Academic literature on the topic 'Polymerasa'

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Journal articles on the topic "Polymerasa"

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Panjkovic, Milana, and Tatjana Ivkovic-Kapicl. "Etiology and pathogenesis of precancerous lesions and invasive cervical carcinoma." Medical review 61, no. 7-8 (2008): 364–68. http://dx.doi.org/10.2298/mpns0808364p.

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Cervical cancer is the second most common gynecological malignancy in the world. Human papilloma virus (HPV) infection is the leading ethiologic agent in the development of premalignant and malignant cervical diseases. HPV is a member of the Papovaviridae family and until now over 100 types have been recognized. There are two types of viral infection: latent and productive. Virus induced oncogenesis is the result of interaction between virus oncoproteins E6 and E7 and tumor supresor host genes p53 and Rb. Many cofactors such as immunosuppression, early sexual relationship, multiple sexual partners, other sexualy transsmited infections and smooking are contributing factors of the precancerous and invasive cervical lesions. According to the oncogenic potential HPV are divided into three groups: low, intermediate and high oncogenic risk viruses. Molecular technics which are used for the virus detection are: In situ hibridisation,, Hybrid capture test and polymerasa chain reaction. Human papilloma virus testing has an important role in the follow up and treatment of women with 'atypical squamous cells of unknown significant' changes in cervical smears and low-grade squamous intraepithelial lesions, changes in punch biopsy.
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Vidić, Branka, Stanko Boboš, Sara Savić, and Živoslav Grgić. "MYCOPLASMA AS THE CAUSE OF INFECTIONS IN CATTLE." Archives of Veterinary Medicine 5, no. 2 (December 26, 2012): 11–18. http://dx.doi.org/10.46784/e-avm.v5i2.166.

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During the last few years more than 20 different types of Mycoplasma, Ureaplasma and Acholeplasma microorganisms have been isolated from cattle with different clinical signs. Most of Mycoplasma microorganisms have a secondary role in the appearance of infection in cattle. Differently, Mycoplasma bovis (M. bovis) has a primary role in the infection of cattle. It has been proved that M. bovis frequently causes pneumonia, mastitis and arthritis in cows. Besides, M. bovis is identified as a causative agent in meningitis, middle ear infection, keratoconjunctivitis, decubitus abscesses, vaginitis and miscarriages in cows. Diagnostic was done based on the clinical signs and detection of the causative agent, in individual animals and in the herds as whole. The methods used for diagnostic can be cultivation of the causative agent or fluorescence test for antigen detection in pathological material. Also, the detection of specific antibodies can be done, applying different serological methods: fast agglutination on a plate, indirect hemiinhibition, agar gel immunodifussion, CF, ELISA, etc. Polymerasa chain reaction (PCR) is a sensitive method which is mostly used for confirmatory etiological diagnostic. The treatment of Mycoplasma infection is very demanding due to the resistance to most frequently used antibiotics and therefore very different from treating any other bacterial infection. M. bovis is one of the most complicated agents for control as its response to the treatment is weak. A good program for eradication of mycoplasmosis is based on early carrier detection and they are excluded the herds.
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Hili, Ryan, Chun Guo, Dehui Kong, and Yi Lei. "Expanding the Chemical Diversity of DNA." Synlett 29, no. 11 (March 20, 2018): 1405–14. http://dx.doi.org/10.1055/s-0036-1591959.

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Nucleic acid polymers can be evolved to exhibit desired properties, including molecular recognition of a molecular target and catalysis of a specific reaction. These properties can be readily evolved despite the dearth of chemical diversity available to nucleic acid polymers, especially when compared to the rich chemical complexity of proteins. Expansion of nucleic acid chemical diversity has therefore been an important thrust for improving their properties for analytical and biomedical applications. Herein, we briefly describe the current state-of-the-art for the sequence-defined incorporation of modifications throughout an evolvable nucleic acid polymer. This includes contributions from our own lab, which have expanded the chemical diversity of nucleic acid polymers closer to the level observed in proteinogenic polymers.1 Introduction2 Polymerase-Catalyzed Synthesis of Modified Nucleic Acid ­Polymers3 Ligase-Catalyzed Oligonucleotide Polymerization (LOOPER)4 LOOPER with Small Modifications5 LOOPER with Large Modifications6 Evolution of Aptamers Derived from LOOPER Libraries7 Outlook
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Gibbs, J. S., K. Weisshart, P. Digard, A. deBruynKops, D. M. Knipe, and D. M. Coen. "Polymerization activity of an alpha-like DNA polymerase requires a conserved 3'-5' exonuclease active site." Molecular and Cellular Biology 11, no. 9 (September 1991): 4786–95. http://dx.doi.org/10.1128/mcb.11.9.4786.

