Plant Diseases: Diseases of plants.Arabidopsis: A plant genus of the family BRASSICACEAE that contains ARABIDOPSIS PROTEINS and MADS DOMAIN PROTEINS. The species A. thaliana is used for experiments in classical plant genetics as well as molecular genetic studies in plant physiology, biochemistry, and development.Soybeans: An annual legume. The SEEDS of this plant are edible and used to produce a variety of SOY FOODS.Cotyledon: A part of the embryo in a seed plant. The number of cotyledons is an important feature in classifying plants. In seeds without an endosperm, they store food which is used in germination. In some plants, they emerge above the soil surface and become the first photosynthetic leaves. (From Concise Dictionary of Biology, 1990)Salicylic Acid: A compound obtained from the bark of the white willow and wintergreen leaves. It has bacteriostatic, fungicidal, and keratolytic actions.Plant Leaves: Expanded structures, usually green, of vascular plants, characteristically consisting of a bladelike expansion attached to a stem, and functioning as the principal organ of photosynthesis and transpiration. (American Heritage Dictionary, 2d ed)Tobacco: A plant genus of the family SOLANACEAE. Members contain NICOTINE and other biologically active chemicals; its dried leaves are used for SMOKING.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.Pseudomonas aeruginosa: A species of gram-negative, aerobic, rod-shaped bacteria commonly isolated from clinical specimens (wound, burn, and urinary tract infections). It is also found widely distributed in soil and water. P. aeruginosa is a major agent of nosocomial infection.Pseudomonas Infections: Infections with bacteria of the genus PSEUDOMONAS.Pseudomonas: A genus of gram-negative, aerobic, rod-shaped bacteria widely distributed in nature. Some species are pathogenic for humans, animals, and plants.Bacterial Proteins: Proteins found in any species of bacterium.Bacterial Toxins: Toxic substances formed in or elaborated by bacteria; they are usually proteins with high molecular weight and antigenicity; some are used as antibiotics and some to skin test for the presence of or susceptibility to certain diseases.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.Vicia sativa: A plant species of the genus VICIA, family FABACEAE. The seed is used for food and contains THIOCYANATES such as prunasin, cyanoalanine, cyanogen, and vicine.DNA Repair-Deficiency Disorders: Disorders resulting from defective DNA REPAIR processes or the associated cellular responses to DNA DAMAGE.Oryza sativa: Annual cereal grass of the family POACEAE and its edible starchy grain, rice, which is the staple food of roughly one-half of the world's population.Bloom Syndrome: An autosomal recessive disorder characterized by telangiectatic ERYTHEMA of the face, photosensitivity, DWARFISM and other abnormalities, and a predisposition toward developing cancer. The Bloom syndrome gene (BLM) encodes a RecQ-like DNA helicase.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.Succinic Anhydrides: A subclass of anhydrides with the general structure of dihydrofurandione. They can be substituted on any carbon atom. They modify and inhibit proteins and enzymes and are used in the acylation of amino- and hydroxyl groups.Nicotinamide Phosphoribosyltransferase: An enzyme that catalyzes the formation of nicotinamide mononucleotide (NMN) from nicotinamide and 5-phosphoribosyl-1-pyrophosphate, the rate-limiting step in the biosynthesis of the NAD coenzyme. It is also known as a growth factor for early B-LYMPHOCYTES, or an ADIPOKINE with insulin-mimetic effects (visfatin).Acrylamides: Colorless, odorless crystals that are used extensively in research laboratories for the preparation of polyacrylamide gels for electrophoresis and in organic synthesis, and polymerization. Some of its polymers are used in sewage and wastewater treatment, permanent press fabrics, and as soil conditioning agents.Triple Negative Breast Neoplasms: Breast neoplasms that do not express ESTROGEN RECEPTORS; PROGESTERONE RECEPTORS; and do not overexpress the NEU RECEPTOR/HER-2 PROTO-ONCOGENE PROTEIN.Tankyrases: A group of telomere associated proteins that interact with TRF1 PROTEIN, contain ANKYRIN REPEATS and have poly(ADP-ribose) polymerase activity.PhthalazinesNAD: 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)Butterflies: Slender-bodies diurnal insects having large, broad wings often strikingly colored and patterned.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.Insect Proteins: Proteins found in any species of insect.Molecular 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.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.Cytotoxins: Substances that are toxic to cells; they may be involved in immunity or may be contained in venoms. These are distinguished from CYTOSTATIC AGENTS in degree of effect. Some of them are used as CYTOTOXIC ANTIBIOTICS. The mechanism of action of many of these are as ALKYLATING AGENTS or MITOSIS MODULATORS.Metabolomics: The systematic identification and quantitation of all the metabolic products of a cell, tissue, organ, or organism under varying conditions. The METABOLOME of a cell or organism is a dynamic collection of metabolites which represent its net response to current conditions.Canada: The largest country in North America, comprising 10 provinces and three territories. Its capital is Ottawa.Alberta: A province of western Canada, lying between the provinces of British Columbia and Saskatchewan. Its capital is Edmonton. It was named in honor of Princess Louise Caroline Alberta, the fourth daughter of Queen Victoria. (From Webster's New Geographical Dictionary, 1988, p26 & Room, Brewer's Dictionary of Names, 1992, p12)British Columbia: A province of Canada on the Pacific coast. Its capital is Victoria. The name given in 1858 derives from the Columbia River which was named by the American captain Robert Gray for his ship Columbia which in turn was named for Columbus. (From Webster's New Geographical Dictionary, 1988, p178 & Room, Brewer's Dictionary of Names, 1992, p81-2)Genomics: The systematic study of the complete DNA sequences (GENOME) of organisms.Health Records, Personal: Longitudinal patient-maintained records of individual health history and tools that allow individual control of access.Academies and Institutes: Organizations representing specialized fields which are accepted as authoritative; may be non-governmental, university or an independent research organization, e.g., National Academy of Sciences, Brookings Institution, etc.O-Acetyl-ADP-Ribose: An acetyl ester of ADENOSINE DIPHOSPHATE RIBOSE formed during NAD-dependent deacetylation of proteins by SIRTUINS. The acetate group resides on the ribose ring where nicotinamide was cleaved from NAD during the reaction. Several isomers of O-acetyl-ADP-ribose have been isolated from the reaction.Sirtuin 2: A sirtuin family member found primarily in the CYTOPLASM. It is a multifunctional enzyme that contains a NAD-dependent deacetylase activity that is specific for HISTONES and a mono-ADP-ribosyltransferase activity.Sirtuins: A homologous family of regulatory enzymes that are structurally related to the protein silent mating type information regulator 2 (Sir2) found in Saccharomyces cerevisiae. Sirtuins contain a central catalytic core region which binds NAD. Several of the sirtuins utilize NAD to deacetylate proteins such as HISTONES and are categorized as GROUP III HISTONE DEACETYLASES. Several other sirtuin members utilize NAD to transfer ADP-RIBOSE to proteins and are categorized as MONO ADP-RIBOSE TRANSFERASES, while a third group of sirtuins appears to have both deacetylase and ADP ribose transferase activities.Silent Information Regulator Proteins, Saccharomyces cerevisiae: A set of nuclear proteins in SACCHAROMYCES CEREVISIAE that are required for the transcriptional repression of the silent mating type loci. They mediate the formation of silenced CHROMATIN and repress both transcription and recombination at other loci as well. They are comprised of 4 non-homologous, interacting proteins, Sir1p, Sir2p, Sir3p, and Sir4p. Sir2p, an NAD-dependent HISTONE DEACETYLASE, is the founding member of the family of SIRTUINS.Sirtuin 1: A sirtuin family member found primarily in the CELL NUCLEUS. It is an NAD-dependent deacetylase with specificity towards HISTONES and a variety of proteins involved in gene regulation.Scintillation Counting: Detection and counting of scintillations produced in a fluorescent material by ionizing radiation.Histone Deacetylases: Deacetylases that remove N-acetyl groups from amino side chains of the amino acids of HISTONES. The enzyme family can be divided into at least three structurally-defined subclasses. Class I and class II deacetylases utilize a zinc-dependent mechanism. The sirtuin histone deacetylases belong to class III and are NAD-dependent enzymes.Biopharmaceutics: The study of the physical and chemical properties of a drug and its dosage form as related to the onset, duration, and intensity of its action.Antigens, CD3: Complex of at least five membrane-bound polypeptides in mature T-lymphocytes that are non-covalently associated with one another and with the T-cell receptor (RECEPTORS, ANTIGEN, T-CELL). The CD3 complex includes the gamma, delta, epsilon, zeta, and eta chains (subunits). When antigen binds to the T-cell receptor, the CD3 complex transduces the activating signals to the cytoplasm of the T-cell. The CD3 gamma and delta chains (subunits) are separate from and not related to the gamma/delta chains of the T-cell receptor (RECEPTORS, ANTIGEN, T-CELL, GAMMA-DELTA).Antigens, CD8: Differentiation antigens found on thymocytes and on cytotoxic and suppressor T-lymphocytes. CD8 antigens are members of the immunoglobulin supergene family and are associative recognition elements in MHC (Major Histocompatibility Complex) Class I-restricted interactions.CD40 Ligand: A membrane glycoprotein and differentiation antigen expressed on the surface of T-cells that binds to CD40 ANTIGENS on B-LYMPHOCYTES and induces their proliferation. Mutation of the gene for CD40 ligand is a cause of HYPER-IGM IMMUNODEFICIENCY SYNDROME, TYPE 1.Antigens, CD40: A member of the tumor necrosis factor receptor superfamily with specificity for CD40 LIGAND. It is found on mature B-LYMPHOCYTES and some EPITHELIAL CELLS, lymphoid DENDRITIC CELLS. Evidence suggests that CD40-dependent activation of B-cells is important for generation of memory B-cells within the germinal centers. Mutations of the gene for CD40 antigen result in HYPER-IGM IMMUNODEFICIENCY SYNDROME, TYPE 3. Signaling of the receptor occurs through its association with TNF RECEPTOR-ASSOCIATED FACTORS.Antigens, CD28: Costimulatory T-LYMPHOCYTE receptors that have specificity for CD80 ANTIGEN and CD86 ANTIGEN. Activation of this receptor results in increased T-cell proliferation, cytokine production and promotion of T-cell survival.Antigens, CD44: Acidic sulfated integral membrane glycoproteins expressed in several alternatively spliced and variable glycosylated forms on a wide variety of cell types including mature T-cells, B-cells, medullary thymocytes, granulocytes, macrophages, erythrocytes, and fibroblasts. CD44 antigens are the principle cell surface receptors for hyaluronate and this interaction mediates binding of lymphocytes to high endothelial venules. (From Abbas et al., Cellular and Molecular Immunology, 2d ed, p156)

