Relevant bibliographies by topics / Dihydrofolate reductase

Academic literature on the topic 'Dihydrofolate reductase'

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Published: 4 June 2021
Last updated: 25 January 2023

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Journal articles on the topic "Dihydrofolate reductase"

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Wilquet, Valérie, Mark Van de Casteele, Daniel Gigot, Christianne Legrain, and Nicolas Glansdorff. "Dihydropteridine Reductase as an Alternative to Dihydrofolate Reductase for Synthesis of Tetrahydrofolate in Thermus thermophilus." Journal of Bacteriology 186, no. 2 (January 15, 2004): 351–55. http://dx.doi.org/10.1128/jb.186.2.351-355.2004.

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ABSTRACT A strategy devised to isolate a gene coding for a dihydrofolate reductase from Thermus thermophilus DNA delivered only clones harboring instead a gene (the T. thermophilus dehydrogenase [DH Tt ] gene) coding for a dihydropteridine reductase which displays considerable dihydrofolate reductase activity (about 20% of the activity detected with 6,7-dimethyl-7,8-dihydropterine in the quinonoid form as a substrate). DH Tt appears to account for the synthesis of tetrahydrofolate in this bacterium, since a classical dihydrofolate reductase gene could not be found in the recently determined genome nucleotide sequence (A. Henne, personal communication). The derived amino acid sequence displays most of the highly conserved cofactor and active-site residues present in enzymes of the short-chain dehydrogenase/reductase family. The enzyme has no pteridine-independent oxidoreductase activity, in contrast to Escherichia coli dihydropteridine reductase, and thus appears more similar to mammalian dihydropteridine reductases, which do not contain a flavin prosthetic group. We suggest that bifunctional dihydropteridine reductases may be responsible for the synthesis of tetrahydrofolate in other bacteria, as well as archaea, that have been reported to lack a classical dihydrofolate reductase but for which possible substitutes have not yet been identified.
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Dedhar, S., D. Hartley, D. Fitz-Gibbons, G. Phillips, and J. H. Goldie. "Heterogeneity in the specific activity and methotrexate sensitivity of dihydrofolate reductase from blast cells of acute myelogenous leukemia patients." Journal of Clinical Oncology 3, no. 11 (November 1985): 1545–52. http://dx.doi.org/10.1200/jco.1985.3.11.1545.

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Dihydrofolate reductase activity was found to be highly heterogeneous in terms of its specific activity and methotrexate sensitivity in the blast cells of patients with acute myelogenous leukemia. None of the patients had previously been treated with methotrexate (MTX). The blast cells of four of 12 patients studied contained methotrexate-insensitive forms of dihydrofolate reductase, and the blast cells of three (distinct from the four mentioned previously) of the 12 had significantly higher dihydrofolate reductase activities than the rest. The presence of MTX-insensitive dihydrofolate reductases and high levels of enzyme activity represent intrinsic mechanisms of resistance and may explain the apparent clinical resistance of acute myelogenous leukemia to methotrexate.
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Young, H. K., R. A. Skurray, and S. G. B. Amyes. "Plasmid-mediated trimethoprim-resistance in Staphylococcus aureus. Characterization of the first gram-positive plasmid dihydrofolate reductase (type S1)." Biochemical Journal 243, no. 1 (April 1, 1987): 309–12. http://dx.doi.org/10.1042/bj2430309.

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The trimethoprim-resistance gene located on plasmid pSK1, originally identified in a multi-resistant Staphylococcus aureus from Australia, encodes the production of a dihydrofolate reductase (type S1), which confers a high degree of resistance to its host and is quite unlike any plasmid-encoded dihydrofolate reductase hitherto described. It has a low Mr (19,700) and has a higher specific activity than the constitutive Gram-negative plasmid dihydrofolate reductases. The type S1 enzyme is heat-stable and has a relatively low affinity for the substrate, dihydrofolate (Km 10.8 microM). It is moderately resistant to trimethoprim, and is competitively inhibited by this drug with an inhibitor-binding constant of 11.6 microM. This is the first identification and characterization of a plasmid-encoded trimethoprim-resistant dihydrofolate reductase derived from a Gram-positive species.
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Hammond, S. J., B. Birdsall, M. S. Searle, G. C. K. Roberts, and J. Feeney. "Dihydrofolate reductase." Journal of Molecular Biology 188, no. 1 (March 1986): 81–97. http://dx.doi.org/10.1016/0022-2836(86)90483-3.

