ADP Ribose Transferases: Enzymes that transfer the ADP-RIBOSE group of NAD or NADP to proteins or other small molecules. Transfer of ADP-ribose to water (i.e., hydrolysis) is catalyzed by the NADASES. The mono(ADP-ribose)transferases transfer a single ADP-ribose. POLY(ADP-RIBOSE) POLYMERASES transfer multiple units of ADP-ribose to protein targets, building POLY ADENOSINE DIPHOSPHATE RIBOSE in linear or branched chains.Ribose: A pentose active in biological systems usually in its D-form.Cyclic ADP-Ribose: A pyridine nucleotide that mobilizes CALCIUM. It is synthesized from nicotinamide adenine dinucleotide (NAD) by ADP RIBOSE CYCLASE.Poly(ADP-ribose) Polymerases: Enzymes that catalyze the transfer of multiple ADP-RIBOSE groups from nicotinamide-adenine dinucleotide (NAD) onto protein targets, thus building up a linear or branched homopolymer of repeating ADP-ribose units i.e., POLY ADENOSINE DIPHOSPHATE RIBOSE.Adenosine Diphosphate Ribose: An ester formed between the aldehydic carbon of RIBOSE and the terminal phosphate of ADENOSINE DIPHOSPHATE. It is produced by the hydrolysis of nicotinamide-adenine dinucleotide (NAD) by a variety of enzymes, some of which transfer an ADP-ribosyl group to target proteins.Poly Adenosine Diphosphate Ribose: A polynucleotide formed from the ADP-RIBOSE moiety of nicotinamide-adenine dinucleotide (NAD) by POLY(ADP-RIBOSE) POLYMERASES.Transferases: Transferases are enzymes transferring a group, for example, the methyl group or a glycosyl group, from one compound (generally regarded as donor) to another compound (generally regarded as acceptor). The classification is based on the scheme "donor:acceptor group transferase". (Enzyme Nomenclature, 1992) EC 2.Receptor, Muscarinic M1: A specific subtype of muscarinic receptor that has a high affinity for the drug PIRENZEPINE. It is found in the peripheral GANGLIA where it signals a variety of physiological functions such as GASTRIC ACID secretion and BRONCHOCONSTRICTION. This subtype of muscarinic receptor is also found in neuronal tissues including the CEREBRAL CORTEX and HIPPOCAMPUS where it mediates the process of MEMORY and LEARNING.ADP-ribosyl Cyclase: A membrane-bound or cytosolic enzyme that catalyzes the synthesis of CYCLIC ADP-RIBOSE (cADPR) from nicotinamide adenine dinucleotide (NAD). This enzyme generally catalyzes the hydrolysis of cADPR to ADP-RIBOSE, as well, and sometimes the synthesis of cyclic ADP-ribose 2' phosphate (2'-P-cADPR) from NADP.Glutathione Transferase: A transferase that catalyzes the addition of aliphatic, aromatic, or heterocyclic FREE RADICALS as well as EPOXIDES and arene oxides to GLUTATHIONE. Addition takes place at the SULFUR. It also catalyzes the reduction of polyol nitrate by glutathione to polyol and nitrite.Ruthenium Red: An inorganic dye used in microscopy for differential staining and as a diagnostic reagent. In research this compound is used to study changes in cytoplasmic concentrations of calcium. Ruthenium red inhibits calcium transport through membrane channels.Superior Cervical Ganglion: The largest and uppermost of the paravertebral sympathetic ganglia.Alkyl and Aryl Transferases: A somewhat heterogeneous class of enzymes that catalyze the transfer of alkyl or related groups (excluding methyl groups). EC 2.5.NAD: A coenzyme composed of ribosylnicotinamide 5'-diphosphate coupled to adenosine 5'-phosphate by pyrophosphate linkage. It is found widely in nature and is involved in numerous enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). (Dorland, 27th ed)Ribosemonophosphates: Ribose substituted in the 1-, 3-, or 5-position by a phosphoric acid moiety.Ryanodine: A methylpyrrole-carboxylate from RYANIA that disrupts the RYANODINE RECEPTOR CALCIUM RELEASE CHANNEL to modify CALCIUM release from SARCOPLASMIC RETICULUM resulting in alteration of MUSCLE CONTRACTION. It was previously used in INSECTICIDES. It is used experimentally in conjunction with THAPSIGARGIN and other inhibitors of CALCIUM ATPASE uptake of calcium into SARCOPLASMIC RETICULUM.Apoptosis: One of the mechanisms by which CELL DEATH occurs (compare with NECROSIS and AUTOPHAGOCYTOSIS). Apoptosis is the mechanism responsible for the physiological deletion of cells and appears to be intrinsically programmed. It is characterized by distinctive morphologic changes in the nucleus and cytoplasm, chromatin cleavage at regularly spaced sites, and the endonucleolytic cleavage of genomic DNA; (DNA FRAGMENTATION); at internucleosomal sites. This mode of cell death serves as a balance to mitosis in regulating the size of animal tissues and in mediating pathologic processes associated with tumor growth.Adenosine Diphosphate: Adenosine 5'-(trihydrogen diphosphate). An adenine nucleotide containing two phosphate groups esterified to the sugar moiety at the 5'-position.Ryanodine Receptor Calcium Release Channel: A tetrameric calcium release channel in the SARCOPLASMIC RETICULUM membrane of SMOOTH MUSCLE CELLS, acting oppositely to SARCOPLASMIC RETICULUM CALCIUM-TRANSPORTING ATPASES. It is important in skeletal and cardiac excitation-contraction coupling and studied by using RYANODINE. Abnormalities are implicated in CARDIAC ARRHYTHMIAS and MUSCULAR DISEASES.Transferases (Other Substituted Phosphate Groups): A class of enzymes that transfers substituted phosphate groups. EC 2.7.8.Caspase 3: A short pro-domain caspase that plays an effector role in APOPTOSIS. It is activated by INITIATOR CASPASES such as CASPASE 9. Isoforms of this protein exist due to multiple alternative splicing of its MESSENGER RNA.Caspases: A family of intracellular CYSTEINE ENDOPEPTIDASES that play a role in regulating INFLAMMATION and APOPTOSIS. They specifically cleave peptides at a CYSTEINE amino acid that follows an ASPARTIC ACID residue. Caspases are activated by proteolytic cleavage of a precursor form to yield large and small subunits that form the enzyme. Since the cleavage site within precursors matches the specificity of caspases, sequential activation of precursors by activated caspases can occur.Calcium: A basic element found in nearly all organized tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes.DNA Nucleotidylexotransferase: A non-template-directed DNA polymerase normally found in vertebrate thymus and bone marrow. It catalyzes the elongation of oligo- or polydeoxynucleotide chains and is widely used as a tool in the differential diagnosis of acute leukemias in man. EC 2.7.7.31.Enzyme Inhibitors: Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.Coenzyme A-Transferases: Enzymes which transfer coenzyme A moieties from acyl- or acetyl-CoA to various carboxylic acceptors forming a thiol ester. Enzymes in this group are instrumental in ketone body metabolism and utilization of acetoacetate in mitochondria. EC 2.8.3.Hybrid Cells: Any cell, other than a ZYGOTE, that contains elements (such as NUCLEI and CYTOPLASM) from two or more different cells, usually produced by artificial CELL FUSION.PentosephosphatesMolecular Sequence Data: Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.Kinetics: The rate dynamics in chemical or physical systems.Mitochondrial ADP, ATP Translocases: A class of nucleotide translocases found abundantly in mitochondria that function as integral components of the inner mitochondrial membrane. They facilitate the exchange of ADP and ATP between the cytosol and the mitochondria, thereby linking the subcellular compartments of ATP production to those of ATP utilization.Adenosine Triphosphate: An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.Cell Line, Tumor: A cell line derived from cultured tumor cells.Substrate Specificity: A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.Peptidyl Transferases: Acyltransferases that use AMINO ACYL TRNA as the amino acid donor in formation of a peptide bond. There are ribosomal and non-ribosomal peptidyltransferases.N-Acetylglucosaminyltransferases: Enzymes that catalyze the transfer of N-acetylglucosamine from a nucleoside diphosphate N-acetylglucosamine to an acceptor molecule which is frequently another carbohydrate. EC 2.4.1.-.Amino Acid Sequence: The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.Farnesyltranstransferase: An enzyme that catalyzes the synthesis of geranylgeranyl diphosphate from trans, trans-farnesyl diphosphate and isopentenyl diphosphate.Nucleoside Diphosphate SugarsEscherichia coli: A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.Pentoses: A class of carbohydrates that contains five carbon atoms.Nucleotidyltransferases: A class of enzymes that transfers nucleotidyl residues. EC 2.7.7.Acyltransferases: Enzymes from the transferase class that catalyze the transfer of acyl groups from donor to acceptor, forming either esters or amides. (From Enzyme Nomenclature 1992) EC 2.3.Binding Sites: The parts of a macromolecule that directly participate in its specific combination with another molecule.Adenine NucleotidesBase Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Phosphoribosyl Pyrophosphate: The key substance in the biosynthesis of histidine, tryptophan, and purine and pyrimidine nucleotides.Dinitrochlorobenzene: A skin irritant that may cause dermatitis of both primary and allergic types. Contact sensitization with DNCB has been used as a measure of cellular immunity. DNCB is also used as a reagent for the detection and determination of pyridine compounds.Galactosyltransferases: Enzymes that catalyze the transfer of galactose from a nucleoside diphosphate galactose to an acceptor molecule which is frequently another carbohydrate. EC 2.4.1.-.N-Acetylgalactosaminyltransferases: Enzymes that catalyze the transfer of N-acetylgalactosamine from a nucleoside diphosphate N-acetylgalactosamine to an acceptor molecule which is frequently another carbohydrate. EC 2.4.1.-.Models, Molecular: Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.Nucleotides: The monomeric units from which DNA or RNA polymers are constructed. They consist of a purine or pyrimidine base, a pentose sugar, and a phosphate group. (From King & Stansfield, A Dictionary of Genetics, 4th ed)Ribose-Phosphate Pyrophosphokinase: An enzyme that catalyzes the formation of phosphoribosyl pyrophosphate from ATP and ribose-5-phosphate. EC 2.7.6.1.Catalysis: The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.Pentosyltransferases: Enzymes of the transferase class that catalyze the transfer of a pentose group from one compound to another.Protein Prenylation: A post-translational modification of proteins by the attachment of an isoprenoid to the C-terminal cysteine residue. The isoprenoids used, farnesyl diphosphate or geranylgeranyl diphosphate, are derived from the same biochemical pathway that produces cholesterol.Liver: A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.Pentose Phosphate Pathway: An oxidative decarboxylation process that converts GLUCOSE-6-PHOSPHATE to D-ribose-5-phosphate via 6-phosphogluconate. The pentose product is used in the biosynthesis of NUCLEIC ACIDS. The generated energy is stored in the form of NADPH. This pathway is prominent in tissues which are active in the synthesis of FATTY ACIDS and STEROIDS.gamma-Glutamyltransferase: An enzyme, sometimes called GGT, with a key role in the synthesis and degradation of GLUTATHIONE; (GSH, a tripeptide that protects cells from many toxins). It catalyzes the transfer of the gamma-glutamyl moiety to an acceptor amino acid.Phosphotransferases: A rather large group of enzymes comprising not only those transferring phosphate but also diphosphate, nucleotidyl residues, and others. These have also been subdivided according to the acceptor group. (From Enzyme Nomenclature, 1992) EC 2.7.
(1/1266) Transcutaneous immunization with bacterial ADP-ribosylating exotoxins as antigens and adjuvants.

