(Q44563564)

English

Reversible inhibition of the protein phosphatase 1 by hydrogen peroxide. Potential regulation of eIF2 alpha phosphorylation in differentiated PC12 cells

scientific article published in September 2003

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scholarly article

1 reference

Europe PubMed Central

4 December 2017

Reversible inhibition of the protein phosphatase 1 by hydrogen peroxide. Potential regulation of eIF2 alpha phosphorylation in differentiated PC12 cells (English)

1 reference

Europe PubMed Central

4 December 2017

phosphorylation

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based on heuristic

inferred from title

1

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Europe PubMed Central

4 December 2017

author name string

Pérez-Morgado MI

2

1 reference

Europe PubMed Central

4 December 2017

Salinas M

3

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Europe PubMed Central

4 December 2017

Martín ME

4

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Europe PubMed Central

4 December 2017

language of work or name

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publication date

1 September 2003

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Europe PubMed Central

4 December 2017

Archives of Biochemistry and Biophysics

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Europe PubMed Central

4 December 2017

417

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Europe PubMed Central

4 December 2017

2

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Europe PubMed Central

4 December 2017

194-202

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Europe PubMed Central

4 December 2017

Reactive oxygen species and the central nervous system

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Role of oxidants in ischemic brain damage

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Measurement of striatal H2O2 by microdialysis following global forebrain ischemia and reperfusion in the rat: correlation with the cytotoxic potential of H2O2 in vitro

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Redox regulation of cellular signalling

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Novel protein serine/threonine phosphatases: variety is the spice of life

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Sensing electrons: protein phosphatase redox regulation

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Oxygen radicals and signaling

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Characterization of Calcineurin in Human Neutrophils

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Redox regulation of calcineurin in T-lymphocytes

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Inactivation of calcineurin by hydrogen peroxide and phenylarsine oxide. Evidence for a dithiol-disulfide equilibrium and implications for redox regulation

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Differential susceptibilities of serine/threonine phosphatases to oxidative and nitrosative stress.

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Acidosis potentiates oxidative neuronal death by multiple mechanisms

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Phosphorylation of the alpha subunit of initiation factor 2 correlates with the inhibition of translation following transient cerebral ischaemia in the rat.

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Changes in the phosphorylation of initiation factor eIF-2alpha, elongation factor eEF-2 and p70 S6 kinase after transient focal cerebral ischaemia in mice.

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Activity of protein phosphatases against initiation factor-2 and elongation factor-2.

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Type 1 phosphatase inhibitors reduce the restoration of guanine nucleotide exchange activity of eukaryotic initiation factor 2B inhibited reticulocyte lysates rescued by hemin

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The gamma(1)34.5 protein of herpes simplex virus 1 complexes with protein phosphatase 1alpha to dephosphorylate the alpha subunit of the eukaryotic translation initiation factor 2 and preclude the shutoff of protein synthesis by double-stranded RNA-

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Ischemia-induced phosphorylation of initiation factor 2 in differentiated PC12 cells: role for initiation factor 2 phosphatase

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Neuromagnetic localization of N15, the initial cortical response to lip stimulus

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Increased activity of eukaryotic initiation factor 2B in PC12 cells in response to differentiation by nerve growth factor

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A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding

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Cellular mechanisms regulating protein phosphatase-1. A key functional interaction between inhibitor-2 and the type 1 protein phosphatase catalytic subunit

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Fostriecin, an antitumor antibiotic with inhibitory activity against serine/threonine protein phosphatases types 1 (PP1) and 2A (PP2A), is highly selective for PP2A.

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Protein phosphatase type 1, the product of the retinoblastoma susceptibility gene, and cell cycle control

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Combinatorial control of protein phosphatase-1

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Cell death, calcium mobilization, and immunostaining for phosphorylated eukaryotic initiation factor 2-alpha (eIF2alpha) in neuronally differentiated NB-104 cells: arachidonate and radical-mediated injury mechanisms.

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Inhibition of protein synthesis in cortical neurons during exposure to hydrogen peroxide

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Cellular stresses profoundly inhibit protein synthesis and modulate the states of phosphorylation of multiple translation factors

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Peroxidative stress selectively down-regulates the neuronal stress response activated under conditions of endoplasmic reticulum dysfunction

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Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo

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Inhibition of PTPs by H(2)O(2) regulates the activation of distinct MAPK pathways

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Neuregulin rescues PC12-ErbB4 cells from cell death induced by H(2)O(2). Regulation of reactive oxygen species levels by phosphatidylinositol 3-kinase.

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Regulation of antioxidant enzyme expression by NGF

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Free radicals in the physiological control of cell function

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AlaArg motif in the carboxyl terminus of the gamma(1)34.5 protein of herpes simplex virus type 1 is required for the formation of a high-molecular-weight complex that dephosphorylates eIF-2alpha

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Feedback inhibition of the unfolded protein response by GADD34-mediated dephosphorylation of eIF2alpha

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Growth arrest and DNA damage-inducible protein GADD34 assembles a novel signaling complex containing protein phosphatase 1 and inhibitor 1.

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Crystal structure of the catalytic subunit of human protein phosphatase 1 and its complex with tungstate

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Activation of protein phosphatase 1. Formation of a metalloenzyme

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Superoxide dismutase protects calcineurin from inactivation.

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Calcineurin: From structure to function

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Reactivity of sulfhydryl groups of the catalytic subunits of rabbit skeletal muscle protein phosphatases 1 and 2A

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Activation of the ATP.Mg-dependent type 1 protein phosphatase by the Fe2+/ascorbate system

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The antioxidant action of N-acetylcysteine: its reaction with hydrogen peroxide, hydroxyl radical, superoxide, and hypochlorous acid

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N-acetylcysteine

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Global brain ischemia and reperfusion: modifications in eukaryotic initiation factors associated with inhibition of translation initiation.

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based on heuristic

inferred from DOI database lookup

Structure-based functional motif identifies a potential disulfide oxidoreductase active site in the serine/threonine protein phosphatase-1 subfamily

1 reference

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based on heuristic

inferred from DOI database lookup

Identifiers

10.1016/S0003-9861(03)00368-0

1 reference

Europe PubMed Central

4 December 2017

1 reference

Europe PubMed Central

4 December 2017

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