Human p53 is inhibited by glutathionylation of cysteines present in the proximal DNA-binding domain during oxidative stress. - Wikidata - wikimedia - TriplyDB

Human p53 is inhibited by glutathionylation of cysteines present in the proximal DNA-binding domain during oxidative stress.

Human p53 is inhibited by glutathionylation of cysteines present in the proximal DNA-binding domain during oxidative stress.

http://www.wikidata.org/entity/Q36841921

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The role of glutathione S-transferase P in signaling pathways and S-glutathionylation in cancer Computational identification of a transiently open L1/S3 pocket for reactivation of mutant p53 Role of Natural Radiosensitizers and Cancer Cell Radioresistance: An Update Targeting Oncogenic Mutant p53 for Cancer Therapy Reactive Oxygen Species in Mesenchymal Stem Cell Aging: Implication to Lung Diseases Mechanisms of altered redox regulation in neurodegenerative diseases--focus on S--glutathionylation Redox control of microglial function: molecular mechanisms and functional significance Protein glutathionylation in cardiovascular diseases Regulation of signal transduction by reactive oxygen species in the cardiovascular system Redox homeostasis: the linchpin in stem cell self-renewal and differentiation Protein Oxidative Modifications: Beneficial Roles in Disease and Health Multiple functions of Nm23-H1 are regulated by oxido-reduction system Posttranslational modification of human glyoxalase 1 indicates redox-dependent regulation S-glutathionylation: from molecular mechanisms to health outcomes MAOA-a novel decision maker of apoptosis and autophagy in hormone refractory neuroendocrine prostate cancer cells.Glutathionylation of the pro-apoptotic protein p53 in Alzheimer's disease brain: implications for AD pathogenesis.Inhibition of glutathione synthesis distinctly alters mitochondrial and cytosolic redox poise Cys-141 glutathionylation of human p53: Studies using specific polyclonal antibodies in cancer samples and cell lines.The NADPH oxidases NOX4 and DUOX2 regulate cell cycle entry via a p53-dependent pathway.Redox control systems in the nucleus: mechanisms and functions.Targeted quantitation of site-specific cysteine oxidation in endogenous proteins using a differential alkylation and multiple reaction monitoring mass spectrometry approach New insights into the link between DNA damage and apoptosis.Stem cells and the impact of ROS signaling.Cysteine-mediated redox signaling: chemistry, biology, and tools for discovery Reversible and irreversible protein glutathionylation: biological and clinical aspects.Protein S-glutathiolation: redox-sensitive regulation of protein function.Corticotropin-Releasing Factor Receptor-1 Antagonism Reduces Oxidative Damage in an Alzheimer’s Disease Transgenic Mouse Model.Manganese porphyrin, MnTE-2-PyP5+, Acts as a pro-oxidant to potentiate glucocorticoid-induced apoptosis in lymphoma cells.Glutathione synthesis and its role in redox signaling.Individual interferon regulatory factor-3 thiol residues are not critical for its activation following virus infection.Metabolic regulation of oxygen and redox homeostasis by p53: lessons from evolutionary biology?A role for DNA-mediated charge transport in regulating p53: Oxidation of the DNA-bound protein from a distance.In vivo tagging and characterization of S-glutathionylated proteins by a chemoenzymatic method.Reduced glutathione: a radioprotector or a modulator of DNA-repair activity?Degradation of NF-κB, p53 and other regulatory redox-sensitive proteins by thiol-conjugating and -nitrosylating drugs in human tumor cells.Effective elimination of fludarabine-resistant CLL cells by PEITC through a redox-mediated mechanism.Cysteine S-Glutathionylation Promotes Stability and Activation of the Hippo Downstream Effector Transcriptional Co-activator with PDZ-binding Motif (TAZ).Redox regulation of multidrug resistance in cancer chemotherapy: molecular mechanisms and therapeutic opportunities Phenylethyl isothiocyanate reverses cisplatin resistance in biliary tract cancer cells via glutathionylation-dependent degradation of Mcl-1 The chemistry of cell signaling by reactive oxygen and nitrogen species and 4-hydroxynonenal.

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P2860

Human p53 is inhibited by glutathionylation of cysteines present in the proximal DNA-binding domain during oxidative stress.

http://www.wikidata.org/entity/Q36841921

description

2007 nî lūn-bûn

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2007年论文

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2007年论文

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name

Human p53 is inhibited by glut ...... omain during oxidative stress.

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type

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Human p53 is inhibited by glut ...... omain during oxidative stress.

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Human p53 is inhibited by glut ...... omain during oxidative stress.

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Human p53 is inhibited by glut ...... domain during oxidative stress

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Catalin E Doneanu

http://www.w3.org/2001/XMLSchema#string

Chinavenmeni S Velu

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Nagarajan Pattabiraman

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Suryakant K Niture

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P2860

Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations

Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide Gels

Probability-based protein identification by searching sequence databases using mass spectrometry data

Protein-sulfenic acids: diverse roles for an unlikely player in enzyme catalysis and redox regulation

p53 serine 392 phosphorylation increases after UV through induction of the assembly of the CK2.hSPT16.SSRP1 complex

Glutathionylation of two cysteine residues in paired domain regulates DNA binding activity of Pax-8

The antioxidant function of the p53 tumor suppressor

Integrating mutation data and structural analysis of the TP53 tumor-suppressor protein.

Dopamine biosynthesis is regulated by S-glutathionylation. Potential mechanism of tyrosine hydroxylast inhibition during oxidative stress.

Fluorescent photoaffinity labeling of cytochrome P450 3A4 by lapachenole: identification of modification sites by mass spectrometry.

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26

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K S Srivenugopal

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