Relevant bibliographies by topics / '-nucleotidase

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Academic literature on the topic ''-nucleotidase'

Author: Grafiati
Published: 4 June 2021
Last updated: 20 February 2023

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Journal articles on the topic "'-nucleotidase"

1

Darvish, A., R. W. Pomerantz, P. G. Zografides, and P. J. Metting. "Contribution of cytosolic and membrane-bound 5'-nucleotidases to cardiac adenosine production." American Journal of Physiology-Heart and Circulatory Physiology 271, no. 5 (November 1, 1996): H2162—H2167. http://dx.doi.org/10.1152/ajpheart.1996.271.5.h2162.

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The purpose of this study was to evaluate the relative contributions of AMP-specific cytosolic 5'-nucleotidase and ecto-5'-nucleotidase to cardiac adenosine production and its regulation by ADP and Mg2+. 5'-Nucleotidase activity was measured spectrophotometrically in the total homogenate, the 150,000-g supernatant fraction (cytosolic 5'-nucleotidase), and the membrane pellet fraction (ecto-5'-nucleotidase) of dog left ventricles. Increasing [MgCl2] over a range from 0 to 6 mmol/l increased 5'-nucleotidase activity in both the supernatant and pellet; only cytosolic 5'-nucleotidase exhibited an absolute requirement for Mg2+. ADP, (20-480 mumol/l) activated supernatant and inhibited membrane-bound 5'-nucleotidase activity. At 80 mumol/l ADP, 5 mmol/l MgCl2, 100 mumol/l AMP, and pH 7.3, the average 5'-nucleotidase activities of the supernatant vs. pellet were 74% of total and 26% of total, respectively. Total adenosine production in unfractionated samples of ventricular homogenates decreased an average of 73% by specific inhibition of cytosolic 5'-nucleotidase, using antibodies against the cytosolic enzyme, and 46% by specific inhibition of ecto-5'-nucleotidase with alpha, beta-methylene adenosine 5'-diphosphate (AOPCP). These findings support the hypotheses that 1) both cytosolic and ecto-5'-nucleotidase contribute to cardiac adenosine production in dog heart homogenates; 2) AMP-specific cytosolic 5'-nucleotidase activity exceeds ecto-5'-nucleotidase activity at physiological concentrations of ADP, AMP, and Mg2+; and 3) Mg2+ is an important regulator of cardiac adenosine production via activation of both ecto- and AMP-specific cytosolic 5'-nucleotidases.
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2

Stochaj, U., and H. G. Mannherz. "Affinity labelling of 5′-nucleotidases with 5′-p-fluorosulphonylbenzoyladenosine." Biochemical Journal 266, no. 2 (March 1, 1990): 447–51. http://dx.doi.org/10.1042/bj2660447.

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5′-Nucleotidases play an important role in the metabolism of nucleosides; for example, the hydrolysis of AMP generates adenosine, which can modulate a variety of cellular functions. We have used the membrane-bound AMPase from chicken gizzard and a secreted form of these enzymes to analyse their modification by the substrate analogue 5′-p-fluorosulphonylbenzoyladenosine (5′-FSBA). 5′-FSBA irreversibly inactivates 5′-nucleotidases by means of covalent modification of the proteins. ATP, a competitive inhibitor of chicken gizzard and snake-venom 5′-nucleotidase, abolished the inactivation by 5′-FSBA, demonstrating that the inactivation was due to the modification of amino acid residues essential for AMPase activity. We have synthesized radioactive 5′-FSBA, which was employed for the radiolabelling of chicken gizzard 5′-nucleotidase. Incorporation of radioactivity was completely abolished in the presence of ATP, which showed that 5′-FSBA acted by the selective modification of amino acid residues at the active site whereas other potential reactive residues of the protein were not attacked. Limited proteolysis of affinity-labelled chicken gizzard 5′-nucleotidase permitted the identification of digestion products containing the catalytic centre. Pseudo-first-order kinetics indicate that modification of a minimum of one amino acid side chain at the active centre is sufficient to result in inactivation of both chicken gizzard and snake-venom 5′-nucleotidases. Incorporation of the radioactive p-sulphonylbenzoyladenosine moiety parallels the inactivation of 5′-nucleotidase by 5′-FSBA and further substantiated the idea that modification of one amino acid residue at the active centre results in loss of the AMPase activity.
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Headrick, J. P., and R. J. Willis. "5′-Nucleotidase activity and adenosine formation in stimulated, hypoxic and underperfused rat heart." Biochemical Journal 261, no. 2 (July 15, 1989): 541–50. http://dx.doi.org/10.1042/bj2610541.

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Changes in 5′-nucleotidase activity were calculated on the basis of alterations in ATP, ADP, phosphocreatine, Pi, Mg2+, IMP and AMP, determined by using 31P n.m.r. spectroscopy and h.p.l.c., during isoprenaline infusion, graded hypoxia and graded underperfusion in isolated rat heart. Calculated activity changes were compared with the total efflux of purines (adenosine + inosine + hypoxanthine) in order to assess the involvement of various 5′-nucleotidases in formation of adenosine. Purine efflux exhibited an exponential relation with cytosolic [AMP] during isoprenaline infusion and hypoxia (r = 0.92 and 0.95 respectively), supporting allosteric activation of 5′-nucleotidase under these conditions. Purine efflux displayed a linear relation with cytosolic [AMP] during graded ischaemia (r = 0.96), supporting substrate regulation in the ischaemic heart. The calculated activities of membrane-bound ecto-5′-nucleotidase were similar to the observed relations between purine efflux and cytosolic [AMP] in all hearts. The calculated activities of the ATP-activated cytosolic and lysosomal enzymes and of the ATP-inhibited cytosolic 5′-nucleotidase could not explain the observed release of purines under the conditions examined. These results indicate that the kinetic characteristics of the membrane-bound ecto-enzyme are consistent with an important role in the formation of extracellular adenosine, whereas the characteristics of the other 5′-nucleotidases are inconsistent with roles in adenosine formation under the conditions of the present study.
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4

Biswas, Nabanita, Marta Rodriguez-Garcia, Zheng Shen, Sarah G. Crist, Jack E. Bodwell, John V. Fahey, and Charles R. Wira. "Effects of Tenofovir on Cytokines and Nucleotidases in HIV-1 Target Cells and the Mucosal Tissue Environment in the Female Reproductive Tract." Antimicrobial Agents and Chemotherapy 58, no. 11 (August 18, 2014): 6444–53. http://dx.doi.org/10.1128/aac.03270-14.

