Relevant bibliographies by topics / Pyrimidine nucleotides – Metabolism

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Academic literature on the topic 'Pyrimidine nucleotides – Metabolism'

Author: Grafiati
Published: 4 June 2021
Last updated: 2 February 2022

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Journal articles on the topic "Pyrimidine nucleotides – Metabolism"

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Deng, Wei-Wei, Riko Katahira, and Hiroshi Ashihara. "Short Term Effect of Caffeine on Purine, Pyrimidine and Pyridine Metabolism in Rice (Oryza sativa) Seedlings." Natural Product Communications 10, no. 5 (2015): 1934578X1501000. http://dx.doi.org/10.1177/1934578x1501000510.

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As part of our studies on the physiological and ecological function of caffeine, we investigated the effect of exogenously supplied caffeine on purine, pyrimidine and pyridine metabolism in rice seedlings. We examined the effect of 1 mM caffeine on the in situ metabolism of 14C-labelled adenine, guanine, inosine, uridine, uracil, nicotinamide and nicotinic acid. The segments of 4-day-old dark-grown seedlings were incubated with these labelled compounds for 6 h. For purines, the incorporation of radioactivity from [8-14C]adenine and [8-14C]guanine into nucleotides was enhanced by caffeine; in c
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Pels Rijcken, W. R., B. Overdijk, D. H. van den Eijnden, and W. Ferwerda. "Pyrimidine nucleotide metabolism in rat hepatocytes: evidence for compartmentation of nucleotide pools." Biochemical Journal 293, no. 1 (1993): 207–13. http://dx.doi.org/10.1042/bj2930207.

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Pyrimidine nucleotide metabolism in rat hepatocytes was studied by measurement of the labelling kinetics of the various intermediates after double labelling with [14C]orotic acid and [3H]cytidine, the precursors for the de novo and the salvage pathways respectively. For the uridine nucleotides, differences were found for the 14C/3H ratios in the UDP-sugars, in UMP (of RNA) and in their precursor UTP, suggesting the existence of separated flows of the radioactive precursors through the de novo and the salvage pathways. Higher ratios in the UDP-sugars, which are synthesized in the cytoplasm, and
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Pels Rijcken, W. R., G. J. M. Hooghwinkel, and W. Ferwerda. "Pyrimidine metabolism and sugar nucleotide synthesis in rat liver." Biochemical Journal 266, no. 3 (1990): 777–83. http://dx.doi.org/10.1042/bj2660777.

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With radioactive precursors, the labelling kinetics of the soluble pyrimidine nucleotides and of RNA were measured in rat liver to determine the contribution of the metabolic flows through synthesis de novo and the salvage pathway. To separate and quantify all pyrimidine nucleotides, an h.p.l.c. technique was developed using anion-exchange chromatography and reversed-phase chromatography. The concentrations of cytidine nucleotides were in the range of 30-45 nmol/g wet weight, and the concentrations of the uridine phosphates and of the UDP-sugars were approx. 6 and 20 times higher respectively.
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Sprenger, Hans-Georg, Thomas MacVicar, Amir Bahat, et al. "Cellular pyrimidine imbalance triggers mitochondrial DNA–dependent innate immunity." Nature Metabolism 3, no. 5 (2021): 636–50. http://dx.doi.org/10.1038/s42255-021-00385-9.

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AbstractCytosolic mitochondrial DNA (mtDNA) elicits a type I interferon response, but signals triggering the release of mtDNA from mitochondria remain enigmatic. Here, we show that mtDNA-dependent immune signalling via the cyclic GMP–AMP synthase‒stimulator of interferon genes‒TANK-binding kinase 1 (cGAS–STING–TBK1) pathway is under metabolic control and is induced by cellular pyrimidine deficiency. The mitochondrial protease YME1L preserves pyrimidine pools by supporting de novo nucleotide synthesis and by proteolysis of the pyrimidine nucleotide carrier SLC25A33. Deficiency of YME1L causes i
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Rowe, Peter B., and Annette Kalaizis. "Serine metabolism in rat embryos undergoing organogenesis." Development 87, no. 1 (1985): 137–44. http://dx.doi.org/10.1242/dev.87.1.137.