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Adrian, P. V., and K. P. Klugman. "Mutations in the dihydrofolate reductase gene of trimethoprim-resistant isolates of Streptococcus pneumoniae." Antimicrobial Agents and Chemotherapy 41, no. 11 (November 1997): 2406–13. http://dx.doi.org/10.1128/aac.41.11.2406.

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Streptococcus pneumoniae isolates resistant to several antimicrobial agent classes including trimethoprim-sulfamethoxazole have been reported with increasing frequency throughout the world. The MICs of trimethoprim, sulfamethoxazole, and trimethoprim-sulfamethoxazole (1:19) for 259 clinical isolates from South Africa were determined, and 166 of these 259 (64%) isolates were resistant to trimethoprim-sulfamethoxazole (MICs > or =20 mg/liter). Trimethoprim resistance was found to be more strongly correlated with trimethoprim-sulfamethoxazole resistance (correlation coefficient, 0.744) than was sulfamethoxazole resistance (correlation coefficient, 0.441). The dihydrofolate reductase genes from 11 trimethoprim-resistant (MICs, 64 to 512 microg/ml) clinical isolates of Streptococcus pneumoniae were amplified by PCR, and the nucleotide sequences were determined. Two main groups of mutations to the dihydrofolate reductase gene were found. Both groups shared six amino acid changes (Glu20-Asp, Pro70-Ser, Gln81-His, Asp92-Ala, Ile100-Leu, and Leu135-Phe). The first group included two extra changes (Lys60-Gln and Pro111-Ser), and the second group was characterized by six additional amino acid changes (Glu14-Asp, Ile74-Leu, Gln91-His, Glu94-Asp, Phe147-Ser, and Ala149-Thr). Chromosomal DNA from resistant isolates and cloned PCR products of the genes encoding resistant dihydrofolate reductases were capable of transforming a susceptible strain of S. pneumoniae to trimethoprim resistance. The inhibitor profiles of recombinant dihydrofolate reductase from resistant and susceptible isolates revealed that the dihydrofolate reductase from trimethoprim-resistant isolates was 50-fold more resistant (50% inhibitory doses [ID50s], 3.9 to 7.3 microM) than that from susceptible strains (ID50s, 0.15 microM). Site-directed mutagenesis experiments revealed that one mutation, Ile100-Leu, resulted in a 50-fold increase in the ID50 of trimethoprim. The resistant dihydrofolate reductases were characterized by highly conserved redundant changes in the nucleotide sequence, suggesting that the genes encoding resistant dihydrofolate reductases may have evolved as a result of inter- or intraspecies recombination by transformation.
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Al-Rubeai, M., and J. W. Dale. "Purification and characterization of dihydrofolate reductase from Mycobacterium phlei." Biochemical Journal 235, no. 1 (April 1, 1986): 301–3. http://dx.doi.org/10.1042/bj2350301.

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The dihydrofolate reductase from Mycobacterium phlei was purified and characterized; it has an Mr of 15 000 and a pI of 4.8. It is competitively inhibited by both methotrexate and trimethoprim, although the affinity is less than for other bacterial dihydrofolate reductases.
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Strehl, Elke, Ingrid Schneider, and Erich F. Elstner. "Inhibition of Dihydrofolate Reductase by Mofebutazon." Zeitschrift für Naturforschung C 48, no. 9-10 (October 1, 1993): 815–17. http://dx.doi.org/10.1515/znc-1993-9-1022.

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Abstract Mofebutazon, Dihydrofolate Reductase, Non-Steroidal Antiinflammatory Drugs (NSAIDs) Mofebutazon, in contrast to phenylbutazon, inhibits dihydrofolate reductase in a concentration-dependent manner. An apparent for mofebutazon and dihydrofolate reductase in the presence of NADPH as electron donor and dihydrofolate as electron acceptor of approx­imately 0.2 mM was calculated.
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Kehrenberg, Corinna, and Stefan Schwarz. "dfrA20, a Novel Trimethoprim Resistance Gene from Pasteurella multocida." Antimicrobial Agents and Chemotherapy 49, no. 1 (January 2005): 414–17. http://dx.doi.org/10.1128/aac.49.1.414-417.2005.