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ABSTRACTTenofovir (TFV) is a reverse transcriptase inhibitor used in microbicide preexposure prophylaxis trials to prevent HIV infection. Recognizing that changes in cytokine/chemokine secretion and nucleotidase biological activity can influence female reproductive tract (FRT) immune protection against HIV infection, we tested the hypothesis that TFV regulates immune protection in the FRT. Epithelial cells, fibroblasts, CD4+T cells, and CD14+cells were isolated from the endometrium (Em), endocervix (Cx), and ectocervix (Ecx) following hysterectomy. The levels of proinflammatory cytokines (macrophage inflammatory protein 3α [MIP-3α], interleukin 8 [IL-8], and tumor necrosis factor alpha [TNF-α]), the expression levels of specific nucleotidases, and nucleotidase biological activities were analyzed in the presence or absence of TFV. TFV influenced mRNA and/or protein cytokines and nucleotidases in a cell- and site-specific manner. TFV significantly enhanced IL-8 and TNF-α secretion by epithelial cells from the Em and Ecx but not from the Cx. In contrast, in response to TFV, IL-8 secretion was significantly decreased in Em and Cx fibroblasts but increased with fibroblasts from the Ecx. When incubated with CD4+T cells from the FRT, TFV increased IL-8 (Em and Ecx) and TNF-α (Cx and Ecx) secretion levels. Moreover, when incubated with Em CD14+cells, TFV significantly increased MIP-3α, IL-8, and TNF-α secretion levels relative to those of the controls. In contrast, nucleotidase biological activities were significantly decreased by TFV in epithelial (Cx) and CD4+T cells (Em) but increased in fibroblasts (Em). Our findings indicate that TFV modulates proinflammatory cytokines, nucleotidase gene expression, and nucleotidase biological activity in epithelial cells, fibroblasts, CD4+T cells, and CD14+cells at distinct sites within the FRT.
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Skladanowski, A. C., G. B. Sala, and A. C. Newby. "Inhibition of IMP-specific cytosolic 5′-nucleotidase and adenosine formation in rat polymorphonuclear leucocytes by 5′-deoxy-5′-isobutylthio derivatives of adenosine and inosine." Biochemical Journal 262, no. 1 (August 15, 1989): 203–8. http://dx.doi.org/10.1042/bj2620203.

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1. The partially purified IMP-specific cytosolic 5′-nucleotidases from rat liver, polymorphonuclear leucocytes and heart were inhibited by 50% by 2-6 mM-5′-deoxy-5′-isobutylthioadenosine (IBTA) or 7-10 mM-5′-deoxy-5′-isobutylthioinosine (IBTI). IBTA and IBTI inhibited the rat liver and polymorphonuclear-leucocyte enzymes non-competitively. IBTA, but not IBTI, also inhibited the ecto-5′-nucleotidase of polymorphonuclear leucocytes. IBTI was, by contrast, a more potent inhibitor than IBTA of the AMP-specific soluble 5′-nucleotidase from pigeon heart. 2. During 2-deoxyglucose-induced ATP-catabolism in rat polymorphonuclear leucocytes, adenosine formation was inhibited by approx. 80% by 3 mM-IBTA and by approx. 70% by 7 mM-IBTI. 3. The results show that 5′-modified nucleosides are inhibitors of cytosolic 5′-nucleotidases and that they penetrate to inhibit their target enzymes in intact cells. Such inhibitors may be useful to clarify the mechanisms of adenosine formation and to prevent mononucleotide hydrolysis during ATP breakdown.
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Aslam, Nazia, Syeda Fatima, Sofia Khalid, Shahzad Hussain, Mughal Qayum, Khurram Afzal, and Muhammad Hassham Hassan Bin Asad. "Anti-5 ′ -Nucleotidases (5 ′ -ND) and Acetylcholinesterase (AChE) Activities of Medicinal Plants to Combat Echis carinatus Venom-Induced Toxicities." BioMed Research International 2021 (February 4, 2021): 1–10. http://dx.doi.org/10.1155/2021/6631042.

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Echis carinatus is one of the highly venomous snakes of Pakistan that is responsible for numerous cases of envenomation and deaths. In Pakistan, medicinal plants are commonly used traditionally for snakebite treatment because of their low cost and easy availability in comparison with antivenom. The current research is aimed at evaluating the inhibitory activity of Pakistani medicinal plants against acetylcholinesterase and 5 ′ -nucleotidases present in Echis carinatus venom. Acetylcholinesterase and 5 ′ -nucleotidase enzymatic assays were performed at different venom concentrations to check the activity of these enzymes. Methanolic extracts from different parts of plants were used for in vitro determination of their inhibitory activity against 5 ′ -nucleotidases in snake venom. Active methanolic extracts were subsequently fractioned using different solvents, and these fractions were also assessed for their anti-5 ′ -nucleotidase activity. Results of this study exhibited that Eugenia jambolana Willd. ex O. Berg, Rubia cordifolia L., Trichodesma indicum (L.) R. Br., Calotropis procera (Wild.) R. Br., Curcuma longa L., and Fagonia arabica L. were able to significantly ( p > 0.5 ) neutralize the 5 ′ -nucleotidase activity by 88%, 86%, 86%, 85%, 83.7%, and 83%, respectively, compared with a standard antidote (snake venom antiserum). Thus, this study indicates that these plants possess the potential to neutralize one of the toxic enzymatic components of Echis carinatus venom and hence can help to augment the future efforts of developing alternative therapy for the management of snakebites.
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Skladanowski, A. C., R. T. Smolenski, M. Tavenier, J. W. de Jong, M. H. Yacoub, and A. M. Seymour. "Soluble forms of 5'-nucleotidase in rat and human heart." American Journal of Physiology-Heart and Circulatory Physiology 270, no. 4 (April 1, 1996): H1493—H1500. http://dx.doi.org/10.1152/ajpheart.1996.270.4.h1493.