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Rat embryos (9·5 days gestation) were cultured for 48 h in heat-inactivated homologous serum containing [3-14C] serine. Analysis of the distribution of the radioactive label in the conceptus demonstrated that almost one half of the incorporated serine was cleaved to provide one-carbon units for the synthesis of purine and pyrimidine nucleotides. Analysis of the free amino acids in the serum, the exocoelomic fluid and the cells of the yolk sac and the embryo showed that there was a variably selective increase in the concentration of amino acids in the exocoelomic fluid compared with the serum a
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Chiarelli, Laurent, Andrea Mattevi, Alessandro Galizzi, et al. "Functional Analysis of Two Mutants of Pyrimidine 5′ Nucleotidase Causing Nonspherocytic Hemolytic Anemia." Blood 104, no. 11 (2004): 1592. http://dx.doi.org/10.1182/blood.v104.11.1592.1592.

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Abstract Pyrimidine 5′-nucleotidase type-I (P5′N-1) catalyzes the dephosphorylation of UMP and CMP to their respective nucleosides. In red blood cells, the enzyme has a major role in the catabolism of nucleotides formed from RNA degradation. P5′N-1 possesses also phospho-transferase activity suggesting an additional role of the enzyme in nucleotide metabolism. P5′N-1 deficiency is an autosomal recessive disorder characterized by hemolytic nonspherocytic anemia, heavy basophilic stippling in the peripheral blood smear, and accumulation of pyrimidine nucleotides within the erythrocytes. P5′N-1 d
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Yao, Yixin, Yang Liu, Hui Guo, et al. "Metabolic Profiling Identifies De Novo Nucleotide Synthesis As a Potential Metabolic Vulnerability for Targeted Therapy Against Mantle Cell Lymphoma." Blood 132, Supplement 1 (2018): 2945. http://dx.doi.org/10.1182/blood-2018-99-112192.

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Abstract Introduction: Cancer cells exhibit dramatic alterations in cellular metabolism, such as enhanced de novo nucleotide synthesis, to support cell growth, proliferation and survival. The abundance of the nucleotide pool as well as the level and activity of different rate-limiting enzymes belonging to the nucleotide synthetic pathway limit the maximal proliferative capacity of cells. Maintenance of an adequate pool of deoxyribonucleotide triphosphates is essential for DNA replication and DNA repair, and consequently, the genetic integrity of nuclear and mitochondrial genomes. We and others
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Kartha, S., and F. G. Toback. "Purine nucleotides stimulate DNA synthesis in kidney epithelial cells in culture." American Journal of Physiology-Renal Physiology 249, no. 6 (1985): F967—F972. http://dx.doi.org/10.1152/ajprenal.1985.249.6.f967.

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Adenine nucleotides infused into animals with acute renal failure appear to enhance recovery of kidney function and structure. To determine whether these compounds could act by a direct effect on renal cell metabolism, their capacity to stimulate DNA synthesis was evaluated in cultures of monkey kidney epithelial cells (BSC-1 line). AMP and ADP enhanced DNA synthesis by threefold more than was previously observed with other mitogens for these cells. Guanosine and inosine and their nucleotides and adenosine and ATP were also mitogenic but to a lesser extent, whereas pyrimidine derivatives were
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Fermo, Elisa, Anna Marcello, Paola Bianchi, et al. "Pyrimidine 5′ Nucleotidase Deficiency: Clinical and Molecular Characterization of Two New Italian Patients." Blood 106, no. 11 (2005): 3711. http://dx.doi.org/10.1182/blood.v106.11.3711.3711.

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Abstract Hereditary pyrimidine 5′ nucleotidase deficiency (P5′N) is the most frequent abnormality of the red cell nucleotide metabolism causing hereditary non-spherocytic hemolytic anemia. The disorder is characterized by mild-to-moderate hemolytic anemia associated with reticulocytosis and hyperbilirubinemia and the accumulation of high concentrations of pyrimidine nucleotides within the erythrocyte. P5′N-1 gene is localized on 7p15-p14; eighteen mutations have been so far identified in 27 unrelated families, 6 of them of Italian origin. The aim of this study is to describe the hematological,
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Arbade, Gajanan Kashinathrao, and Sandeep Kumar Srivastava. "Cloning, expression, purification, crystallization and preliminary X-ray diffraction studies of NAD synthetase from methicillin-resistantStaphylococcus aureus." Acta Crystallographica Section F Structural Biology Communications 71, no. 6 (2015): 763–69. http://dx.doi.org/10.1107/s2053230x15007906.