Transcutaneous immunization (TCI) is a new technique that uses the application of vaccine antigens in a solution on the skin to induce potent antibody responses without systemic or local toxicity. We have previously shown that cholera toxin (CT), a potent adjuvant for oral and nasal immunization, can induce both serum and mucosal immunoglobulin G (IgG) and IgA and protect against toxin-mediated mucosal disease when administered by the transcutaneous route. Additionally, CT acts as an adjuvant for coadministered antigens such as tetanus and diphtheria toxoids when applied to the skin. CT, a member of the bacterial ADP-ribosylating exotoxin (bARE) family, is most potent as an adjuvant when the A-B subunits are present and functional. We now show that TCI induces secondary antibody responses to coadministered antigens as well as to CT in response to boosting immunizations. IgG antibodies to coadministered antigens were also found in the stools and lung washes of immunized mice, suggesting that TCI may target mucosal pathogens. Mice immunized by the transcutaneous route with tetanus fragment C and CT developed anti-tetanus toxoid antibodies and were protected against systemic tetanus toxin challenge. We also show that bAREs, similarly organized as A-B subunits, as well as the B subunit of CT alone, induced antibody responses to themselves when given via TCI. Thus, TCI appears to induce potent, protective immune responses to both systemic and mucosal challenge and offers significant potential practical advantages for vaccine delivery.  (+info)

(2/1266) Pseudomonas aeruginosa exoenzyme S is a biglutamic acid ADP-ribosyltransferase.

Kinetic analysis of two mutations within Pseudomonas aeruginosa exoenzyme S (ExoS) showed that a E379D mutation inhibited expression of ADP-ribosyltransferase activity but had little effect on the expression of NAD glycohydrolase activity while a E381D mutation inhibited expression of both activities. These data identify ExoS as a biglutamic acid ADP-ribosyltransferase, where E381 is the catalytic residue and E379 contributes to the transfer of ADP-ribose to the target protein.  (+info)

(3/1266) Correlation of activity regulation and substrate recognition of the ADP-ribosyltransferase that regulates nitrogenase activity in Rhodospirillum rubrum.

