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Downregulation of the expression of DUSP1 or protein phosphatase 1 led to a decline in the beta2adrenergic receptormediated dephosphorylation of ERK1/2
human plasma protects against endothelial cell apoptosis through sustained BAD phosphorylation, which is achieved by, at least in part, a novel interaction between PP1 (show PPA1 Proteins) with PAI1 (show SERPINE1 Proteins).
Data show that protein phosphatase-1 (show PPP1CB Proteins) alpha (PP1alpha) is required to maintain checkpoint kinase 1 (CHK1 (show CHEK1 Proteins)) in a dephosphorylated state and for the accelerated replication fork progression in Spi1 (show SPI1 Proteins)/PU.1 transcription factor-overexpressing cells.
Data suggest that protein phosphatase 1 (show PPP1CB Proteins), catalytic subunit, alpha isoform (PPP1CA) is a candidate sero-diagnostic and prognostic marker for badder cancer (BC).
Rif1 (show INSL6 Proteins) can mediate MCM dephosphorylation at replication forks and that the stability of dephosphorylated replisomes strongly depends on Chk1 (show CHEK1 Proteins) activity.
Data, including data from studies using cells from knockout mice, suggest that gasotransmitter H(2)S up-regulates eIF2a (show EIF2S1 Proteins) phosphorylation by inhibiting PPP1CA via persulfidation, which in turn leads to transient suppression of global translation and activation of Atf4 (show ATF4 Proteins) expression. (eIF2a (show EIF2S1 Proteins) = eukaryotic initiation factor-2alpha (show EIF2S1 Proteins); PPP1CA = protein phosphatase 1 catalytic subunit alpha; Atf4 (show ATF4 Proteins) = activating transcription factor 4 (show ATF4 Proteins))
Protein phosphatase 1 (show PPP1CB Proteins) (PP1 (show PPA1 Proteins)) forms stable complexes with PP1 (show PPA1 Proteins)-interacting proteins (PIPs (show GPRASP1 Proteins)) that guide the phosphatase throughout its life cycle and control its fate and function.
The authors found that RNA recognition motif 1 (RRM1) in SRSF1 binds PP1 and represses its catalytic function through an allosteric mechanism.
this study shows a pivotal role for PP1 (show PPA1 Proteins) in impeding IRF7 (show IRF7 Proteins)-mediated IFN-alpha (show IFNA Proteins) production in host immune responses
The data support a model where Cdc7 (show CDC7 Proteins) (de)phosphorylation is the molecular switch for the activation and inactivation of DNA replication in mitosis, directly connecting Cdc7 (show CDC7 Proteins) and PP1a/Cdk1 (show CDK1 Proteins) to the regulation of once-per-cell cycle DNA replication in mammalian cells.
Data, including data from studies using transgenic/knockout mice, suggest that Ppp1ca and Gnb1 (show GNB1 Proteins) interact in quiescent platelets; then, Ppp1ca and Plcb3 (show PLCB3 Proteins) interact during platelet aggregation; thus, Gnb1 (show GNB1 Proteins) enlists Ppp1ca to modulate G protein-coupled receptor (show GPR34 Proteins) signaling. (Ppp1ca = protein phosphatase 1 (show PPP1CB Proteins), catalytic subunit alpha; Gnb1 (show GNB1 Proteins) = guanine nucleotide-binding protein (show TRIM23 Proteins), subunit beta-1; Plcb3 (show PLCB3 Proteins) = phospholipase C (show PLC Proteins), subunit beta-3)
Ang IV functions via regulating the activity of PP1
Cell surface expression of the major amyloid-beta peptide (Abeta (show APP Proteins))-degrading enzyme, neprilysin (show MME Proteins), depends on phosphorylation by mitogen-activated protein kinase (show MAPK1 Proteins)/extracellular signal-regulated kinase kinase (MEK (show MDK Proteins)) and dephosphorylation by protein phosphatase 1a (show PPM1A Proteins).
analysis of selective regulation of NR2B (show GRIN2B Proteins) by protein phosphatase-1 (show PPP1CB Proteins) for the control of the NMDA receptor in neuroprotection
alteration of lipid rafts is an early event in the apoptotic cascade indirectly induced by interleukin-4 (show IL4 Proteins) deprivation via PP1alpha activation, dephosphorylation of cytoplasmic Bad, and caspase (show CASP3 Proteins) activation
Data show that Nck (show NCK1 Proteins) (isoforms 1 and 2) as a component of the CReP (show PPP1R15B Proteins)/PP1c holophosphatase complex contributes to maintain eIF2alpha (show EIF2A Proteins) in a hypophosphorylated state, and modulates translation and eIF2alpha (show EIF2A Proteins) signaling in response to ER stress.
Our system may be useful for the elucidation of the mechanism of morphological maturation of neuronal cells such as dorsal root ganglion neurons that express SREC-I (show SCARF1 Proteins) during early development.
Ppp1ca was identified in the study.
overexpression of two out of five PPP1CA alternative spliced variants reduced tumor cell growth and the downregulation of the protein to hemizygosity increased the anchorage-independent growth
Results demonstrate myofilament regulation by protein phosphatase type 1 alpha and CapZ (show CAPZA1 Proteins), and support the concept that cardiac Z-discs are vital components in intracellular signalling.
The protein encoded by this gene is one of the three catalytic subunits of protein phosphatase 1 (PP1). PP1 is a serine/threonine specific protein phosphatase known to be involved in the regulation of a variety of cellular processes, such as cell division, glycogen metabolism, muscle contractility, protein synthesis, and HIV-1 viral transcription. Increased PP1 activity has been observed in the end stage of heart failure. Studies in both human and mice suggest that PP1 is an important regulator of cardiac function. Mouse studies also suggest that PP1 functions as a suppressor of learning and memory. Three alternatively spliced transcript variants encoding different isoforms have been found for this gene.
protein phosphatase 1, catalytic subunit, alpha isoform
, serine/threonine protein phosphatase PP1-alpha 1 catalytic subunit
, serine/threonine-protein phosphatase PP1-alpha catalytic subunit
, Protein phosphatase type 1 alpha, catalytic subunit
, protein phosphatase-1d
, protein phosphatase 1, catalytic subunit, alpha
, PP1 alpha
, protein phosphatase 1 alpha