Transcutaneous immunization with bacterial ADP-ribosylating exotoxins as antigens and adjuvants. (1/1266)

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)

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

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)

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

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)

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

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)

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

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)

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

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)

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

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)

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. (8/1266)

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)

Poly [ADP Ribose] Polymerase 2 (ADP Ribosyltransferase Diphtheria Toxin Like 2 or NAD(+) ADP Ribosyltransferase 2 or Poly[ADP Ribose] Synthase 2 or PARP2 or EC 2.4.2.30)-Pipeline Review, H1 2017. Summary. According to the recently published report Poly [ADP Ribose] Polymerase 2-Pipeline Review, H1 2017; Poly [ADP Ribose] Polymerase 2 (ADP Ribosyltransferase Diphtheria Toxin Like 2 or NAD(+) ADP Ribosyltransferase 2 or Poly[ADP Ribose] Synthase 2 or PARP2 or EC 2.4.2.30) pipeline Target constitutes close to 18 molecules. Out of which approximately 16 molecules are developed by companies and remaining by the universities/institutes. Poly [ADP Ribose] Polymerase 2 (ADP Ribosyltransferase Diphtheria Toxin Like 2 or NAD(+) ADP Ribosyltransferase 2 or Poly[ADP Ribose] Synthase 2 or PARP2 or EC 2.4.2.30)-Poly [ADP-ribose] polymerase 2 is an enzyme encoded by the PARP2 gene. It is involved in the base excision repair (BER) pathway, by catalyzing the poly (ADP-ribosylation) of a limited number of ...
Mono-ADP-ribosyltransferase that mediates mono-ADP-ribosylation of target proteins (By similarity). Plays a role in nuclear envelope stability and nuclear remodeling during spermiogenesis (PubMed:25673562).
Exoenzyme S (ExoS) is a mono-ADP-ribosyltransferase secreted by the opportunistic pathogen Pseudomonas aeruginosa. ExoS requires a eukaryotic factor, the 14-3-3 protein, for enzymatic activity. Here, two aspects of the activation of the ADP-ribosyltransferase activity of ExoS by 14-3-3 proteins are …
Bruno, Tony F. et al " Pseudomonas aeruginosa Exoenzyme S Is a Mitogen but Not a Superantigen for Human T Lymphocytes." Infection and Immunity 66.7 (1998): 3072-3079. Web. 15 Dec. 2019. ...
Arnoldo A, Curak J, Kittanakom S, Chevelev I, Lee VT, Sahebol-Amri M, Koscik B, Ljuma L, Roy PJ, Bedalov A et al.. 2008. Identification of small molecule inhibitors of Pseudomonas aeruginosa exoenzyme S using a yeast phenotypic screen.. PLoS genetics. 4(2):e1000005. Abstract ...
Clostridium botulinum C3 exoenzyme inactivates the small GTP-binding protein family Rho by ADP-ribosylating asparagine 41, which depolymerizes the actin cytoskeleton. C3 thus represents a major family of the bacterial toxins that transfer the ADP-ribose moiety of NAD to specific amino acids in acceptor proteins to modify key biological activities in eukaryotic cells, including protein synthesis, differentiation, transformation, and intracellular signaling. The 1.7 A resolution C3 exoenzyme structure establishes the conserved features of the core NAD-binding beta-sandwich fold with other ADP-ribosylating toxins despite little sequence conservation. Importantly, the central core of the C3 exoenzyme structure is distinguished by the absence of an active site loop observed in many other ADP-ribosylating toxins. Unlike the ADP-ribosylating toxins that possess the active site loop near the central core, the C3 exoenzyme replaces the active site loop with an alpha-helix, alpha3. Moreover, structural ...
14-3-3 proteins belong to a family of conserved molecules, which play a regulatory role and participate in signal transduction and checkpoint control pathways. 14-3-3 proteins bind phosphoserine-phosphorylated ligands, such as the Raf-1 kinase and Bad, through recognition of the phosphorylated consensus motif, RSXpSXP (where pS is phosphoserine). Recently, a phosphorylation-independent interaction has been reported to occur between 14-3-3 and a small number of proteins, for example the 43 kDa inositol polyphosphate 5-phosphatase, glycoprotein Ib, p75NTR-associated cell-death executor (NADE) and the bacterial ADP-ribosyltransferase toxin exoenzyme S (ExoS). It has been suggested that specific residues of 14-3-3 proteins are required for activation of the bacterial toxin ExoS. An unphosphorylated peptide derived from a phage display library, known as the R18 peptide, and a synthetic peptide derived from ExoS inhibit the interaction between ExoS and 14-3-3. In this report we identify the amino acid ...
Ecto-ADP-ribosyltransferase 4 is an enzyme that in humans is encoded by the ART4 gene. ART4 has also been designated as CD297 (cluster of differentiation 297). This gene encodes a protein that contains a mono-ADP-ribosylation (ART) motif. It is a member of the ADP-ribosyltransferase gene family but enzymatic activity has not been demonstrated experimentally. Antigens of the Dombrock blood group system are located on the gene product, which is glycosylphosphatidylinositol-anchored to the erythrocyte membrane. Allelic variants, some of which lead to adverse transfusion reactions, are known. Several antigens have been recognised in this family. These are DO*A, DO*JO1, DO*A-WL, DO*DOYA, DO*B, DO*B-WL, DO*B-SH-Q149K, DO*B-(WL)-I175N, DO*HY1, DO*HY2 and DO*DOMR. Model organisms have been used in the study of ART4 function. A conditional knockout mouse line called Art4tm1a(KOMP)Wtsi was generated at the Wellcome Trust Sanger Institute. Male and female animals underwent a standardized phenotypic screen ...
Populärvetenskaplig sammanfattning. Små molekyler för att identifiera proteiners funktion. Vår arvsmassa innehåller cirka 24000 gener som i sin tur innehåller information för hur de tusentals proteiner vi är uppbyggda av ska framställas. Många läkemedel fungerar genom att en molekyl interagerar med ett av dessa proteiner och hämmar dess funktion för att på så sätt framkalla en önskad effekt. Vi vet dock inte vilken funktion många av våra proteiner fyller vilket ofta gör utvecklingen av nya läkemedel svår eller omöjlig. Den första delen av denna avhandling beskriver en grupp proteiner kallade ARTDs och hur små molekyler kan framställas och systematiskt förbättras för att till slut helt kunna slå ut vissa av dessa ARTDs. Genom att sedan studera vilka effekter detta medför kan man ta reda på vilken funktion proteinet fyller. På längre sikt skulle denna kunskap sedan kunna användas för att utveckla nya läkemedel genom att till exempel slå ut de proteiner som ...
Earlier we demonstrated that meta-iodobenzylguanidine (MIBG), a specific inhibitor of arginine mono-ADP-ribosylation blocks proliferation and differentiation of chick skeletal myogenic cells in...
Pseudomonas are a common cause of hospital-acquired infections that may be lethal. ADP-ribosyltransferase activities of Pseudomonas exotoxin-S and -T depend on 14-3-3 proteins inside the host cell. By binding in the 14-3-3 phosphopeptide binding groove, an amphipathic C-terminal helix of ExoS and ExoT has been thought to be crucial for their activation. However, crystal structures of the 14-3-3 beta: ExoS and -ExoT complexes presented here reveal an extensive hydrophobic interface that is sufficient for complex formation and toxin activation. We show that C-terminally truncated ExoS ADP-ribosyltransferase domain lacking the amphipathic binding motif is active when co-expressed with 14-3-3. Moreover, swapping the amphipathic C-terminus with a fragment from Vibrio Vis toxin creates a 14-3-3 independent toxin that ADP-ribosylates known ExoS targets. Finally, we show that 14-3-3 stabilizes ExoS against thermal aggregation. Together, this indicates that 14-3-3 proteins activate exotoxin ...