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Intracellular AMP hydrolysis probably produces sufficient adenosine in ischemic heart to exert physiological activity. Because data on adenosine-producing systems in human heart are scarce, we measured 1) formation of adenosine (catabolites) in ischemic human heart slices and 2) cytoplasmic 5'-nucleotidase activity in human left ventricle. We also measured the latter in rat ventricle and cardiomyocytes. During the first 5 min of incubation, adenosine production in slices (n = 5) equaled 26 +/- 10 (SD) nmol.min-1.g wet wt-1, and total AMP content was 0.81 +/- 0.46 mM. Cytoplasmic IMP-preferring 5'-nucleotidase activity in homogenates of human heart (N-II, 167 +/- 78 mU/g, n = 23) was significantly higher than that of the AMP-preferring one (N-I, 107 +/- 61 mU/g, n = 24). Both isozymes were two to three times more active in rat heart than in human heart. Rat cardiomyocytes contained comparable amounts of the two 5'-nucleotidases. Kinetics of N-I isolated from explanted human heart displayed features similar to the enzyme from animal heart, with a Michaelis constant of 1.5 mM under maximally stimulated conditions. This form can provide the amount of adenosine found in ischemic slices. In conclusion, human heart shows lower cytosolic 5'-nucleotidase activities than rat heart. Nevertheless, cytosolic 5'-nucleotidase activity in human heart can easily account for adenosine formation during ischemia.
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Borowiec, Agnieszka, Katarzyna Lechward, Kinga Tkacz-Stachowska, and Andrzej C. Składanowski. "Adenosine as a metabolic regulator of tissue function: production of adenosine by cytoplasmic 5'-nucleotidases." Acta Biochimica Polonica 53, no. 2 (June 12, 2006): 269–78. http://dx.doi.org/10.18388/abp.2006_3339.

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Adenosine is a product of complete dephosphorylation of adenine nucleotides which takes place in various compartments of the cell. This nucleoside is a significant signal molecule engaged in regulation of physiology and modulation of the function of numerous cell types (i.e. neurons, platelets, neutrophils, mast cells and smooth muscle cells in bronchi and vasculature, myocytes etc.). As part a of purinergic signaling system, adenosine mediates neurotransmission, conduction, secretion, vasodilation, proliferation and cell death. Most of the effects of adenosine help to protect cells and tissues during stress conditions such as ischemia or anoxia. Adenosine receptors and nucleoside transporters are targets for potential drugs in many pathophysiological situations. The adenosine-producing system in vertebrates involves a cascade dephosphorylating ATP and ending with 5'-nucleotidase (EC 3.1.3.5) localized either on the membrane or inside the cell. In this paper the cytoplasmic variants of 5'-nucleotidase are broadly characterized as well as their clinical relevance. The role of AMP-selective 5'-nucleotidase (cN-I) in the heart, skeletal muscle and brain is highlighted. cN-I action is crucial during ischemia and important for the efficacy of some nucleoside-based drugs and in the regulation of the substrate pool for nucleic acids synthesis. Inhibitors used in studying the roles of cytoplasmic and membrane-bound 5'-nucleotidases are also described.
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Piec, G., and M. Le Hir. "The soluble ‘low-Km’ 5′-nucleotidase of rat kidney represents solubilized ecto-5′-nucleotidase." Biochemical Journal 273, no. 2 (January 15, 1991): 409–13. http://dx.doi.org/10.1042/bj2730409.

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A soluble ‘low-Km’ 5′-nucleotidase has been described previously in several organs. It has been presumed to be of cytosolic origin and thus to play a role in the intracellular production of adenosine. Its catalytic properties are similar to those of the ecto-5′-nucleotidase of cell membranes. In the present study we compared molecular properties of the two enzymes in the kidney of the rat. The Mr of the main peak of soluble ‘low-Km‘ 5′-nucleotidase in gel-filtration chromatography was similar to that of the ecto-5′-nucleotidase solubilized by a phosphatidylinositol-specific phospholipase C from renal brush-border membranes. In phase-partition experiments using Triton X-114, the soluble enzyme appeared to be hydrophobic. Its hydrophobicity was decreased on treatment with a phosphatidylinositol-specific phospholipase C, suggesting that the soluble ‘low-Km’ 5′-nucleotidase contains the phosphatidylinositol anchor which is characteristic for the ecto-enzyme. An anti-ecto-5′-nucleotidase antiserum provoked an almost complete inhibition of the soluble enzyme. Immunoblotting using anti-ecto-5′-nucleotidase antiserum revealed in the high-speed supernatants a polypeptide with a similar Mr to the subunit of the ecto-5′-nucleotidase. The soluble ‘low-Km’ 5′-nucleotidase, like the ecto-5′-nucleotidase, bound specifically to concanavalin A. We conclude that the soluble ‘low-Km’ 5′-nucleotidase is not a cytosolic enzyme, but that it most probably originates from the solubilization of the ecto-5′-nucleotidase, and that it therefore cannot participate in the intracellular production of adenosine.
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Moses, G. C., J. F. Tuckerman, and A. R. Henderson. "Biological variance of cholinesterase and 5'-nucleotidase in serum of healthy persons." Clinical Chemistry 32, no. 1 (January 1, 1986): 175–77. http://dx.doi.org/10.1093/clinchem/32.1.175.

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Abstract We measured cholinesterase (EC 3.1.1.8) and 5'-nucleotidase (EC 3.1.3.5) activities in serum of 24 healthy laboratory staff during 12 months. Overall mean activities ranged from 5.3 to 13.4 kU/L for cholinesterase and 5.4 to 9.8 U/L for 5'-nucleotidase. Cholinesterase activity was significantly (p less than 0.01) higher for men than for women. 5'-Nucleotidase activity was significantly (p = 0.01) higher for subjects 40 years or older than for those younger than 40, but was not different with respect to sex or time of year. Average intra- and interindividual variances (SD2) were 0.38 and 2.69 for cholinesterase and 1.41 and 0.97 for 5'-nucleotidase, respectively. Intra- to interindividual standard deviation ratios were 0.38 for cholinesterase and 1.21 for 5'-nucleotidase. Average within-run analytical variances were 0.13 and 0.3 (4% and 13% of total variance) for cholinesterase and 5'-nucleotidase, respectively. The importance of these findings in regards to diagnostic interpretation of serum cholinesterase and 5'-nucleotidase results is discussed.
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Dissertations / Theses on the topic "'-nucleotidase"

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SIEGFRIED, GERALDINE. "Modulation de l'activite 5'-nucleotidase tubulaire renale." Paris 7, 1996. http://www.theses.fr/1996PA077134.