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Staphylococcus aureusis an important human and animal pathogen that causes a wide range of infections. The prevalence of multidrug-resistantS. aureusstrains in both hospital and community settings makes it imperative to characterize new drug targets to combatS. aureusinfections. In this context, enzymes involved in NAD metabolism and synthesis are significant drug targets as NAD is a central player in several cellular processes. NAD synthetase catalyzes the last step in the biosynthesis of nicotinamide adenine dinucleotide, making it a crucial intermediate enzyme linked to the biosynthesis of
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Dissertations / Theses on the topic "Pyrimidine nucleotides – Metabolism"

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Eguae, Samuel Iyamu. "Pyrimidine nucleotide metabolism in Rhizobium meliloti: purification of aspartate transcarbamoylase from a pyrimidine auxotroph." Thesis, University of North Texas, 1990. https://digital.library.unt.edu/ark:/67531/metadc332674/.

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Rhizobium aspartate transcarbamoylase (ATCase; EC 2.1.3.2) was previously believed to be similar to the Pseudomonas ATCase which has been studied extensively. To facilitate the study of the Rhizobium ATCase a pyrimidine-requiring mutant of R. meliloti was isolated and used in the purification of the enzyme.
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Stewart, John E. B. (John Edward Bakos). "Characterization of Aspartate Transcarbamoylase in the Archaebacterium Methanococcus Jannaschii." Thesis, University of North Texas, 1996. https://digital.library.unt.edu/ark:/67531/metadc935724/.

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Asparate transcarbamoylase catalyzes the first committed step in the de novo synthesis of pyrmidine nucleotides UMP, UDP, UTP, and CTP. The archetype enzyme found in Escherichia coli (310 kDa) exhibits sigmodial substrate binding kinetics with positive control by ATP and negative control with CTP and UTP. The ATCase characterized in this study is from the extreme thermophilic Archaebacterium, Methanococcus jannaschii. The enzyme was very stable at elevated temperatures and possessed activity from 20 degrees Celsius to 90 degrees Celsius. M. Jannaschii ATCase retained 75% of its activity after
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Brichta, Dayna Michelle. "Construction of a Pseudomonas aeruginosa Dihydroorotase Mutant and the Discovery of a Novel Link between Pyrimidine Biosynthetic Intermediates and the Ability to Produce Virulence Factors." Thesis, University of North Texas, 2003. https://digital.library.unt.edu/ark:/67531/metadc4344/.

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The ability to synthesize pyrimidine nucleotides is essential for most organisms. Pyrimidines are required for RNA and DNA synthesis, as well as cell wall synthesis and the metabolism of certain carbohydrates. Recent findings, however, indicate that the pyrimidine biosynthetic pathway and its intermediates maybe more important for bacterial metabolism than originally thought. Maksimova et al., 1994, reported that a P. putida M, pyrimidine auxotroph in the third step of the pathway, dihydroorotase (DHOase), failed to produce the siderophore pyoverdin. We created a PAO1 DHOase pyrimidine auxotr
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Vickrey, John F. (John Fredrick) 1959. "Isolation and Characterization of the Operon Containing Aspartate Transcarbamoylase and Dihydroorotase from Pseudomonas aeruginosa." Thesis, University of North Texas, 1993. https://digital.library.unt.edu/ark:/67531/metadc278859/.

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The Pseudomonas aeruginosa ATCase was cloned and sequenced to determine the correct size, subunit composition and architecture of this pivotal enzyme in pyrimidine biosynthesis. During the course of this work, it was determined that the ATCase of Pseudomonas was not 360,000 Da but rather present in a complex of 484,000 Da consisting of two different polypeptides (36,000 Da and 44,000 Da) with an architecture similar to that of E. coli ATCase, 2(C3):3(r2). However, there was no regulatory polypeptide found in the Pseudomonas ATCase.
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AsFour, Hani. "Effector Response of the Aspartate Transcarbamoylase From Wild Type Pseudomonas Putida and a Mutant with 11 Amino Acids Deleted at the N-terminus of PyrB." Thesis, University of North Texas, 2002. https://digital.library.unt.edu/ark:/67531/metadc3163/.

