Relevant bibliographies by topics / Dna polymerase enzymes

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers
  6. Reports

Academic literature on the topic 'Dna polymerase enzymes'

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

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Journal articles on the topic "Dna polymerase enzymes"

1

McInerney, Peter, Paul Adams, and Masood Z. Hadi. "Error Rate Comparison during Polymerase Chain Reaction by DNA Polymerase." Molecular Biology International 2014 (August 17, 2014): 1–8. http://dx.doi.org/10.1155/2014/287430.

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As larger-scale cloning projects become more prevalent, there is an increasing need for comparisons among high fidelity DNA polymerases used for PCR amplification. All polymerases marketed for PCR applications are tested for fidelity properties (i.e., error rate determination) by vendors, and numerous literature reports have addressed PCR enzyme fidelity. Nonetheless, it is often difficult to make direct comparisons among different enzymes due to numerous methodological and analytical differences from study to study. We have measured the error rates for 6 DNA polymerases commonly used in PCR applications, including 3 polymerases typically used for cloning applications requiring high fidelity. Error rate measurement values reported here were obtained by direct sequencing of cloned PCR products. The strategy employed here allows interrogation of error rate across a very large DNA sequence space, since 94 unique DNA targets were used as templates for PCR cloning. The six enzymes included in the study, Taq polymerase, AccuPrime-Taq High Fidelity, KOD Hot Start, cloned Pfu polymerase, Phusion Hot Start, and Pwo polymerase, we find the lowest error rates with Pfu, Phusion, and Pwo polymerases. Error rates are comparable for these 3 enzymes and are >10x lower than the error rate observed with Taq polymerase. Mutation spectra are reported, with the 3 high fidelity enzymes displaying broadly similar types of mutations. For these enzymes, transition mutations predominate, with little bias observed for type of transition.
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Pospiech, Helmut, and Juhani E. Syväoja. "DNA Polymerase e - More Than a Polymerase." Scientific World JOURNAL 3 (2003): 87–104. http://dx.doi.org/10.1100/tsw.2003.08.

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This paper presents a comprehensive review of the structure and function of DNA polymerase e. Together with DNA polymerases a and d, this enzyme replicates the nuclear DNA in the eukaryotic cell. During this process, DNA polymerase a lays down RNA-DNA primers that are utilized by DNA polymerases d and e for the bulk DNA synthesis. Attempts have been made to assign these two enzymes specifically to the synthesis of the leading and the lagging strand. Alternatively, the two DNA polymerases may be needed to replicate distinct regions depending on chromatin structure. Surprisingly, the essential function of DNA polymerase e does not depend on its catalytic activity, but resides in the nonenzymatic carboxy-terminal domain. This domain not only mediates the interaction of the catalytic subunit with the three smaller regulatory subunits, but also links the replication machinery to the S phase checkpoint. In addition to its role in DNA replication, DNA polymerase e fulfils roles in the DNA synthesis step of nucleotide excision and base excision repair, and has been implicated in recombinational processes in the cell.
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McDonald, John P., Agnès Tissier, Ekaterina G. Frank, Shigenori Iwai, Fumio Hanaoka, and Roger Woodgate. "DNA polymerase iota and related Rad30–like enzymes." Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences 356, no. 1405 (January 29, 2001): 53–60. http://dx.doi.org/10.1098/rstb.2000.0748.

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Until recently, the molecular mechanisms of translesion DNA synthesis (TLS), a process whereby a damaged base is used as a template for continued replication, was poorly understood. This area of scientific research has, however, been revolutionized by the finding that proteins long implicated in TLS are, in fact, DNA polymerases. Members of this so–called UmuC/DinB/Rev1/Rad30 superfamily of polymerases have been identified in prokaryotes, eukaryotes and archaea. Biochemical studies with the highly purified polymerases reveal that some, but not all, can traverse blocking lesions in template DNA. All of them share a common feature, however, in that they exhibit low fidelity when replicating undamaged DNA. Of particular interest to us is the Rad30 subfamily of polymerases found exclusively in eukaryotes. Humans possess two Rad30 paralogs, Rad30A and Rad30B. The RAD30A gene encodes DNA polymerase η and defects in the protein lead to the xeroderma pigmentosum variant (XP–V) phenotype in humans. Very recently RAD30B has also been shown to encode a novel DNA polymerase, designated as Pol ι. Based upon in vitro studies, it appears that Pol ι has the lowest fidelity of any eukaryotic polymerase studied to date and we speculate as to the possible cellular functions of such a remarkably error–prone DNA polymerase.
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MIZUSHINA, Yoshiyuki, Akira IIDA, Keisuke OHTA, Fumio SUGAWARA, and Kengo SAKAGUCHI. "Novel triterpenoids inhibit both DNA polymerase and DNA topoisomerase." Biochemical Journal 350, no. 3 (September 8, 2000): 757–63. http://dx.doi.org/10.1042/bj3500757.

