Paper
myo‐Inositol 1,4,5‐trisphosphorothioate is a potent competitive inhibitor of human erythrocyte 5‐phosphatase
Published Jan 2, 1989 · A. Cooke, S. Nahorski, B. Potter
FEBS Letters
Q1 SJR score
37
Citations
0
Influential Citations
Abstract
Abstract hidden due to publisher request; this does not indicate any issues with the research. Click the full text link above to read the abstract and view the original source.
In Vitro StudyStudy Snapshot
Myo-inositol 1,4,5-trisphosphorothioate (IPS3) is the most potent inhibitor of human erythrocyte 5-phosphatase, with a K i of 6 M and a K i of 124 M.
PopulationOlder adults (50-71 years)
Sample size24
MethodsObservational
OutcomesBody Mass Index projections
ResultsSocial networks mitigate obesity in older groups.
Sign up to use Study Snapshot
Consensus is limited without an account. Create an account or sign in to get more searches and use the Study Snapshot.
Full text analysis coming soon...
References
Myo-inositol(1,4,5)trisphosphorothioate binds to specific [3H]inositol(1,4,5)trisphosphate sites in rat cerebellum and is resistant to 5-phosphatase.
Myo-inositol(1,4,5)trisphosphorothioate binds to specific sites in rat cerebellum and is resistant to 5-phosphatase, offering potential for studying phosphoinositide-linked receptors.
1988·37citations·A. L. Willcocks et al.·European journal of pharmacology
European journal of pharmacology
Stereospecific mobilization of intracellular Ca2+ by inositol 1,4,5-triphosphate. Comparison with inositol 1,4,5-trisphosphorothioate and inositol 1,3,4-trisphosphate.
Inositol 1,4,5-triphosphate has a marked stereospecificity in mobilizing intracellular calcium, with the L isomer being less potent and efficacious, and the naturally occurring D-Ins(1,3,4)P3 being inactive in cellular calcium mobilization.
1988·70citations·J. Strupish et al.·The Biochemical journal
The Biochemical journal
Inositol phosphates: synthesis and degradation.
Inositol phosphates are metabolized by highly specific kinases and phosphatases, with complex pathways for formation and degradation.
1988·286citations·P. Majerus et al.·The Journal of biological chemistry
The Journal of biological chemistry
A stable colorimetric assay to measure toxin elevation of inorganic phosphate in bile.
The modified assay effectively measures nanomole amounts of inorganic phosphate in bile, providing a stable indicator of aberrant hepatobiliary function.
1988·21citations·M. T. Moslen et al.·Analytical biochemistry
Analytical biochemistry
DL-myo-inositol 1,4,5-trisphosphorothioate mobilizes intracellular calcium in Swiss 3T3 cells and Xenopus oocytes.
DL-myo-inositol 1,4,5-trisphosphorothioate stimulates intracellular calcium release in Swiss 3T3 cells and Xenopus oocytes, while L-myo-inositol 1,4,5-trisphosphate is inactive.
1988·44citations·Colin W. Taylor et al.·Biochemical and biophysical research communications
Biochemical and biophysical research communications
Citations
Small-Molecule Allosteric Triggers of Clostridium difficile Toxin B Auto-proteolysis as a Therapeutic Strategy.
Small-molecule allosteric triggers of Clostridium difficile toxin B auto-proteolysis can reduce inflammation and promote survival in mouse models of C. difficile infection.
2019·17citations·M. Ivarsson et al.·Cell chemical biology
Cell chemical biology
Inositol 1,4,5 trisphosphate is inactivated by a 5-phosphatase in stamen hair cells of Tradescantia
The 5-phosphatase pathway is the preferred pathway for inactivating Ins(1,4,5)P3 in Tradescantia stamen hair cells, resulting in sustained intracellular Ca2+ increase.
2001·5citations·A. Depass et al.·Planta
Planta
D-myo-Inositol 1,4,5-Trisphosphate Analogues Modified at the 3-Position Inhibit Phosphatidylinositol 3-Kinase (*)
The orientation of hydroxyl groups at the 2- and 3-positions plays a crucial role in the inhibitory action of inositol phosphate analogues on PI 3-kinase.
1995·13citations·S. Ward et al.·The Journal of Biological Chemistry
The Journal of Biological Chemistry
Design of potent and selective inhibitors of myo-inositol 1,4,5-trisphosphate 5-phosphatase.
L-chiro-inositol 1,4,6-trisphosphorothioate is the most potent and selective inhibitor of 5-phosphatase, making it the ideal tool for studying this enzyme in a broken cell or cell-free system.
1994·19citations·S. Safrany et al.·Biochemistry
Biochemistry
Inhibition of porcine brain inositol 1,3,4-trisphosphate kinase by inositol polyphosphates, other polyol phosphates, polyanions and polycations.
Inhibition by inositol 3,4,5,6-tetrakisphosphate and other compounds may restrict the synthesis of inositol 1,3,4,6-tetrakisphosphate, regulating the rate of inositol penta- and hexaki
1994·7citations·P. J. Hughes et al.·Biochimica et biophysica acta
Biochimica et biophysica acta
Modification at C2 of myo-inositol 1,4,5-trisphosphate produces inositol trisphosphates and tetrakisphosphates with potent biological activities.
Ins(1,4,5)P3 analogues show potent biological activities, including displaced [3H]Ins(1,4,5)P3 from its receptor and Ca2+ mobilization in SH-SY5Y cells, with sc-Ins(1,2,4,5)P4 being the most potent
1994·40citations·R. A. Wilcox et al.·European journal of biochemistry
European journal of biochemistry
Calcium release activity and metabolism of inositol 1,4,5-trisphosphate in T cells. Modulation by novel inositol 1,4,5-trisphosphate 5-phosphatase inhibitors.
Novel 5-phosphatase inhibitors can be used to study the complex metabolism and function of Ins(1,4,5)P3 and Ins(1,3,4,5)P4 in T cell activation and proliferation.
1994·5citations·S. Ward et al.·European journal of biochemistry
European journal of biochemistry