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@ARTICLE{Sandal:201303,
author = {Sandal, Massimo and Paltrinieri, Daniele and Carloni, Paolo
and Musiani, Francesco and Giorgetti, Alejandro},
title = {{S}tructure/{F}unction {R}elationships of {P}hospholipases
{C} {B}eta},
journal = {Current protein $\&$ peptide science},
volume = {14},
number = {8},
issn = {1389-2037},
address = {Hilversum},
publisher = {Bentham Science Publ.},
reportid = {FZJ-2015-03608},
pages = {650 - 657},
year = {2013},
abstract = {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},
cin = {GRS / IAS-5},
ddc = {610},
cid = {I:(DE-Juel1)GRS-20100316 / I:(DE-Juel1)IAS-5-20120330},
pnm = {899 - ohne Topic (POF2-899)},
pid = {G:(DE-HGF)POF2-899},
typ = {PUB:(DE-HGF)16 / PUB:(DE-HGF)36},
pubmed = {pmid:24384033},
UT = {WOS:000329125100002},
doi = {10.2174/13892037113146660085},
url = {https://juser.fz-juelich.de/record/201303},
}