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Most DNA polymerases are multifunctional proteins that possess both polymerizing and exonucleolytic activities. For Escherichia coli DNA polymerase I and its relatives, polymerase and exonuclease activities reside on distinct, separable domains of the same polypeptide. The catalytic subunits of the alpha-like DNA polymerase family share regions of sequence homology with the 3'-5' exonuclease active site of DNA polymerase I; in certain alpha-like DNA polymerases, these regions of homology have been shown to be important for exonuclease activity. This finding has led to the hypothesis that alpha-like DNA polymerases also contain a distinct 3'-5' exonuclease domain. We have introduced conservative substitutions into a 3'-5' exonuclease active site homology in the gene encoding herpes simplex virus DNA polymerase, an alpha-like polymerase. Two mutants were severely impaired for viral DNA replication and polymerase activity. The mutants were not detectably affected in the ability of the polymerase to interact with its accessory protein, UL42, or to colocalize in infected cell nuclei with the major viral DNA-binding protein, ICP8, suggesting that the mutation did not exert global effects on protein folding. The results raise the possibility that there is a fundamental difference between alpha-like DNA polymerases and E. coli DNA polymerase I, with less distinction between 3'-5' exonuclease and polymerase functions in alpha-like DNA polymerases.
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Gibbs, J. S., K. Weisshart, P. Digard, A. deBruynKops, D. M. Knipe, and D. M. Coen. "Polymerization activity of an alpha-like DNA polymerase requires a conserved 3'-5' exonuclease active site." Molecular and Cellular Biology 11, no. 9 (September 1991): 4786–95. http://dx.doi.org/10.1128/mcb.11.9.4786-4795.1991.

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Most DNA polymerases are multifunctional proteins that possess both polymerizing and exonucleolytic activities. For Escherichia coli DNA polymerase I and its relatives, polymerase and exonuclease activities reside on distinct, separable domains of the same polypeptide. The catalytic subunits of the alpha-like DNA polymerase family share regions of sequence homology with the 3'-5' exonuclease active site of DNA polymerase I; in certain alpha-like DNA polymerases, these regions of homology have been shown to be important for exonuclease activity. This finding has led to the hypothesis that alpha-like DNA polymerases also contain a distinct 3'-5' exonuclease domain. We have introduced conservative substitutions into a 3'-5' exonuclease active site homology in the gene encoding herpes simplex virus DNA polymerase, an alpha-like polymerase. Two mutants were severely impaired for viral DNA replication and polymerase activity. The mutants were not detectably affected in the ability of the polymerase to interact with its accessory protein, UL42, or to colocalize in infected cell nuclei with the major viral DNA-binding protein, ICP8, suggesting that the mutation did not exert global effects on protein folding. The results raise the possibility that there is a fundamental difference between alpha-like DNA polymerases and E. coli DNA polymerase I, with less distinction between 3'-5' exonuclease and polymerase functions in alpha-like DNA polymerases.
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Jadranin, Zeljko, Vesna Suljagic, Veljko Todorovic, Miroljub Trkuljic, and Dusan Vucetic. "HIV/AIDS and other sexually transmitted infections among military members of the armed forces of Serbia." Vojnosanitetski pregled 69, no. 1 (2012): 43–48. http://dx.doi.org/10.2298/vsp1201043j.