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Dans le rein, la 5'-nucleotidase est principalement localisee au niveau de la bordure en brosse apicale des cellules tubulaires proximales. Elle est ancree dans le feuillet membranaire externe par un glycosyl-phosphatidyl-inositol. Elle est l'enzyme cle d'une cascade faisant intervenir diverses ectoenzymes conduisant a la formation d'adenosine par l'hydrolyse des nucleotides adenyliques (atp, adp, et ampc). La degradation de l'ampc extracellulaire luminal suivie de la capture d'adenosine sont indispensables a l'effet inhibiteur de l'ampc extracellulaire sur la reabsorption proximale de phosphate. L'ampc luminal ajoute au fluide tubulaire sous l'influence de la pth (ampc nephrogenique) participe a son effet phosphaturique et n'est pas seulement un marqueur de l'activite de cette hormone. La 5'-nucleotidase, en hydrolysant l'amp ou en produisant de l'adenosine, est a la base de ces regulations physiologiques. Cette etude presente differents aspects de la modulation de l'activite de l'ecto-5'-nucleotidase tubulaire renale, et les consequences de cette modulation de l'activite du cotransport sodium-phosphate: (1) dans les cellules ok, la pth stimule l'activite 5'-nt en impliquant une synthese proteique et l'activation de la pkc. Cette modulation se traduit de maniere fonctionnelle en termes de modulation de transport de phosphate. La 5'-nt participe ainsi a l'effet phosphaturique de la pth. (2) le monoxyde d'azote produit au cours d'une ischemie renale transitoire inhibe l'activite 5'-nt en se liant a ses groupements sh par un mecanisme de s-nitrosylation. Cette inhibition attenue l'effet inhibiteur de l'ampc extracellulaire sur le cotransport sodium-phosphate. L'expression, par infection stable, de l'ecto-5'-nt humaine dans les cellules mxx depourvues d'activite ecto5'-nt endogene permet d'etablir une lignee de cellules renales. L'enzyme est distribuee majoritairement au niveau de la membrane apicale des cellules. Son activite n'affecte ni l'activite du transport de phosphate ni son adaptation a la depletion phosphatee
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Roever, Lisa. "Inhibitor Studies for 5’-ecto-nucleotidase (CD73)." Ohio University / OhioLINK, 2019. http://rave.ohiolink.edu/etdc/view?acc_num=ohiou1553892946798977.

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Zanin, Rafael Fernandes. "Investigação das ectonucleotidases na diferenciação de macrófagos e na ativação de plaquetas : o papel da homocisteína." reponame:Biblioteca Digital de Teses e Dissertações da UFRGS, 2010. http://hdl.handle.net/10183/61004.

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Os nucleotídeos extracelulares modulam uma variedade de ações biológicas via ativação de receptores purinérgicos. Esses efeitos são controlados pela ação de ectonucleotidases, tais como as E-NTPDases e a ecto-5´-NT/CD73, as quais hidrolisam o ATP até adenosina no meio extracelular. Nas células imunes, o ATP pode atuar como uma molécula sinalizadora de perigo enquanto a adenosina, um produto da degradação do ATP, serve como um mecanismo que controla/limita a inflamação. Já, no sistema vascular, o ADP é um agonista fisiológico envolvido na hemostasia normal e na trombose. Considerando que os macrófagos são elementos chave para processos inflamatórios e quando estímulados exibibem um fenótipo pró-inflamatório/defesa (clássico/M1) ou antiinflamatório/reparatório (alterantivo/M2). O objetivo foi investigar a atividade e expressão das ectonuclotidases em diferentes fenótipos de macrófago e avaliar o efeito da homocisteína sobre essas enzimas em macrófagos e plaquetas.. As análises da diferenciação de macrófagos em fenótipo próinflamatório/ M1 e antiinflamatório/M2 revelaram presença igual de receptores purinérgicos. Entretanto, mudança no perfil das ectonucleotidases como E-NTPDase1, E-NTPDase3 e ecto-5’- nucleotidase foram encontradas, sugerindo que os macrófagos devem alterar a casacata purinérgica durante a ativação fenotípica. No fenótipo pró-inflamatório/M1 houve uma diminuição na hidrólise de ATP, sugerindo um acúmulo do mesmo, enquanto no fenótipo antiinflamatório/M2 as enzimas conduzem para uma progressiva diminuição nas concentrações de nucleotídeos (ATP) e aumento na disponibilidade de adenosina. Já os macrófagos expostos a homocisteína apresentaram uma polarização para o fenótipo pro-inflamatório (M1) e nossos achados sugerem o envolvimento da ENTPDase3 e da ecto-5’-nucleotidase em macrófagos nas complicações inflamatórias associadas a homocisteína. Nas plaquetas, as quais são elementos fundamentais no processo de trombogênese, a homocisteína causou uma diminuição na hifrólise de ADP. Essa elevação no nível de ADP ao redor das plaquetas devido a inativação das ectonucleotidases, causada pela homocisteína, deve estar contribuindo para o aumento do risco trombótico descrito em pacientes com hiperhomocisteinemia. Além disso, os animais que receberam homocisteína tiveram um aumento na agregação plaquetária induzida por ADP. Em conclusão, os resultados do presente estudo reforçam o envolvimento do sistema purinérgico em processos inflamatórios/trombóticos e apontam parar o desenvolvimeto de tratamentos para doenças inflamatórias/trobóticas.
Extracellular nucleotides modulate a variety of biological actions via purinergic receptor activation. These effects are modulated by ectonucleotidases, such as ENTPDases and ecto-5´- NT/CD73, which hydrolyze ATP to adenosine in the extracellular milieu. In the cells of the immune system, the ATP can act as danger signaling whereas adenosine, the ATP breakdown product, serves as a negative feedback mechanism to limit inflammation. Already, in the vasculare system, the ADP is a physiological agonist involved in normal hemostasis and thrombosis. Since, macrophages are key to inflammatory process, that depending on the microenvironmental stimulation exhibit proinflammatory/ defense (classical/M1) and antiinflammatory/reparatory (alternative/M2) phenotype. The objective of this study was investigate the activity and expression of the ectonuclotidases in differential macrophage phenotype and evaluate the homocysteine (Hcy) effects on theses enzymes in macrophages and platelets. . The analysis of differential macrophages in phenotype proinflamatory/ M1 and antiinflamatory/M2 showed the same expression to P1 and P2 purinoreceptors. However, change profile of the ectonucleotidases as E-NTPDase1, E-NTPDase3 and ecto-5’- nucleotidase enzymes in macrophages during phenotypic differentiation were found, suggesting that macrophages must alter the purinergic cascade during macrophages differentiation phenotypic. In the pro-inflamatory/M1 phenotype the ATP hydrolysis decreased, suggesting ATP accumulation. On the other hand, the antiinflamatory/M2 phenotype the enzymes lead to a progressive decrease in nucleotides (ATP) concentrations and an increase the adenosine availability. Already, the macrophages exposed to Hcy present a polarized pro-inflammatory profile (M1) and our findings suggest the involvement of the E-NTPDase3 and ecto-5’-nucleotidase in the inflammatory complications associates to homocysteine. In the Platelets, which are fundamental elements to the thrombogenesis process, the homocysteine decreased ADP hydrolysis. This elevation of ADP around of the platelets due inactivating of ectonucleotidase, probably by the indirect action of Hcy, may be contributing to increase thrombotic risk described in individuals with hyperhomocysteinemia. In addition, the animals that received Hcy treatment potentiate platelet aggregation induced by ADP. In conclusion, in the present study the results reinforce purinergic signaling involvement in inflammatory/thrombosis process and point to development of treatments to inflammatory/thrombotic diseases.
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4