PARP catalysed ADP-ribosylation is a post-translational modification involved in several physiological and pathological processes, including cellular stress. In order to visualise both Poly-, and Mono-, ADP-ribosylation in vivo, we engineered specific fluorescent probes. Using them, we show that amino-acid starvation triggers an unprecedented display of mono-ADP-ribosylation that governs the formation ... read more of Sec body, a recently identified stress assembly that forms in Drosophila cells. We show that dPARP16 catalytic activity is necessary and sufficient for both amino-acid starvation induced mono-ADP-ribosylation and subsequent Sec body formation and cell survival. Importantly, dPARP16 catalyses the modification of Sec16, a key Sec body component, and we show that it is a critical event for the formation of this stress assembly. Taken together our findings establish a novel example for the role of mono-ADP-ribosylation in the formation of stress assemblies, and link this modification ...
The extent of the transfer of the adenosine 5-diphosphate ribose (ADPR) moiety of nicotinamide adenine dinucleotide onto elongation factor 2 (EF-2) catalyzed by Pseudomonas aeruginosa exotoxin A (PA-toxin) was dependent upon the presence of a reducing agent, dithiotheritol (DTT). The reaction requires DTT in low concentration (1 to 10 mM) and in the absence of DTT less product, ADPR-EF 2, was formed. PA-toxin was fully activated by treatment with a denaturing agent, sodium dodecyl sulphate (SDS), in conjunction with DTT. In the presence of activated toxin, the maximum transfer of ADPR onto EF-2 was observed when EF-2 had been previously reduced with DTT. Denaturation of EF-2 prior to reduction did not produce a further increase in its ability to act as a substrate for PA-toxin ...
Stuart, R K. and Pollack, M, "Pseudomonas aeruginosa exotoxin a inhibits proliferation of human bone marrow progenitor cells in vitro." (1982). Subject Strain Bibliography 1982. 3514 ...
This gene encodes a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes. The functions of human sirtuins have not yet been determined; however, yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA. Studies suggest that the human sirtuins may function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity. The protein encoded by this gene is included in class I of the sirtuin family. Two alternatively spliced transcript variants that encode different proteins have been described for this gene. [provided by RefSeq, Jul 2008] ...
This gene encodes a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes. The functions of human sirtuins have not yet been determined; however, yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA. Studies suggest that the human sirtuins may function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity. The protein encoded by this gene is included in class I of the sirtuin family. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Dec 2008 ...
This gene encodes a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes. The functions of human sirtuins have not yet been determined; however, yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA. Studies suggest that the human sirtuins may function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity. The protein encoded by this gene is included in class III of the sirtuin family. Alternative splicing of this gene results in multiple transcript variants ...
Some pathogenic spore-forming bacilli employ a binary protein mechanism for intoxicating the intestinal tracts of insects, animals, and humans. These Gram-positive bacteria and their toxins include Clostridium botulinum (C2 toxin), Clostridium difficile (C. difficile toxin or CDT), Clostridium perfringens (ι-toxin and binary enterotoxin, or BEC), Clostridium spiroforme (C. spiroforme toxin or CST), as well as Bacillus cereus (vegetative insecticidal protein or VIP). These gut-acting proteins form an AB complex composed of ADP-ribosyl transferase (A) and cell-binding (B) components that intoxicate cells via receptor-mediated endocytosis and endosomal trafficking. Once inside the cytosol, the A components inhibit normal cell functions by mono-ADP-ribosylation of globular actin, which induces cytoskeletal disarray and death. Important aspects of each bacterium and binary enterotoxin will be highlighted in this review, with particular focus upon the disease process involving the biochemistry and modes of
We herein demonstrated that Tat PTD-mediated protein transduction was successfully applied to intact arterial strips. It was reported earlier that Clostridium botulinum exoenzyme C3 tagged with Tat PTD inhibited the urotensin-induced contraction in the rat aorta.29 In the present study, the introduction of the protein into the cells by Tat PTD was clearly proved by the observation of GFP fluorescence in the TAT-GFP-treated strips, and by immunoblot detection of Tat PTD-tagged MYPT1 fragments in the extract of the strips. The introduction of protein is also supported by the observation that the MYPT1 fragments enhanced the Ca2+-induced contraction only when tagged with Tat PTD. The time needed to obtain a significant enhancement of contraction suggested that the transduction of functional protein into the intact arterial strips takes place within 10 minutes, which is consistent with previous reports.22,23⇓. Treatment with TAT-MYPT11-374 enhanced the Ca2+-induced contraction with no effect on ...
Pierisin-1 is an 850-aa cytotoxic protein found in the cabbage butterfly, Pieris rapae, and has been suggested to consist of an N-terminal region with ADP-ribosyltransferase domain and of a C-terminal region that might have a receptor-binding domain.
An enzyme that catalyzes the Transfer of the ADP-Ribose moiety from NAD+ or NADP+ to specific protein substrates with Arginine, Arginine-type compounds, Agmatine, or Guanidine as acceptors. This mono-ADP-ribosylation reaction is the mechanism of action common to several Bacterial Toxins affecting profound changes in cellular Metabolism, such as activation of Adenylate Cyclase, Regulation of protein synthesis at the level of Elongation Factor 2, and Ion Transport across biological Membranes ...
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Arginine adenosine-5′-diphosphoribosylation (ADP-ribosylation) is an enzyme-catalyzed potentially reversible posttranslational changes where the ADP-ribose moiety is transferred from NAD+ towards the guanidino CHR2797 moiety of arginine. proteins with binding companions e.g. toxin-catalyzed ADP-ribosylation of actin at R177 blocks actin polymerization sterically. In case there is the nucleotide-gated P2X7 ion route ADP-ribosylation at R125 near the ligand-binding site causes route Rabbit Polyclonal to SF3B3. gating. Arginine-specific ADP-ribosyltransferases (ARTs) bring a quality R-S-EXE theme that distinguishes these enzymes from structurally related enzymes which catalyze ADP-ribosylation of additional amino acid part chains DNA or little substances. Arginine-specific ADP-ribosylation could be inhibited by little molecule arginine analogues such as for example CHR2797 agmatine or meta-iodobenzylguanidine (MIBG) which themselves can serve as focuses on for arginine-specific ARTs. ...