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Like its enteric counterpart, aspartate transcarbamoylase (ATCase) from Pseudomonas putida is a dodecamer of two different polypeptides. Unlike the enterics, the Pseudomonas ATCase lacks regulatory polypeptides but employs instead inactive dihydroorotases for an active dodecamer. Previous work showed that PyrB contains not only the active site but also the effector binding sites for ATP, UTP and CTP at its N-terminus. In this work, 11 amino acids were deleted from the N-terminus of PyrB and the ATCase with the truncated protein was expressed in E. coli pyrB- and purified. The wild type enzym
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Hammerstein, Heidi Carol. "Isolation of a Pseudomonas aeruginosa Aspartate Transcarbamoylase Mutant and the Investigation of Its Growth Characteristics, Pyrimidine Biosynthetic Enzyme Activities, and Virulence Factor Production." Thesis, University of North Texas, 2004. https://digital.library.unt.edu/ark:/67531/metadc4704/.

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The pyrimidine biosynthetic pathway is an essential pathway for most organisms. Previous research on the pyrimidine pathway in Pseudomonas aeruginosa (PAO1) has shown that a block in the third step of the pathway resulted in both a requirement for exogenous pyrimidines and decreased ability to produce virulence factors. In this work an organism with a mutation in the second step of the pathway, aspartate transcarbamoylase (ATCase), was created. Assays for pyrimidine intermediates, and virulence factors were performed. Results showed that the production of pigments, haemolysin, and rhamnoli
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Kumar, Alan P. "Structure-Function Studies on Aspartate Transcarbamoylase and Regulation of Pyrimidine Biosynthesis by a Positive Activator Protein, PyrR in Pseudomonas putida." Thesis, University of North Texas, 2003. https://digital.library.unt.edu/ark:/67531/metadc4362/.

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The regulation of pyrimidine biosynthesis was studied in Pseudomonas putida. The biosynthetic and salvage pathways provide pyrimidine nucleotides for RNA, DNA, cell membrane and cell wall biosynthesis. Pyrimidine metabolism is intensely studied because many of its enzymes are targets for chemotheraphy. Four aspects of pyrimidine regulation are described in this dissertation. Chapter I compares the salvage pathways of Escherichia coli and P. putida. Surprisingly, P. putida lacks several salvage enzymes including nucleoside kinases, uridine phosphorylase and cytidine deaminase. Without a funct
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Kim, Hyunju. "Multiple Activities of Aspartate Transcarbamoylase in Burkholderia cepacia: Requirement for an Active Dihydroorotase for Assembly into the Dodecameric Holoenzyme." Thesis, University of North Texas, 2010. https://digital.library.unt.edu/ark:/67531/metadc33176/.

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The aspartate transcarbamoylase (ATCase) was purified from Burkholderia cepacia 25416. In the course of purification, three different ATCase activities appeared namely dodecameric 550 kDa holoenzyme, and two trimeric ATCases of 140 kDa (consists of 47 kDa PyrB subunits) and 120 kDa (consists of 40 kDa PyrB subunits) each. The 120 kDa PyrB polypeptide arose by specific cleavage of the PyrB polypeptide between Ser74 and Val75 creating an active polypeptide short by 74 amino acids. Both the 40 and 47 kDa polypeptides produced active trimers. To compare the enzyme activity of these trimers, an eff
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Linscott, Andrea J. (Andrea Jane). "Regulatory Divergence of Aspartate Transcarbamoylase from the Pseudomonads." Thesis, University of North Texas, 1996. https://digital.library.unt.edu/ark:/67531/metadc277625/.

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Aspartate transcarbamoylase (ATCase) was purified from 16 selected bacterial species including existing Pseudomonas species and former species reassigned to new genera. An enormous diversity was seen among the 16 enzymes with each class of ATCase being represented. The smallest class, class C, with a catalytically active homotrimer, at 100 kDa, was found in Bacillus and other Gram positive bacteria. In this report, the ATCases from the Gram negatives, Shewanella putrefaciens and Stenotrophomonas maltophilia were added to class C membership. The enteric bacteria typify class B ATCases at 310 kD
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Barron, Vincent N. (Vincent Neal). "Comparison of Aspartate Transcarbamoylase and Pyrimidine Salvage in Sporosarcina urea, Sprolactobacillus inulinus, Lactobacillus fermentum, and Micrococcus luteus." Thesis, University of North Texas, 1994. https://digital.library.unt.edu/ark:/67531/metadc278938/.