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ABSTRACT A novel trimethoprim resistance gene, designated dfrA20, was detected on the 11-kb plasmid pCCK154 from Pasteurella multocida. The dfrA20 gene codes for a dihydrofolate reductase of 169 amino acids. Sequence comparisons revealed that the DfrA20 protein differed distinctly from all dihydrofolate reductases known so far.
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Farnham, P. J., and R. T. Schimke. "Murine dihydrofolate reductase transcripts through the cell cycle." Molecular and Cellular Biology 6, no. 2 (February 1986): 365–71. http://dx.doi.org/10.1128/mcb.6.2.365-371.1986.

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The murine dihydrofolate reductase gene codes for mRNAs that differ in the length of their 3' untranslated region as well as in the length of their 5' leader sequence. In addition, the dihydrofolate reductase promoter functions bidirectionally, producing a series of RNAs from the opposite strand than the dihydrofolate reductase mRNAs. We have examined the production of these RNAs and their heterogeneous 5' and 3' termini as mouse 3T6 cells progress through a physiologically continuous cell cycle. We found that all of the transcripts traverse the cell cycle in a similar manner, increasing at the G1/S boundary without significantly changing their ratios relative to one another. We conclude that cell-cycle regulation of dihydrofolate reductase is achieved without recruiting new transcription initiation sites and without a change in polyadenylation sites. It appears that the mechanism responsible for the transcriptional cell-cycle regulation of the dihydrofolate reductase gene is manifested only by transiently increasing the efficiency of transcription at the dihydrofolate reductase promoter.
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Farnham, P. J., and R. T. Schimke. "Murine dihydrofolate reductase transcripts through the cell cycle." Molecular and Cellular Biology 6, no. 2 (February 1986): 365–71. http://dx.doi.org/10.1128/mcb.6.2.365.

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The murine dihydrofolate reductase gene codes for mRNAs that differ in the length of their 3' untranslated region as well as in the length of their 5' leader sequence. In addition, the dihydrofolate reductase promoter functions bidirectionally, producing a series of RNAs from the opposite strand than the dihydrofolate reductase mRNAs. We have examined the production of these RNAs and their heterogeneous 5' and 3' termini as mouse 3T6 cells progress through a physiologically continuous cell cycle. We found that all of the transcripts traverse the cell cycle in a similar manner, increasing at the G1/S boundary without significantly changing their ratios relative to one another. We conclude that cell-cycle regulation of dihydrofolate reductase is achieved without recruiting new transcription initiation sites and without a change in polyadenylation sites. It appears that the mechanism responsible for the transcriptional cell-cycle regulation of the dihydrofolate reductase gene is manifested only by transiently increasing the efficiency of transcription at the dihydrofolate reductase promoter.
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Dissertations / Theses on the topic "Dihydrofolate reductase"

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Shrimpton, Paul James. "A computational investigation of dihydrofolate reductase." Thesis, University of Birmingham, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.403014.

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Haddow, J. "Potential suicide inhibitors of dihydrofolate reductase." Thesis, University of Strathclyde, 1986. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.381497.

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Fan, Yongjia. "Bistability in Human Dihydrofolate Reductase Catalysis." The Ohio State University, 2010. http://rave.ohiolink.edu/etdc/view?acc_num=osu1280243471.

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Chui, Wai K. "Non-classical inhibitors of dihydrofolate reductase." Thesis, Aston University, 1990. http://publications.aston.ac.uk/12623/.

