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retinoblastoma/phosphatase
Линкът е запазен в клипборда
Страница 1 от 302 резултата
The B″ regulatory subunit of protein phosphatase 2A mediates the dephosphorylation of rice retinoblastoma-related protein-1.
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The phosphorylation of plant retinoblastoma-related (RBR) proteins by cyclin-dependent kinases (CDKs) is well documented, but the counteracting phosphatases have not been identified yet. We report here that rice retinoblastoma-related protein-1 (OsRBR1) interacted with the B″ subunit of rice protein
Inhibition of histone H1 kinase expression, retinoblastoma protein phosphorylation, and cell proliferation by the phosphatase inhibitor okadaic acid.
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Phosphorylation events are major regulatory mechanisms of signal transduction pathways that regulate gene expression and cell growth. To study the potential involvement of serine-threonine specific phosphatases in these processes we used okadaic acid (OA), an inhibitor of type 1 and type 2A protein
Protein phosphatase type 1-dependent dephosphorylation of the retinoblastoma tumor suppressor protein in ultraviolet-irradiated human skin and keratinocytes.
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This study provides evidence for the involvement of a type 1 protein serine/threonine phosphatase in the ultraviolet radiation-induced dephosphorylation of retinoblastoma tumor suppressor protein in human skin and cultured keratinocytes. The retinoblastoma gene product was localized to the nuclei
Fas-mediated apoptosis in T cells involves the dephosphorylation of the retinoblastoma protein by type 1 protein phosphatases.
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Apoptosis is triggered by a number of different stimuli including the activation of Fas antigen, a member of the TNF family, by the Fas ligand. The signal transduction events implicated in apoptosis are complex and remain only partially understood. In this study, we used calyculin A, a potent
Interaction between the retinoblastoma protein and protein phosphatase 1 during the cell cycle.
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The functions of the retinoblastoma protein (pRb) are in part regulated by reversible and cell cycle-dependent phosphorylation. While the regulation of pRb by cyclin-dependent kinases (Cdks) has been studied extensively, the role(s) of protein phosphatase 1 (PP1) in controlling pRb are only
Protein Phosphatase 1 binds strongly to the retinoblastoma protein but not to p107 or p130 in vitro and in vivo.
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OBJECTIVE
To identify and characterize retinoblastoma protein (pRb) binding proteins that may influence retinoblast proliferation and retinal pigment epithelial cell survival.
METHODS
The yeast two-hybrid system was used to screen a bovine retinal cDNA library and to characterize positive clones.
Functional interaction between a novel protein phosphatase 2A regulatory subunit, PR59, and the retinoblastoma-related p107 protein.
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The proteins of the retinoblastoma family are potent inhibitors of cell cycle progression. It is well documented that their growth-inhibitory activity can be abolished by phosphorylation on serine and threonine residues by cyclin dependent kinases. In contrast, very little is known about the
Protein phosphatase-1 activation and association with the retinoblastoma protein in colcemid-induced apoptosis.
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Protein phosphatase-1 (PP1) is cell cycle regulated and potentially related to apoptosis. We studied PP1 in HeLa cells exposed to colcemid, which leads first to mitotic block, then to cell death within 72 h. The soluble PP1 activity, which was low at 14 h (mitosis), was then reversibly activated
Binding of phosphatase-1 delta to the retinoblastoma protein pRb involves domains that include substrate recognition residues and a pRB binding motif.
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Protein Ser/Thr phosphatase-1 (PP1) controls the retinoblastoma protein (pRb) function, including its dephosphorylation at mitotic exit. Since PP1delta was found to coimmunoprecipitate with pRb from mitotic and early G1 cells, we further investigated the PP1delta-pRb association using GST-full
Protein phosphatase 1alpha-mediated stimulation of apoptosis is associated with dephosphorylation of the retinoblastoma protein.
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Protein phosphatase 1 (PP1) plays important roles in many different aspects of cellular activities including cell cycle control. One important function of PP1 is to activate the retinoblastoma protein pRB. Here we show that pRB is one of PP1's downstream targets during apoptosis. When HL-60 cells
PNUTS (phosphatase nuclear targeting subunit) inhibits retinoblastoma-directed PP1 activity.
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Protein phosphatase type 1 catalytic subunit (PP1c) is a serine/threonine phosphatase involved in the dephosphorylation of many proteins in eukaryotic cells. It associates with several known targeting or regulatory subunits that directly regulate PP1c activity toward specific substrates. The
Induction of a retinoblastoma phosphatase activity by anticancer drugs accompanies p53-independent G1 arrest and apoptosis.
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DNA-damaging agents induce accumulation of the tumor suppressor and G1 checkpoint protein p53, leading cells to either growth arrest in G1 or apoptosis (programmed cell death). The p53-dependent G1 arrest involves induction of p21 (also called WAF1/CIP1/SDI1), which prevents cyclin kinase-mediated
Expression of CDC25A and CDC25B phosphatase proteins in human retinoblastoma and its correlation with clinicopathological parameters.
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BACKGROUND
CDC25 proteins play a pivotal role in controlling cell proliferation during development and tumorigenesis. The aim of the study is to elucidate the role of CDC25A and CDC25B proteins in retinoblastoma and their association with the clinical and histopathological parameters.
METHODS
One
Myosin phosphatase interacts with and dephosphorylates the retinoblastoma protein in THP-1 leukemic cells: its inhibition is involved in the attenuation of daunorubicin-induced cell death by calyculin-A.
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Reversible phosphorylation of the retinoblastoma protein (pRb) is an important regulatory mechanism in cell cycle progression. The role of protein phosphatases is less understood in this process, especially concerning the regulatory/targeting subunits involved. It is shown that pretreatment of THP-1
PP1 and PP2A phosphatases--cooperating partners in modulating retinoblastoma protein activation.
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The retinoblastoma/pocket protein family is one of the master regulators of the eukaryotic cell cycle. It includes the retinoblastoma protein (Rb) and the related p107 and p130 proteins. The importance of the Rb pathway for homeostasis and tumour suppression is evident from the fact that
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