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| 100 | 1 | _ | |0 P:(DE-HGF)0 |a Sandal, Massimo |b 0 |
| 245 | _ | _ | |a Structure/Function Relationships of Phospholipases C Beta |
| 260 | _ | _ | |a Hilversum |b Bentham Science Publ. |c 2013 |
| 336 | 7 | _ | |a Journal Article |0 PUB:(DE-HGF)16 |2 PUB:(DE-HGF) |m journal |
| 336 | 7 | _ | |a Review |b review |m review |0 PUB:(DE-HGF)36 |s 1434006938_12153 |2 PUB:(DE-HGF) |
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| 336 | 7 | _ | |a ARTICLE |2 BibTeX |
| 520 | _ | _ | |a Phospholipases C beta (PLC-βs) are essential components of the signal transduction of metazoans. They catalyze the production of the second messengers inositol-1,4,5-trisphosphate (IP3) and diacylglycerol (DAG) from the hydrolysis of phosphatidylinositol-4,5-bisphosphate (PIP2). These enzymes are activated by G-protein-coupled receptors (GPCRs) through the interaction with the alpha subunit of heterotrimeric G-proteins belonging to the Gq family (Gαq), the Gβγ subunits released by the inhibitory G-protein (Gi) and Ca2+ ions. Here we review current structural insights on these important proteins, with a particular focus on the most structurally characterized isoform (PLC-β3) and the activation mechanism operated by Gαq. We propose, following the lead of recent studies, that a tight combination of experiments and molecular simulations are instrumental in further enlightening the structure/function understanding of PLC-βs. - See more at: http://www.eurekaselect.com/116059/article#sthash.cojH1BB1.dpuf |
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| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Paltrinieri, Daniele |b 1 |
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| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Musiani, Francesco |b 3 |e Corresponding Author |
| 700 | 1 | _ | |0 P:(DE-HGF)0 |a Giorgetti, Alejandro |b 4 |e Corresponding Author |
| 773 | _ | _ | |0 PERI:(DE-600)2044612-3 |a 10.2174/13892037113146660085 |g Vol. 14, no. 8, p. 650 - 657 |n 8 |p 650 - 657 |t Current protein & peptide science |v 14 |x 1389-2037 |y 2013 |
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