Relevant bibliographies by topics / Thymidine monophosphate

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  1. Journal articles
  2. Dissertations / Theses
  3. Book chapters
  4. Conference papers

Academic literature on the topic 'Thymidine monophosphate'

Author: Grafiati
Published: 6 September 2023

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Journal articles on the topic "Thymidine monophosphate"

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Miyasaki, Taiko, and Katsuhiko Harada. "Effects of specific purine and pyrimidine compounds on the ingestion of test diets by the abalone Haliotis discus and the oriental weatherfish Misgurnus anguillicaudatus." Marine and Freshwater Research 54, no. 3 (2003): 235. http://dx.doi.org/10.1071/mf02066.

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To improve the feed ingestion of cultured fish and shellfish, 26 purine and pyrimidine compounds were examined as dietary supplements at a concentration of 1.0 mmol kg–1 (or L–1) of diet. For the black abalone Haliotis discus, feeding was significantly (P < 0.05) increased by thymidine, adenosine-5�-monophosphate, adenosine- 5�-diphosphate (ADP), adenosine-5�-triphosphate, guanosine-5�-monophosphate (GMP), inosine-5- monophosphate (IMP) and 2�-deoxycytidine-5�-monophosphate. For the oriental weatherfish Misgurnus anguillicaudatus, feeding was significantly (P < 0.05) increased by thymidine, ADP, IMP and thymidine-5�-monophosphate (TMP). At one-tenth of the initial concentration, ADP, GMP and IMP were effective for the abalone and thymidine and TMP were effective for the weatherfish. None of the compounds inhibited feeding of either species.
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Gogolin, Lars, Ralf Seidel, Martin Engelhard, Roger S. Goody, and Christian F. W. Becker. "Semisynthesis of human thymidine monophosphate kinase." Biopolymers 94, no. 4 (June 3, 2010): 433–40. http://dx.doi.org/10.1002/bip.21398.

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Wu, R. R., L. A. Hamlow, C. C. He, Y. w. Nei, G. Berden, J. Oomens, and M. T. Rodgers. "The intrinsic basicity of the phosphate backbone exceeds that of uracil and thymine residues: protonation of the phosphate moiety is preferred over the nucleobase for pdThd and pUrd." Physical Chemistry Chemical Physics 19, no. 45 (2017): 30351–61. http://dx.doi.org/10.1039/c7cp05521h.

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Thompson, L. F. "Ecto-5'-nucleotidase can provide the total purine requirements of mitogen-stimulated human T cells and rapidly dividing human B lymphoblastoid cells." Journal of Immunology 134, no. 6 (June 1, 1985): 3794–97. http://dx.doi.org/10.4049/jimmunol.134.6.3794.

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Abstract The ability of mitogen-stimulated human T cells or rapidly dividing human B lymphoblastoid cells to drive their total purine requirements from inosine 5'-monophosphate, inosine, or hypoxanthine was compared. Inosine 5'-monophosphate first must be converted to inosine by the action of the enzyme ecto-5'-nucleotidase before it can be transported into the cell; inosine and hypoxanthine, however, can be transported directly. Mitogen-stimulated human peripheral blood T cells were treated with aminopterin to inhibit purine synthesis de novo and to make the cells dependent on an exogenous purine source. Thymidine was added as a source of pyrimidines. Under these conditions, 30 microM inosine 5'-monophosphate, inosine, and hypoxanthine showed comparable abilities to support [3H]thymidine incorporation into DNA or [3H]leucine incorporation into protein at rates equal to that of untreated control cultures. Similar results were found when azaserine was used to inhibit purine synthesis de novo, and thus DNA synthesis. In parallel experiments with the rapidly dividing human B lymphoblastoid cell line WI-L2, treatment with aminopterin (plus thymidine) inhibited the growth rate by greater than 95%. The normal growth rate was restored by the addition of 30 microM inosine 5'-monophosphate, inosine, or hypoxanthine to the medium. However, in similar experiments with cell line 1254, a derivative of WI-L2 which lacks detectable ecto-5'-nucleotidase activity, inosine and hypoxanthine (plus thymidine), but not inosine 5'-monophosphate (and thymidine) were able to restore the growth inhibition due to aminopterin. These results show that the catalytic activity of ecto-5'-nucleotidase is sufficient to meet the total purine requirements of mitogen-stimulated human T cells or rapidly dividing human B lymphoblastoid cells, and suggest that this enzyme may be important for purine salvage when rates of purine synthesis de novo are limited and/or an extracellular source of purine nucleotides is available.
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Gul, Sana, Ruqaiya Khalil, Zaheer Ul-Haq, and Mohammad S. Mubarak. "Computational Overview of Mycobacterial Thymidine Monophosphate Kinase." Current Pharmaceutical Design 26, no. 15 (May 18, 2020): 1676–81. http://dx.doi.org/10.2174/1381612826666200403114152.