Some pathogenic species of Clostridium employ the classic enzymatic "AB" binary protein toxins for poisoning cells. Clostridium perfringens, C. difficile, C. spiroforme, and C. botulinum all use similar binary toxins (iota toxin (Ia and Ib), CDT (CDTa and CDTb), CST (CSTa and CSTb), and C2 toxin (C2I and C2II), respectively). They consist of the enzymatic A component, an actin-specific ADP-ribosyltransferase and the B component that binds to the host cell and forms a membrane-spanning pore that functions as the translocation channel for each enzymatic component. The B component translocates the A component into the host cell via the membrane in the acidic endosome. In contrast, the Bacillus anthracis species uses a different binary toxin, which consists of two enzymatic proteins: the lethal (LF) and edema (EF) factors, and a protein translocation channel, PA. The PA heptameric pore structure was revealed to have extremely narrow φ-clamp passageway and a long membrane-spanning channel. ...
B3(Fv)-PE38KDEL recombinant immunotoxin: composed of the heavy chain V(H) region of the carcinoma specific Mab B3 connected by a flexible linker peptide to the corresponding light chain V(L) which is in turn fused to a truncated form of Pseudomonas exotoxin
IL-4 is survival factor for lymphocytes and other hematopoietic cells. Whether there are mechanisms of pro-survival signaling induced by IL-4 apart from PI3K-Akt activation is not fully clear. Our laboratory identified PARP-14, a poly-ADP-ribose polymerase subfamily member, as a Stat6-interacting protein. PARP-14 is highly expressed in lymphoid organs, influences B cell subset ratios as well as the IgA response to antigen, and has intrinsic ADP-ribosyltransferase activity. ADP-ribosyltransferases and PARPs catalyze mono- and poly-ADP-ribosylation, transferring ADP from NAD+ to target proteins. ADP-ribosylation is a post-translational modification used by bacterial exotoxins to impact signal transduction, or, in the case of the mammalian PARP-1, to influence gene transcription and DNA repair or trigger apoptosis. Almost nothing is known about biological roles or mechanisms of action of other mammalian PARPs. We now show that PARP-14 is essential for full survival signaling despite normal Akt ...
Endotoxins are the lipopolysaccharides that are an integral part of the cell membrane of the gram-negative bacteria and become toxin in some conditions. Exotoxins are heat labile, proteinaceous substances or toxoids that are liberated by mostly gram-positive bacteria but sometimes also by gram-negative bacteria into its surrounding. Endotoxins are the associated cell toxins whereas exotoxins are the extracellular diffusible toxins. The molecular weight of endotoxins ranges from 50 to 1000KDa and associated with the lipopolysaccharide complex whereas the molecular weight of the exotoxin is about ten kDa and associated with the protein complex. Endotoxins show stability to heat at about 250°C and do no denature on heating whereas exotoxins are heat labile and get denatured at a minute temperature. Immune reactions get weak when endotoxins attack the cell and have high enzymatic activity but poor antigenicity whereas immune responses get stronger in the case of exotoxins but with no enzymatic ...
Heiko Koch ,Heiko.Koch at ruhr-uni-bochum.de, wrote: , The radioactive label is transferred to the target and the amount of , labeled target is determine in a scintilator. , The reaction is stopped by adding 25 µl 50% TCA to the 100 µl , incubation mixture. , The mixture should be transfered to an Nitrocellulose filter , and the filter must be washed to remove the unbound labeled NAD. , , And this is the problem. Controls with no ribosyltransferase have as , much cpm´s as the tests with ribosyltransferase , , The problem is how to remove the non bound radioactive NAD. How high is your background (i.e. buffer without protein on the filter) ? What amount of incorporated radioactivity do you expect? It is generally important to prewet the filters. If that doesnt help, try separating the protein from nonincorporated NAD by SDS gel electrophoresis. This method is obviously not suitable for large numbers of samples but it should help you to pinpoint the problem. Good luck, --Cornelius. -- /* ...
A range of 3-oxybenzamide compounds and related quinazolinone compounds are disclosed which can act as potent inhibitors of the DNA repair enzyme poly(ADP-ribose) polymerase or PARP enzyme (EC 2.4.2.3
A phase I protocol has been initiated to investigate the treatment related toxicity of immunotoxin treatment with an antibody targeted to the epithelial cell marker EGP2 (ESA/Ep-CAM), conjugated to pseudomonas exotoxin A (PE). A total of 27 patients with antigen positive epithelial tumors were treated with up to 8 injections of the immunoconjugate, given every second week. On the currrent dose level, 6.5 ng/kg, one patient experienced dose limiting toxicity (DLT), a grade 4 elevation in liver enzymes after the first administration of the immunotoxin. No other serious adverse events have been associated with the study treatment ...
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The Pseudomonas exotoxin (or exotoxin A) is an exotoxin produced by Pseudomonas aeruginosa. It inhibits elongation factor-2. It does so by ADP-ribosylation of EF2. This then causes the elongation of polypeptides to cease. (The mechanism of the toxin is similar to that of Diphtheria toxin.) It has been investigated as a treatment for hepatitis B and cancer. Yates SP, Taylor PL, Jørgensen R, et al. (February 2005). "Structure-function analysis of water-soluble inhibitors of the catalytic domain of exotoxin A from Pseudomonas aeruginosa". Biochem. J. 385 (Pt 3): 667-75. doi:10.1042/BJ20041480. PMC 1134741 . PMID 15458385. Yates SP, Merrill AR (May 2004). "Elucidation of eukaryotic elongation factor-2 contact sites within the catalytic domain of Pseudomonas aeruginosa exotoxin A". Biochem. J. 379 (Pt 3): 563-72. doi:10.1042/BJ20031731. PMC 1224111 . PMID 14733615. Hafkemeyer P, Brinkmann U, Brinkmann E, Pastan I, Blum HE, Baumert TF (May 2008). "Pseudomonas exotoxin antisense RNA selectively kills ...
A number of mouse and rat cells and their virus-transformed counterparts were tested for sensitivity to Pseudomonas aeruginosa exotoxin A (PEA). In each case, the transformed cells were considerably less sensitive than were the nontransformed cells. In the presence of trifluoperazine, N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide, or retinoic acid, the transformed cells became as sensitive as the nontransformed cells, whereas these drugs had little or no effect on the sensitivity to PEA of the nontransformed cells. Temperature-sensitive virus-transformed normal rabbit kidney cells were sensitized to PEA by N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide, when these cells were grown as the transformed phenotype, whereas the nontransformed phenotype could not be sensitized. The possibility is discussed that upon malignant transformation a process which is dependent upon calmodulin or protein kinase C strongly decreases the sensitivity of the cells to PEA.. ...
This invention relates to the production and use of recombinant Pseudomonas-derived toxins modified to increase their toxicity and potency in therapy. More particularly, the invention relates to certain deletions in domain II of the amino acid sequence of Pseudomonas exotoxin the domain which relates to the toxins natural proteolytic processing.
Background: The C3bot1 protein (~23 kDa) from Clostridium botulinum ADP-ribosylates and thereby inactivates Rho. C3bot1 is selectively taken up into the cytosol of monocytes/macrophages but not of other cell types such as epithelial cells or fibroblasts. Most likely, the internalization occurs by a specific endocytotic pathway via acidified endosomes. Methodology/Principal Findings: Here, we tested whether enzymatic inactive C3bot1E174Q serves as a macrophage-selective transport system for delivery of enzymatic active proteins into the cytosol of such cells. Having confirmed that C3bot1E174Q does not induce macrophage activation, we used the actin ADP-ribosylating C2I (~50 kDa) from Clostridium botulinum as a reporter enzyme for C3bot1E174Q-mediated delivery into macrophages. The recombinant C3bot1E174Q-C2I fusion toxin was cloned and expressed as GST-protein in Escherichia coli. Purified C3bot1E174Q-C2I was recognized by antibodies against C2I and C3bot and showed C2I-specific enzyme activity ...