In Rhodospirillum rubrum, nitrogenase activity is regulated posttranslationally through the ADP-ribosylation of dinitrogenase reductase by dinitrogenase reductase ADP-ribosyltransferase (DRAT). Several DRAT variants that are altered both in the posttranslational regulation of DRAT activity and in the ability to recognize variants of dinitrogenase reductase have been found. This correlation suggests that these two properties are biochemically connected.  (+info)

(4/1266) Lymphocyte migration through brain endothelial cell monolayers involves signaling through endothelial ICAM-1 via a rho-dependent pathway.

Lymphocyte extravasation into the brain is mediated largely by the Ig superfamily molecule ICAM-1. Several lines of evidence indicate that at the tight vascular barriers of the central nervous system (CNS), endothelial cell (EC) ICAM-1 not only acts as a docking molecule for circulating lymphocytes, but is also involved in transducing signals to the EC. In this paper, we examine the signaling pathways in brain EC following Ab ligation of endothelial ICAM-1, which mimics adhesion of lymphocytes to CNS endothelia. ICAM-1 cross-linking results in a reorganization of the endothelial actin cytoskeleton to form stress fibers and activation of the small guanosine triphosphate (GTP)-binding protein Rho. ICAM-1-stimulated tyrosine phosphorylation of the actin-associated molecule cortactin and ICAM-1-mediated, Ag/IL-2-stimulated T lymphocyte migration through EC monolayers were inhibited following pretreatment of EC with cytochalasin D. Pretreatment of EC with C3 transferase, a specific inhibitor of Rho proteins, significantly inhibited the transmonolayer migration of T lymphocytes, endothelial Rho-GTP loading, and endothelial actin reorganization, without affecting either lymphocyte adhesion to EC or cortactin phosphorylation. These data show that brain vascular EC are actively involved in facilitating T lymphocyte migration through the tight blood-brain barrier of the CNS and that this process involves ICAM-1-stimulated rearrangement of the endothelial actin cytoskeleton and functional EC Rho proteins.  (+info)

(5/1266) Pseudomonas aeruginosa exoenzyme S, a double ADP-ribosyltransferase, resembles vertebrate mono-ADP-ribosyltransferases.

Previous data indicated that Pseudomonas aeruginosa exoenzyme S (ExoS) ADP-ribosylated Ras at multiple sites. One site appeared to be Arg41, but the second site could not be localized. In this study, the sites of ADP-ribosylation of c-Ha-Ras by ExoS were directly determined. Under saturating conditions, ExoS ADP-ribosylated Ras to a stoichiometry of 2 mol of ADP-ribose incorporated per mol of Ras. Nucleotide occupancy did not influence the stoichiometry or velocity of ADP-ribosylation of Ras by ExoS. Edman degradation and mass spectrometry of V8 protease generated peptides of ADP-ribosylated Ras identified the sites of ADP-ribosylation to be Arg41 and Arg128. ExoS ADP-ribosylated the double mutant, RasR41K,R128K, to a stoichiometry of 1 mol of ADP-ribose incorporated per mol of Ras, which indicated that Ras possessed an alternative site of ADP-ribosylation. The alternative site of ADP-ribosylation on Ras was identified as Arg135, which was on the same alpha-helix as Arg128. Arg41 and Arg128 are located within two different secondary structure motifs, beta-sheet and alpha-helix, respectively, and are spatially separated within the three-dimensional structure of Ras. The fact that ExoS could ADP-ribosylate a target protein at multiple sites, along with earlier observations that ExoS could ADP-ribosylate numerous target proteins, were properties that have been attributed to several vertebrate ADP-ribosyltransferases. This prompted a detailed alignment study which showed that the catalytic domain of ExoS possessed considerably more primary amino acid homology with the vertebrate mono-ADP-ribosyltransferases than the bacterial ADP-ribosyltransferases. These data are consistent with the hypothesis that ExoS may represent an evolutionary link between bacterial and vertebrate mono-ADP-ribosyltransferases.  (+info)

(6/1266) Chemotaxin-dependent translocation of immunoreactive ADP-ribosyltransferase-1 to the surface of human neutrophil polymorphs.

mRNA from human polymorphonuclear neutrophil leucocytes (PMNs) was probed with cDNA encoding human skeletal muscle arginine-specific ADP-ribosyltransferase (ART1). A single 2.6-kb transcript was identified, which was similar in size to that observed in human skeletal muscle RNA. An 872-bp cDNA fragment, corresponding to the amino acid sequence of the processed human skeletal muscle enzyme, was generated by reverse transcription-PCR amplification of RNA from human PMNs, and was found to be identical to the ART1 cDNA derived from human skeletal muscle. ART1 was expressed as a fusion protein with glutathione S-transferase (GST) in insect cells, and antibodies were raised against the fusion protein in a rabbit. Following removal of GST immunoreactivity by immunoprecipitation, these antibodies were used to measure the abundance of immunoreactive ART1 on the surface of PMNs. Exposure of PMNs to formyl-Met-Leu-Phe (FMLP) was followed by a rapid increase in the abundance of cell surface ART1 (T1/2 = 1.9 min), and the concentration of FMLP for half-maximum response was 28.6 nM. Similar responses were observed after exposure of the cells to platelet-activating factor or interleukin-8, and we conclude that some of the effects of these chemotaxins are mediated by translocation of an intracellular pool of ART1 to its site of catalytic activity on the outer aspect of the plasma membrane.  (+info)

(7/1266) Evidence for a structural motif in toxins and interleukin-2 that may be responsible for binding to endothelial cells and initiating vascular leak syndrome.

The dose-limiting toxicity of interleukin-2 (IL-2) and immunotoxin (IT) therapy in humans is vascular leak syndrome (VLS). VLS has a complex etiology involving damage to vascular endothelial cells (ECs), extravasation of fluids and proteins, interstitial edema, and organ failure. IL-2 and ITs prepared with the catalytic A chain of the plant toxin, ricin (RTA), and other toxins, damage human ECs in vitro and in vivo. Damage to ECs may initiate VLS; if this damage could be avoided without losing the efficacy of ITs or IL-2, larger doses could be administered. In this paper, we provide evidence that a three amino acid sequence motif, (x)D(y), in toxins and IL-2 damages ECs. Thus, when peptides from RTA or IL-2 containing this sequence motif are coupled to mouse IgG, they bind to and damage ECs both in vitro and, in the case of RTA, in vivo. In contrast, the same peptides with a deleted or mutated sequence do not. Furthermore, the peptide from RTA attached to mouse IgG can block the binding of intact RTA to ECs in vitro and vice versa. In addition, RTA, a fragment of Pseudomonas exotoxin A (PE38-lys), and fibronectin also block the binding of the mouse IgG-RTA peptide to ECs, suggesting that an (x)D(y) motif is exposed on all three molecules. Our results suggest that deletions or mutations in this sequence or the use of nondamaging blocking peptides may increase the therapeutic index of both IL-2, as well as ITs prepared with a variety of plant or bacterial toxins.  (+info)

(8/1266) Heparin-binding EGF-like growth factor interacts with mouse blastocysts independently of ErbB1: a possible role for heparan sulfate proteoglycans and ErbB4 in blastocyst implantation.

