Identification of protein phosphatase-1-binding proteins by microcystin-biotin affinity chromatography. - Wikidata - awgldk - TriplyDB

Identification of protein phosphatase-1-binding proteins by microcystin-biotin affinity chromatography.

Identification of protein phosphatase-1-binding proteins by microcystin-biotin affinity chromatography.

http://www.wikidata.org/entity/Q30469609

about

Purification and identification of a novel subunit of protein serine/threonine phosphatase 4 Growth arrest and DNA damage-inducible protein GADD34 targets protein phosphatase 1 alpha to the endoplasmic reticulum and promotes dephosphorylation of the alpha subunit of eukaryotic translation initiation factor 2 Isolation and characterization of PNUTS, a putative protein phosphatase 1 nuclear targeting subunit Positive regulation of IkappaB kinase signaling by protein serine/threonine phosphatase 2A SIPP1, a novel pre-mRNA splicing factor and interactor of protein phosphatase-1 The C-terminus of NIPP1 (nuclear inhibitor of protein phosphatase-1) contains a novel binding site for protein phosphatase-1 that is controlled by tyrosine phosphorylation and RNA binding Characterization of the interaction between DARPP-32 and protein phosphatase 1 (PP-1): DARPP-32 peptides antagonize the interaction of PP-1 with binding proteins Protein phosphatase 2A and its B56 regulatory subunit inhibit Wnt signaling in Xenopus Mutations of the serine phosphorylated in the protein phosphatase-1-binding motif in the skeletal muscle glycogen-targeting subunit Ionizing radiation activates nuclear protein phosphatase-1 by ATM-dependent dephosphorylation.Molecular biologist's guide to proteomics Rapid identification of protein phosphatase 1-binding proteins by mixed peptide sequencing and data base searching. Characterization of a novel holoenzymic form of protein phosphatase 1.Displacement affinity chromatography of protein phosphatase one (PP1) complexes.Multiple interactions within the AKAP220 signaling complex contribute to protein phosphatase 1 regulation.PNUTS, a protein phosphatase 1 (PP1) nuclear targeting subunit. Characterization of its PP1- and RNA-binding domains and regulation by phosphorylation.Deactylase inhibitors disrupt cellular complexes containing protein phosphatases and deacetylases.The regulation of glycogen synthase by protein phosphatase 1 in 3T3-L1 adipocytes. Evidence for a potential role for DARPP-32 in insulin action.A protein phosphatase-1-binding motif identified by the panning of a random peptide display library.Identification of MYPT1 and NIPP1 as subunits of protein phosphatase 1 in rat liver cytosol.Epigallocatechin-3-gallate and penta-O-galloyl-β-D-glucose inhibit protein phosphatase-1.Modulation of ion transport by direct targeting of protein phosphatase type 1 to the Na-K-Cl cotransporter.Differential inhibition and posttranslational modification of protein phosphatase 1 and 2A in MCF7 cells treated with calyculin-A, okadaic acid, and tautomycin.Inhibitory phosphorylation of PP1alpha catalytic subunit during the G(1)/S transition.Protein-tyrosine phosphatases: biological function, structural characteristics, and mechanism of catalysis.Identification and localization of myosin phosphatase in human platelets.Use of protein phosphatase inhibitors.Involvement of protein phosphatase 2A nuclear accumulation and subsequent inactivation of activator protein-1 in leptomycin B-inhibited cyclin D1 expression.Importance of a surface hydrophobic pocket on protein phosphatase-1 catalytic subunit in recognizing cellular regulators.Identification of kinase-phosphatase signaling modules composed of p70 S6 kinase-protein phosphatase 2A (PP2A) and p21-activated kinase-PP2A.Characterization of the inhibition of protein phosphatase-1 by DARPP-32 and inhibitor-2.Inhibitor-1 interaction domain that mediates the inhibition of protein phosphatase-1.Microcystin affinity purification of plant protein phosphatases: PP1C, PP5 and a regulatory A-subunit of PP2A.Neurofilament-L Is a Protein Phosphatase-1-binding Protein Associated with Neuronal Plasma Membrane and Post-synaptic Density Importance of the β12-β13 Loop in Protein Phosphatase-1 Catalytic Subunit for Inhibition by Toxins and Mammalian Protein Inhibitors Histopathological Evaluation of the Exposure by Cyanobacteria Cultive Containing [d-Leu¹]Microcystin-LR on Tadpoles

P2860

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P2860

Identification of protein phosphatase-1-binding proteins by microcystin-biotin affinity chromatography.

http://www.wikidata.org/entity/Q30469609

description

1996 nî lūn-bûn

@nan

1996 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

1996 թվականի նոյեմբերին հրատարակված գիտական հոդված

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1996年の論文

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1996年論文

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1996年論文

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1996年論文

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1996年論文

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1996年論文

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1996年论文

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name

Identification of protein phos ...... iotin affinity chromatography.

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Identification of protein phos ...... iotin affinity chromatography.

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Identification of protein phos ...... iotin affinity chromatography.

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Identification of protein phos ...... iotin affinity chromatography.

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Identification of protein phos ...... iotin affinity chromatography.

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Journal of Biological Chemistry

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Identification of protein phos ...... iotin affinity chromatography.

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Alms G

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P2860

Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase)

Renaturation and partial peptide sequencing of mitogen-activated protein kinase (MAP kinase) activator from rabbit skeletal muscle

Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1

DARPP-32, a dopamine-regulated neuronal phosphoprotein, is a potent inhibitor of protein phosphatase-1

Protein phosphatase 1 interacts with p53BP2, a protein which binds to the tumour suppressor p53

Association of protein kinase A and protein phosphatase 2B with a common anchoring protein

Interaction of the ribosomal protein, L5, with protein phosphatase type 1

Purification of the hepatic glycogen-associated form of protein phosphatase-1 by microcystin-Sepharose affinity chromatography

Amino acid sequence and expression of the hepatic glycogen-binding (GL)-subunit of protein phosphatase-1

Molecular cloning and functional expression of a recombinant 72.5 kDa fragment of the 110 kDa regulatory subunit of smooth muscle protein phosphatase 1M

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