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As described previously, we found that new triterpenoid compounds, designated fomitellic acids A and B, which selectively inhibit the activities of mammalian DNA polymerases α and β [Mizushina, Tanaka, Kitamura, Tamai, Ikeda, Takemura, Sugawara, Arai, Matsukage, Yoshida and Sakaguchi (1998) Biochem. J. 330, 1325–1332; Tanaka, Kitamura, Mizushina, Sugawara and Sakaguchi (1998) J. Nat. Prod. 61, 193–197] and that a known triterpenoid, ursolic acid, is an inhibitor of human DNA topoisomerases I and II (A. Iida, Y. Mizushina and K. Sakaguchi, unpublished work). Here we report that all of these triterpenoids are potent inhibitors of calf DNA polymerase α, rat DNA polymerase β and human DNA topoisomerases I and II, and show moderate inhibitory effects on plant DNA polymerase II and human immunodeficiency virus reverse transcriptase. However, these compounds did not influence the activities of prokaryotic DNA polymerases such as Escherichia coli DNA polymerase I or other DNA metabolic enzymes such as human telomerase, T7 RNA polymerase and bovine deoxyribonuclease I. These triterpenoids were not only mammalian DNA polymerase inhibitors but also inhibitors of DNA topoisomerases I and II even though the enzymic characteristics of DNA polymerases and DNA topoisomerases, including their modes of action, amino acid sequences and three-dimensional structures, differed markedly. These triterpenoids did not bind to DNA, suggesting that they act directly on these enzymes. Because the three-dimensional structures of fomitellic acids were shown by computer simulation to be very similar to that of ursolic acid, the DNA-binding sites of both enzymes, which compete for the inhibitors, might be very similar. Fomitellic acid A and ursolic acid prevented the growth of NUGC cancer cells, with LD50 values of 38 and 30µM respectively.
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Wright, G. E. "Nucleotide probes of DNA polymerases." Acta Biochimica Polonica 43, no. 1 (March 31, 1996): 115–24. http://dx.doi.org/10.18388/abp.1996_4522.

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The modified nucleotides, N2-(p-n-butylphenyl)dGTP and 2-(p-n-butylanilino) dATP and related compounds have been developed as inhibitor-probes of B family DNA polymerases. Synthetic approaches to these compounds are summarized. The nucleotides are potent, non-substrate inhibitors of DNA polymerase a. In contrast, they inhibit other members of the family with less potency but act as substrates for these enzymes. Modelling of the inhibitor: enzyme binding mechanism has been done based on the known structure of E. coli DNA polymerase I, and site-directed mutagenesis experiments to evaluate this mechanism are proposed.
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Makioka, A., B. Stavros, J. T. Ellis, and A. M. Johnson. "Detection and characterization of DNA polymerase activity in Toxoplasma gondii." Parasitology 107, no. 2 (August 1993): 135–39. http://dx.doi.org/10.1017/s0031182000067238.

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SUMMARYA DNA polymerase activity has been detected and characterized in crude extracts from tachzoites of Toxoplasma gondii. The enzyme has a sedimentation coefficient of 6·4 S, corresponding to an approximate molecular weight of 150000 assuming a globular shape. Like mammalian DNA polymerase α, the DNA polymerase of T. gondii was sensitive to N-ethylmaleimide and inhibited by high ionic strength. However, the enzyme activity was not inhibited by aphidicolin which is an inhibitor of mammalian DNA polymerases α, δ and ε and also cytosine-β-D-arabinofuranoside-5′-triphosphate which is an inhibitor of α polymerase. The activity was inhibited by 2′,3′-dideoxythymidine-5′-triphosphate which is an inhibitor of mammalian DNA polymerase β and γ. Magnesium ions (Mg2+) were absolutely required for activity and its optimal concentration was 6 mM. The optimum potassium (K+) concentration was 50 mM and a higher concentration of K+ markedly inhibited the activity. Activity was optimal at pH 8. Monoclonal antibodies against human DNA polymerase did not bind to DNA polymerase of T. gondii. Thus the T. gondii enzyme differs from the human enzymes and may be a useful target for the design of toxoplasmacidal drugs.
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Mattila, P., J. Korpela, T. Tenkanen, and K. Pitkämem. "Fidelity of DNA synthesis by the Thermococcus litoralis DNA polymerase—an extremely heat stable enzyme with proofreading activity." Nucleic Acids Research 19, no. 18 (September 25, 1991): 4967–73. http://dx.doi.org/10.1093/nar/19.18.4967.