Blastocyst implantation requires molecular and cellular interactions between the uterine luminal epithelium and blastocyst trophectoderm. We have previously shown that heparin-binding EGF-like growth factor (HB-EGF) is induced in the mouse luminal epithelium solely at the site of blastocyst apposition at 16:00 hours on day 4 of pregnancy prior to the attachment reaction (22:00-23:00 hours), and that HB-EGF promotes blastocyst growth, zona-hatching and trophoblast outgrowth. To delineate which EGF receptors participate in blastocyst activation, the toxicity of chimeric toxins composed of HB-EGF or TGF-(&agr;) coupled to Pseudomonas exotoxin (PE) were used as measures of receptor expression. TGF-(&agr;) or HB-EGF binds to EGF-receptor (ErbB1), while HB-EGF, in addition, binds to ErbB4. The results indicate that ErbB1 is inefficient in mediating TGF-(&agr;)-PE or HB-EGF-PE toxicity as follows: (i) TGF-(&agr;)-PE was relatively inferior in killing blastocysts, 100-fold less than HB-EGF-PE, (ii) analysis of blastocysts isolated from cross-bred egfr+/- mice demonstrated that HB-EGF-PE, but not TGF-(&agr;)-PE, killed egfr-/- blastocysts, and (iii) blastocysts that survived TGF-(&agr;)-PE were nevertheless killed by HB-EGF-PE. HB-EGF-PE toxicity was partially mediated by cell surface heparan sulfate proteoglycans (HSPG), since a peptide corresponding to the heparin-binding domain of HB-EGF as well as heparitinase treatment protected the blastocysts from the toxic effects of HB-EGF-PE by about 40%. ErbB4 is a candidate for being an HB-EGF-responsive receptor since RT-PCR analysis demonstrated that day 4 mouse blastocysts express two different erbB4 isoforms and immunostaining with anti-ErbB4 antibodies confirmed that ErbB4 protein is expressed at the apical surface of the trophectoderm cells. It is concluded that (i) HB-EGF interacts with the blastocyst cell surface via high-affinity receptors other than ErbB1, (ii) the HB-EGF interaction with high-affinity blastocysts receptors is regulated by heparan sulfate, and (iii) ErbB4 is a candidate for being a high-affinity receptor for HB-EGF on the surface of implantation-competent blastocysts.  (+info)