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: Tuberculosis (TB) ranks among the diseases with the highest morbidity rate with significantly high prevalence in developing countries. Globally, tuberculosis poses the most substantial burden of mortality. Further, a partially treated tuberculosis patient is worse than untreated; they may lead to standing out as a critical obstacle to global tuberculosis control. The emergence of multi-drug resistant (MDR) and extremely drug-resistant (XDR) strains, and co-infection of HIV further worsen the situation. The present review article discusses validated targets of the bacterial enzyme thymidine monophosphate kinase (TMPK). TMPKMTB enzyme belongs to the nucleoside monophosphate kinases (NMPKs) family. It is involved in phosphorylation of TMP to TDP, and TDP is phosphorylated to TTP. This review highlights structure elucidation of TMP enzymes and their inhibitors study on TMP scaffold, and it also discusses different techniques; including molecular docking, virtual screening, 3DPharmacophore, QSAR for finding anti-tubercular agents.
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Gustavsson, Thomas, Alexei Sharonov, and Dimitra Markovitsi. "Thymine, thymidine and thymidine 5′-monophosphate studied by femtosecond fluorescence upconversion spectroscopy." Chemical Physics Letters 351, no. 3-4 (January 2002): 195–200. http://dx.doi.org/10.1016/s0009-2614(01)01375-6.

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Schlosser, Julika, Julian F. M. Hebborn, Daria V. Berdnikova, and Heiko Ihmels. "Selective Fluorimetric Detection of Pyrimidine Nucleotides in Neutral Aqueous Solution with a Styrylpyridine-Based Cyclophane." Chemistry 5, no. 2 (May 11, 2023): 1220–32. http://dx.doi.org/10.3390/chemistry5020082.

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A styrylpyridine-containing cyclophane with diethylenetriamine linkers is presented as a host system whose association with representative nucleotides was examined with photometric and fluorimetric titrations. The spectrometric titrations revealed the formation of 1:1 complexes with log Kb values in the range of 2.3–3.2 for pyrimidine nucleotides TMP (thymidine monophosphate), TTP (thymidine triphosphate) and CMP (cytidine monophosphate) and 3.8–5.0 for purine nucleotides AMP (adenosine monophosphate), ATP (adenosine triphosphate), and dGMP (deoxyguanosine monophosphate). Notably, in a neutral buffer solution, the fluorimetric response to the complex formation depends on the type of nucleotide. Hence, quenching of the already weak fluorescence was observed with the purine bases, whereas the association of the cyclophane with pyrimidine bases TMP, TTP, and CMP resulted in a significant fluorescence light-up effect. Thus, it was demonstrated that the styrylpyridine unit is a useful and complementary fluorophore for the development of selective nucleotide-targeting fluorescent probes based on alkylamine-linked cyclophanes.
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Tomasz, Jeno, Barbara Ramsay Shaw, Ken Porter, Bernard F. Spielvogel, and Anup Sood. "5′-P-Borane-Substituted Thymidine Monophosphate and Triphosphate." Angewandte Chemie International Edition in English 31, no. 10 (October 1992): 1373–75. http://dx.doi.org/10.1002/anie.199213731.

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Van Poecke, Sara, Hélène Munier-Lehmann, Olivier Helynck, Matheus Froeyen, and Serge Van Calenbergh. "Synthesis and inhibitory activity of thymidine analogues targeting Mycobacterium tuberculosis thymidine monophosphate kinase." Bioorganic & Medicinal Chemistry 19, no. 24 (December 2011): 7603–11. http://dx.doi.org/10.1016/j.bmc.2011.10.021.