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Abstract We demonstrate that the DNA polymerase isolated from Thermococcus litoralis (VentTM DNA polymerase) is the first thermostable DNA polymerase reported having a 3′—5′ proofreading exonuclease activity. This facilitates a highly accurate DNA synthesis in vitro by the polymerase. Mutational frequencies observed in the base substitution fidelity assays were in the range of 30×10−6. These values were 5–10 times lower compared to other thermostable DNA polymerases lacking the proofreading activity. All classes of DNA polymerase errors (transitions, transversions, frameshift mutations) were assayed using the forward mutational assay (1). The mutation frequencies of Thermococcus litoralis DNA polymerase varied between 15−35×10−4 being 2 – 4 times lower than the respective values obtained using enzymes without proofreading activity. We also noticed that the fidelity of the DNA polymerase from Thermococcus litoralis responds to changes in dNTP concentration, units of enzyme used per one reaction and the concentration of MgSO4 relative to the total concentration of dNTPs present in the reaction. The high fidelity DNA synthesis In vitro by Thermococcus litoralis DNA polymerase provides good possibilities for maintaining the genetic information of original target DNA sequences intact in the DNA amplification applications.
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Pezo, Valerie, Faten Jaziri, Pierre-Yves Bourguignon, Dominique Louis, Deborah Jacobs-Sera, Jef Rozenski, Sylvie Pochet, et al. "Noncanonical DNA polymerization by aminoadenine-based siphoviruses." Science 372, no. 6541 (April 29, 2021): 520–24. http://dx.doi.org/10.1126/science.abe6542.

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Bacteriophage genomes harbor the broadest chemical diversity of nucleobases across all life forms. Certain DNA viruses that infect hosts as diverse as cyanobacteria, proteobacteria, and actinobacteria exhibit wholesale substitution of aminoadenine for adenine, thereby forming three hydrogen bonds with thymine and violating Watson-Crick pairing rules. Aminoadenine-encoded DNA polymerases, homologous to the Klenow fragment of bacterial DNA polymerase I that includes 3′-exonuclease but lacks 5′-exonuclease, were found to preferentially select for aminoadenine instead of adenine in deoxynucleoside triphosphate incorporation templated by thymine. Polymerase genes occur in synteny with genes for a biosynthesis enzyme that produces aminoadenine deoxynucleotides in a wide array of Siphoviridae bacteriophages. Congruent phylogenetic clustering of the polymerases and biosynthesis enzymes suggests that aminoadenine has propagated in DNA alongside adenine since archaic stages of evolution.
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Kropp, Heike Maria, Simon Leonard Dürr, Christine Peter, Kay Diederichs, and Andreas Marx. "Snapshots of a modified nucleotide moving through the confines of a DNA polymerase." Proceedings of the National Academy of Sciences 115, no. 40 (September 17, 2018): 9992–97. http://dx.doi.org/10.1073/pnas.1811518115.

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DNA polymerases have evolved to process the four canonical nucleotides accurately. Nevertheless, these enzymes are also known to process modified nucleotides, which is the key to numerous core biotechnology applications. Processing of modified nucleotides includes incorporation of the modified nucleotide and postincorporation elongation to proceed with the synthesis of the nascent DNA strand. The structural basis for postincorporation elongation is currently unknown. We addressed this issue and successfully crystallized KlenTaq DNA polymerase in six closed ternary complexes containing the enzyme, the modified DNA substrate, and the incoming nucleotide. Each structure shows a high-resolution snapshot of the elongation of a modified primer, where the modification “moves” from the 3′-primer terminus upstream to the sixth nucleotide in the primer strand. Combining these data with quantum mechanics/molecular mechanics calculations and biochemical studies elucidates how the enzyme and the modified substrate mutually modulate their conformations without compromising the enzyme’s activity significantly. The study highlights the plasticity of the system as origin of the broad substrate properties of DNA polymerases and facilitates the design of improved systems.
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Bebenek, Anna, Geraldine T. Carver, Holly Kloos Dressman, Farid A. Kadyrov, Joseph K. Haseman, Vasiliy Petrov, William H. Konigsberg, Jim D. Karam, and John W. Drake. "Dissecting the Fidelity of Bacteriophage RB69 DNA Polymerase: Site-Specific Modulation of Fidelity by Polymerase Accessory Proteins." Genetics 162, no. 3 (November 1, 2002): 1003–18. http://dx.doi.org/10.1093/genetics/162.3.1003.