*  Zaleplon
ADP-ribose) synthetase and mono(ADP-ribosyl)transferase". The Journal of Biological Chemistry. 267 (3): 1569-75. PMID 1530940. ...
*  ADP-ribosylation
... leading to the discovery of enzymatic conjugation of a single ADP-ribose group by mono-ADP-ribosyl transferase. It was ... ADP-ribose) glycohydrolase, an enzyme that hydrolyses poly(ADP-ribose) to produce free ADP-ribose. Studies have shown poly-ADP- ... mono-ADP ribosylation and poly-ADP ribosylation. Mono-ADP ribosyltransferases commonly catalyze the addition of ADP-ribose to ... Poly-(ADP-ribose) polymerases (PARPs) are found mostly in eukaryotes and catalyze the transfer of multiple ADP-ribose molecules ...
*  List of MeSH codes (D08)
... adp ribose transferases MeSH D08.811.913.400.725.115.180 --- cholera toxin MeSH D08.811.913.400.725.115.220 --- diphtheria ... adp-ribose) polymerases MeSH D08.811.913.400.725.115.690.840 --- tankyrases MeSH D08.811.913.400.725.115.845 --- sirtuins MeSH ... adp-ribosylation factors MeSH D08.811.277.040.330.300.400.100.100 --- ADP-ribosylation factor 1 MeSH D08.811.277.040.330.300. ... glutathione transferase MeSH D08.811.913.225.500.500 --- glutathione S-transferase pi MeSH D08.811.913.225.575 --- ...
*  NMNAT1
ADP-ribose) polymerase 1 activity by the phosphorylation state of the nuclear NAD biosynthetic enzyme NMN adenylyl transferase ... The coenzyme NAD and its derivatives are involved in hundreds of metabolic redox reactions and are utilized in protein ADP- ... "Characterization of recombinant human nicotinamide mononucleotide adenylyl transferase (NMNAT), a nuclear enzyme essential for ...
*  Ribose-5-phosphate adenylyltransferase
... whereas its two products are phosphate and ADP-ribose. This enzyme belongs to the family of transferases, specifically those ... ADP-ribose Thus, the two substrates of this enzyme are ADP and D-ribose 5-phosphate, ... D-ribose-5-phosphate adenylyltransferase. Other names in common use include ADP ribose phosphorylase, and adenosine ... In enzymology, a ribose-5-phosphate adenylyltransferase (EC 2.7.7.35) is an enzyme that catalyzes the chemical reaction ADP + D ...
*  PARP4
... transferase protein". Genomics. 62 (3): 533-6. doi:10.1006/geno.1999.6024. PMID 10644454. "Entrez Gene: PARP4 poly (ADP-ribose ... Poly [ADP-ribose] polymerase 4 is an enzyme that in humans is encoded by the PARP4 gene. This gene encodes poly(ADP-ribosyl) ... ADP-ribosyl)ation reaction. This protein has a catalytic domain which is homologous to that of poly (ADP-ribosyl) transferase, ... 2004). "Vault poly(ADP-ribose) polymerase is associated with mammalian telomerase and is dispensable for telomerase function ...
*  2'-phosphotransferase
ADP-ribose 1'',2''-phosphate, nicotinamide, and H2O. This enzyme belongs to the family of transferases, specifically those ... ADP-ribose 1,2-phosphate + nicotinamide + H2O Thus, the two substrates of this enzyme are [[2'-phospho-[ligated tRNA]]] and ... Spinelli SL, Kierzek R, Turner DH, Phizicky EM (1999). "Transient ADP-ribosylation of a 2'-phosphate implicated in its removal ...
*  Phosphoribokinase
... whereas its two products are ADP and D-ribose 1,5-bisphosphate. This enzyme belongs to the family of transferases, specifically ... ADP + D-ribose 1,5-bisphosphate Thus, the two substrates of this enzyme are ATP and D-ribose 5-phosphate, ... In enzymology, a phosphoribokinase (EC 2.7.1.18) is an enzyme that catalyzes the chemical reaction ATP + D-ribose 5-phosphate ... The systematic name of this enzyme class is ATP:D-ribose-5-phosphate 1-phosphotransferase. This enzyme is also called ...
*  PARP2
ADP-ribose) polymerase gene family (ADPRTL): cDNA cloning of two novel poly(ADP-ribose) polymerase homologues". Genomics. 57 (3 ... ADP-ribosyl)ation reaction. This protein has a catalytic domain which is homologous to that of poly (ADP-ribosyl) transferase, ... Poly [ADP-ribose] polymerase 2 is an enzyme that in humans is encoded by the PARP2 gene. It is one of the PARP family of ... Schreiber V, Amé JC, Dollé P, Schultz I, Rinaldi B, Fraulob V, Ménissier-de Murcia J, de Murcia G (2002). "Poly(ADP-ribose) ...
*  Adenosine thiamine triphosphate
ADP-ribose) polymerase-1(PARP-1) activity". J Nutr Sci Vitaminol (Tokyo). 57 (2): 192-6. PMID 21697640. Makarchikov AF, Brans A ... according to the following reaction catalyzed by thiamine diphosphate adenylyl transferase: ThDP + ATP (ADP) ↔ AThTP + PPi (Pi ... Bettendorff L (2007). "Thiamine diphosphate adenylyl transferase from E. coli: functional characterization of the enzyme ...
*  PARP3
ADP-ribose) polymerase gene family (ADPRTL): cDNA cloning of two novel poly(ADP-ribose) polymerase homologues". Genomics. 57 (3 ... Berghammer H, Ebner M, Marksteiner R, Auer B (1999). "pADPRT-2: a novel mammalian polymerizing(ADP-ribosyl)transferase gene ... Poly [ADP-ribose] polymerase 3 is an enzyme that in humans is encoded by the PARP3 gene. The protein encoded by this gene ... "Entrez Gene: PARP3 poly (ADP-ribose) polymerase family, member 3". Bashford CL, Chance B, Lloyd D, Poole RK (1981). " ...
*  S-methyl-5-thioribose kinase
ADP + S-methyl-5-thio-alpha-D-ribose 1-phosphate Thus, the two substrates of this enzyme are ATP and S-methyl-5-thio-D-ribose, ... This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups ( ... whereas its two products are ADP and S-methyl-5-thio-alpha-D-ribose 1-phosphate. ... The systematic name of this enzyme class is ATP:S-methylmethyl-5-thio-D-ribose 1-phosphotransferase. Other names in common use ...
*  Ribose 1,5-bisphosphate phosphokinase
... whereas its two products are ADP and 5-phospho-alpha-D-ribose 1-diphosphate. This enzyme belongs to the family of transferases ... ADP + 5-phospho-alpha-D-ribose 1-diphosphate Thus, the two substrates of this enzyme are ATP and ribose 1,5-bisphosphate, ... In enzymology, a ribose 1,5-bisphosphate phosphokinase (EC 2.7.4.23) is an enzyme that catalyzes the chemical reaction ATP + ... The systematic name of this enzyme class is ATP:ribose-1,5-bisphosphate phosphotransferase. Other names in common use include ...
*  Sirtuin
This hydrolysis yields O-acetyl-ADP-ribose, the deacetylated substrate and nicotinamide, itself an inhibitor of sirtuin ... which make them exclusive ADP-ribosyl transferases. Sirtuin list based on North/Verdin diagram. Sirtuin activity is inhibited ... "Structural basis for nicotinamide cleavage and ADP-ribose transfer by NAD(+)-dependent Sir2 histone/protein deacetylases". Proc ... Sirtuins are a class of proteins that possess either mono-ADP-ribosyltransferase, or deacylase activity, including deacetylase ...
*  Chromatin remodeling
This is quickly followed by accumulation of chromatin remodeler Alc1, which has an ADP-ribose-binding domain, allowing it to be ... Mutations in Histone Acetyl Transferases (HAT) p300 (missense and truncating type) are most commonly reported in colorectal, ... ADP-ribose)-dependent chromatin remodeler Alc1 induces local chromatin relaxation upon DNA damage". Mol. Biol. Cell. 27 (24): ... Acetylation - by HAT (histone acetyl transferase); deacetylation - by HDAC (histone deacetylase) Acetylation tends to define ...