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This thesis comprises two main objectives. The first objective involved the stereochemical studies of chiral 4,6-diamino-1-aryl-1,2-dihydro-s-triazines and an investigation on how the different conformations of these stereoisomers may affect their binding affinity to the enzyme dihydrofolate reductase (DHFR). The ortho-substituted 1-aryl-1,2-dihydro-s-triazines were synthesised by the three component method. An ortho-substitution at the C6' position was observed when meta-azidocycloguanil was decomposed in acid. The ortho-substituent restricts free rotation and this gives rise to atropisomerism. Ortho-substituted 4,6-diamino-1-aryl-2-ethyl-1,2-dihydro-2-methyl-s-triazine contains two elements of chirality and therefore exists as four stereoisomers: (S,aR), (R,aS), (R,aR) and (S,aS). The energy barriers to rotation of these compounds were calculated by a semi-empirical molecular orbital program called MOPAC and they were found to be in excess of 23 kcal/mol. The diastereoisomers were resolved and enriched by C18 reversed phase h.p.l.c. Nuclear overhauser effect experiments revealed that (S,aR) and (R,aS) were the more stable pair of stereoisomers and therefore existed as the major component. The minor diastereoisomers showed greater binding affinity for the rat liver DHFR in in vitro assay. The second objective entailed the investigation into the possibility of retaining DHFR inhibitory activity by replacing the classical diamino heterocyclic moiety with an amidinyl group. 4-Benzylamino-3-nitro-N,N-dimethyl-phenylamidine was synthesised in two steps. One of the two phenylamidines indicated weak inhibition against the rat liver DHFR. This weak activity may be due to the failure of the inhibitor molecule to form strong hydrogen bonds with residue Glu-30 at the active site of the enzyme.
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El-Hamamsy, Mervat Hamed Rabu Ibrahem. "Potential antimycobacterial agents targeting dihydrofolate reductase." Thesis, University of Bath, 2005. https://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.418600.

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Guo, Jian Nan. "Thermophilicity and catalytic efficiency in dihydrofolate reductase." Thesis, Cardiff University, 2013. http://orca.cf.ac.uk/56290/.

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This thesis presents an investigation of the hydrogen transfer reactions between dihydrofolate (H2F) and NADPH that are catalysed by the dihydrofolate reductase (DHFR) isolated from Geobacillus stearothermophilus (BsDHFR) as well as an artificial hybrid originating from the DHFRs from mesophilic Escherichia coli (EcDHFR) and hyperthermophilic Thermotoga maritima (TmDHFR). A broad spectrum of studies, focusing on the relationship between structure, thermostability and kinetics, showed that the catalytic behaviour of BsDHFR is generally similar to other monomeric DHFRs, including ones found in the mesophile Escherichia coli and the psychrophile Moritella profunda, but significantly different from the dimeric TmDHFR. The fact that all monomeric DHFRs display similar catalytic behaviour, regardless of their widely different optimal temperatures, suggests that thermostability does not directly relate to catalytic efficiency. The biophysical differences between monomeric DHFRs and TmDHFR are likely derived from the dimeric nature of the hyperthermophilic enzyme. An artificial dimeric variant of EcDHFR, Xet-3, was prepared by introducing residues at the dimer interface of TmDHFR. While thermostability of this variant is enhanced, it showed a great decrease in its steady-state and pre-steady-state rate constants. Given that the corresponding rate constants did not increase when the loops are released in the monomeric variant of TmDHFR, the lowered catalytic ability in Xet-3 is likely a consequence of geometric distortion of the active site and loss of loop flexibility that is catalytically important in EcDHFR. In contrast, the relatively poor activity of TmDHFR is not simply a consequence of reduced loop flexibility; the dimer interface of TmDHFR plays a rather complicated role in catalysis.
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Bevan, A. W. "Specificity of inhibitor binding to dihydrofolate reductase." Thesis, University College London (University of London), 1985. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.352532.

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Singh, Priyanka. "Enzyme catalysis and dynamics in dihydrofolate reductase." Diss., University of Iowa, 2015. https://ir.uiowa.edu/etd/5635.