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Abstract Bacteriophage RB69 encodes a replicative B-family DNA polymerase (RB69 gp43) with an associated proofreading 3′ exonuclease. Crystal structures have been determined for this enzyme with and without DNA substrates. We previously described the mutation rates and kinds of mutations produced in vivo by the wild-type (Pol+ Exo+) enzyme, an exonuclease-deficient mutator variant (Pol+ Exo-), mutator variants with substitutions at Tyr567 in the polymerase active site (PolM Exo+), and the double mutator PolM Exo-. Comparing the mutational spectra of the Pol+ Exo- and Pol+ Exo+ enzymes revealed the patterns and efficiencies of proofreading, while Tyr567 was identified as an important determinant of base-selection fidelity. Here, we sought to determine how well the fidelities of the same enzymes are reflected in vitro. Compared to their behavior in vivo, the three mutator polymerases exhibited modestly higher mutation rates in vitro and their mutational predilections were also somewhat different. Although the RB69 gp43 accessory proteins exerted little or no effect on total mutation rates in vitro, they strongly affected mutation rates at many specific sites, increasing some rates and decreasing others.
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Dissertations / Theses on the topic "Dna polymerase enzymes"

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Talanian, Robert Vincent. "Development of Selective Inhibitors of DNA Polymerase Delta: A Thesis." eScholarship@UMMS, 1989. https://escholarship.umassmed.edu/gsbs_diss/66.

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This thesis is divided into three parts, united by the theme of the development of selective inhibitors of mammalian cell DNA polymerase delta (pol δ). The first part consists of an investigation of the cytotoxic mechanism(s) of certain 2-substituted adenine analogs, selected on the basis of their inhibitory properties towards DNA polymerase alpha (pol α) and mammalian cell DNA synthesis. The second is a direct search for inhibitors of isolated pol δ, and an investigation of inhibitory mechanisms. The third consists of measurement of the effects of a selective pol δ inhibitor on cellular DNA synthesis. Mechanism of Cytotoxicity of 2-substituted adenine analoqs. The mechanism of inhibition by 2-(p-n-butylanilino)-2'-deoxyadenosine (BuAdA), and related compounds, of Chinese hamster ovary (CHO) cell ([3H]thymidine [3H]TdR) incorporation, was investigated. The potency of the compound could largely be explained by its potency (IC50 = 23 μM) as an inhibitor of CHO cell [3H]TdR uptake. BuAdA inhibited incorporation by CHO cells of [32p]phosphate into DNA relatively weakly, displaying an IC50value of 80 μM. Differential inhibition of DNA polymerases alpha and delta. Known DNA polymerase inhibitors of a structurally wide range were screened for their ability to inhibit pol δ derived from calf thymus selectively with respect to pol α derived from the same tissue. Pyrophosphate (PPi) and difluoromethanediphosphonate each inhibited pol δ weakly, but with greater potency than pol α. Based on this lead, an expanded series of PPi analogs was screened. Carbonyldiphosphonate (COMDP) inhibited pol δ with a potency (Ki = 1.8 μM) twenty-two times greater than that displayed for pol α. Kinetic studies indicated that COMDP inhibited pol δ competitively with the dNTP specified by the template, but not competitively with the template:primer. Analogous experiments with pol α showed that the compound inhibited that enzyme uncompetitively with the dNTP, and not competitively with the template:primer. COMDP was a weak inhibitor of the 3' → 5' exonuclease activity of pol δ, displaying an IC50value greater than 1 mM. Inhibition of permeabilized cell DNA synthesis bv a selective pol δ inhibitor. The potency of COMDP as an inhibitor of permeabilized CHO cell DNA synthesis (IC50= 200 μM) did not clearly indicate the participation of pol δ in cellular DNA replication. Prospectus. The thesis concludes with a prospectus for the development of pol δ inhibitors with improved properties compared to COMDP.
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Nourizad, Nader. "Recombinant Enzymes in Pyrosequencing Technology." Doctoral thesis, KTH, Biotechnology, 2004. http://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-3765.