*  DNA repair
PARP1 synthesizes polymeric adenosine diphosphate ribose (poly (ADP-ribose) or PAR) chains on itself. Next the chromatin ... Another type of damage, methylation of guanine bases, is directly reversed by the protein methyl guanine methyl transferase ( ... Li D, Bi FF, Cao JM, Cao C, Li CY, Liu B, Yang Q (2014). "Poly (ADP-ribose) polymerase 1 transcriptional regulation: a novel ... In further steps, Poly (ADP-ribose) polymerase 1 (PARP1) is required and may be an early step in MMEJ. There is pairing of ...
*  ATP phosphoribosyltransferase
The systematic name of this enzyme class is 1-(5-phospho-D-ribosyl)-ATP:diphosphate phospho-alpha-D-ribosyl-transferase. Other ... and ADP and AMP (which reflect the overall energy status of the cell). As this pathway of histidine biosynthesis is present ... 5-phospho-alpha-D-ribose 1-diphosphate Thus, the two substrates of this enzyme are 1-(5-phospho-D-ribosyl)-ATP and diphosphate ... whereas its two products are ATP and 5-phospho-alpha-D-ribose 1-diphosphate. This enzyme belongs to the family of ...
*  Purine metabolism
PRPP + L-Glutamine + H2O → PRA + L-Glutamate + PPi In the second step react PRA, glycine and ATP to create GAR, ADP, and ... Inosine monophosphate is synthesized on a pre-existing ribose-phosphate through a complex pathway (as shown in the figure on ... phosphoribosyalamine from glutamine and PRPP catalysed by PRPP amino transferase is the site point for purine synthesis.The ... fGAR + L-Glutamine + ATP → fGAM + L-Glutamate + ADP + Pi The fifth is catalyzed by AIR synthetase (FGAM cyclase). fGAM + ATP → ...
*  Adenosine triphosphate
ATP hydrolyses to ADP and phosphate. Living cells maintain the ratio of ATP to ADP at a point ten orders of magnitude from ... Aminoacyl transferase binds AMP-amino acid to tRNA. The coupling reaction proceeds in two steps: aa + ATP --> aa-AMP + PPi aa- ... the sugar ribose, and the triphosphate. It is used in cells as a coenzyme. In terms of its structure, ATP consists of an ... The hydrolysis of ATP into ADP and inorganic phosphate releases 30.5 kJ/mol of enthalpy, with a change in free energy of 3.4 kJ ...
*  Nucleotide
Both steps are fueled by ATP hydrolysis: ATP + UMP → ADP + UDP UDP + ATP → UTP + ADP CTP is subsequently formed by amination of ... The covalent linkage between the ribose and pyrimidine occurs at position C1 of the ribose unit, which contains a pyrophosphate ... Orotate phosphoribosyltransferase (PRPP transferase) catalyzes the net reaction yielding orotidine monophosphate (OMP): Orotate ... Uric acid is formed when GMP is split into the base guanine and ribose. Guanine is deaminated to xanthine which in turn is ...
*  Ribonucleotide
DNA is defined by containing 2'-deoxy-ribose nucleic acid while RNA is defined by containing ribose nucleic acid. In some ... Orotate is covalently linked with phosphoribosyl pyrophosphate (PRPP) by orotate phosphoribysol-transferase yielding orotidine ... dATP and dGTP are synthesized from ADP and GTP, respectively. They are first reduced by RNR and then phosphorylated by ... The pathway begins with the conversion of Ribose-5-Phosphate(R5P) to phosphoribosyl pyrophosphate (PRPP) by enzyme ribose- ...
*  Amidophosphoribosyltransferase
The allosteric (A) site overlaps with the site for the ribose-5-phosphate of PRPP, while the catalytic (C) site overlaps with ... Amidophosphoribosyl transferase at the US National Library of Medicine Medical Subject Headings (MeSH) Human PPAT genome ... ADP, and GDP. Each enzyme subunit from the homotetramer has two binding sites for these inhibitors. ... that produces ammonia from glutamine by hydrolysis and a phosphoribosyltransferase domain that binds the ammonia to ribose-5- ...
*  List of EC numbers (EC 2)
... diacetylbacillosamine 1-phosphate transferase EC 2.7.8.37: alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase EC 2.7. ... ADP-dependent phosphofructokinase EC 2.7.1.147: ADP-dependent glucokinase EC 2.7.1.148: 4-(cytidine 5'-diphospho)-2-C-methyl-D- ... oxalate CoA-transferase EC 2.8.3.3: malonate CoA-transferase EC 2.8.3.4: deleted EC 2.8.3.5: 3-oxoacid CoA-transferase EC 2.8. ... acetate CoA-transferase EC 2.8.3.9: butyrate-acetoacetate CoA-transferase EC 2.8.3.10: citrate CoA-transferase EC 2.8.3.11: ...
*  Uridine monophosphate synthetase
After addition of ribose-P to orotate by OPRTase to form orotidine-5'-monophosphate (OMP), OMP is decarboxylated to form ... Orotate PRTase activity is activated by low concentrations of OMP, phosphate, and ADP. P. falciparum OPRTase follows a random ... Nio Y, Toga T, Maruyama R, Fukushima M (Jul 2007). "Expression of orotate phosphoribosyl transferase in human pancreatic cancer ... Lin T, Suttle DP (May 1995). "UMP synthase activity expressed in deficient hamster cells by separate transferase and ...
*  Cancer epigenetics
Li D, Bi FF, Cao JM, Cao C, Li CY, Liu B, Yang Q (2014). "Poly (ADP-ribose) polymerase 1 transcriptional regulation: a novel ... Treatment with HDAC inhibitors has been found to promote gene reactivation after DNA methyl-transferases inhibitors have ... ADP-ribose) polymerase 1 in BRCA-mutated serous ovarian cancer". BMC Cancer. 13: 90. doi:10.1186/1471-2407-13-90. PMC 3599366 ...
*  Arsenic biochemistry
This compound is then converted to a mono-methylated arsenic (III) compound using Glutathione S-Transferase Omega-1 (GSTO1). ... Arsenic-containing ribose derivatives (R = several groups) A topical source of arsenic are the green pigments once popular in ... arsenate uncouples the synthesis of ATP by binding to ADP in the presence of succinate, thus forming an unstable compound that ... compound by Glutathione S-Transferase Omega-1 (GTSO1). The other route uses glutathione (GSH) to conjugate with arsenic (III) ...
CD38 (ADP Ribosyl Cyclase I) Antibody - Without BSA and Azide - Mouse Monoclonal Antibody [Clone AT2 ] IF, FC - Buy Now! |Abgent  CD38 (ADP Ribosyl Cyclase I) Antibody - Without BSA and Azide - Mouse Monoclonal Antibody [Clone AT2 ] IF, FC - Buy Now! |Abgent
CD38 (ADP Ribosyl Cyclase I) Antibody - Without BSA and Azide, Mouse Monoclonal Antibody [Clone AT2 ] validated in IF, FC ( ... phospho-ADP-ribosyl cyclase/2'-phospho-cyclic-ADP-ribose transferase, 2.4.99.20, 2'-phospho-cyclic-ADP-ribose transferase, ADP- ... ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1, 3.2.2.6, 2'-phospho-ADP-ribosyl cyclase, 2'- ... AH12734: CD38 (ADP Ribosyl Cyclase 1) Antibody - With BSA and Azide. AH12735: CD38 (ADP Ribosyl Cyclase 1) Antibody - Without ...
more infohttp://www.abgent.com/products/AH12737-CD38-ADP-Ribosyl-Cyclase-I-Antibody-Without-BSA-and-Azide
Elephantopus scaber -              EVIDENCE BASED NATURAL HEALTH  Elephantopus scaber - EVIDENCE BASED NATURAL HEALTH