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Enzyme motions on a broad range of time scales can play an important role in various intra- and intermolecular events, including substrate bindings, chemical conversions, and products release. The relationship between protein motions and catalytic activity is of considerable contemporary interest in enzymology. To understand the factors influencing the rates of enzyme catalyzed reactions, the dynamics of the protein-solvent-substrate complex must be considered. The enzyme dihydrofolate reductase from Escherichia coli (EcDHFR) is often used as a model system in various biophysical studies, including those aimed at the examination of motions across the protein that may affect the catalyzed chemical transformation. Previously, molecular dynamics calculations, bioinformatics studies and intrinsic kinetic isotope effects (KIEs) of DHFR have suggested a network of coupled motions across the whole protein that is correlated to the reaction coordinate. This thesis describes studies that extend upon those initial results by studying the nature and extent of enzyme dynamics and motions in DHFR, both by using traditional experimental methods and by developing new biophysical probes of protein dynamics in this system. Kinetic techniques, site directed mutagenesis, methods involving isotopic labeling of substrates and proteins, immobilization techniques and molecular recognition force spectroscopy were combined to study EcDHFR. The major experimental methodology described in the subsequent chapters is the determination and analysis of intrinsic KIEs in a variety of EcDHFR mutants. The studies demonstrated that residues G121, M42 and F125, all of which are remote from the active site, FR participate in a network of coupled motions across the enzyme. Until recently, the missing link in our understanding of DHFR catalysis was the lack of a path by which such remote residues can affect the catalyzed chemistry at the active site. A later chapter describes studies that indicate synergism between a residue, G121, in that remote dynamic network and an active site residue, I14. In another related study all carbons and nitrogens, as well as non-exchangeable protons in EcDHFR were changed to their heavy isotopes (13C, 15N, 2H). This heavy enzyme has also been shown to be an efficient tool in addressing the heated debate regarding the role of protein dynamics in catalysis. Such enzyme generates a vibrationally perturbed "heavy ecDHFR", and the effect on the altered vibrations on catalysis was studied. Finally, the last two chapters describe techniques developed to immobilize DHFR on an AFM-mica chip via DNA linkers, concentration and activity assays of the immobilized enzyme, and single-molecule studies of the interaction between a tight inhibitor (methotrexate) and the enzyme. These studies reveal the distribution of states and interactions with ligands - a property not accessible for studies of a large ensemble of molecules. The high spatial and force resolution provided by AFM under physiological conditions have been utilized in this study to quantify the force-distance relationships of DHFR-methotrexate interactions. In the future, such an understanding of the interplay between enzyme function, structure and dynamics could eventually permit improved de novo construction of artificial biocatalysts, enable better inhibitor and drug design, and in general, further advance our ability to manipulate enzyme catalysis to our ultimate benefit.
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Al-Batayneh, Khalid Mubarak. "Mutations in Drosophila dihydrofolate reductase and methotrexate resistance." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 2001. http://www.collectionscanada.ca/obj/s4/f2/dsk3/ftp05/NQ63399.pdf.

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Khaw, Lake Ee. "Isotopic labelling of dihydrofolate reductase for NMR studies." Thesis, Georgia Institute of Technology, 1991. http://hdl.handle.net/1853/25179.

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Books on the topic "Dihydrofolate reductase"

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Chui, Wai Keung. Non-classical inhibitors of dihydrofolate reductase. Birmingham: Aston University. Department of Pharmaceutical Sciences, 1990.

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Meek, Michelle Anne. Design and synthesis of inhibibitors of dihydrofolate reductase. Birmingham: Aston University. Departmentof Pharmaceutical Sciences, 1988.

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Yap, Chee Hoong. Potential inhibitors of dihydrofolate reductase: Synthesis and NMR spectroscopy. Birmingham: University of Aston. Department of Molecular Sciences (Chemistry), 1985.

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Rooke, Stuart. Some reactions of vinyl sulfimides and synthesis of novel inhibitors of dihydrofolate reductase. [s.l.]: typescript, 1997.

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Schesser, Kurt. E2F site-dependent regulation of dihydrofolate reductase promotor activity during myogenesis. 1994.

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Schesser, Kurt. E2F site-dependent regulation of dihydrofolate reductase promotor activity during myogenesis. 1994.

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Kolmodin, Karin. Computer Simulation of Protein Tyrosine Phosphatase Reaction Mechanisms and Dihydrofolate Reductase Inhibition. Uppsala Universitet, 2001.

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Schmidt, Edward Eric. Repression of dihydrofolate reductase synthesis during myogenesis: Identification and characterization of a transcriptional regulatory mechanism. 1990.