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Pyrosequencing is a DNA sequencing method based on thedetection of released pyrophosphate (PPi) during DNA synthesis.In a cascade of enzymatic reactions, visible light isgenerated, which is proportional to the number of nucleotidesincorporated into the DNA template. When dNTP(s) areincorporated into the DNA template, inorganic PPi is released.The released PPi is converted to ATP by ATP sulfurylase, whichprovides the energy to luciferase to oxidize luciferin andgenerate light. The excess of dNTP(s) and the ATP produced areremoved by the nucleotide degrading enzyme apyrase.

The commercially available enzymes, isolated from nativesources, show batch-tobatch variations in activity and quality,which decrease the efficiency of the Pyrosequencing reaction.Therefore, the aim of the research presented in this thesis wasto develop methods to recombinantly produce the enzymes used inthe Pyrosequencing method. Production of the nucleotidedegrading enzyme apyrase by Pichia pastoris expression system,both in small-scale and in an optimized large-scale bioreactor,is described. ATP sulfurylase, the second enzyme in thePyrosequencing reaction, was produced inEscherichia coli. The protein was purified and utilizedin the Pyrosequencing method. Problems associated with enzymecontamination (NDP kinase) and batch-to-batch variations wereeliminated by the use of the recombinant ATP sulfurylase.

As a first step towards sequencing on chip-format,SSB-(single-strand DNA binding protein)-luciferase and KlenowDNA polymerase-luciferase fusion proteins were generated inorder to immobilize the luciferase onto the DNA template.

The application field for the Pyrosequencing technology wasexpanded by introduction of a new method for clone checking anda new method for template preparation prior the Pyrosequencingreaction.

Keywords:apyrase, Pyrosequencing technology, Zbasictag fusion, luciferase, ATP sulfurylase, dsDNAsequencing, clone checking, Klenow-luciferase, SSB-luciferase,Pichia pastoris, Echerichia coli.

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Evans, Geraint Wyn. "Real-time single-molecule observations of conformational changes in DNA polymerase." Thesis, University of Oxford, 2013. http://ora.ox.ac.uk/objects/uuid:fdf11b59-2e58-4174-9219-9d61e4528f65.

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Genetic information is encoded in the long sequence of bases which form DNA, which is replicated during cell division by enzymes known as DNA Polymerases. Polymerases replicate DNA extremely accurately to avoid errors which can cause cell death and diseases such as cancer, although the mechanisms behind these extraordinary fidelities are not well understood. A large conformational change in the protein, in which the “fingers" subdomain closes around an incoming nucleotide, is thought to be implicated in these fidelity mechanisms. Here we present an assay to monitor this conformational change in single polymerase molecules, in real-time. We achieve this using total-internal-reflection-fluorescence (TIRF) microscopy to monitor the fluorescence resonance energy transfer (FRET) of an intra-protein dye labelled DNA Polymerase I (KF) as it binds to surface-immobilised DNA. Initially, we investigated the polymerase fingers-conformations during the pre-chemistry polymerisation reaction, resolving forward and backward rates which would be challenging to observe using ensemble techniques. These observations confirmed that KF closes rapidly around complementary nucleotide, but we discovered that the reverse step, fingers-opening, is particularly slow relative to chemistry. These finger kinetics act to remove the influence of the reaction rate-limiting step on fidelity, surprising given decades of investigations have focused on the rate-limiting step as the key determinant of fidelity. We also use our kinetic measurements to quantify contributions of different reaction steps to the macroscopic error rate of the polymerase. Subsequently, we developed our assay to investigate the fingers-conformations across the entire DNA polymerisation reaction. We observed single-nucleotide incorporations, and processive DNA polymerisation at high and low nucleotide concentrations, which suggested heterogeneous nucleotide incorporation rates. The observations demonstrated that the post-chemistry slow step that limits processive polymerisation occurs before post-chemistry fingers-opening, or is accounted for by post-chemistry fingers-opening. We observe a correlation in turn-over kinetics and binary complex kinetics, suggesting that turn-over rates could be limited by the intrinsic dynamics of the binary complex, as seen in other protein systems, although more work is needed on this.
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Showalter, Alexander Keith. "KINETIC STUDIES OF TWO ERROR-PRONE DNA REPAIR ENZYMES: POSSIBLE MECHANISMS FOR VIRAL MUTAGENESIS." Connect to this title online, 2002. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1016207119.