ZEKRI, MUSTAPHA. "Heterogeneite structurale et fonctionnelle de la 5-nucleotidase." Nantes, 1990. http://www.theses.fr/1990NANT2056.

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La 5-nucleotidase cytosolique de foie de buf a ete purifiee a l'homogeneite par une double chromatographie d'affinite sur concanavaline a sepharose, puis 5-amp sepharose. L'enzyme purifie est un heterodimere de 130000 daltons avec deux sous-unites de 57000 et 65000 daltons, contrairement a l'isoenzyme membranaire qui presente une structure homodimerique (140000 daltons). L'enzyme hydrolyse specifiquement les 5-mononucleotides et le 5-cmp serait son meilleur substrat. Son activite maximale intervient a ph 7,5 et 9,5, et necessite l'apport de cations divalents exogenes. Par contre, la 5-nucleotidase membranaire ne possede qu'un seul ph optimum a 7,5. L'etude des interactions des diverses lectines avec le glycanne de la 5-nucleotidase cytosolique prouve sa nature glycoproteique, et suggere une structure glycannique differente de l'enzyme membranaire. Cependant, les anticorps produits contre la 5-nucleotidase membranaire reconnaissent et inhibent l'enzyme cytosolique. Cette reactivite croisee demontre l'existence d'epitopes communs proches du site catalytique. Par ailleurs, nous avons realise une etude de l'effet de la phospholipase c specifique du phosphatidylinositol (pi-plc) sur l'attachement de la 5-nucleotidase a la membrane plasmique. Nous avons ainsi montre que seule une faible proportion de la molecule est convertie en une forme soluble par ce traitement. De plus, nous avons note une grande variation de sensibilite a l'action de la pi-plc entre la 5-nucleotidase et la phosphatase alcaline, dependante de la nature du tissu et de l'espece etudiee. Les differences de pourcentage de solubilisation des deux enzymes par la pi-plc pourraient etre dues a des raisons d'ordre sterique liees a la topographie des proteines dans la membrane plasmique ou a un polymorphisme d'ancrage de ces proteines dans la membrane
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5

Bavaresco, Luci. "Estudo do papel da ecto-5'-nucleotidase/CD73 na proliferação de gliomas." reponame:Biblioteca Digital de Teses e Dissertações da UFRGS, 2008. http://hdl.handle.net/10183/12713.

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Os gliomas são os tumores primários mais comuns e devastadores que atingem o sistema nervoso central. O prognóstico para pacientes com estes tumores é ruim, e apesar de intensos esforços para o desenvolvimento de novas terapias, agentes efetivos ainda não estão disponíveis. A ecto-5‟-nucleotidase/CD73 (ecto-5‟-NT/CD73) regula os níveis extracelulares de AMP e adenosina, a qual tem sido amplamente descrita como fator indutor de proliferação celular. A ecto-5‟-NT/CD73 per se tem sido relatada como proteína envolvida no controle dos processos de crescimento, maturação, diferenciação, invasão e migração celular, além do processo de formação de metástases. No presente estudo nós avaliamos a atividade enzimática e as funções da ecto-5‟-NT/CD73 durante o processo proliferativo em linhagens de glioma C6 e U138-MG. Os resultados obtidos demonstram que ocorre um aumento da atividade da ecto-5‟-NT/CD73 com o aumento da confluência celular, quer seja esta obtida por semeadura de crescentes densidades celulares ou por crescentes dias de cultivo, em ambas as linhagens estudadas. As análises por RT-PCR e citometria de fluxo revelaram um aumento dos níveis de mRNA e proteína da ecto-5‟-NT/CD73, respectivamente quando comparadas culturas confluentes com culturas subconfluentes em linhagem de glioma humano U138-MG. Nesta mesma linhagem, o tratamento com 1 M de APCP, inibidor competitivo da ecto-5‟-NT/CD73 causou uma significativa redução de 20% na proliferação celular, enquanto a adenosina aumentou este processo em 25%. Por outro lado, 1 mM e 3 mM de AMP reduziram a proliferação em 29% e 42% respectivamente. Além disso, o silenciamento estável da ecto-5‟-NT/CD73 pela técnica do RNAi reduziu o processo de migração celular na linhagem de glioma humano U138-MG. Em conjunto, Estes resultados sugerem a participação da ecto-5‟-NT/CD73 na proliferação celular, sendo este processo desencadeado pela geração de adenosina (fator proliferativo), pela remoção dos níveis citotóxicos de AMP e pela participação per se da ecto-5‟-NT/CD73 como proteína de adesão.
Malignant gliomas are the most common and devastating primary tumors in the central nervous system. Despite treatment, patients with these tumors have a poor prognosis. Ecto-5‟-nucleotidase/CD73 (ecto-5‟-NT/CD73) may regulate the extracellular AMP and adenosine levels, which have been described as proliferation factor. The participation of ecto-5‟-NT/CD73 per se has been proposed as a proliferative factor, being involved in the control of cell growth, maturation, differentiation, invasion, migration and metastases processes. In the present study, we evaluate the ecto-5‟-NT/CD73 activity and functions in rat C6 and human U138-MG glioma cell lines proliferation process. Crescent confluences and culture times leads to an increase on ecto-5‟-NT/CD73 activity in both C6 and U138-MG glioma cells. RT-PCR analysis and flow cytometry showed a significant increase on ecto-5‟-NT/CD73 mRNA and protein levels respectively, when compared confluent cultures with subconfluent one in human U138-MG glioma cells. Treatment with 1 M APCP, a competitive ecto-5‟-NT inhibitor, caused a significant reduction in glioma cell proliferation of 20% for U138-MG glioma cell line. In addition, 100 M adenosine increases cell proliferation in 25% and AMP 1m M and 3 mM decrease U138-MG glioma cells proliferation in 29% and 42% respectively. The stable silencement of ecto-5‟-NT/CD73 by RNAi technique reduces cell migration in human U138-MG glioma cell line. Taken together these results suggest the participation of ecto-5‟-NT/CD73 in cell proliferation, being this process dependent of enzymatic activity generating adenosine, a proliferative factor and removing toxic levels of AMP, as well as a function as adhesive molecule.
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Knöfel, Thomas. "Röntgenstrukturanalyse der 5'-Nucleotidase aus Escherichia coli mit dinuklearem Metallzentrum." [S.l. : s.n.], 2000. http://www.diss.fu-berlin.de/2000/131/index.html.