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The enzyme that catalyzes the committed step in pyrimidine biosynthesis, aspartate transcarbamoylase, has been compared in selected endospore-forming organisms and in morphologically similar control organisms. The ATCases and pyrimidine salvage from Sporosarcina ureae, Sporolactobacillus inulinus, Lactobacillus fermentum, and Micrococcus luteus were compared to those of Bacillus subtilis. While the ATCases from Sporosarcina ureae, Sporolactobacillus inulinus, and L. fermentum were found to exhibit characteristics to that of Bacillus with respect to molecular weight and kinetics, M. luteus ATCa
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Books on the topic "Pyrimidine nucleotides – Metabolism"

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Pharmacology of purine and pyrimidine receptors. Elsevier, 2011.

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Jensen, Christine May. Vitamin B-6 and pyrimidine deoxynucleoside metabolism in the rat. 1989.

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Jensen, Christine May. Vitamin B-6 and pyrimidine deoxynucleoside metabolism in the rat. 1989.

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Book chapters on the topic "Pyrimidine nucleotides – Metabolism"

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Rudolph, Frederick B., William C. Fanslow, Anil D. Kulkarni, Sulabha S. Kulkarni, and Charles T. Van Buren. "Effect of Dietary Nucleotides on Lymphocyte Maturation." In Purine and Pyrimidine Metabolism in Man V. Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-5104-7_83.

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Peters, Godefridus J. "Therapy Related Disturbances in Nucleotides in Cancer Cells." In Purine and Pyrimidine Metabolism in Man VIII. Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-2584-4_24.

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Havel, Michael, Werner Monl, Gerhard Schopf, and Mathias M. Müller. "Purine Nucleotides in Human Hearts During Open Heart Surgery." In Purine and Pyrimidine Metabolism in Man V. Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-1248-2_82.

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Nuki, G., K. Astrini, D. Brenton, M. Cruikshank, J. Lever, and J. E. Seegmiller. "Purine and Pyrimidine Nucleotides in Some Mutant Human Lymphoblasts." In Ciba Foundation Symposium 48 - Purine and Pyrimidine Metabolism. John Wiley & Sons, Ltd., 2008. http://dx.doi.org/10.1002/9780470720301.ch9.

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Grune, Tilman, and David Perrett. "Rapid Simultaneous Measurement of Nucleotides, Nucleosides and Bases in Tissues by Capillary Electrophoresis." In Purine and Pyrimidine Metabolism in Man VIII. Springer US, 1995. http://dx.doi.org/10.1007/978-1-4615-2584-4_169.

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Edwards, N. Lawrence, Annette M. Zaytoun, and Gail A. Renard. "Separate Mechanisms for Cellular uptake of Purine Nucleotides by B- and T-Lymphoblasts." In Purine and Pyrimidine Metabolism in Man V. Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-1248-2_72.

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Switzer, Robert L., Howard Zalkin, and Hans Henrik Saxild. "Purine, Pyrimidine, and Pyridine Nucleotide Metabolism." In Bacillus subtilis and Its Closest Relatives. ASM Press, 2014. http://dx.doi.org/10.1128/9781555817992.ch19.

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Micheli, Vanna, Carlo Ricci, Sylvia Sestini, Marina Rocchigiani, Monica Pescaglini, and Giuseppe Pompucci. "Pyridine Nucleotide Metabolism: Purine and Pyrimidine Interconnections." In Advances in Experimental Medicine and Biology. Springer US, 1991. http://dx.doi.org/10.1007/978-1-4615-7703-4_72.

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Gutensohn, Wolf, and Juliane Rieger. "Ectoenzymes of Nucleotide Metabolism on Human Lymphoid Cells." In Purine and Pyrimidine Metabolism in Man V. Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-1248-2_71.

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Bontemps, F., G. Van den Berghe, and H. G. Hers. "Pathways of Adenine Nucleotide Catabolism in Human Erythrocytes." In Purine and Pyrimidine Metabolism in Man V. Springer US, 1986. http://dx.doi.org/10.1007/978-1-4684-1248-2_53.

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