Dr. Onda is focusing on the pre-clinical development of recombinant immunotoxins (RITs) as new immunotherapy reagents. RITs are genetically modified forms of Pseudomonas exotoxin A that are targeted to cancer cells by the Fv portion of antibodies. These RITs are now in clinical trials and have produced many complete remissions in cancer. As a staff scientist, Dr. Onda uses protein engineering to make these proteins more useful in patients by decreasing their immunogenicity so more treatment cycles can be given before antibodies develop in the patients. New RITs were designed by identifying and silencing the major B cell epitopes. These new RITs are being developed for clinical trials.. ...
Nare Bandaranayake is raising funds for Cancer Research UK. She is running the Race for Life in Regents Park this May 31st.. Nare says; "In 2011, I ran (well, walked) this race in the memory of my best friends father who passed away from pancreatic cancer that year. Since then the spectre of cancer has come closer and closer to my own home, and in February 2013, my mother was diagnosed with breast cancer. Since then, we have had a number of close friends been diagnosed with various forms of this awful disease - lung, liver, duodenum, prostate, throat and even tongue.". To donate click here. ...
Seagate is launching their 16 TB CMR (conventional magnetic recording) helium drives today under two product lines - the Exos X for datacenter usage, and the IronWolf / IronWolf Pro for NAS units. The company has been actively shipping the Exos X drives to hyperscale customers, and todays launch is geared more towards the retail market. Similar to the currently available 14TB drives from Seagate, the new 16TB variants also use TDMR (two-dimensional magnetic recording) technology for the heads. The Exos X16 is a 3.5 7200 RPM drive with SED (self-encrypting drive) options. It is currently the leading capacity point available across all HDD vendors, but, not the first 16 TB drive publicly announced - that credit goes to Toshibas MG08 series launched in January 2019. Similar to Toshibas MG08 series, the Seagate 16TB drives also use nine platters to achieve the capacity point.. Seagate claims that the new Exos X16 delivers 33% additional storage per rack compared to the 12 TB variants - thereby ...
If youre growing Cole crops such as cabbage, broccoli, kale, collards, and brussels sprouts, your garden is probably a habitat for the cabbage butterfly and its troublesome offspring, the infamous cabbage worm. Identifying Cabbage Butterflies at Work Youve seen the […]
Dual B- and T-cell de-immunization of recombinant immunotoxin targeting mesothelin with high cytotoxic activity. See Mazor et al.
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Poly(ADP-ribose) polymerase-1 (PARP-1) is a member of the PARP enzyme family consisting of PARP-1 and several recently identified novel poly(ADP-ribosylating ...
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The global Immunotoxins market is valued at USD XX million in 2016 and is expected to reach USD XX million by the end of 2022, growing at a CAGR of XX% between 2016 and 2022
Hi, as task #1 ist a one time task you can also send my a list (all contributions of Fale I think) and I let my bot do the work. If you are planing to create a internationalisation bot of your own you should add more than just one task, way more. And it is really tricky to avoid all the problems. But as you are a native Italian Speaker you can help me improve my bot in this language or I can borrow you code unfortunately I write in a totally differen language. --Schlurcher (talk) 21:48, 23 November 2009 (UTC ...
ADP-ribose) synthetase and mono(ADP-ribosyl)transferase". The Journal of Biological Chemistry. 267 (3): 1569-75. PMID 1530940. ...
... 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 ...
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 ...
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 ...
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) ...
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 ...
... 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 ...
... 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 --- ...
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). " ...
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 ...
... 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 ...
... 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 ...
... 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 ...
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 ...
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 ...
transferases. Ribose. ADP-ribosyltransferase. *NAD+:diphthamide ADP-ribosyltransferase *Diphtheria toxin. *NAD(P)+:arginine ADP ... Dempski RE, Imperiali B (December 2002). "Oligosaccharyl transferase: gatekeeper to the secretory pathway". Curr Opin Chem Biol ... oligosaccharyl transferase complex) the newly synthesized protein is transported across the membrane (gray) into the interior ... "Structure of the mammalian oligosaccharyl-transferase complex in the native ER protein translocon". Nat. Commun. (5): 3072. ...
transferases. Ribose. ADP-ribosyltransferase. *NAD+:diphthamide ADP-ribosyltransferase *Diphtheria toxin. *NAD(P)+:arginine ADP ... The CTA1 fragment catalyses ADP-ribosylation of the Gs alpha subunit (Gαs) proteins using NAD. The ADP-ribosylation causes the ... The A1 portion of the chain (CTA1) is a globular enzyme payload that ADP-ribosylates G proteins, while the A2 chain (CTA2) ... CTA1 is then free to bind with a human partner protein called ADP-ribosylation factor 6 (Arf6); binding to Arf6 drives a change ...
transferases. Ribose. ADP-ribosyltransferase. *NAD+:diphthamide ADP-ribosyltransferase *Diphtheria toxin. *Pseudomonas exotoxin ...
transferases. Ribose. ADP-ribosyltransferase. *NAD+:diphthamide ADP-ribosyltransferase *Diphtheria toxin. *NAD(P)+:arginine ADP ... In addition, the enzyme transferase shifts a block of 3 glucosyl residues from the outer branch to the other end, and then a α1 ...
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 ...
... is a multifunctional ectoenzyme that catalyzes the synthesis and hydrolysis of cyclic ADP-ribose (cADPR) from NAD+ to ADP- ... transferase activity. • hydrolase activity, acting on glycosyl bonds. • NAD(P)+ nucleosidase activity. • hydrolase activity. • ... ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase), to chromosome 4p15". Cytogenetics and Cell Genetics. 69 (1-2): 38-9. doi: ... ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase): organization, nucleotide sequence and alternative splicing". Gene. 186 (2): ...
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 ...
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 → ...
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 ...
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 ...
transferase activity. • nucleotide binding. • protein kinase activator activity. • 1-phosphatidylinositol-4-phosphate 3-kinase ...
O-acetyl-ADP-ribose could bind poly(ADP-ribosyl)transferases and block poly(ADP ribosyl)ation. Moreover, NAD+ levels in cells ... ribose (1-O-acetyl-ADP-ribose). For comparison, authentic ADP-ribose yielded a predicted mass of 560 m/z. With both ADP-ribose ... 1B). However, to our great surprise, no significant amounts of ADP-ribose were detected (Fig. 1B). Nicotinamide and ADP-ribose ... 3A), consistent with the enzymatic formation of acetyl-ADP-ribose. For comparison, the mass results of an ADP-ribose standard ...