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Osborne, Foy Naomi. "Over-Expression of Ecto-5'-Nucleotidase in Pig Endothelial Cells." Thesis, Imperial College London, 2007. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.487200.

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Ecto-5'-nucleotidase (E5'N) is an endothelial surface enzyme that controls conversion of extracellular nucleotides into immunosuppressive adenosine. Species differences and especially lO-fold higher activity of E5'N in human endothelial cells (EC) than in pig EC could be important barrier for xenotransplantation.The major aim ofmy thesis is evaluation whether expression of human E5'N on pig EC is able to attenuate cell death mediated by components ofhuman blood responsible for delayed xenograft rejection (DXR). A pig cell line was transfected with human E5'N and efficiency assessed with flow cytometry and nucleotide breakdown assays using cell monolayers and lysates. Transfected cells were >95% positive for human E5'N/There was a massive increase in E5'N activity in transfected pig EC lysates and intact cells using extracellu~ar AMP as the substrate. Adenosine production from the breakdown of ATP was also significantly higher in transfected cells, proving E5'N to be the rate-limiting enzyme in adenosine production by pig EC. Incubation of transfected cells with AMP showed a time-dependent induction of the antiapoptotic protein Bcl-2 mediated via AI receptors, and subsequent protection of these cells from hydrogen peroxide-mediated apoptosis through AI receptors. Human natural killer (NK) cells were significantly less cytotoxic towards transfected than non-transfected pig EC. This effect was abrogated by an inhibitor of E5'N and mimicked by prior incubation of NK cells with adenosine. Supernatants from transfected cells also significantly inhibited platelet aggregation and expression of E5'N attenuated platelet adhesion to EC compared to nontransfected cells. However, transfection with E5'N did not protect cells from antibody and complement-mediated cytotoxicity. Functional expression of human E5'N in pig EC provided significant protection from apoptosis, NK cell-mediated lysis and platelet adhesion and aggregation, the main mechanisms of xenograft r~jection once hyperacute rejection has been overcome. E5'N is thus a potential candidate for. engineering of transgenic animals for xenotransplantation.
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McMillen, Lyle, and l. mcmillen@sct gu edu au. "Isolation and Characterisation of the 5'-Nucleotidase from Escherichia coli." Griffith University. School of Biomolecular and Biomedical Science, 2001. http://www4.gu.edu.au:8080/adt-root/public/adt-QGU20030226.153545.

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Escherichia coli 5'-nucleotidase is a periplasmically localised enzyme capable of hydrolysing a broad range of substrates, including all 5'-ribo- and 5'-deoxyribonucleotides, uridine diphosphate sugars, and a number of synthetic substrates such as bis (r-nitrophenyl) phosphate. The enzyme has been shown to contain at least one zinc ion following purification, and to have two metal binding sites in the catalytic cleft. 5'-Nucleotidase activity is significantly stimulated by the addition of particular divalent metal ions, most notably cobalt which results in a 30-50 fold increase in activity. Significant sequence homology between the E. coli 5'-nucleotidase and members of the Ser/Thr protein phosphatase family in the catalytic site has lead to 5'-nucleotidase being included in this protein family. This thesis describes the development of a rapid purification methodology for milligram quantities of 5'-nucleotidase, and the investigation of a number of physical and biochemical properties of the enzyme with the aim of comparing these properties to those of certain catalytic site mutants. The molecular weight of the mature protein was estimated as 58219 daltons, with a specific activity for 5'-AMP, in the presence of 4 mM Co2+ and 13 mM Ca2+ at pH 6.0, of 730 mmol/min/mg. The presence of up to two zinc ions associated with the purified enzyme was observed using ICP-ES analysis, suggesting both metal ion binding sites are occupied by zinc in vivo, and some degree of displacement of zinc by cobalt could be observed. Mass spectrometry data, gathered at 60 and 70 mS orifice potential, suggested the presence of a small proportion of material with a mass 118 to 130 daltons greater than the main 5'-nucleotidase mass estimation. This study suggests that this mass difference, only evident at the lower orificepotential, is due to the presence of two zinc ions closely associated with 5'-nucleotidase. To account for the observed high level of activation of 5'-nucleotidase activity by particular divalent metal ions, this thesis describes a proposed model in which these divalent ions may displace the zinc ion at one of the metal ion binding sites. This displacement only occurs at one of the two metal ion binding sites, with the other metal binding site retaining the zinc ion already present. Studies with purified enzyme, each with a single amino acid substitution, lend support to this hypothesis and suggest the identity of the metal ion binding site at which displacement occurs. Seven key catalytic site residues (Asp-41, His-43, Asp-84, His-117, Glu-118, His-217 and His-252) were selected on the basis of sequence conservation within the Ser/Thr protein phosphatases and 5'-nucleotidases. X-ray crystallographic data published by others during this study implicated five of the selected residues (Asp-41, His-43, Asp-84, His-217 and His-252) directly in metal ion binding, including two residues from each metal ion binding site and one directly involved in both sites (Asp-84). The remaining two residues (His-117 and Glu-118) are highly conserved but were not thought to play direct roles in metal ion binding. The seven selected residues were modified by site-directed mutagenesis, and the effect of the amino acid substitutions upon the kinetic properties of 5'-nucleotidase activity was determined. Residues hypothesised to be involved in metal ion displacement, and subsequent activation of 5'-nucleotidase activity, were identified by reductions in metal ion affinity and increased levels of activation by cobalt compared to the wild type 5'-nucleotidase. This study suggests that the metal binding site, M2, that includes residues Asp-84, His-217 and His-252, is involved in metal ion displacement, while the other metal binding site, M1, is not. This, in turn, suggests the metal binding sites are functionally non-equivalent and kinetically distinct. No residues were identified in this study as playing significant roles in substrate binding, as there was no significant reduction observed in affinity for 5'-AMP observed in any of the catalytic site mutants.
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黎錦明 and Kam-ming Lai. "Structure and function of 5'-nucleotidase of the rat brain." Thesis, The University of Hong Kong (Pokfulam, Hong Kong), 1991. http://hub.hku.hk/bib/B31232280.

