic phosphorothioate-containing analogues of inositol 1,4,5-trisphosphate mobilize intracellular Ca2+ stores and interact differentially with inositol 1,4,5-trisphosphate 5-phosphatase and 3-kinaseS T Safrany, R J Wojcikiewicz, J Strupish, et al.
Biochemistry|September 6, 1994
Design of potent and selective inhibitors of myo-inositol 1,4,5-trisphosphate 5-phosphataseS T Safrany, S J Mills, C Liu, et al.
The EMBO Journal|November 21, 1998
A novel context for the 'MutT' module, a guardian of cell integrity, in a diphosphoinositol polyphosphate phosphohydrolaseS T Safrany, J J Caffrey, X Yang, et al.
The Journal of Biological Chemistry|July 27, 1999
The diadenosine hexaphosphate hydrolases from Schizosaccharomyces pombe and Saccharomyces cerevisiae are homologues of the human diphosphoinositol polyphosphate phosphohydrolase. Overlapping substrate specificities in a MutT-type proteinS T Safrany, S W Ingram, J L Cartwright, et al.
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