The total cellular DNA content and expression of cleaved poly (ADP-ribose) polymerase was also analyzed.. RESULTS: ... terminal deoxynucleotidyl transferase-mediated dUTP biotin nick end-labeling (TUNEL) assay, DNA fragmentation analysis and ...
more infohttp://evidencebasednaturalhealth.weebly.com/elephantopus-scaber.html
The Small Molecule GMX1778 Is a Potent Inhibitor of NAD+ Biosynthesis: Strategy for Enhanced Therapy in Nicotinic Acid...  The Small Molecule GMX1778 Is a Potent Inhibitor of NAD+ Biosynthesis: Strategy for Enhanced Therapy in Nicotinic Acid...
ADP-ribose) polymerase 1 for efficient DNA repair and poly(ADP-ribose) polymerase 1 is known to be one of the major cellular ... Preclinical development of the nicotinamide phosphoribosyl transferase inhibitor prodrug GMX1777. Anticancer Drugs 20:346-354. ... The ribose portion of NAD+ is utilized or broken down by multiple enzymes, including poly(ADP-ribose) polymerase (PARP) and ... Poly(ADP-ribose): novel functions for an old molecule. Nat. Rev. Mol. Cell Biol. 7:517-528. ...
more infohttps://mcb.asm.org/content/29/21/5872?ijkey=1ea8ce6088c9da2aec00428a0c4fac9117239882&keytype2=tf_ipsecsha
Diphtheria Toxin   < ADP-ribose transferases (diphthamide-specific)  << ADP Ribose Transferases (ADP-Ribosyltransferases)  <<<...  Diphtheria Toxin < ADP-ribose transferases (diphthamide-specific) << ADP Ribose Transferases (ADP-Ribosyltransferases) <<<...
... an ADP-ribosylating polypeptide, produced by the toxigenic bacteria Corynebacterium diphtheriae ... ADP Ribose Transferases (ADP-Ribosyltransferases). ⌊ADP-ribose transferases (diphthamide-specific). ⌊Diphtheria Toxin ... Transferases [EC 2]. ⌊Glycosyltransferases (Glycoside Transferases) [EC 2.4]. ⌊Pentosyltransferases [EC 2.4.2]. ⌊ ... In our body, the Diphtheria Toxin (Corynebacterium Diphtheriae Toxin), an exogenous ADP-ribosylating polypeptidee, produced by ...
more infohttp://wellnessadvocate.com/?dgl=67888
Distinct roles for the N- and C-terminal regions in the cytotoxicity of pierisin-1, a putative ADP-ribosylating toxin from...  Distinct roles for the N- and C-terminal regions in the cytotoxicity of pierisin-1, a putative ADP-ribosylating toxin from...
... and has been suggested to consist of an N-terminal region with ADP-ribosyltransferase domain and of a C-terminal region that ... ADP Ribose Transferases. ADP-Ribosylation Factors / chemistry, pharmacology*. Amino Acid Sequence. Animals. Apoptosis / drug ... ADP Ribose Transferases; EC 3.6.5.2/ADP-Ribosylation Factors ... a putative ADP-ribosylating toxin from cabbage butterfly, ... and has been suggested to consist of an N-terminal region with ADP-ribosyltransferase domain and of a C-terminal region that ...
more infohttp://www.biomedsearch.com/nih/Distinct-roles-N-C-terminal/11226221.html
Drug CategoriesBrowse DrugBank Categories - DrugBank  Drug CategoriesBrowse DrugBank Categories - DrugBank
ADP Ribose Transferases. Enzymes that transfer the ADP-RIBOSE group of NAD or NADP to proteins or other small mo... more. 1. 3 ... Enzymes from the transferase class that catalyze the transfer of acyl groups from donor... more. 1. 0. Details. ...
more infohttps://www.drugbank.ca/categories
EC 2.4.2  EC 2.4.2
D-ribosyl-transferase. Systematic name: NAD+:poly(ADP-D-ribosyl)-acceptor ADP-D-ribosyl-transferase. Comments: The ADP-D- ... Other name(s): poly(ADP-ribose) synthase; ADP-ribosyltransferase (polymerizing); NAD ADP-ribosyltransferase; PARP; PARP-1; NAD+ ... Other name(s): ADP-ribosyltransferase; mono(ADP-ribosyl)transferase; NAD+:L-arginine ADP-D-ribosyltransferase; NAD(P)+-arginine ... ADP-D-ribosyl)transferase. Systematic name: NAD+:diphthamide-[translation elongation factor 2] N-(ADP-D-ribosyl)transferase. ...
more infohttps://www.qmul.ac.uk/sbcs/iubmb/enzyme/EC2/0402.html
metastatic malignant neoplasm to the spinal cord drug therapy 2000:2010[pubdate] *count=100 - BioMedLib™ search engine  metastatic malignant neoplasm to the spinal cord drug therapy 2000:2010[pubdate] *count=100 - BioMedLib™ search engine
MeSH-major] ADP Ribose Transferases. Antibodies, Monoclonal / therapeutic use. Bacterial Toxins. Breast Neoplasms / therapy. ... ADP Ribose Transferases; EC 2.4.2.31 / toxA protein, Pseudomonas aeruginosa; EC 2.7.10.1 / Receptor, Epidermal Growth Factor; ...
more infohttp://www.bmlsearch.com/?kwr=metastatic+malignant+neoplasm+to+the+spinal+cord+drug+therapy+2000:2010%5Bpubdate%5D&cxts=100&stmp=b1
Metabolomic Endotype of Asthma | The Journal of Immunology  Metabolomic Endotype of Asthma | The Journal of Immunology
These are ADP-ribose transferase, cADP-ribose synthase, and sirtuins (protein lysine deacetylases). Of these, cADP-ribose ... CD38/cyclic ADP-ribose-mediated Ca2+ signaling contributes to airway smooth muscle hyper-responsiveness. FASEB J. 17: 452-454. ... resulted in lower levels of cADP-ribose and increased intracellular levels of NAD+ (37). We postulate that the higher levels of ... role of CD38/cyclic adenosine diphosphate ribose pathway. Am. J. Respir. Cell Mol. Biol. 31: 36-42. ...
more infohttps://www.jimmunol.org/content/195/2/643?ijkey=18792c75d48e02a673b355ff6183ad849aeacc5a&keytype2=tf_ipsecsha
Frontiers | The Effect of Nicotinamide on Gene Expression in a Traumatic Brain Injury Model | Neuroscience  Frontiers | The Effect of Nicotinamide on Gene Expression in a Traumatic Brain Injury Model | Neuroscience
ADP-ribose) transferase inhibitors. Biochem. Int. 15, 329-337. ... ADP-ribose) polymerase (PARP) and caspase family of proteases, ... catalyzes the cleavage of NAD+ into nicotinamide and ADP-ribose, and then uses the ADP-ribose to synthesize polymers which ... Virag, L., and Szabo, C. (2002). The therapeutic potential of poly(ADP-ribose) polymerase inhibitors. Pharmacol. Rev. 54, 375- ...
more infohttps://www.frontiersin.org/articles/10.3389/fnins.2013.00021/full
SCOPe 2.06: Structural Classification of Proteins - extended  SCOPe 2.06: Structural Classification of Proteins - extended
Class: transferase/transferase inhibitor. Keywords: DIPHTHERIA TOXIN LIKE ADP-RIBOSE TRANSFERASE, TRANSFERASE, ADP-RIBOSYLATION ... Compound: Poly [ADP-ribose] polymerase 3. Species: Homo sapiens [TaxId:9606]. Gene: ADPRT3, ADPRTL3, PARP3. Database cross- ... transferase-transferase inhibitor complex. Deposited on 2013-06-14, released 2014-02-19. The last revision prior to the SCOPe ...
more infohttp://scop.berkeley.edu/pdb/code=4l7o&ver=2.06
SCOPe 2.07: Structural Classification of Proteins - extended  SCOPe 2.07: Structural Classification of Proteins - extended
Class: transferase/transferase inhibitor. Keywords: DIPHTHERIA TOXIN LIKE ADP-RIBOSE TRASNFERASE, TRANSFERASE, ADP-RIBOSYLATION ... Compound: Poly [ADP-ribose] polymerase 3. Species: Homo sapiens [TaxId:9606]. Gene: ADPRT3, ADPRTL3, PARP3. Database cross- ... transferase-transferase inhibitor complex. Deposited on 2013-06-14, released 2014-02-19. The last revision prior to the SCOPe ...
