Zobrazeno 1 - 10
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pro vyhledávání: '"Irene Litosch"'
Autor:
Irene Litosch
Publikováno v:
Life Sciences. 152:99-106
Gαq signals with phospholipase C-β (PLC-β) to modify behavior in response to an agonist-bound GPCR. While the fundamental steps which prime Gαq to interact with PLC-β have been identified, questions remain concerning signal strength with PLC-β
Autor:
Irene Litosch
Publikováno v:
IUBMB Life. 65:936-940
How cells regulate Gq efficacy (initiation and termination of Gq signaling) to effect response remains a central question in pharmacology and drug discovery. Phospholipase C-β1 (PLC-β1) is an effector and a GTPase activating protein (GAP) specific
Autor:
Irene Litosch
Publikováno v:
Biochemical and Biophysical Research Communications. 417:956-960
Cellular response to G(q)-linked agonists is shaped by regulatory inputs which determine signal strength and duration. Stimulation of phospholipase C-β (PLC-β) lipase activity results in an increase in the levels of diacylglycerol (DAG) and activat
Autor:
Irene Litosch
Publikováno v:
Biochemical and Biophysical Research Communications. 415:215-219
Heterotrimeric G proteins have a critical role in mediating signal transduction by ligand-stimulated GPCRs. While activation of heterotrimeric G proteins is known to proceed via the G protein guanine nucleotide cycle, there is much uncertainty regard
Autor:
Irene Litosch
Publikováno v:
Biochemical and Biophysical Research Communications. 390:603-607
Phosphatidic acid (PA) is interactive with G(alpha)q-linked agonists to stimulate GPCR signaling via phospholipase C-beta(1) (PLC-beta(1)). Phorbol 12-myristate 13-acetate (PMA) increases cellular levels of PA and phospholipase D activity (PLD). This
Publikováno v:
Cellular Signalling. 21:1379-1384
Phosphatidic acid (PA), generated downstream of monomeric Rho GTPases via phospholipase D (PLD) and additionally by diacylglycerol kinases (DGK), both stimulates phospholipase C-beta(1) (PLC-beta(1)) and potentiates stimulation of PLC-beta(1) activit
Autor:
Irene Litosch
Publikováno v:
Life sciences. 137
The phosphatidylinositol-specific phospholipase C (PLC) family is known to regulate physiological response through an increase in the levels of cytosolic Ca(2+). PLC hydrolyzes phosphatidylinositol-4, 5-bisphosphate (PIP2) to inositol-1, 4, 5-trispho
Autor:
Irene Litosch
Publikováno v:
Biochemistry. 42:1618-1623
Phosphatidic acid (PA) stimulates phospholipase C-beta(1) (PLC-beta(1)) activity and promotes G protein stimulation of PLC-beta(1) activity. The isoform dependence for PA regulation of PLC-beta activity as well as the role of PA in modulating regulat
Autor:
Irene Litosch
Publikováno v:
IUBMB Life (International Union of Biochemistry and Molecular Biology: Life). 54:253-260
The receptor-regulated phospholipase C-beta (PLC-beta) signaling pathway is an important component in a network of signaling cascades that regulate cell function. PLC-beta signaling has been implicated in the regulation of cardiovascular function and
Autor:
Irene Litosch
Publikováno v:
Biochemistry. 39:7736-7743
The role of phosphatidic acid (PA) in regulating phospholipase C-beta(1) (PLC-beta(1)) activity was determined. PA promoted the binding of PLC-beta(1) to sucrose-loaded unilamellar vesicles (SLUV) containing phosphatidylcholine. PA increased enzymati