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Keita, M., A. Kumar, B. Dali, E. Megnassan, M. I. Siddiqi, V. Frecer, and S. Miertus. "Quantitative structure–activity relationships and design of thymine-like inhibitors of thymidine monophosphate kinase of Mycobacterium tuberculosis with favourable pharmacokinetic profiles." RSC Adv. 4, no. 99 (2014): 55853–66. http://dx.doi.org/10.1039/c4ra06917j.

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Dissertations / Theses on the topic "Thymidine monophosphate"

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Tourneux, Lise. "Propriétés structurales et catalytiques des thymidine monophosphate kinases bactériennes." Paris 6, 1999. http://www.theses.fr/1999PA066499.

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Les nucleotides representent une classe majeure de composants cellulaires. Certains enzymes responsables de leur synthese, degradation ou interconversion ont deja ete utilises comme cibles de drogues antivirales, antibacteriennes ou anticancereuses. Parmi eux, la thymidine monophosphate (tmp) kinase qui catalyse une etape limitante de phosphorylation dans la synthese du dttp, pourrait constituer une nouvelle cible en therapie antibacterienne. Le clonage des genes tmk codant pour les tmp kinases d'escherichia coli, yersinia pestis, salmonella typhi, haemophilus influenzae et bacillus subtilis a permis d'aborder leur caracterisation physicochimique. Sous forme native, ce sont des homodimeres de 48 kda, d'activite specifique faible (50 u/mg pour la tmp kinase d'e. Coli) par rapport aux autres nucleoside monophosphate kinases. Seuls les enzymes d'e. Coli et de s. Typhi phosphorylent significativement l'aztmp (17% de l'activite dtmp), activite considerable comparee a celle des tmp kinases humaine ou de levure. Les structures-3d des tmp kinases de levure et d'e. Coli, recemment resolues, ont permis d'apporter un element d'explication a cette difference d'activite, mais nos donnees cinetiques sur la phosphorylation de l'aztmp par les enzymes de y. Pestis et h. Influenzae moderent l'interpretation. La tmp kinase de b. Subtilis, qui ne phosphoryle pas l'aztmp est responsable du phenotype de resistance naturelle de la bacterie a l'azt. Dans le cas de la resistance acquise par une souche d'e. Coli, nous avons montre que ce phenotype est du ici a l'insertion d'une sequence de type is3 dans le gene tdk, codant pour la thymidine kinase. La caracterisation de la tmp kinase d'une souche d'e. Coli mutee dans le gene tmk a revele qu'une mutation ponctuelle provoquant le changement du residu gly 146 en ala dans le domaine lid (domaine flexible qui subit un mouvement au moment de la catalyse), pouvait etre a l'origine d'un changement de specificite de substrat, responsable de l'hypersensibilite de la souche au budr. Nous avons egalement etudie, par mutagenese dirigee, le role fonctionnel des differents residus arg (149, 151, 153, 158) du domaine lid de la tmp kinase d'e. Coli. Cette etude a souligne l'importance des residus arg 149, 153 et 158.
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Gasse, Cécile. "Synthèse et évaluation d'inhibiteurs de la thymidine monophosphate kinase de "mycobacterium tuberculosis"." Paris 5, 2006. http://www.theses.fr/2006PA05P628.