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Saraiva, Antonio Marcos. "Caracterização funcional e estrutural da nucleotidase SurE de Xyllela fastidiosa." [s.n.], 2009. http://repositorio.unicamp.br/jspui/handle/REPOSIP/316474.

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Orientador: Anete Pereira de Souza
Tese (doutorado) - Universidade Estadual de Campinas, Instituto de Biologia
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Resumo: A linhagem 9a5c da bactéria Xylella fastidiosa foi o primeiro fitopatógeno a ter seu genoma completamente sequenciado, o qual gerdu diversas informações sobre seu metabolismo e patogenicidade. Das orfs codificadas por esta bactéria, destaca-se; no presente trabalho, a XF0703, cuja proteína correlata (com 28,3 kDa) possui similaridade com proteínas SurE de várias outras bactérias. Proteínas SurEs são nucleotidases que desfosforilam diversos nucleosideos monofosforilados para seus respectivos nucleosideos. Tal função é de fundamental importância para manter o pool balanceado dos quatro (deoxi)ribonucleosideos para síntese de DNA e RNA, respectivamente. Este trabalho descreve a clonagem da orfXF0703 no vetor pET29a, a expressão da proteína recombinante (XfSurE) em Escheríchia coli BL21(DE3) e a purificação da mesma por cromatografia de afinidade ao níquel. A análise da estrutura secundária foi feita por dicroísmo circular e realizou-se a determinação do estado oligomérico por cromatografia de gel filtração e espalhamento de luz a baixo ângulo (SAXS), os quais revelaram que a proteína é um tetrâmero. Dados de caracterização funcional indicam que a proteína possui maior atividade em pH neutro na presença do íon manganês como cofator, com uma maior afinidade pelo substrato 3'-AMP (K0,5=0,16 mM). Além disso, ensaios cinéticos mostram que a proteína possui um comportamento alostérico com alta cooperatividade positiva (coeficiente de Hill em torno de 2,6) com todos os quatro substratos naturais testados (3'-AMP, 5'-dAMP, 5'-AMP e 5-GMP). Experimentos com a técnica de SAXS permitiram calcular o raio de giro (32,7 ± 0.2 A), distância máxima intramolecular (100 A) e a simetria do envelope da molécula (222). A estrutura de diversas SurEs homólogas já cristalizadas foram superpostas ao envelope obtido, sendo que StSurE (SurE de Salmonella com maior idenjidade de aminoácidos) mostrou ter o melhor ajuste. No entanto, notou-se que havia espaços vazios no envelope de XfSurE e tais espaços podiam ser preenchidos a partir do afastamento das alças responsáveis pela tetramerização e pela rotação dos f dímeros. Estes movimentos (translação e rotação) podem explicar o comportamento alostérico da proteína, facilitando a entrada de substrato ao sítio catalítico da molécula.
Abstract: The 9a5c strain from bacterium Xylella fastidiosa was the first phytopathogen to have its genome completely sequenced, which revealed a lot of information about its metabolism and its pathogenicity. 'From a variety of orfs encoded by this bacterium, we highlight, in this work, the XF0703, which correlated protein (with 28.3 kDa) has similarity with SurE proteins from several other bacteria. The SurE proteins *are nucleotidases that dephosphorylate various monophosphorylated nucleosides to their respective nucleosides. This function is critical for maintaining the balanced pool of four (deoxy) ribonucleosides for DNA and RNA synthesis. In this work, we describes the cloning of the XF0703 orf into the vector pET29a, the recombinant protein overexpression (XfSurE) in Escherichia coli BL21(DE3) and the protein purification by nickel affinity chromatography. The secondary structure analysis was done by circular dichroism, while oligomeric state determination was achieved by gel filtration chromatography and small-angle X-ray light scattering (SAXS), which showed that the protein is a tetramer. Functional characterization data indicate that the protein has a highest activity at neutral pH in the presence of manganese as a cofactor, with a highest affinity for the 3-AMP substrate (K0,5 = 0,16 mM). Furthermore, kinetic tests showed that the protein has a allosteric behavior with a high positive cooperativity (Hill coefficient around 2.6) for all natural substrates screened (3-AMP, 5'-dAMP, 5'-AMP and 5'-GMP). Experiments with SAXS technique have allowed to calculate the radius of gyration (32.7 ± 0.2 A), maximum intramolecular distance (100 A) and molecule symmetry.
Doutorado
Genetica de Microorganismos
Doutor em Genetica e Biologia Molecular
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Books on the topic "'-nucleotidase"

1

Barber, Ian Stuart. 5'-nucleotidase: It's [sic]Membrane/cytoskeletal associations. Birmingham: Universityof Birmingham, 1989.

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Marani, Enrico. Topographic histochemistry of the cerebellum: 5'-nucleotidase, acetylocholinesterase, immunology of FAL. Stuttgart: G. Fischer Verlag, 1986.

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Book chapters on the topic "'-nucleotidase"

1

Schomburg, Dietmar, and Margit Salzmann. "Nucleotidase." In Enzyme Handbook 3, 437–42. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-76463-9_92.

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Schomburg, Dietmar, and Margit Salzmann. "5’-Nucleotidase." In Enzyme Handbook 3, 309–14. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-76463-9_66.

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Schomburg, Dietmar, and Margit Salzmann. "3’-Nucleotidase." In Enzyme Handbook 3, 315–18. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-76463-9_67.

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Schomburg, Dietmar, and Margit Salzmann. "Phosphoadenylate 3’-nucleotidase." In Enzyme Handbook 3, 319–21. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-76463-9_68.

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Froehlich, Stephan J., Carlo A. Lackerbauer, Guenter Rudolph, Jan Rémi, Soheyl Noachtar, Werner J. Heppt, Annette Cryer, et al. "5′-Nucleotidase Hyperactivity." In Encyclopedia of Molecular Mechanisms of Disease, 1501–2. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-29676-8_4.

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Braun-Falco, Markus, Henry J. Mankin, Sharon L. Wenger, Markus Braun-Falco, Stephan DiSean Kendall, Gerard C. Blobe, Christoph K. Weber, et al. "Pyrimidine 5′ Nucleotidase Deficiency." In Encyclopedia of Molecular Mechanisms of Disease, 1798. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-29676-8_8047.