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Nordberg, Malin Graffner. Approaches to Soft Drug Analogues of Dihydrofolate Reductase Inhibitors: Design and Synthesis (Comprehensive Summaries of Uppsala Dissertations from the Faculty of Pharmacy, 252). Uppsala Universitet, 2001.

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Book chapters on the topic "Dihydrofolate reductase"

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Schomburg, D., M. Salzmann, and D. Stephan. "Dihydrofolate reductase." In Enzyme Handbook 7, 11–24. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-78521-4_3.

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Benkovic, Stephen J., and Carston R. Wagner. "Dihydrofolate Reductase." In Protein Design and the Development of New Therapeutics and Vaccines, 237–49. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4684-5739-1_12.

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Blakley, Raymond L. "Eukaryotic Dihydrofolate Reductase." In Advances in Enzymology - and Related Areas of Molecular Biology, 23–102. Hoboken, NJ, USA: John Wiley & Sons, Inc., 2006. http://dx.doi.org/10.1002/9780470123164.ch2.

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Ranaghan, Kara E. "Dihydrofolate Reductase - Computational Studies." In Encyclopedia of Biophysics, 472–74. Berlin, Heidelberg: Springer Berlin Heidelberg, 2013. http://dx.doi.org/10.1007/978-3-642-16712-6_263.

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Ledbetter, John W., Wolfgang Pfleiderer, and James H. Freisheim. "Laser-Sensitized Tautomers in Dihydrofolate Reductase." In Advances in Experimental Medicine and Biology, 499–502. Boston, MA: Springer US, 1993. http://dx.doi.org/10.1007/978-1-4615-2960-6_100.

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Ferrari, Stefania, Valeria Losasso, Puneet Saxena, and Maria Paola Costi. "Targeting the Trypanosomatidic Enzymes Pteridine Reductase and Dihydrofolate Reductase." In Trypanosomatid Diseases, 445–72. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2013. http://dx.doi.org/10.1002/9783527670383.ch24.

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Mayer, Ruth J., Jin-Tann Chen, Kazunari Taira, and Stephen J. Benkovic. "Site-Specific Mutations in Dihydrofolate Reductase at the Dihydrofolate Binding Site." In Proteins, 513–19. Boston, MA: Springer US, 1987. http://dx.doi.org/10.1007/978-1-4613-1787-6_52.

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Kuyper, Lee F. "Receptor-Based Design of Dihydrofolate Reductase Inhibitors." In Protein Design and the Development of New Therapeutics and Vaccines, 297–327. Boston, MA: Springer US, 1990. http://dx.doi.org/10.1007/978-1-4684-5739-1_15.

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Goldstein, Melanie, and Nina M. Goodey. "Distal Regions Regulate Dihydrofolate Reductase-Ligand Interactions." In Methods in Molecular Biology, 185–219. New York, NY: Springer US, 2020. http://dx.doi.org/10.1007/978-1-0716-1154-8_12.

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Pompe, Matevž, Marjana Novič, Jure Zupan, and Marjan Veber. "Predicting Maximum Bioactivity of Dihydrofolate Reductase Inhibitors." In Molecular Modeling and Prediction of Bioactivity, 305–6. Boston, MA: Springer US, 2000. http://dx.doi.org/10.1007/978-1-4615-4141-7_53.

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Conference papers on the topic "Dihydrofolate reductase"

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Sittikornpaiboon, Pimonluck, Pisanu Toochinda, and Luckhana Lawtrakul. "The interactions of dihydrofolate with M. tuberculosis dihydrofolate reductase." In 2016 Second Asian Conference on Defence Technology (ACDT). IEEE, 2016. http://dx.doi.org/10.1109/acdt.2016.7437667.

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Heppler, Lisa N., Sarah R. Walker, Sanaz Attarha, Brent D. Page, and David A. Frank. "Abstract 387: Pyrimethamine inhibits STAT3 transcriptional activity via dihydrofolate reductase." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.am2019-387.