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Background/Aim. Military personnel is a population group at special risk of exposure to sexually transmitted diseases (STD). In peacetime, STD infection rates among service members are generally 2 to 5 times higher than among civilian population. In time of conflict, the differences can be 50 or more times greater. This study describes sexual behavior as a risk factor for STD in the Armed Forces of Serbia. Methods. The sample of 5 617 voluntary blood donors from the Armed Forces of Serbia gave blood and filled World Health Organization Questionnaire about sexual behavior within January 2007 - December 2008 period. The mandatory testing of voluntary blood donors was performed in the Institute of Transfusiology Military Medical Academy in Belgrade, by the specific immunoenzyme tests and polymerasa chain reaction tests for HIV, hepatitis B, C and syphilis. Statistical analysis of data was done using State for Windows 93, USA, 1996. Results. We identified 36 soldiers with some form of STDs. This study showed that 1 668 (29.7%) tested soldiers reported always using condoms, 1 725 (30.72%) almost always, 1 238 (20.04%) sometimes, 495 (8.81%) almost never and 490 (8.73%) never. Among the sample, 449 (7.99%) soldiers reported sexual contacts with partners with high risk of sexual behavior, whilst 22 (0.37%) of them reported homosexual and bisexual contacts. Conclusion. This study reported STDs found in voluntary blood donors among the service members of the Armed Forces of Serbia, but none of them was identified to be HIV positive. Soldiers with the most frequent risk behavior were reported to be those with inconsistent condom use. In the future, the STD Control and Prevention Program should be more intensively conducted among the members of the Armed Forces of Serbia.
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Raia, Pierre, Marc Delarue, and Ludovic Sauguet. "An updated structural classification of replicative DNA polymerases." Biochemical Society Transactions 47, no. 1 (January 15, 2019): 239–49. http://dx.doi.org/10.1042/bst20180579.

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AbstractReplicative DNA polymerases are nano-machines essential to life, which have evolved the ability to copy the genome with high fidelity and high processivity. In contrast with cellular transcriptases and ribosome machines, which evolved by accretion of complexity from a conserved catalytic core, no replicative DNA polymerase is universally conserved. Strikingly, four different families of DNA polymerases have evolved to perform DNA replication in the three domains of life. In Bacteria, the genome is replicated by DNA polymerases belonging to the A- and C-families. In Eukarya, genomic DNA is copied mainly by three distinct replicative DNA polymerases, Polα, Polδ, and Polε, which all belong to the B-family. Matters are more complicated in Archaea, which contain an unusual D-family DNA polymerase (PolD) in addition to PolB, a B-family replicative DNA polymerase that is homologous to the eukaryotic ones. PolD is a heterodimeric DNA polymerase present in all Archaea discovered so far, except Crenarchaea. While PolD is an essential replicative DNA polymerase, it is often underrepresented in the literature when the diversity of DNA polymerases is discussed. Recent structural studies have shown that the structures of both polymerase and proofreading active sites of PolD differ from other structurally characterized DNA polymerases, thereby extending the repertoire of folds known to perform DNA replication. This review aims to provide an updated structural classification of all replicative DNAPs and discuss their evolutionary relationships, both regarding the DNA polymerase and proofreading active sites.
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Jung, G. H., M. C. Leavitt, J. C. Hsieh, and J. Ito. "Bacteriophage PRD1 DNA polymerase: evolution of DNA polymerases." Proceedings of the National Academy of Sciences 84, no. 23 (December 1, 1987): 8287–91. http://dx.doi.org/10.1073/pnas.84.23.8287.

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Walsh, Jason M., and Penny J. Beuning. "Synthetic Nucleotides as Probes of DNA Polymerase Specificity." Journal of Nucleic Acids 2012 (2012): 1–17. http://dx.doi.org/10.1155/2012/530963.