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La thymidine monophosphate kinase de M. Tuberculosis (TMPKmt) est une cible potentielle pour le développement de nouveaux agents antituberculeux. Cette enzyme directement impliquée dans la croissance de M. Tuberculosis, catalyse la dernière étape spécifique de synthèse du dTTP. Le travail présenté a consisté en la synthèse et l’évaluation d’inhibiteurs spécifiques de la TMPKmt. Des analogues nucléosidiques ont été conçus à partir du modèle de l’Ap5T, inhibiteur connu des nucléoside monophosphate kinases. Pour cela, des analogues des deux substrats ont été reliès par un bras espaceur. Par ailleurs, une nouvelle famille de molécules de nature non nucléosidique a été définie à l'aide d'un programme de modélisation (LEA3D) et synthétisée. De même que pour les analogues nucléosidiques, l’affinité de cette nouvelle famille de molécules a été déterminée in vitro sur la TMPKmt et sur la TMPK humaine. Certains analogues ont révélé une activité inhibitrice sur des cultures de M. Bovis BCG
M. Tuberculosis thymidine monophosphate kinase (TMPKmt) is a potential target for the development of new antituberculous agents. This enzyme is directly implied in M. Tuberculosis growth and catalyses the last specific step of the dTTP synthesis i. E. The phosphorylation of the dTMP in dTDP by using ATP as preferred phosphate donor. This manuscript describes the synthesis and evaluation of TMPKmt specific inhibitors. Thus, nucleosidic analogues were synthesized using Ap5T as a well known inhibitor of the nucleoside monophosphate kinases model. Hence, analogues of the two substrates were linked by a spacer. In a second approach, a new family of non-nucleosidic molecules were designed using a modelling program (LEA3D) and were synthesized. The affinities of both families of molecules were determined in vitro on TMPKmt and the human TMPK. Moreover, some of the non-nucleosidic analogues also turned out to be active on M. Bovis BCG growth
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El, Omari Kamel. "Etudes structurales et biochimiques de protéines cibles pour le développement de molécules antivirales et antitumorales." Paris 6, 2007. http://www.theses.fr/2007PA066024.

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Le manque de thérapies efficaces contre différents cancers et virus a montré l’importance de comprendre les mécanismes impliqués dans les activités virales et tumorales et, également, de produire et caractériser des drogues spécifiques de protéines cibles. Pour développer des molécules efficaces, une synergie entre la chimie, la biologie, la biochimie et la biologie structurale est essentielle. Ce travail de thèse a pour but de définir des propriétés structurales de protéines qui pourraient aider au développement de nouvelles drogues et/ou à l’amélioration des molécules existantes. Nous nous sommes servis de la cristallographie aux rayons X pour déterminer différentes structures. Dans cette thèse sont proposées les structures de CC3, de l’ARN ligase du bactériophage T4, de la thymidine phosphorylase humaine, de la thymidine kinase du virus vaccinia et celle de la guanylate monophosphate kinase de Staphylococcus aureus.
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Chen, Jun-Xian, and 陳俊賢. "Monitoring thymidine monophosphate and thymidne diphosphate by capillary electrophoresis with pH junction and formation of ion complex for online preconcentration." Thesis, 2012. http://ndltd.ncl.edu.tw/handle/74049617344436707965.

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碩士
國立暨南國際大學
應用化學系
100
The formation of thymidine monophosphate (TMP) and thymidine diphosphate (TDP), which are precursors for DNA synthesis, are catalyzed by thymidine kinase (TK) and thymidylate kinase (TMPK), respectively. Therefore, TK and TMPK activity can be used as markers of DNA synthesis and cell proliferation. In this study, capillary electrophoresis coupled with online preconcentration techniques was used to quantify TMP and TDP in order to estimate the activity of TK and TMPK. Prior to sample injection, a small plug of HCl was pushed into the capillary. The cationic polymer Polyethylenimine (PEI) 2000 in the sample buffer (pH 8.0) formed a complex with ATP primarily. Therefore TMP and TDP were injected selectively into a PEI 2000 modified capillary with a reversed electroosmotic flow by the electrokinetic injection. Then the pH junction of the alkaline sample buffer and the HCl plug made TMP and TDP accumulated. The analyte and PEI 2000 in the background electrolyte (BGE) formed ion-paired complex, thereby decreasing its mobility and resulting in sample stacking. Several parameters affecting the online preconcentration and separation were investigated, including the pH and concentration of the BGE, the concentrations of cationic modifier PEI 2000 in the sample buffer and the BGE, the concentration and the injection volume of the HCl plug, the voltage and time period of the electrokinetic injection, and the separation voltage. The results showed that the PEI 2000 in the BGE resolved the analytes from ATP effectively. Good separation with high separation efficiency and reproducibility was achieved within 7 min under optimal conditions. In comparison with the previous method, the sensitivity was enhanced up to two orders of magnitude with the present method. The linear range of the method was 50-5000 nM for TDP and TMP. The limits of detection of TDP and TMP were 34.9 nM and14.8 nM, respectively. The proposed method may be applied to TK and TMPK activity assays in cells.
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Luo, Yaling, and 羅雅玲. "Monitoring thymidine monophosphate by capillary electrophoresis with pH junction and formation of ion complex for online preconcentration." Thesis, 2011. http://ndltd.ncl.edu.tw/handle/01897101812372573201.