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Thesis (Ph. D.)--Ohio State University, 2002.
Title from first page of PDF file. Document formatted into pages; contains xii, 97 p.; also contains graphics (some col.). Includes abstract and vita. Advisor: Ming-Daw Tsai, Dept. of Chemistry. Includes bibliographical references (p. 92-97).
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Stephenson, Anthony Aaron. "Mechanistic studies of enzymes involved in DNA transactions." The Ohio State University, 2018. http://rave.ohiolink.edu/etdc/view?acc_num=osu1531497128385619.

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Madsen, Susan M. "Divergence in repetitive DNA sequences among three sitopsis wheat species /." free to MU campus, to others for purchase, 1998. http://wwwlib.umi.com/cr/mo/fullcit?p9901260.

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Arndt, Joseph W. "Characterization and structural determination of metalloenzymes DNA polymerase beta, carboxypeptidase, and acetyl coenzyme-A decarbonylase/synthase /." Columbus, OH : Ohio State University, 2003. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1061312369.

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Thesis (Ph. D.)--Ohio State University, 2003.
Title from first page of PDF file. Document formatted into pages; contains xxii, 172 p. : ill., some col. Includes abstract and vita. Advisor: Michael K. Chan, Dept. of Chemistry. Includes bibliographical references (p. 165-172).
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Pessoa-Brandão, Luis. "Genetic and molecular studies of Saccharomyces cerevisiae Cdc7-Dbf4 kinase function in DNA damage-induced mutagenesis /." Connect to full text via ProQuest. IP filtered, 2005.

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Walker, Alice Rachel. "Computational Simulations of Cancer and Disease-Related Enzymatic Systems Using Molecular Dynamics and Combined Quantum Methods." Thesis, University of North Texas, 2018. https://digital.library.unt.edu/ark:/67531/metadc1157647/.

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This work discusses applications of computational simulations to enzymatic systems with a particular focus on the effects of various small perturbations on cancer and disease-related systems. First, we cover the development of carbohydrate-based PET imaging ligands for Galectin-3, which is a protein overexpressed in pancreatic cancer tumors. We uncover several structural features for the ligands that can be used to improve their binding and efficacy. Second, we discuss the AlkB family of enzymes. AlkB is the E. coli DNA repair protein for alkylation damage, and has human homologues with slightly different functions and substrates. Each has a conserved active site with a catalytic iron and a coordinating His...His...Asp triad. We have applied molecular dynamics (MD) to investigate the effect of a novel single nucleotide polymorphism for AlkBH7, which is correlated with prostate cancer and has an unknown function. We show that the mutation leads to active site distortion, which has been confirmed by experiments. Thirdly, we investigate the unfolding of hen egg white lysozyme in 90% ethanol solution and low pH, to show the initial steps of unfolding from a native-like state to the disease-associated beta-sheet structure. We compare to mass spectrometry experiments and also show differing pathways based on protonation state. Finally, we discuss three different DNA polymerase systems. DNA polymerases are the primary proteins that replicate DNA during cell division, and have various extra or specific functions. We look at a proofreading-deficient DNA polymerase III mutant, the effects of solvent on DNA polymerase IV's ability to bypass bulky DNA adducts, and a variety of mutations on DNA polymerase kappa.
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O'Hanlon, Karen Ann. "Studies on the enzyme DNA-dependent RNA polymerase." Thesis, University of Reading, 1998. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.266340.

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Books on the topic "Dna polymerase enzymes"

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Emperor of enzymes: A biography of Arthur Kornberg, biochemist and Nobel laureate. [Hackensack], New Jersey: World Scientific, 2016.

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D, Knudsen Walter, and Bruns Sam S, eds. Bacterial DNA, DNA polymerase, and DNA helicases. Hauppauge, NY: Nova Science, 2009.

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Book chapters on the topic "Dna polymerase enzymes"

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Schomburg, Dietmar, and Dörte Stephan. "DNA-directed DNA polymerase." In Enzyme Handbook, 493–508. Berlin, Heidelberg: Springer Berlin Heidelberg, 1997. http://dx.doi.org/10.1007/978-3-642-59025-2_92.

