Results 181 to 190 of about 28,584 (233)

Patatin-domain-containing (phospho)lipases under control: Mammalian co-regulators and pathogenic activation mechanisms. [PDF]

FEBS Open Bio
Dubey N, Riegler-Berket L, Oberer M.
europepmc   +1 more source

Increased secreted PLA2 in epithelial cells promotes the progression of chronic non-atrophic gastritis to chronic atrophic gastritis through the TGF-β signaling. [PDF]

PLoS One
Hao H, An Y, Liu Y, Li B, Zhang R, Hao Y, Pan Y, Li N, Kang J.   +8 more
europepmc   +1 more source

Cytosolic phospholipase A2 links tau pathology to insulin signaling impairment in Alzheimer's disease. [PDF]

Front Aging Neurosci
Hossen F, Hung J, Odeh H, Sun GY, Lee JC.   +4 more
europepmc   +1 more source

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Phospholipase A2 receptor: a regulator of biological functions of secretory phospholipase A2

Prostaglandins & Other Lipid Mediators, 2002
The phospholipase A2 receptor (PLA2R) is a type I transmembrane glycoprotein related to the C-type animal lectin family that includes the mannose receptor. PLA2R regulates a variety of biological responses elicited by specific types of secretory PLA2s (sPLA2s).
Kohji, Hanasaki, Hitoshi, Arita
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Structure and function of phospholipase A2 receptor

Progress in Lipid Research, 1995
Phospholipase A2 (EC 3.1.1.4: PLA2) is the group name of enzymes that cleave an acyl ester bond at the sn-2 position of glycerophospholipid (1). Mammalian PLA2s are classified into two types, secretory 14 kDa PLA2 and cytosolic higher molecular weight of PLA2 (2).
O, Ohara, J, Ishizaki, H, Arita
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Inactivation and solubilization of opiate receptors by phospholipases A2

Biochimica et Biophysica Acta (BBA) - Biomembranes, 1982
(1) As previously shown, stereospecific binding of opiates to membrane bound receptors is inhibited by treatment with small amounts of phospholipase A2 from Vipera russelli. This effect is quantified and compared with the enzymes from the venoms of Naja Naja siamensis, Apis Mellifica and from porcine pancreas. All enzymes are equally effective.
U T, Rüegg, S, Cuénoud, B W, Fulpius, E J, Simon   +3 more
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Receptors for a growing family of secreted phospholipases A2

Trends in Pharmacological Sciences, 1999
Phospholipases A2 (PLA2s) are enzymes that catalyse the hydrolysis of the sn-2 acyl bond of glycerophospholipids to produce free fatty acids and lysophospholipids. Numerous intracellular and secreted PLA2s (sPLA2s) have now been characterized. Because PLA2 products are important for cell signalling and the biosynthesis of biologically active lipids ...
G, Lambeau, M, Lazdunski
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Inhibitory mechanism of opioid binding to receptor by phospholipase A2

General Pharmacology: The Vascular System, 1988
1. The inhibition of [3H]naloxone binding to the opioid receptor upon short-term incubation with phospholipase A2 (Plase A2) was abolished by treatment with BSA, but not after long-term incubation. 2. In contrast to the restorative effect of BSA on the strong inhibition occurring with Plase A2, BSA only partially abolished the inhibitory effect of ...
M, Makimura, Y, Ito, Y, Murakoshi
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Properties of receptors for neurotoxic phospholipases A2 in different tissues

Neurochemical Research, 1991
A radioiodinated derivative of OS2 (125I-OS2), a neurotoxic monochain phospholipase A2 isolated from taipan venom, was previously found to bind to a specific brain membrane receptor with very high affinity. 125I-OS2 is now used to identify the properties of neurotoxic phospholipase receptors in other tissues. Heart, skeletal muscle, kidney, lung, liver,
G, Lambeau, M, Lazdunski, J, Barhanin
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