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The genetic code is continuously expanding with new nucleobases designed to suit specific research needs. These synthetic nucleotides are used to study DNA polymerase dynamics and specificity and may even inhibit DNA polymerase activity. The availability of an increasing chemical diversity of nucleotides allows questions of utilization by different DNA polymerases to be addressed. Much of the work in this area deals with the A family DNA polymerases, for example,Escherichia coliDNA polymerase I, which are DNA polymerases involved in replication and whose fidelity is relatively high, but more recent work includes other families of polymerases, including the Y family, whose members are known to be error prone. This paper focuses on the ability of DNA polymerases to utilize nonnatural nucleotides in DNA templates or as the incoming nucleoside triphosphates. Beyond the utility of nonnatural nucleotides as probes of DNA polymerase specificity, such entities can also provide insight into the functions of DNA polymerases when encountering DNA that is damaged by natural agents. Thus, synthetic nucleotides provide insight into how polymerases deal with nonnatural nucleotides as well as into the mutagenic potential of nonnatural nucleotides.
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Miura, Masashi, Chihiro Tanigawa, Yoshito Fujii, and Satoshi Kaneko. "COMPARISON OF SIX COMMERCIALLY-AVAILABLE DNA POLYMERASES FOR DIRECT PCR." Revista do Instituto de Medicina Tropical de São Paulo 55, no. 6 (December 2013): 401–6. http://dx.doi.org/10.1590/s0036-46652013000600005.

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SUMMARY The use of a “direct PCR” DNA polymerase enables PCR amplification without any prior DNA purification from blood samples due to the enzyme's resistance to inhibitors present in blood components. Such DNA polymerases are now commercially available. We compared the PCR performance of six direct PCR-type DNA polymerases (KOD FX, Mighty Amp, Hemo KlenTaq, Phusion Blood II, KAPA Blood, and BIOTAQ) in dried blood eluted from a filter paper with TE buffer. GoTaq Flexi was used as a standard DNA polymerase. PCR performance was evaluated by a nested PCR technique for detecting Plasmodium falciparum genomic DNA in the presence of the blood components. Although all six DNA polymerases showed resistance to blood components compared to the standard Taq polymerase, the KOD FX and BIOTAQ DNA polymerases were resistant to inhibitory blood components at concentrations of 40%, and their PCR performance was superior to that of other DNA polymerases. When the reaction mixture contained a mild detergent, only KOD FX DNA polymerase retained the original amount of amplified product. These results indicate that KOD FX DNA polymerase is the most resistant to inhibitory blood components and/or detergents. Thus, KOD FX DNA polymerase could be useful in serological studies to simultaneously detect antibodies and DNA in eluents for antibodies. KOD FX DNA polymerase is thus not limited to use in detecting malaria parasites, but could also be employed to detect other blood-borne pathogens.
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Dissertations / Theses on the topic "Polymerasa"

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Leavitt, Markley Carl. "Bacteriophage T5 DNA polymerase relationships of DNA polymerases." Diss., The University of Arizona, 1990. http://hdl.handle.net/10150/185335.

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T5 DNA polymerase, a highly processive single polypeptide enzyme, and PRD1 DNA polymerase, a protein-primed DNA polymerase, have been analyzed for their primary structural features. The amino acid sequence of T5 DNA polymerase reveals a high degree of homology with DNA polymerase I (Pol I) of Escherichia coli and retains many of the amino acid residues which have been implicated in the 3'-5' exonuclease and DNA polymerase activities of that enzyme. Alignment with sequences of polymerase I and T7 DNA polymerase (family A polymerases) was used to identify regions possibly involved in the high processivity of this enzyme. Further amino acid sequence comparisons of T5 DNA polymerase with a large group of DNA polymerases (family B) previously shown to exhibit little similarity to Pol I, indicate certain sequence segments are shared among distantly related DNA polymerases. These shared regions have been implicated in the 3'-5' exonuclease function of Pol I which suggests that the proofreading domains of all these enzymes may be related. Mutations in these segments in T5 DNA polymerase (family A) and PRD1 DNA polymerase (family B) greatly decrease the exonuclease activity of these enzymes but leave the polymerase activities intact. Additionally, an exonuclease deficient T5 DNA polymerase is used in DNA sequencing reactions and yields consistent results with low background contamination on autoradiographs of polyacrylamide/urea gels. PRD1 mutants defective in 3 regions which are highly conserved among family B DNA polymerases, are deficient in DNA polymerase activity but retain exonuclease activity.
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Roettger, Michelle P. "Insight into the Fidelity of Two X-Family Polymerases: DNA Polymerase Mu and DNA Polymerase Beta." Columbus, Ohio : Ohio State University, 2008. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=osu1211074588.

