| Name | protein phosphatase 1 (protein family or complex) |
|---|---|
| Synonyms | PPP1; Protein phosphatase 1 |
| Name | cypermethrin |
|---|---|
| CAS | cyano(3-phenoxyphenyl)methyl 3-(2,2-dichloroethenyl)-2,2-dimethylcyclopropanecarboxylate |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 10936494 | Thompson TL, Moore CC, Smith B: priming modulates autoreceptor-mediated potentiation of uptake. Eur J Pharmacol. 2000 Aug 11;401(3):357-63. Pretreatment with protein phosphatase 2B (deltamethrin, cypermethrin) or protein phosphatase 1 (tautomycin) inhibitors attenuated basal and quinpirole-potentiated uptake in ovariectomized but not -primed tissue. |
0(0,0,0,0) | Details |
| 17981404 | Moreno-Delgado D, Blanco I, Ortiz J: Phosphatases regulate synthesis in rat brain. . Neuroscience. 2007 Dec 12;150(3):616-24. Epub 2007 Sep 21. In this work we show that the protein phosphatase 2A (PP2A)/protein phosphatase 1 (PP1) inhibitor okadaic acid increases synthesis up to twofold in rat cortical miniprisms containing histaminergic nerve endings. Other phosphatase inhibitors like endothall (PP2A), cypermethrin and cyclosporin A (protein phosphatase 2B, PP2B) had much lower effects. |
1(0,0,0,1) | Details |
| 11341974 | Siddiqui RA, Jenski LJ, Neff K, Harvey K, Kovacs RJ, Stillwell W: induces apoptosis in Jurkat cells by a protein phosphatase-mediated process. Biochim Biophys Acta. 2001 Jan 15;1499(3):265-75. DHA-induced apoptosis was effectively inhibited by tautomycin and cypermethrin at concentrations that affect protein phosphatase 1 (PP1) and protein phosphatase 2B (PP2B) activities, respectively, implying a role for these phosphatases in the apoptotic pathway. |
31(0,1,1,1) | Details |
| 16139540 | Shin DS, Wilkie MP, Pamenter ME, Buck LT: and protein phosphatase 1/2A attenuate N-methyl-D-aspartate receptor activity in the anoxic turtle cortex. Comp Biochem Physiol A Mol Integr Physiol. 2005 Sep;142(1):50-7. However, cypermethrin, an inhibitor of the Ca (2+)/calmodulin-dependent PP2B (calcineurin), abolished the anoxic decrease in NMDAR activity at 20, but not 40 min suggesting that this phosphatase might play an early role in attenuating NMDAR activity during anoxia. |
1(0,0,0,1) | Details |
| 10913127 | Mercado A, Song L, Vazquez N, Mount DB, Gamba G: Functional comparison of the K+-Cl- cotransporters KCC1 and KCC4. . J Biol Chem. 2000 Sep 29;275(39):30326-34. Although KCC4 is consistently more volume-sensitive, the hypotonic activation of both isoforms is critically dependent on protein phosphatase 1. |
1(0,0,0,1) | Details |