... 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 ...
ADP-ribose) polymerase as derived from crystal structures and mutagenesis. ... Classification: TRANSFERASE * Deposited: 1998-01-16 Released: 1998-05-27 *Deposition author(s): Ruf, A., Schulz, G.E. ... POLY (ADP-RIBOSE) POLYMERASE A 361 Gallus gallus EC#: 2.4.2.30 IUBMB Fragment: CATALYTIC FRAGMENT Gene Name(s): PARP1 Gene View ... THE CATALYTIC FRAGMENT OF POLY(ADP-RIBOSE) POLYMERASE COMPLEXED WITH CARBA-NAD. *DOI: 10.2210/pdb1a26/pdb ...
Terminal Deoxynucleotidyl Transferase-Mediated dUTP Nick End Labeling Assays. Cells were exposed to olaparib (2.5 μmol/L) for ... Inhibition of poly(ADP-ribose) polymerase in tumors from BRCA mutation carriers. N Engl J Med 2009;361:123-34. ... Poly(ADP-ribose): novel functions for an old molecule. Nat Rev Mol Cell Biol 2006;7:517-28. ... ATM Deficiency Sensitizes Mantle Cell Lymphoma Cells to Poly(ADP-Ribose) Polymerase-1 Inhibitors. Chris T. Williamson, Huong ...
... cyclic ADP ribose; cGMP, cyclic GMP; GPX, glutathione peroxidase; GSNO, S-nitroso-L-glutathione; GST, glutathione S-transferase ... Cyclic ADP ribose has been implicated as another second messenger for NO signalling in animals, acting in a cGMP-dependent ... Nitric oxide signalling often operates in mammalian cells through cyclic GMP (cGMP)- and cyclic ADP ribose (cADPR)-dependent ... and cyclic ADP-ribose. Proc Natl Acad Sci USA 95: 10328-10333.. *CrossRef , ...
ADP Ribose Transferases* * Animals * Bacterial Toxins / genetics * Calcium-Binding Proteins* * Clostridium perfringens / ...
Here, two aspects of the activation of the ADP-ribosyltransferase activity of ExoS by 14-3-3 proteins are … ... is a mono-ADP-ribosyltransferase secreted by the opportunistic pathogen Pseudomonas aeruginosa. ExoS requires a eukaryotic ... ADP Ribose Transferases / metabolism* * Bacterial Toxins* * Binding Sites / genetics * Conserved Sequence * Enzyme Activation ... Here, two aspects of the activation of the ADP-ribosyltransferase activity of ExoS by 14-3-3 proteins are examined. Initial ...
Transferase. Ligand. Metal-bindingUniRule annotation. Automatic assertion according to rulesi ... IPR012317 Poly(ADP-ribose)pol_cat_dom. IPR004102 Poly(ADP-ribose)pol_reg_dom. IPR036616 Poly(ADP-ribose)pol_reg_dom_sf. ... IPR012317 Poly(ADP-ribose)pol_cat_dom. IPR004102 Poly(ADP-ribose)pol_reg_dom. IPR036616 Poly(ADP-ribose)pol_reg_dom_sf. ... Poly [ADP-ribose] polymeraseUniRule annotation. Automatic assertion according to rulesi ...
ADP-ribose) synthetase and mono(ADP-ribosyl)transferase". The Journal of Biological Chemistry. 267 (3): 1569-75. PMID 1530940. ...
Poly ADP-Ribose transferases 1 PARP1 DNA damage repair, cancer AMP-Glo Assay ... Polypeptide GalNAc Transferase 1 GALNT1 Glycosylation, neurological disease UDP-Glo Assay Polypeptide GalNAc Transferase 4 ... Blood Group B Transferase GTB Blood type, cell surface antigen UDP-Glo Assay ...
ADP-ribose) polymerase; NAMPT, nicotinamide phosphoribosyl transferase; NMNAT, nicotinamide mononucleotide adenylyl transferase ... ADP) ribose polymerase (PARP) superfamily. PARP enzymes add ADP-ribose moieties onto proteins, using β-NAD+ as substrate. Of ... The addition of poly(ADP-ribose) chains onto proteins (PARsylation) is a post-translational modification that has been ... ADP-ribose)-directed E3 ligase that regulates axin degradation and Wnt signalling. Nat Cell Biol 13: 623- 629 *CrossRef , ...
... 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 ...
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. ...
... glutathione S-transferase; JNK, c-Jun NH2-terminal kinase; PARP, poly(ADP-ribose) polymerase; ERK, extracellular signal- ... Although pro-caspase 3, poly(ADP-ribose) polymerase, and Bcl-XL levels, as well as nucleosomal DNA integrity, were reduced by ... terminal transferase reaction buffer, 0.25 units/liter terminal transferase, 2.5 mm CoCl2, and 2 pmol fluorescein-12-dUTP ( ... Additional studies were performed using purified preparations of bacterially synthesized glutathione S-transferase (GST)-MDA-7 ...
ADP-ribosylation is a protein post-translational modification catalyzed by ADP-ribose transferases (ARTs). ART activity is ... C) Histones are highly ADP-ribosylated upon incubation with NAD+ in nucleo. A Western blot against poly-ADP-ribose was ... A) Mechanism of covalent interaction between boronate and cis-diols of an ADP-ribose modification. Hydroxylamine removes ADP- ... A Western blot against poly-ADP-ribose was performed to monitor incorporation of ADP-ribosylation. ...
ADP Ribose Transferases/secretion, Antibodies; Monoclonal/metabolism, Bacterial Proteins/metabolism/*physiology/*secretion, ...
Mediates the poly(ADP-ribosyl)ation of histones in a HPF1-dependent manner. Involved in the synthesis of ATP in the nucleus, ... Mediates the poly(ADP-ribosyl)ation of APLF and CHFR. Positively regulates the transcription of MTUS1 and negatively regulates ... Mediates serine ADP-ribosylation of target proteins following interaction with HPF1; HPF1 conferring serine specificity. ... ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism. This ...
Categories: ADP Ribose Transferases Image Types: Photo, Illustrations, Video, Color, Black&White, PublicDomain, ...
Lazebnik Y. A., Kaufmann S. H., Desnoyers S., Poirier G. G., Earnshaw W. C. Cleavage of poly(ADP-ribose) polymerase by a ... Glutathione-S-transferase (GST)-TRAIL extracellular domain fusion proteins were produced to analyze TRAIL-induced apoptosis. ... Kaufmann S. H., Desnoyers S., Ottaviano Y., Davidson N. E., Poirier G. G. Specific proteolytic cleavage of poly(ADP-ribose) ... ADP-ribose) polymerase (PARP), and their toxicity was blocked by the caspase inhibitor Z-Val-Ala-Asp(OMe)-CH2 (ZVAD-fmk). The ...
Interaction of the transcription factor YY1 with human poly(ADP-ribosyl) transferase. Biochem Biophys Res Commun 1997; 240: 108 ... Poly(ADP-ribose) polymerase (PARP)-1, an enzyme that catalyzes the attachment of ADP ribose to target proteins, acts as a ... Poly(ADP-ribose) polymerase (PARP)-1 is the principal member of a family of enzymes possessing poly(ADP-ribosylation) catalytic ... Shall S, de Murcia G. Poly(ADP-ribose) polymerase-1: what have we learned from the deficient mouse model? Mutat Res 2000; 460: ...
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 ...
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. ...
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- ...
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 ...
ADP-ribose in the Screening Technologies research area. ... ADP-ribosyl transferases (ADPRTs) catalyze the transfer of ADP- ... ADP-ribosylation is reversible and can be degraded down to a single ADP-ribose unit by poly-ADP-ribose glycohydrolase (PARG) or ... transfer a single ADP-ribose unit to the target residue (MARylation). The poly-ADP-ribose polymerases (polyPARPs) or ... Poly/Mono-ADP Ribose (E6F6A) RmAb recognizes endogenous levels of ADP ribosylated proteins and does not cross-react with other ...
  • Poly(ADP-ribose) polymerase-1 (PARP-1) inhibition is toxic to cells with mutations in the breast and ovarian cancer susceptibility genes BRCA1 or BRCA2 , a concept termed synthetic lethality. (aacrjournals.org)
  • PARP-1 ADP-ribosylates Asp and Glu residues of histone proteins in vitro . (nih.gov)
  • A) in vitro PARP-1 assay effectively ADP-ribosylates histone proteins. (nih.gov)
  • Total histones extracted from HeLa cells (20ug) were incubated with PARP-1 and a short double-stranded DNA molecule with or without NAD+ for 30 minutes at 30°C. The reaction was quenched by freezing and a Western blot against poly-ADP-ribose was performed. (nih.gov)