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Schomburg, Dietmar, and Dörte Stephan. "RNA-directed DNA polymerase." In Enzyme Handbook, 717–28. Berlin, Heidelberg: Springer Berlin Heidelberg, 1997. http://dx.doi.org/10.1007/978-3-642-59025-2_130.

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Schomburg, Dietmar, and Dörte Stephan. "DNA-directed RNA polymerase." In Enzyme Handbook, 481–92. Berlin, Heidelberg: Springer Berlin Heidelberg, 1997. http://dx.doi.org/10.1007/978-3-642-59025-2_91.

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Mizrahi, V., P. A. Benkovic, R. D. Kuchta, M. C. Young, K. A. Johnson, and S. J. Benkovic. "Mechanistic Studies on DNA Polymerase I." In Enzyme Dynamics and Regulation, 1–5. New York, NY: Springer New York, 1988. http://dx.doi.org/10.1007/978-1-4612-3744-0_1.

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Imanaka, Tadayuki. "Enzymes Involved in DNA Amplification (e.g. Polymerases) from Thermophiles: Evolution of PCR Enzymes." In Extremophiles Handbook, 475–95. Tokyo: Springer Japan, 2011. http://dx.doi.org/10.1007/978-4-431-53898-1_22.

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Pustowoit, B. "Semiquantitative Detection of Viral DNA, e.g. for CMV, by Using the DNA Enzyme Immunoassay (DEIA)." In Quantitation of mRNA by Polymerase Chain Reaction, 125–33. Berlin, Heidelberg: Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-79712-5_12.

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Ittel, Marie E., Jenny Jongstra-Bilen, Claude Niedergang, Paul Mandel, and Etienne Delain. "DNA-Poly(ADP-Ribose) Polymerase Complex: Isolation of the DNA Wrapping the Enzyme Molecule." In Proceedings in Life Sciences, 60–68. Berlin, Heidelberg: Springer Berlin Heidelberg, 1985. http://dx.doi.org/10.1007/978-3-642-70589-2_8.

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Knopf, Charles W., and Reiner Strick. "Herpes Simplex Virus Type 1 DNA Polymerase: Eukaryotic Model Enzyme and Principal Target of Antiviral Therapy." In Pathogenicity of Human Herpesviruses due to Specific Pathogenicity Genes, 87–135. Berlin, Heidelberg: Springer Berlin Heidelberg, 1994. http://dx.doi.org/10.1007/978-3-642-85004-2_6.

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Pflug, W., G. Mai, G. Wahl, S. Aab, B. Eberspächer, and U. Keller. "A Simple Method to Prevent Inhibition of Taq Polymerase and Hinfi Restriction Enzyme in DNA Analysis of Stain Material." In Advances in Forensic Haemogenetics, 163–65. Berlin, Heidelberg: Springer Berlin Heidelberg, 1992. http://dx.doi.org/10.1007/978-3-642-77324-2_47.

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Bauer, Pal I., and Ernest Kun. "The Role of Lysine Residues in the Catalytic Function and DNA Binding of Poly(ADP-Ribose) Polymerase as Determined by the Covalent Modification of the Enzyme Protein with Methyl Acetimidate." In Proceedings in Life Sciences, 69–73. Berlin, Heidelberg: Springer Berlin Heidelberg, 1985. http://dx.doi.org/10.1007/978-3-642-70589-2_9.

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Conference papers on the topic "Dna polymerase enzymes"

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Lee, Tae Yoon, Dimistris E. Nikitopoulos, Daniel S. Park, Steven A. Soper, and Michael C. Murphy. "Design and Fabrication of a Ligase Detection Reaction (LDR) Microchip With an Integrated Passive Micromixer." In ASME 2007 International Mechanical Engineering Congress and Exposition. ASMEDC, 2007. http://dx.doi.org/10.1115/imece2007-42216.

