Functional aspects of protein mono-ADP-ribosylation - Wikidata - awgldk - TriplyDB

Functional aspects of protein mono-ADP-ribosylation

Functional aspects of protein mono-ADP-ribosylation

http://www.wikidata.org/entity/Q24675892

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Identification of the proteins required for biosynthesis of diphthamide, the target of bacterial ADP-ribosylating toxins on translation elongation factor 2 2,3,7,8-Tetrachlorodibenzo-p-dioxin poly(ADP-ribose) polymerase (TiPARP, ARTD14) is a mono-ADP-ribosyltransferase and repressor of aryl hydrocarbon receptor transactivation Subcellular compartmentation and differential catalytic properties of the three human nicotinamide mononucleotide adenylyltransferase isoforms Spermatid head elongation with normal nuclear shaping requires ADP-ribosyltransferase PARP11 (ARTD11) in mice PARP16/ARTD15 is a novel endoplasmic-reticulum-associated mono-ADP-ribosyltransferase that interacts with, and modifies karyopherin-ß1 The macro domain is an ADP-ribose binding module Nuclear ADP-ribosylation reactions in mammalian cells: where are we today and where are we going?The power to reduce: pyridine nucleotides--small molecules with a multitude of functions The structure of human ADP-ribosylhydrolase 3 (ARH3) provides insights into the reversibility of protein ADP-ribosylation Regulation of poly(ADP-ribose) polymerase 1 activity by the phosphorylation state of the nuclear NAD biosynthetic enzyme NMN adenylyl transferase 1 NAD⁺-Metabolizing Ectoenzymes in Remodeling Tumor-Host Interactions: The Human Myeloma Model The nature and character of the transition state for the ADP-ribosyltransferase reaction Crystal Structure of Human ADP-ribose Transferase ARTD15/PARP16 Reveals a Novel Putative Regulatory Domain Structural and biochemical analyses of the catalysis and potency impact of inhibitor phosphoribosylation by human nicotinamide phosphoribosyltransferase Disruption of Macrodomain Protein SCO6735 Increases Antibiotic Production in Streptomyces coelicolor ADP-ribosyltransferases and poly ADP-ribosylation Single domain antibodies: promising experimental and therapeutic tools in infection and immunity Arginine ADP-ribosyltransferase 1 promotes angiogenesis in colorectal cancer via the PI3K/Akt pathway Cholera- and anthrax-like toxins are among several new ADP-ribosyltransferases The RST and PARP-like domain containing SRO protein family: analysis of protein structure, function and conservation in land plants.Evidence that mono-ADP-ribosylation of CtBP1/BARS regulates lipid storage.Identification of two regulatory binding sites which confer myotube specific expression of the mono-ADP-ribosyltransferase ART1 gene.ADP-ribosylation of arginine.Compartmentation of NAD+-dependent signalling.A role of intracellular mono-ADP-ribosylation in cancer biology.Quantitative analysis of cellular metabolic dissipative, self-organized structures SpyA, a C3-like ADP-ribosyltransferase, contributes to virulence in a mouse subcutaneous model of Streptococcus pyogenes infection.The natural history of ADP-ribosyltransferases and the ADP-ribosylation system.Nicotinamide Phosphoribosyltransferase in Human Diseases.The Neisseria meningitidis ADP-Ribosyltransferase NarE Enters Human Epithelial Cells and Disrupts Epithelial Monolayer Integrity.A Catalog of Proteins Expressed in the AG Secreted Fluid during the Mature Phase of the Chinese Mitten Crabs (Eriocheir sinensis).SpyA is a membrane-bound ADP-ribosyltransferase of Streptococcus pyogenes which modifies a streptococcal peptide, SpyB.A Review of Tandem Mass Spectrometry Characterization of Adenosine Diphosphate-Ribosylated Peptides.ADP-ribosylhydrolase 3 (ARH3), not poly(ADP-ribose) glycohydrolase (PARG) isoforms, is responsible for degradation of mitochondrial matrix-associated poly(ADP-ribose).ADP-ribosylarginine hydrolase regulates cell proliferation and tumorigenesis Pathogen virulence factors as molecular probes of basic plant cellular functions.Polyvalent Proteins, a Pervasive Theme in the Intergenomic Biological Conflicts of Bacteriophages and Conjugative Elements.ADP-ribosylation of membrane proteins: unveiling the secrets of a crucial regulatory mechanism in mammalian cells.Mutations of the functional ARH1 allele in tumors from ARH1 heterozygous mice and cells affect ARH1 catalytic activity, cell proliferation and tumorigenesis.Identification of ADP-ribosylation sites of CD38 mutants by precursor ion scanning mass spectrometry

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P2860

Functional aspects of protein mono-ADP-ribosylation

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2003 nî lūn-bûn

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2003 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2003 թվականի մայիսին հրատարակված գիտական հոդված

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2003年の論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年論文

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2003年论文

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name

Functional aspects of protein mono-ADP-ribosylation

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Functional aspects of protein mono-ADP-ribosylation

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Functional aspects of protein mono-ADP-ribosylation

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type

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Functional aspects of protein mono-ADP-ribosylation

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Functional aspects of protein mono-ADP-ribosylation

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Functional aspects of protein mono-ADP-ribosylation

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Functional aspects of protein mono-ADP-ribosylation

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Functional aspects of protein mono-ADP-ribosylation

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Functional aspects of protein mono-ADP-ribosylation

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The EMBO Journal

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Functional aspects of protein mono-ADP-ribosylation

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Maria Di Girolamo

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P2860

Initial sequencing and analysis of the human genome

Characterization of five human cDNAs with homology to the yeast SIR2 gene: Sir2-like proteins (sirtuins) metabolize NAD and may have protein ADP-ribosyltransferase activity

The family of toxin-related ecto-ADP-ribosyltransferases in humans and the mouse

Silent information regulator 2 family of NAD- dependent histone/protein deacetylases generates a unique product, 1-O-acetyl-ADP-ribose

Phylogenetic classification of prokaryotic and eukaryotic Sir2-like proteins

Conserved enzymatic production and biological effect of O-acetyl-ADP-ribose by silent information regulator 2-like NAD+-dependent deacetylases

Mono-ADP-ribosylation: a tool for modulating immune response and cell signaling

Molecular and immunological characterization of ADP-ribosylarginine hydrolases

An enzymatic activity in the yeast Sir2 protein that is essential for gene silencing

Characterization of glycosylphosphatidylinositiol-anchored, secreted, and intracellular vertebrate mono-ADP-ribosyltransferases.

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1953-1958

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scholarly article

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3521586

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10.1093/EMBOJ/CDG209

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9

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22

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2003-05-01T00:00:00Z

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12727863

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156081

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