  • This was evidenced by the fact that chemotherapy agents that synergized with TRAIL ( e.g. , doxorubicin) themselves caused cleavage of caspase-3 and poly(ADP-ribose) polymerase (PARP), and their toxicity was blocked by the caspase inhibitor Z-Val-Ala-Asp(OMe)-CH 2 (ZVAD-fmk). (aacrjournals.org)
  • Poly(ADP-ribose) polymerase (PARP)-1, an enzyme that catalyzes the attachment of ADP ribose to target proteins, acts as a component of enhancer/promoter regulatory complexes. (aacrjournals.org)
  • Poly(ADP-ribose) polymerase (PARP)-1 is the principal member of a family of enzymes possessing poly(ADP-ribosylation) catalytic capacity. (aacrjournals.org)
  • 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)
  • Furthermore, dysregulation of ADP-ribosylation has been linked to diseases including cancers, diabetes, neurodegenerative disorders, and heart failure, leading to the development of therapeutic PARP inhibitors, many of which are currently in clinical trials. (elsevier.com)
  • Recognizes human poly (ADP-ribose) polymerase (PARP). (lsbio.com)
  • Poly (ADP-ribose) polymerase (PARP) catalyzes the post-translational modification of proteins by the addition of multiple ADP-ribose moieties. (genecards.org)
  • PARP transfers ADP-ribose from nicotinamide dinucleotide (NAD) to Glu/Asp residues on the substrate protein. (genecards.org)
  • Poly(ADP-ribose) polymerases (PARP) are a family of enzymes present in eukaryotes, which catalyze the poly(ADP-ribosyl)ation of a limited number of proteins involved in chromatin architecture, DNA repair, or in DNA metabolism, including PARP itself. (ebi.ac.uk)
  • PARP, also known as poly(ADP-ribose) synthetase and poly(ADP-ribose) transferase, transfers the ADP-ribose moiety from its substrate, nicotinamide adenine dinucleotide (NAD), to carboxylate groups of aspartic and glutamic residues. (ebi.ac.uk)
  • Poly(ADP-ribose) polymerase (PARP) inhibitors are strikingly toxic to cells with defects in homologous recombination (HR). The mechanistic basis for these findings is incompletely understood. (pnas.org)
  • Recently we proposed the importance of oxidant-induced DNA strand breakage and activation of the nuclear enzyme poly(ADP-ribose) polymerase (PARP) in the pathogenesis of diabetic endothelial dysfunction. (ahajournals.org)
  • Poly(ADP-ribose) polymerase (PARP) is an abundant nuclear enzyme that has been implicated in the cellular response to DNA injury. (ahajournals.org)
  • The other specimen was snap frozen in liquid nitrogen and stored at -80°C for active caspase-3, poly(ADP-ribose) polymerase (PARP), SLC2A1 and SLC2A3 gene expression analysis. (biomedsearch.com)
  • We analyzed the interleukin-6 (IL-6) levels as an inflammation marker and the expression of caspase-3 and poly (ADP-ribose) polymerase 1 (PARP-1) as apoptosis markers. (molvis.org)
  • Here we report a robust NAD + analog-sensitive approach for PARPs, which allows PARP-specific ADP-ribosylation of substrates that is suitable for subsequent copper-catalyzed azide-alkyne cycloaddition reactions. (sciencemag.org)
  • Using this approach, we mapped hundreds of sites of ADP-ribosylation for PARPs 1, 2, and 3 across the proteome, as well as thousands of PARP-1-mediated ADP-ribosylation sites across the genome. (sciencemag.org)
  • We found that PARP-1 ADP-ribosylates and inhibits negative elongation factor (NELF), a protein complex that regulates promoter-proximal pausing by RNA polymerase II (Pol II). (sciencemag.org)
  • Depletion or inhibition of PARP-1 or mutation of the ADP-ribosylation sites on NELF-E promotes Pol II pausing, providing a clear functional link between PARP-1, ADP-ribosylation, and NELF. (sciencemag.org)
  • This analog-sensitive approach should be broadly applicable across the PARP family and has the potential to illuminate the ADP-ribosylated proteome and the molecular mechanisms used by individual PARPs to mediate their responses to cellular signals. (sciencemag.org)
  • Most of the 17 poly(ADP-ribose) polymerase (PARP) family members encoded in the human genome are enzymes with either mono- or poly(ADP-ribosyl) transferase activities, which covalently link ADP-ribose derived from the oxidized form of nicotinamide adenine dinucleotide (NAD + ) to their target proteins, primarily at glutamate, aspartate, and lysine residues ( 2 ). (sciencemag.org)
  • Poly (ADP-ribose) synthetase (PARP) is a nuclear enzyme activated by strand breaks in DNA, which are caused inter alia by reactive oxygen species (ROS). (sigmaaldrich.com)
  • Icariside II was able to activate caspase-3 and cleaved poly (ADP-ribose) polymerase (PARP) in a time-dependent manner. (harvard.edu)
  • The DNA damage-dependent poly(ADP-ribose) polymerase-2 (PARP-2) is, together with PARP-1, an active player of the base excision repair process, thus defining its key role in genome surveillance and protection. (asm.org)
  • In addition, our data show that PARP activity regulates the DNA binding activity of TRF2 via both a covalent heteromodification of the dimerization domain of TRF2 and a noncovalent binding of poly(ADP-ribose) to the myb domain of TRF2. (asm.org)
  • PARP family members display complex patterns of subcellular localization, thus extending the biological relevance of poly(ADP-ribosyl)ation ( 50 ). (asm.org)
  • In vitro, phenhexyl isothiocyanate (PHITC) increases caspase 3 activity and cleavage of poly(ADP)-ribose polymerase (PARP), inducing caspase-mediated apoptosis in cellular models. (agscientific.com)
  • 2004, 2008), poly(ADP-ribose) polymerase (PARP) overactivation (Racz et al. (420magazine.com)
  • In addition, some PARP family members, which lack conserved residues crucial for polymer elongation, could instead be mono(ADPribose) transferases. (embopress.org)
  • CD38 acts as NAD+ glycohydrolase converting NAD+ into ADP-ribose, as ADP-ribosyl cyclase producing cADPR and as cADPR hydrolase, thus affecting levels of calcium-mobilizing metabolites. (thermofisher.com)
  • Enzymes from the transferase class that catalyze the transfer of acyl groups from donor. (drugbank.ca)
  • Additionally, Hepad reduced MPTP-induced oxidative damage by increasing the expression of anti-oxidant defense enzymes (superoxide dismutase and glutathione S-transferase) and downregulating the levels of nicotinamide adenine dinucleotide phosphate oxidase 4. (mdpi.com)
  • This post-translational modification and the ADP-ribosyltransferases (also known as PARPs) responsible for its synthesis have been found to play a role in nearly all major cellular processes, including DNA repair, transcription, translation, cell signaling, and cell death. (elsevier.com)
  • Gupte R, Liu Z, Kraus WL (2017) PARPs and ADP-ribosylation: recent advances linking molecular functions to biological outcomes. (springer.com)
  • During many cell processes, ADP-ribose is transferred from NAD + onto protein substrates by poly(ADP-ribose) polymerases (PARPs). (sciencemag.org)
  • developed a method to track ribose transfer events and mapped hundreds of sites of ADP-ribosylation for PARPs 1, 2, and 3 across the proteome and genome. (sciencemag.org)
  • Effects of 5-aminoisoquinolinone, a water-soluble, potent inhibitor of the activity of poly (ADP-ribose) polymerase on the organ injury and dysfunction caused by haemorrhagic shock. (sigmaaldrich.com)
  • one was fixed in 4% paraformaldehyde for immunostaining using terminal deoxynucleotidyl transferase dUTP-mediated nick-end labeling (TUNEL) and activated caspase-3. (biomedsearch.com)
  • In this anti-proliferation process, this herb compound rendered the cells susceptible to apoptosis, manifested by enhanced accumulation of sub-G1 cell population and increased the terminal deoxynucleotidyl transferase dUTP nick end labeling (TUNEL)-positive cells. (harvard.edu)