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SALHI, SAMIA. "Dna polymerase de sulfolobus acidocaldarius : interet de l'etude des dna polymerases thermophiles." Paris 7, 1989. http://www.theses.fr/1989PA077169.

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La copie par la dna polymerase de sulfolobus acidocaldarius d'un dna simple brin uni-amorce de sequence connue a ete etudiee. Les parametres cinetiques affectant cette synthese dependent de la sequence du dna. La temperature de reaction a son importance. Les methodes employees sont la reaction polymerase en chaine, la mutagenese dirigee, le sequencage de sanger
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Pospiech, H. (Helmut). "The role of DNA polymerases, in particular DNA polymerase ε in DNA repair and replication." Doctoral thesis, University of Oulu, 2002. http://urn.fi/urn:isbn:9514266692.

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Abstract Analysis of the primary structure of DNA polymerase ε B subunit defined similarities to B subunits of eukaryotic DNA polymerases α, δ and ε as well as the small subunits of DNA polymerase DI of Euryarchaeota. Multiple sequence alignment of these proteins revealed the presence of 12 conserved motifs and defined a novel protein superfamily. The members of the B subunit family share a common domain architecture, suggesting a similar fold, and arguing for a conserved function among these proteins. The contribution of human DNA polymerase ε to nuclear DNA replication was studied using the antibody K18 that specifically inhibits the activity of this enzyme in vitro. This antibody significantly inhibited DNA synthesis both when microinjected into nuclei of exponentially growing human fibroblasts and in isolated HeLa cell nuclei, but did not inhibit SV40 DNA replication in vitro. These results suggest that the human DNA polymerase ε contributes substantially to the replicative synthesis of DNA and emphasises the differences between cellular replication and viral model systems. The human DNA polymerases ε and δ were found capable of gap-filling DNA synthesis during nucleotide excision repair in vitro. Both enzymes required PCNA and the clamp loader RFC, and in addition, polymerase δ required Fen-1 to prevent excessive displacement synthesis. Nucleotide excision repair of a defined DNA lesion was completely reconstituted utilising largely recombinant proteins, only ligase I and DNA polymerases δ and ε provided as highly purified human enzymes. This system was also utilised to study the role of the transcription factor II H during repair. Human non-homologous end joining of model substrates with different DNA end configurations was studied in HeLa cell extracts. This process depended partially on DNA synthesis as an aphidicolin-dependent DNA polymerase was required for the formation of a subset of end joining products. Experiments with neutralising antibodies reveal that DNA polymerase α but not DNA polymerases β or ε, may represent this DNA polymerase activity. Our results indicate that DNA synthesis contributes to the stability of DNA ends, and influences both the efficiency and outcome of the end joining event. Furthermore, our results suggest a minor role of PCNA in non-homologous end joining.
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Mischo, Hannah. "Disengaging Polymerases : Transcriptional termination by RNA polymerase II in Saccharomyces cerevisiae and the maintenance of genome integrity." Thesis, University of Oxford, 2008. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.514968.

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Efthimiopoulos, Georgia. "Bypass of N2-Deoxyguanosinyl Adducts by DNA Polymerases and Kinetic Implications for Polymerase Switching." The Ohio State University, 2013. http://rave.ohiolink.edu/etdc/view?acc_num=osu1366297865.

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Siot, Alexandra. "Elaboration et caractérisation de polymères nanochargés." Thesis, IMT Mines Alès, 2018. http://www.theses.fr/2018EMAL0001.

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Linley, M. "The detection of polymerase inhibiting lesions using the polymerase arrest polymerase chain reaction assay." Thesis, Swansea University, 2004. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.637924.

