Results 201 to 210 of about 19,927,495 (255)

Mammalian Phospholipase C

Annual Review of Physiology, 2013
Phospholipase C (PLC) converts phosphatidylinositol 4,5-bisphosphate (PIP2) to inositol 1,4,5-trisphosphate (IP3) and diacylglycerol (DAG). DAG and IP3 each control diverse cellular processes and are also substrates for synthesis of other important signaling molecules. PLC is thus central to many important interlocking regulatory networks.
Elliott M. Ross, Ganesh Kadamur
openaire   +4 more sources

Phospholipase C

Advances in Experimental Medicine and Biology, 2012
Phospholipase C (PLC) family members constitute a family of diverse enzymes. Thirteen different family members have been cloned. These family members have unique structures that mediate diverse functions. Although PLC family members all appear to signal through the bi-products of cleaving phospholipids, it is clear that each family member, and at times
C. Vines
openaire   +3 more sources

Primary phospholipase C and brain disorders

Advances in Biological Regulation, 2016
In the brain, the primary phospholipase C (PLC) proteins, PLCβ, and PLCγ, are activated primarily by neurotransmitters, neurotrophic factors, and hormones through G protein-coupled receptors (GPCRs) and receptor tyrosine kinases (RTKs). Among the primary PLC isozymes, PLCβ1, PLCβ4, and PLCγ1 are highly expressed and differentially distributed ...
Yang, Yong Ryoul   +6 more
openaire   +5 more sources

The physiological roles of primary phospholipase C

Advances in Biological Regulation, 2013
The roles of phosphoinositide-specific phospholipase C (PLC) have been extensively investigated in diverse cell lines and pathological conditions. Among the PLC isozmes, primary PLCs, PLC-β and PLC-γ, are directly activated by receptor activation, unlike other secondary PLCs (PLC-ɛ, PLC-δ1, and PLC-η1).
Yang YR   +3 more
openaire   +5 more sources

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