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Braun-Falco, Markus, Henry J. Mankin, Sharon L. Wenger, Markus Braun-Falco, Stephan DiSean Kendall, Gerard C. Blobe, Christoph K. Weber, et al. "Pyrimidine 5′ Nucleotidase-1 Deficiency." In Encyclopedia of Molecular Mechanisms of Disease, 1798. Berlin, Heidelberg: Springer Berlin Heidelberg, 2009. http://dx.doi.org/10.1007/978-3-540-29676-8_8048.

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Kreutzberg, G. W., D. Heymann, and M. Reddington. "5′-Nucleotidase in the Nervous System." In Proceedings in Life Sciences, 147–64. Berlin, Heidelberg: Springer Berlin Heidelberg, 1986. http://dx.doi.org/10.1007/978-3-642-70664-6_11.

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Marinello, E., A. Tabucchi, F. Carlucci, P. Galieni, and F. Rosi. "Isoenzymes of 5′-Nucleotidase in Human Lymphocytes." In Advances in Experimental Medicine and Biology, 555–58. Boston, MA: Springer US, 1998. http://dx.doi.org/10.1007/978-1-4615-5381-6_107.

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Webster, A. D. B., M. Rowe, S. M. Johnson, G. L. Asherson, and A. Harkness. "Ecto 5′-Nucleotidase Deficiency in Primary Hypogammaglobulinaemia." In Ciba Foundation Symposium 68 - Enzyme Defects and Immune Dysfunction, 135–64. Chichester, UK: John Wiley & Sons, Ltd., 2008. http://dx.doi.org/10.1002/9780470720516.ch9.

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Conference papers on the topic "'-nucleotidase"

1

AL-Tikrity, Ilham, Abeer Alattar, Harith Mustafa, and Safaa Sultan. "Biochemical Characterization of Nucleotidase in some Parasites." In Proceedings of the 1st International Multi-Disciplinary Conference Theme: Sustainable Development and Smart Planning, IMDC-SDSP 2020, Cyperspace, 28-30 June 2020. EAI, 2020. http://dx.doi.org/10.4108/eai.28-6-2020.2298245.

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Nguyen, Anna M., Jianhong Zhou, and Yuchun Du. "Abstract B05: Ecto-5’-nucleotidase (CD73) confers radioresistance in pancreatic cancer." In Abstracts: AACR Special Conference on Pancreatic Cancer: Advances in Science and Clinical Care; May 12-15, 2016; Orlando, FL. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.panca16-b05.

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Gerhardt, Josefine, Corinna Steinbrech, Florian Fritzsche, Verena Tischler, Michael Müntener, Tullio Sulser, Carsten Stephan, Klaus Jung, Holger Moch, and Glen Kristiansen. "Abstract 1772: Calcium activated nucleotidase 1 (CANT1) promotes progression of prostate carcinomas." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-1772.

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Jordheim, Lars P., Zsuzsanna Marton, Moez Rhimi, Laurent Chaloin, Emeline Cros-Perrial, Corinne Lionne, Suzanne Peyrottes, Nushin Aghajari, and Charles Dumontet. "Abstract 3835: Identification and characterization of inhibitors of 5′-nucleotidase cN-II issued from virtual screening." In Proceedings: AACR 103rd Annual Meeting 2012‐‐ Mar 31‐Apr 4, 2012; Chicago, IL. American Association for Cancer Research, 2012. http://dx.doi.org/10.1158/1538-7445.am2012-3835.

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Bowser, Jessica L., Michael R. Blackburn, Gregory L. Shipley, Susu Xie, and Russell R. Broaddus. "Abstract 3384: Down-regulation of 5’-nucleotidase (CD73)-generated adenosine: A novel mechanism for regulating endometrial cancer metastasis." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-3384.

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Matsuyama, Masahiro, Masatoshi Wakui, Makoto Monnai, Tomoko Mizushima, Chiyoko NIshime, Kenji Kawai, Hiroshi Suemizu, et al. "Abstract 2366: Reduced ecto-5′-nucleotidase CD73 expression and altered purine nucleotide metabolism in colorectal cancer cells robustly causing liver metastases." In Proceedings: AACR 101st Annual Meeting 2010‐‐ Apr 17‐21, 2010; Washington, DC. American Association for Cancer Research, 2010. http://dx.doi.org/10.1158/1538-7445.am10-2366.

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Zborovsky, AB, BV Zavodovsky, EV Bobicheva, LE Sivordova, and NA Fofanova. "THU0055 Role of antibodies to 5’nucleotidase in rheumatoid arthritis, systemic lupus erythematosus, systemic sclerosis, ankylosing spondylarthritis and reactive arthritis patients." In Annual European Congress of Rheumatology, Annals of the rheumatic diseases ARD July 2001. BMJ Publishing Group Ltd and European League Against Rheumatism, 2001. http://dx.doi.org/10.1136/annrheumdis-2001.899.

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Faulkes, Rosemary, Joanne O’Rourke, Owen Cain, Daniel Patten, Alex Wilkinson, Tahir Shah, Christopher Weston, and Shishir Shetty. "O02 Deep sequencing of HCC endothelium reveals an active role in immunosuppression and highlights the ecto nucleotidase CD73 as a potential therapeutic target." In Abstracts of the British Association for the Study of the Liver Annual Meeting, 22–24 November 2021. BMJ Publishing Group Ltd and British Society of Gastroenterology, 2021. http://dx.doi.org/10.1136/gutjnl-2021-basl.2.

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Zborovsky, AB, BV Zavodovsky, TA Pankratova, AV Rvachev, OV Bykova, and TV Serdukova. "SAT0001 Role of determination of succinate dehydrogenase, myeloperoxidase, na ± k ± atph-ase, 5?-nucleotidase in cells of peripheral blood of ankylosing spondylarthritis patients." In Annual European Congress of Rheumatology, Annals of the rheumatic diseases ARD July 2001. BMJ Publishing Group Ltd and European League Against Rheumatism, 2001. http://dx.doi.org/10.1136/annrheumdis-2001.353.

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Goueli, Said A., and Kevin hsiao. "Abstract 414: Biochemical and cellular monitoring of the activity of the ecto-5’-nucleotidase (CD73), a key cancer modulator using HTS-formatted bioluminescent technology." In Proceedings: AACR 107th Annual Meeting 2016; April 16-20, 2016; New Orleans, LA. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1538-7445.am2016-414.

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