  • The terminal deoxynucleotidyl transferase deoxyuridine triphosphate (dUTP) nick end labeling (TUNEL) demonstrated significantly decreased apoptosis in the CT-administration animals. (jove.com)
  • Cell proliferation was determined by MTT assay and apoptosis induction was evaluated by flow cytometry and terminal deoxynucleotidyl transferase dUTP nick end labeling assay. (sigmaaldrich.com)
  • Together, the data suggest specific Asp/Glu residues are unlikely to be critical for DNA damage repair and rather that this process is likely dependent on ADP-ribosylation of the nucleosomal surface in general. (nih.gov)
  • B) Histone ADP-ribosylation occurs predominantly on Asp/Glu residues. (nih.gov)
  • ADP-ribosylhydrolase 3 from mouse, consisting of 347 amino-acid residues, has been cloned, purified and crystallized. (iucr.org)
  • 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)
  • These include NAD(+)-dependent protein deacetylases, poly(ADP-ribose) polymerases, and transcription factors that affect a large array of cellular functions. (nih.gov)
  • ADP-ribosylation is a protein post-translational modification catalyzed by ADP-ribose transferases (ARTs). (nih.gov)
  • Unfortunately, progress has been hampered by the inherent challenges that stem from the physicochemical properties of ADP-ribose, which as a post-translational modification is highly charged, heterogeneous (linear or branched polymers, as well as monomers), labile, and found on a wide range of amino acid acceptors. (elsevier.com)
  • One molecule of NAD + and one molecule of acetyl-lysine are readily catalyzed to one molecule of deacetylated lysine, nicotinamide, and 1- O -acetyl-ADP-ribose. (pnas.org)
  • Although the existence and nature of the nucleic acid‐like molecule poly(ADPribose) (PAR) has been known for 40 years, understanding its biological functions-originally thought to be only the regulation of chromatin superstructure when DNA is broken-is still the subject of intense research. (embopress.org)
  • 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)
  • Distinct roles for the N- and C-terminal regions in the cytotoxicity of pierisin-1, a putative ADP-ribosylating toxin from cabbage butterfly, against mammalian cells. (biomedsearch.com)
  • Based on a subunit molecular weight of 28 000, its turnover number with arginine as the ADP-ribose acceptor is considerably higher than that of either toxin. (springer.com)
  • 3. The modified cholera toxin of claim 1, which is obtained by site-specific mutagenesis resulting in a mutation of catalytic subunit A which is less active or essentially inactive as determined by assay of ADP-ribosyltransferase activity. (freepatentsonline.com)
  • 7. The improved vaccine of claim 5, wherein the modified cholera toxin has been derived by site-specific mutagenesis resulting in a mutation of catalytic subunit A which has less or essentially no ADP-ribosyltransferase activity. (freepatentsonline.com)
  • The ADP-ribosyltransferase activity required for activation of the cyclase is an intrinsic property of the A 1 peptide of choleragen which is expressed only after the peptide is released from the holotoxin by reduction of a single disulfide bond. (springer.com)
  • CD antigen CD38 is also known as ADP-ribosyl cyclase 1, which belongs to the ADP-ribosyl cyclase family. (news-medical.net)
  • Hepad 1 and 2 remarkably alleviated the enhanced expression of pro-inflammatory cytokines (tumor necrosis factor-α, interleukin-6, inducible nitric oxide synthase, cyclooxygenase-2, macrophage-1, and phosphorylated iκB-α) and apoptotic signals (Bcl-2-associated X protein, caspase-3, and poly [ADP-ribose] polymerase-1). (mdpi.com)
  • arr-2 coded for a protein that shared 54% amino acid identity with the rifampin ADP-ribosylating transferase encoded by the arr-1 gene from Mycobacterium smegmatis DSM43756. (asm.org)
  • PARP4 (Poly(ADP-Ribose) Polymerase Family Member 4) is a Protein Coding gene. (genecards.org)
  • Gene Ontology (GO) annotations related to this gene include enzyme binding and NAD+ ADP-ribosyltransferase activity . (genecards.org)
  • In this Perspective, we discuss the progress that has been made in addressing these challenges, including the recent breakthroughs in proteomics techniques to identify ADP-ribosylation sites, and future developments to provide a proteome-wide view of the many cellular processes regulated by ADP-ribosylation. (elsevier.com)
  • We provide direct evidence that the efficient histone/protein deacetylase reaction is tightly coupled to the formation of a previously unidentified acetyl-ADP-ribose product (1- O -acetyl-ADP ribose). (pnas.org)
  • A unique reaction mechanism involving the attack of enzyme-bound acetate or the direct attack of acetyl-lysine on an oxocarbenium ADP-ribose intermediate is proposed. (pnas.org)
  • We suggest that the reported histone/protein ADP-ribosyltransferase activity is a low-efficiency side reaction that can be explained through the partial uncoupling of the intrinsic deacetylation and acetate transfer to ADP-ribose. (pnas.org)
  • Although pro-caspase 3, poly(ADP-ribose) polymerase, and Bcl- XL levels, as well as nucleosomal DNA integrity, were reduced by combined treatment, cell killing was predominantly nonapoptotic. (aacrjournals.org)
  • It is found primarily in pathogenic microorganisms where it is genetically linked to a distinct class of sirtuins that function as protein ADP-ribosyl transferases [ PMID: 26166706 ]. (ebi.ac.uk)
  • It is assumed, therefore, that the site of ADP-ribosylation in the natural acceptor protein is an arginine or similar amino acid. (springer.com)
  • Exoenzyme S (ExoS) is a mono-ADP-ribosyltransferase secreted by the opportunistic pathogen Pseudomonas aeruginosa. (nih.gov)
  • Western blot analysis of Colo 205 cells treated (+) with combinations of the following treatments as indicated: hydrogen peroxide (500 μM, 5 min), hydrogen peroxide-treated lysates treated with phosphodiesterase 1 (0.5 μg/mL, 4 hr at 37ºC), or with tcPARG (5 μM, 4 hr at 37ºC ) using Poly/Mono-ADP Ribose (E6F6A) Rabbit mAb (upper), or GAPDH (D16H11) XP ® Rabbit mAb #5174 (lower). (cellsignal.com)
  • using Poly/Mono-ADP Ribose (E6F6A) Rabbit mAb (upper), or β-Tubulin (9F3) Rabbit mAb #2128 (lower). (cellsignal.com)
  • We also found that vitamin K as well as novobiocin was much more specific for mono- than poly (ADP-ribosyl) action. (nii.ac.jp)
  • Corda D, Di Girolamo M (2003) Functional aspects of protein mono-ADP-ribosylation. (springer.com)
  • Bütepage M, Eckei L, Verheugd P, Luscher B (2015) Intracellular mono-ADP-ribosylation in signaling and disease. (springer.com)
  • Many of the bacterial mono-ADP-ribosyltransferases (mARTs) are known for their toxicity. (iucr.org)
  • Encodes a protein belonging to the (ADP-ribosyl)transferase domain-containing subfamily of WWE protein-protein interaction domain protein family. (mybiosource.com)
  • Trypan blue dye exclusion was used to assess cell viability, YO-PRO-1 uptake was used to identify cells with P2X 7 -induced pores, and ethenoadenosine antibodies were used to detect ecto-adenosine diphosphate (ADP)-ribosyltransferase (ART) activity. (arvojournals.org)
  • Like choleragen, LT uses guanidino compounds as model ADP-ribose acceptors and catalyzes the ADP-ribosylation of a 42 000 dalton protein in cell membrane prepatations. (springer.com)
  • 3. Induction of tumor cell differentiation : We succeeded in inducing differentiation of teratocarcinoma cells in culture by administrating our new inhibitors of poly (ADP-ribosyl) ation, such as 4-hydroxyquinazoline and arachidonic acid. (nii.ac.jp)
  • The coenzyme NAD and its derivatives are involved in hundreds of metabolic redox reactions and are utilized in protein ADP-ribosylation , histone deacetylation , and in some Ca 2+ signaling pathways. (wikipedia.org)