more infohttps://scop.berkeley.edu/pdb/code=4l7p
NAD+-Induced Vasotoxicity in the Pericyte-Containing Microvasculature of the Rat Retina: Effect of Diabetes | IOVS | ARVO...  NAD+-Induced Vasotoxicity in the Pericyte-Containing Microvasculature of the Rat Retina: Effect of Diabetes | IOVS | ARVO...
Ecto-ADP-ribose transferases: cell-surface response to local tissue injury. Physiology. 2005;20:374-381. [CrossRef] [PubMed] ... However, as shown in Figure 1C , exposure of freshly isolated retinal microvessels to ADP-ribose (1 mM) or nicotinamide (1 mM) ... CD38 controls ADP-ribosyltransferase-2-catalyzed ADP-ribosylation of T cell surface proteins. J Immunol. 2005;174:3298-3305. [ ... Cell-surface ADP-ribosylation of fibroblast growth factor-2 by an arginine-specific ADP-ribosyltransferase. Biochem J. 1997;323 ...
more infohttp://iovs.arvojournals.org/article.aspx?articleid=2125178
KAKEN - Research Projects | Studies on the Role of Poly (ADP-ribosyl) Action in Cell Differentiation and Oncogenesis (KAKENHI...  KAKEN - Research Projects | Studies on the Role of Poly (ADP-ribosyl) Action in Cell Differentiation and Oncogenesis (KAKENHI...
Publications] Banasik, M., et al.: 'Specific inhibitors of poly (ADP-ribose) synthetase and mono(ADP-ribosyl) transferase.' J. ... 1. Cloning of cDNA coding for poly (ADP-ribose) synthetase : A complete amino acid sequence of bovine poly (ADP-ribose) ... Publications] Ueda, K.: 'Poly (ADP-ribose) synthetase.' ADP-ribosylating Toxins and G Proteins : Insights into Signal ... Publications] Ueda,K.: 'Poly(ADP-ribose),its molecular biology and medicine' Kor.J.Biochem.21. (1989). *. Related Report. 1989 ...
more infohttps://kaken.nii.ac.jp/en/grant/KAKENHI-PROJECT-01480146/
New functions of a long-known molecule: Emerging roles of NAD in ...: Ingenta Connect  New functions of a long-known molecule: Emerging roles of NAD in ...: Ingenta Connect
Protein modification is catalyzed by ADP-ribosyl transferases that attach the ADP-ribose moiety of NAD+ to specific amino-acid ... Keywords: ADP ribosylation; NAD; calcium; cyclic ADP-ribose; mitochondria; pyridine nucleotides; signaling ... The cell nucleus contains enzymes catalyzing the transfer of ADP-ribose polymers (polyADP-ribose) onto the acceptor proteins. ... The best known enzyme of this type is poly(ADP-ribose) polymerase 1 (PARP1), which has been implicated in the regulation of ...
more infohttps://www.ingentaconnect.com/content/bsc/ejb/2000/00000267/00000006/art00002
Structure/function analysis of the transmembrane domain of DAB389-interleukin-2, an interleukin-2 receptor-targeted fusion...  Structure/function analysis of the transmembrane domain of DAB389-interleukin-2, an interleukin-2 receptor-targeted fusion...
... but it is essential for the efficient delivery of the ADP-ribosyltransferase from DAB389-IL-2 to the cytosol of target cells. ... but it is essential for the efficient delivery of the ADP-ribosyltransferase from DAB389-IL-2 to the cytosol of target cells.", ... but it is essential for the efficient delivery of the ADP-ribosyltransferase from DAB389-IL-2 to the cytosol of target cells. ... but it is essential for the efficient delivery of the ADP-ribosyltransferase from DAB389-IL-2 to the cytosol of target cells. ...
more infohttps://einstein.pure.elsevier.com/en/publications/structurefunction-analysis-of-the-transmembrane-domain-of-dabsub3
Functional analysis of the contribution of RhoA and RhoC GTPases to in by Kaylene J. Simpson, Aisling S. Dugan et al.  "Functional analysis of the contribution of RhoA and RhoC GTPases to in" by Kaylene J. Simpson, Aisling S. Dugan et al.
ADP Ribose Transferases; Breast Neoplasms; Cell Adhesion; Cell Line, Tumor; Humans; Neoplasm Invasiveness; RNA Interference; ...
more infohttps://escholarship.umassmed.edu/cancerbiology_pp/177/
George-Lucian Moldovan, PhD - Research Output
     - Penn State  George-Lucian Moldovan, PhD - Research Output - Penn State
Loss of E2F7 confers resistance to poly-ADP-ribose polymerase (PARP) inhibitors in BRCA2-deficient cells. Clements, K. E., ... The ADP-ribosyltransferase PARP10/ARTD10 interacts with proliferating cell nuclear antigen (PCNA) and is required for DNA ... A novel role for the mono-ADP-ribosyltransferase PARP14/ARTD8 in promoting homologous recombination and protecting against ...
more infohttps://pennstate.pure.elsevier.com/en/persons/george-lucian-moldovan/publications/
Publications  Publications
ADP Ribose Transferases. 1 Databases, Genetic. 1 Gene Knockdown Techniques. 1 Golgi Apparatus. 1 ...
more infohttps://publications.ncats.nih.gov/sitemap?facet=Author/Ormanoglu,%20Pinar
Find Research Outputs
             - Bond University Research Portal  Find Research Outputs - Bond University Research Portal
ADP Ribose Transferases Submission by Assistant Professor Narelle Bedford to the Inquiry into the Strategic Review of the ... Structure, function and inhibition of poly(ADP-ribose)polymerase, member 14 (PARP14). Schweiker, S. S., Tauber, A., Sherry, M ...
more infohttps://research.bond.edu.au/en/publications/?format=&page=9
  • Enzymes from the transferase class that catalyze the transfer of acyl groups from donor. (drugbank.ca)
  • Enzymes that transfer the ADP-RIBOSE group of NAD or NADP to proteins or other small mo. (drugbank.ca)
  • The etiology of secondary brain injury is multi-factorial, with a host of likely inter-related processes including mitochondrial energy failure, excessive generation of reactive oxygen species, activation of destructive enzymes such as poly (ADP-ribose) polymerase (PARP) and caspase family of proteases, membrane disruption, neuronal death, thrombosis due to intravascular coagulation in small vessels, increased synaptic concentrations of excitatory amino acids, and activation of innate inflammatory responses ( Schouten, 2007 ). (frontiersin.org)
  • The cell nucleus contains enzymes catalyzing the transfer of ADP-ribose polymers (polyADP-ribose) onto the acceptor proteins. (ingentaconnect.com)
  • In our body, the Diphtheria Toxin (Corynebacterium Diphtheriae Toxin) , an exogenous ADP-ribosylating polypeptidee , produced by the toxigenic bacteria Corynebacterium diphtheriae , which can cause myocarditis, polyneuritis, and other systemic toxic effects. (wellnessadvocate.com)
  • Verheugd P, Butepage M, Eckei L, Luscher B (2016) Players in ADP-ribosylation: readers and erasers. (springer.com)
  • Liou GG, Tanny JC, Kruger RG, Walz T, Moazed D (2005) Assembly of the SIR complex and its regulation by O-acetyl-ADP-ribose, a product of NAD-dependent histone deacetylation. (springer.com)
  • Palazzo L, Mikoc A, Ahel I (2017) ADP-ribosylation: new facets of an ancient modification. (springer.com)
  • Borra MT, O'Neill FJ, Jackson MD, Marshall B, Verdin E, Foltz KR, Denu JM (2002) Conserved enzymatic production and biological effect of O-acetyl-ADP-ribose by silent information regulator 2-like NAD+-dependent deacetylases. (springer.com)