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The ligase detection reaction (LDR) is a technique that can distinguish low-abundant mutant DNAs from wild-type DNAs. LDR is usually carried out on DNAs amplified using the polymerase chain reaction (PCR). In the realization of modular microfluidic systems, the DNA output of the PCR handed off to the LDR chip needs to be mixed with LDR reagents before continuing the reaction. Polymer, continuous flow ligase detection reaction (CFLDR) devices with integrated passive micromixers, were designed, fabricated and tested. The devices each consisted of: a passive mixer for mixing a PCR sample, a cocktail of primers, and ligase, an enzyme of DNA; an incubator channel (95°C) for preheating the mixture; and a thermal cycling channel for the LDR. The devices were produced by hot embossing polycarbonate (PC) substrates with brass mold inserts manufactured by micro-milling. Experiments using food dyes showed that the appropriate mixture concentrations were delivered to the preheating channel in both the pulling and pushing modes.
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Zhang, Aili, Chao Chen, and Lisa X. Xu. "Numerical Study of Nanoparticle-Enhanced PCR." In ASME 2008 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2008. http://dx.doi.org/10.1115/sbc2008-192725.

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The polymerase chain reaction (PCR) exponentially amplifies a DNA template and produces large numbers of specific DNA fragments. Because of its high sensitivity and efficiency, it becomes a common technique that is widely used in molecular biological. The addition of nano-gold particles into the template solution was found to greatly enhance the efficacy of PCR [1, 2]. Although the thermal effect has been suggested, the underlying mechanisms are still not clear, e.g. how the temperature field affects the replication of DNA at the molecular level. A typical PCR process consists of repeated cycling of three major steps: (1) fast heating to a temperature around 94°C for separating of the two strands DNA templates into single strand (Denaturation); (2) lowering the temperature to about 54°C for the primers to find the complementary part and anneal to the single stranded templates (Annealing); (3) increase of the temperature again to around 72°C for copying of the single templates with the action of the polymerase enzyme (Extension). The thermal history of the PCR determines the activity of the polymerase and rate of each reaction taken place during the process. And the motion of the primers, the DNA templates and the bases owing to both the Brownian effects and concentration gradients can also influence the specificity and reaction rates. The addition of nano-gold particles is expected to greatly alter both the heat and mass transfer efficiency. Thus, the micro-heat and mass transfer analysis of the nano-gold added PCR process has been performed. The temporal and spatial temperature distribution, and the reactants and products concentration have been numerically simulated. The influence of added nano-gold particles on the polymerase reaction rate, the efficiency and specificity of the PCR has evaluated. The possible thermal wave and resonance of the two-phase fluid at the micro-scale level has also been investigated, as well as the enhanced mass transfer of the templates and the reaction rate. The results show that both the thermal effects and physical properties of the nano-particles have contributed to the increase of the efficiency and specificity in the PCR process.
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Liao, Uland, Armando Tovar, Philip Felgner, and Abraham P. Lee. "A Microfluidic Approach and Enhancement Towards a Colorimetric Enzyme-Linked-Immunosorbant-Assay for Diagnostic Detection of Infectious Diseases." In ASME 2007 2nd Frontiers in Biomedical Devices Conference. ASMEDC, 2007. http://dx.doi.org/10.1115/biomed2007-38105.

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Accounting for more than 13 million deaths a year, infectious diseases have become the world’s biggest killer of children and young adults worldwide [1]. Diagnostic tools and technologies are vital towards identifying the presence and treatment of these diseases. Detection methods have commonly relied on DNA using polymerase-chain-reaction (PCR), however antibody methods have become popular due to growing trends in technology and detection sensitivity. ImmPORT Therapeutics, a leading group in generating infectious disease proteome microarrays, has developed multiplex systems for comprehensive analysis of immune responses to multiple infectious diseases [2]. Current microarray handling however requires conventional lab-bench methods that require whole-day processes and large amounts of user-handling confined to laboratory settings. Miniaturization of laboratory processes would provide numerous advantages in terms of cost, time, portability and multistage automation in addition to what is already offered. The proposed microfluidic device is a colorimetric enzyme-linked-immunosorbant assay (ELISA) for antibody detection of infectious agents that draws on ImmPORT Therapeutics technology with a purpose of decreasing reagent volumes and times potentially unattainable through conventional methods.
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Reports on the topic "Dna polymerase enzymes"

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Mishra, N. C. Characterization of the mammalian DNA polymerase gene(s) and enzyme(s). Annual progress report. Office of Scientific and Technical Information (OSTI), January 1995. http://dx.doi.org/10.2172/89557.

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Mishra, N. C. Characterization of the mammalian DNA polymerase gene(s) and enzyme(s). Annual progress report. Office of Scientific and Technical Information (OSTI), January 1994. http://dx.doi.org/10.2172/89558.

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