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Heppler, Lisa N., Sarah R. Walker, Sanaz Attarha, Brent D. Page, and David A. Frank. "Abstract 387: Pyrimethamine inhibits STAT3 transcriptional activity via dihydrofolate reductase." In Proceedings: AACR Annual Meeting 2019; March 29-April 3, 2019; Atlanta, GA. American Association for Cancer Research, 2019. http://dx.doi.org/10.1158/1538-7445.sabcs18-387.

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Hsieh, Yi-Ching, Rialnat AdeBisi Lawal, Kathleen Scotto, Debabrata Banerjee, Emine Ercikan Abali, and Joseph R. Bertino. "Abstract 4543: Targeting the NADPH binding site of dihydrofolate reductase for cancer therapy." 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.am10-4543.

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Dolzhenko, Anton, Anna Dolzhenko, and Wai-Keung Chui. "Synthesis and Dihydrofolate Reductase Inhibitory Activity of 2-amino-[1,3,5]triazino[1,2-a]benzimidazoles." In The 9th International Electronic Conference on Synthetic Organic Chemistry. Basel, Switzerland: MDPI, 2005. http://dx.doi.org/10.3390/ecsoc-9-01515.

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Zettlmeiβl, G., H. Ragg, and H. Karges. "EXPRESSION OF BIOLOGICALLY ACTIVE HUMAN ANTITHROMBIN III IN CHINESE HAMSTER OVARY CELLS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643683.

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Expression of human antithrombin III (AT III) at high levels has been achieved in Chinese hamster ovary (CH0) cells by cotransfection and subsequent coamplification of the transfected sequences. Expression vectors containing the AT III cDNA gene and a dihydrofolate reductase (DHFR) cDNA gene were transfected into CH0 DHFR-deficient cells. About 20% of the DHFR+ transformants secreted recombinant human AT III into the medium. Stepwise selection of the AT III producing DHFR+ -transformants in increasing concentrations of methotrexate generated cells which had amplified the AT III géne. We determined the copy number of the AT III cDNA and the relative amounts of AT III specific mRNA at different stages of the amplification process. Transfected CH0 cell lines expressed elevated immunreactive levels of human AT III.AT III secreted from these cell lines had the same molecular weight (60 kDa), immunological properties and biological activities as AT III obtained from human plasma. In vivo data concerning the inhibition of glycosylation by different drugs suggest that recombinant AT III from CHO cells is glycosylated according to a complex type pattern.
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Cody, Vivian, Jennifer Piraino, James Pace, and Sherry F. Queener. "Abstract 2676: Unusual binding of TMP in two different sites in the binary complex with the Q35S/N64F double mutant of human dihydrofolate reductase." 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.am10-2676.

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Coy-Barrera, Ericsson, Chonny Herrera-Acevedo, Daissy Monroy-Velandia, and Areli Flores-Gaspar. "IN SILICO STUDIES TO EVALUATE INTERACTIONS BETWEEN KAURANE-TYPE DITERPENES AND THE DIHYDROFOLATE REDUCTASE – THYMILIDINE SYNTHASE OF THREE LEISHMANIA SPECIES." In MOL2NET 2018, International Conference on Multidisciplinary Sciences, 4th edition. Basel, Switzerland: MDPI, 2018. http://dx.doi.org/10.3390/mol2net-04-05517.

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Siam, Mohammad Kawsar Sharif, Muhammad Sameer Hossain, Eva Rahman Kabir, and Samiul Alam Rajib. "In Silico Structure Based Designing of Dihydrofolate Reductase Enzyme Antagonists and Potential Small Molecules That Target DHFR Protein to Inhibit the Folic Acid Biosynthetic Pathways." In CSBio '17: 8th International Conference on Computational Systems-Biology and Bioinformatics. New York, NY, USA: ACM, 2017. http://dx.doi.org/10.1145/3156346.3156358.

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Sandy, Semuel, and Iman H. S. Sasto. "In-silico interaction of antimalarial activity of secondary metabolic compounds Ginkgo biloba L. against wild type protein Plasmodium falciparum dihydrofolate reductase-thymidylate synthase (PfDHFR-TS)." In 10TH INTERNATIONAL CONFERENCE ON APPLIED SCIENCE AND TECHNOLOGY. AIP Publishing, 2022. http://dx.doi.org/10.1063/5.0104438.

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