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碩士
國立暨南國際大學
應用化學系
99
The code of life – DNA is composed by deoxyadenosine triphosphate (dATP), deoxycytidine triphosphate (dCTP), thymidine triphosphate (TTP), and deoxyguanosine triphosphate (dGTP). There are two ways to form thymidine monophosphate (TMP) which is further phosphorylated to TTP. One is de novo pathway, and the other is salvage pathway. In the salvage pathway, thymidine is phosphorylated to TMP catalyzed by thymidine kinase (TK). Therefore, the activity of TK is a marker of DNA synthesis and cell proliferation. This study combined capillary electrophoresis (CE) with online preconcentration techniques to monitor TMP. TMP and adenosine triphosphate (ATP) are negatively charged in the sample buffer at pH 8.0. The dynamic pH junction between the background electrolyte and the sample buffer results in the decrease of the charges of analytes. Addition of hexadimethrine bromide (HDB) into the background electrolyte reverses the electroosmotic flow and speeds up the migration of negatively charged analytes. Furthermore, HDB could form ion complex with negatively charged analytes, which increases mass/charge ratios of the analytes. Besides, -cyclodextrin (-CD) was added to resolve TMP from adenosine monophosphate (AMP). Several parameters affecting the separation were optimized including the concentration of HDB, the concentration and the pH value of the background electrolytes and the concentration of -CD. This method is linear in the range of 0.5 M to 50 M and the limit of detection is 0.85 M for TMP. This method can be applied to determine the cellular TK activity in future.
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Chaudhary, Santosh Kumar. "Structural and functional studies on DNA synthesis and repair proteins." Thesis, 2018. https://etd.iisc.ac.in/handle/2005/5320.

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The work reported in this thesis includes structural and functional studies on thymidylate kinase and RecFOR pathway proteins from Thermus thermophilus HB8. In the first part, a study was performed on the thymidylate kinase from the thymidine tri-phosphate biosynthesis pathway. Thymidylate kinase is an important enzyme in DNA synthesis. It catalyzes the conversion of thymidine monophosphate (TMP) to thymidine diphosphate (TDP), with ATP as the preferred phosphoryl donor, in the presence of Mg2+. In this study, the dynamics of the active site and the communication paths between the substrates, ATP and TMP, are reported for thymidylate kinase from Thermus thermophilus. Conformational changes upon ligand binding and the path for communication between the substrates and the protein are important in understanding the catalytic mechanism of the enzyme. High-resolution X-ray crystal structures of thymidylate kinase in apo and ligand-bound states were solved. Structural analyses provide an insight into the mode of substrate binding at the active site. The residues involved in communication between the substrates were identified through network analysis using molecular dynamics simulations. The analyses of mutants suggest that the proper positioning of TMP is important for catalysis and provide an insight into the phosphoryl-transfer mechanism. The substrate binding, catalysis or the product release could be the rate-limiting step in the enzyme catalysis. Most of the studies on thymidylate kinase have either focused on understanding the mode of substrate binding or the mechanism of catalysis, but the product release event remains largely unexplored. This work reports four high-resolution crystal structures of thymidylate kinase from T. thermophilus in apo and product bound states. Random accelerated molecular dynamics (RAMD) simulations were performed to study the product release from the product bound high-resolution crystal structures of thymidylate kinase from T. thermophilus and human. The water molecules present around the Mg2+ ion contribute to the sequential release of the products. The presence of ADP-Mg2+ complex has a minor effect on the release of TDP. Thus, the release of the products from the active site could be random in order. The second part deals with the homologous recombination pathway, the RecFOR pathway. RecF, RecO and RecR proteins mediate the binding of RecA protein on the single strand binding (SSB) protein coated 3’ overhang of DNA. However, their interaction with each other and the DNA molecule is not clear. RecF exists as a monomer in solution but exhibits ATP dependent dimerization and DNA dependent ATP hydrolysis. The interaction assembly of RecF with RecR and DNA is not clear. RecR exists as a dimer in solution, although the crystallographic assembly suggests a tetramer. Thus, the dimeric assembly and the tetrameric assembly of RecF and RecR were stabilized by cysteine mutations at the interface residues and their interactions have been studied
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Book chapters on the topic "Thymidine monophosphate"

