Academic literature on the topic ''-nucleotidase'

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Journal articles on the topic "'-nucleotidase"

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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
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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′-FS
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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
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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 (macr
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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-cataboli
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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 th
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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
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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 tissue
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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 fro
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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 a
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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 phospha
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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 mac
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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-nucleoti
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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 mi
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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 c
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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.
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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<br>Tese (doutorado) - Universidade Estadual de Campinas, Instituto de Biologia<br>Made available in DSpace on 2018-08-14T21:21:36Z (GMT). No. of bitstreams: 1 Saraiva_AntonioMarcos_D.pdf: 12032714 bytes, checksum: 1262a05ca10735e855fa138a2093d04b (MD5) Previous issue date: 2009<br>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 XF07
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Books on the topic "'-nucleotidase"

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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"

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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"

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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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