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الصفحة 1 من عند 117 النتائج

The cytokinin requirement for cell division in cultured Nicotiana plumbaginifolia cells can be satisfied by yeast Cdc25 protein tyrosine phosphatase: implications for mechanisms of cytokinin response and plant development.

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Cultured cells of Nicotiana plumbaginifolia, when deprived of exogenous cytokinin, arrest in G2 phase prior to mitosis and then contain cyclin-dependent protein kinase (CDK) that is inactive because phosphorylated on tyrosine (Tyr). The action of cytokinin in stimulating the activation of CDK by

Potential role for purple acid phosphatase in the dephosphorylation of wall proteins in tobacco cells.

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It is not yet known whether dephosphorylation of proteins catalyzed by phosphatases occurs in the apoplastic space. In this study, we found that tobacco (Nicotiana tabacum) purple acid phosphatase could dephosphorylate the phosphoryl residues of three apoplastic proteins, two of which were

Structural studies of soybean calmodulin isoform 4 bound to the calmodulin-binding domain of tobacco mitogen-activated protein kinase phosphatase-1 provide insights into a sequential target binding mode.

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The calcium regulatory protein calmodulin (CaM) binds in a calcium-dependent manner to numerous target proteins. The calmodulin-binding domain (CaMBD) region of Nicotiana tabacum MAPK phosphatase has an amino acid sequence that does not resemble the CaMBD of any other known Ca(2+)-CaM-binding

Purification and Properties of 2-Carboxy-d-Arabinitol 1-Phosphatase.

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Carboxyarabinitol 1-phosphatase (2-carboxy-d-arabinitol 1-phosphate phosphohydrolase), a chloroplast enzyme that metabolizes the naturally occurring inhibitor of ribulose-1,5-bisphosphate carboxylase/oxygenase, was isolated from tobacco (Nicotiana tabacum) leaves. The enzyme was purified more than

Acid phosphatase activity of normal and tumor tissue of tobacco grown in vitro and in vivo.

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Tissue cultures of Nicotiana labacum consisting of green, albino and habituated (normal origin) and teratoma (tomorous origin) were grown under asceptic conditions for 6 to 8 weeks and their extracts were analyzed for phosphatase activity. Comparative enzyme analyses were also made on crude stem

Expression and purification of human phosphatase and actin regulator 1 (PHACTR1) in plant-based systems.

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Cardiovascular diseases are a prevalent cause of morbidity and mortality especially in industrialized countries. The human phosphatase and actin regulator 1 (PHACTR1) may be involved in such diseases, but its precise regulatory function remains unclear due to the large number of potential

Molecular cloning and characterization of L-galactose-1-phosphate phosphatase from tobacco (Nicotiana tabacum).

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L-Galactose-1-phosphate phosphatase (GPPase) is an enzyme involved in ascorbate biosynthesis in higher plants. We isolated a cDNA encoding GPPase from tobacco, and named it NtGPPase. The putative amino acid sequence of NtGPPase contained inositol monophosphatase motifs and metal binding sites.

Catalytic activation of the plant MAPK phosphatase NtMKP1 by its physiological substrate salicylic acid-induced protein kinase but not by calmodulins.

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MAPK phosphatases (MKPs) are negative regulators of MAPKs. Previously, we identified NtMKP1 as a novel calmodulin (CaM)-binding protein (Yamakawa, H., Katou, S., Seo, S., Mitsuhara, I., Kamada, H., and Ohashi, Y. (2004) J. Biol. Chem. 279, 928-936). In this study, we characterized the interaction of

Mitogen-activated protein kinase phosphatase 1 reduces the replication efficiency of Bamboo mosaic virus in Nicotiana benthamiana.

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In plants, the mitogen-activated protein kinase (MAPK) cascades are the central signaling pathways of the complicated defense network triggered by the perception of pathogen-associated molecular patterns to repel pathogens. The Arabidopsis thaliana MAPK phosphatase 1 (AtMKP1) negatively regulates

Phosphoglycolate phosphatase: purification and preparation of antibodies.

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Phosphoglycolate phosphatase was partially purified from leaves of Nicotiana rustica using ion exchange and chromatofocusing columns. The native molecular weight of the enzyme was determined to be about 58 kD from Ferguson plots, with a subunit size of about 32 kD. The native enzyme is thus likely

Inhibitors of Protein Phosphatases 1 and 2A Block the Sugar-Inducible Gene Expression in Plants.

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Genes coding for two major proteins of the tuberous root of sweet potato (Ipomoea batatas), namely, sporamin and [beta]-amylase, are inducible in leaves and petioles when they are supplied with high concentrations of sucrose or other metabolizable sugars, such as glucose and fructose, and the

Nuclear localization of the plant protein Ser/Thr phosphatase PP7.

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Recently we identified novel plant Ser/Thr phosphatases, termed PP7, which belong to the PPP family and have no known close homologs in other kingdoms. We now addressed the intracellular location of Arabidopsis thaliana PP7 using GFP fusions and confocal laser scanning microscopy. PP7. GFP fusion

A plant small polypeptide is a novel component of DNA-binding protein phosphatase 1-mediated resistance to plum pox virus in Arabidopsis.

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DNA-binding protein phosphatases (DBPs) have been identified as a novel class of plant-specific regulatory factors playing a role in plant-virus interactions. NtDBP1 from tobacco (Nicotiana tabacum) was shown to participate in transcriptional regulation of gene expression in response to virus

Serine/threonine protein phosphatase is required for tobacco mosaic virus-mediated programmed cell death.

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A major gap in our understanding of host response to virus infection is how the molecular signals are passed within infected cells. Tobacco mosaic virus-mediated programmed cell death in genotype NN tobaccos was used to evaluate the hypothesis that these molecular signals are transduced via

PP2C phosphatase Pic1 negatively regulates the phosphorylation status of Pti1b kinase, a regulator of flagellin-triggered immunity in tomato.

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Plant immune responses, including the production of reactive oxygen species (ROS), are triggered when pattern recognition receptors (PRRs) become activated upon detection of microbe-associated molecular patterns (MAMPs). Receptor-like cytoplasmic kinases are key components of PRR-dependent signaling

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