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YOSHIDA, H., R. L. HETTICH, J. A. LAVERNE, K. B. JACOBSON, and J. E. TURNER. "CHARACTERIZATION OF RADIATION-INDUCED PRODUCTS IN THYMIDINE 3'- MONOPHOSPHATE BY LASER DESORPTION FTMS." In Radiation Research: A Twentieth-century Perspective, 400. Elsevier, 1991. http://dx.doi.org/10.1016/b978-0-12-168561-4.50125-6.

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William Tong, C. Y. "Antivirals." In Tutorial Topics in Infection for the Combined Infection Training Programme. Oxford University Press, 2019. http://dx.doi.org/10.1093/oso/9780198801740.003.0059.

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Viruses are obligate intracellular pathogens that utilize many of the host metabolic machineries for reproduction. Unlike the binary fission of bacteria, the replication process of viruses is more like a production line with a final assembly process to produce their progenies. Any agents used to prevent viral replication must be specific to the virus and cause as little problem for the host as possible. The rate of virus replication can also cause problems. In rapidly reproducing viruses, the high replication rate generates mutants that could be selected for resistance to antivirals. On the other hand, viruses could remain latent with little metabolic activity. None of the current antivirals are effective against latent viruses. The life cycle of a typical virus goes through the following stages: ● Attachment; ● Entry and uncoating; ● Replication of viral nucleic acid; ● Establishing latency or persistent infection (in some viruses); ● Translation of viral protein and post-translational modifications; ● Secretion and assembly of viral particles; and ● Release from host cells. Each of these steps can be used as antiviral targets. The most common strategy is to use a nucleoside analogue as a false substrate. However, such a false substrate can also be taken up by host polymerase and could result in toxicity, e.g. mitochondrial toxicity in some of the earlier antiretroviral drugs. The most successful example to circumvent this problem is aciclovir, which is the prodrug of the active agent aciclovir tri-phosphate. Aciclovir is a substrate for the viral enzyme thymidine kinase carried by the herpes simplex virus (HSV) and varicella-zoster virus (VZV), which converts it into aciclovir monophosphate. As this only happens inside cells infected by HSV or VZV, it is concentrated only in infected cells. Host enzymes then add further phosphates to form the active agent aciclovir triphosphate, which has a higher affinity to viral polymerase than host polymerase. It acts as a false substrate for the viral polymerase and results in premature termination of nucleic acid replication. A similar mechanism is utilized in ganciclovir against cytomegalovirus (CMV). The viral phosphate kinase involved in the case of CMV is the UL97 protein.
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Conference papers on the topic "Thymidine monophosphate"

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Van Rompaey, Philippe, Vanheusden Veerle, Sylvie Pochet, Hélene Munier-Lehmann, Matheus Froeyen, Piet Herdewijn, and Serge Van Calenbergh. "Thymidine (monophosphate) analogues as Mycobacterium tuberculosis thymidylate kinase inhibitors." In XIIth Symposium on Chemistry of Nucleic Acid Components. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 2002. http://dx.doi.org/10.1135/css200205393.

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Van Calenbergh, Serge, Ineke Van Daele, Sara Van Poecke, Matheus Froeyen, Hélene Munier Lehmann, and Jan Balzarini. "From M. tuberculosis thymidine monophosphate kinase (TMPKmt) inhibitors towards mitochondrial thymidine kinase (TK-2) inhibitors." In XIVth Symposium on Chemistry of Nucleic Acid Components. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 2008. http://dx.doi.org/10.1135/css200810087.

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