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There is a constant need to determine the genotoxic potential of the agents to which the human population is exposed. The stringent testing of new products is legislatively controlled and dependent on the accumulation of sufficient scientific data to allow an analysis of the risk. It is important to predetermine any risks in the workplace prior to the presentation of disease and to provide factual public information on personal exposure e.g. the risks associated with UV light. Various experimental assays have been developed to assess the genotoxicity, mutagenicity and mcarcinogenicity of given physical and chemical agents. The Polymerase Arrest- Polymerase Chain Reaction (PA-PCR) assay was employed to investigate the genotoxic effects (DNA adducts, DAN strand breaks and DNA crosslinking) of various physical and chemical agents on naked isolated DNA. The assay was modified to provide two adapted methods, which increased the sensitivity of the assay to report DNA damage at significantly lowered exposure levels. The ability of the PA-PCR assay to perform as an initial screening process for genotoxic activity was assessed and determined.
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Cramer, Janina. "Funktionelle Charakterisierung der RNA-abhängigen RNA-Polymerase des Hepatitis-C-Virus Untersuchung molekularer Mechanismen der Substratspezifität von DNA-abhängigen DNA-Polymerasen /." [S.l. : s.n.], 2004. http://deposit.ddb.de/cgi-bin/dokserv?idn=971700796.

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Sikorsky, Jan A. "Effect of DNA base modification on polymerase chain reaction efficiency and fidelity." Huntington, WV : [Marshall University Libraries], 2005. http://www.marshall.edu/etd/descript.asp?ref=554.

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Books on the topic "Polymerasa"

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Hübscher, Ulrich. DNA polymerases: Discovery, characterization, and functions in cellular DNA transactions. New Jersey: World Scientific, 2010.

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1941-, Ellis John W., ed. Polymer products: Design, materials, and processing. London: Chapman and Hall, 1986.

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E, Carraher Charles, ed. Polymer chemistry: An introduction. 3rd ed. New York: M. Dekker, 1992.

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Introduction to industrial polymers. 2nd ed. Munich: Hanser Publishers, 1993.

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Seymour, Raymond Benedict. Polymer chemistry: An introduction. 2nd ed. New York: M. Dekker, 1988.

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Hernández-Rodríguez, Patricia, and Arlen Patricia Ramirez Gomez. Polymerase chain reaction. Rijeka: Intech, 2012.

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Müller, Hans-Joachim, and Daniel Ruben Prange. PCR - Polymerase-Kettenreaktion. Berlin, Heidelberg: Springer Berlin Heidelberg, 2016. http://dx.doi.org/10.1007/978-3-662-48236-0.

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Pearce, Eli M. Polymers. Washington, D.C: National Academy Press, 1995.

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Phillip, Lorimer J., ed. Polymers. Oxford: Oxford University Press, 2000.

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White, Robert J. RNA polymerase III transcription. Austin: R.G. Landes, 1994.

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Book chapters on the topic "Polymerasa"

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Hübscher, U., G. Cullmann, P. Thömmes, B. Strack, E. Ferrari, B. Senn, A. Georgaki, T. Weiser, M. W. Berchtold, and V. N. Podust. "Mammalian DNA Helicases, DNA Polymerases and DNA Polymerase Auxiliary Proteins." In DNA Replication and the Cell Cycle, 63–78. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-77040-1_6.

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Amils, Ricardo. "Taq Polymerase." In Encyclopedia of Astrobiology, 1648. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-11274-4_1561.

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Münch, Harald. "Polymerase-Kettenreaktion." In Wissenschaftliches Englisch, 73–79. Berlin, Heidelberg: Springer Berlin Heidelberg, 2017. http://dx.doi.org/10.1007/978-3-662-55299-5_14.

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Peretó, Juli. "DNA Polymerase." In Encyclopedia of Astrobiology, 1. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-642-27833-4_5176-2.

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Peretó, Juli. "RNA Polymerase." In Encyclopedia of Astrobiology, 1. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-642-27833-4_5177-2.

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Amils, Ricardo. "Taq Polymerase." In Encyclopedia of Astrobiology, 1. Berlin, Heidelberg: Springer Berlin Heidelberg, 2014. http://dx.doi.org/10.1007/978-3-642-27833-4_1561-2.

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Gooch, Jan W. "DNA Polymerase." In Encyclopedic Dictionary of Polymers, 888. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4419-6247-8_13590.

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Gooch, Jan W. "RNA Polymerase." In Encyclopedic Dictionary of Polymers, 921. New York, NY: Springer New York, 2011. http://dx.doi.org/10.1007/978-1-4419-6247-8_14719.

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Peretó, Juli. "DNA Polymerase." In Encyclopedia of Astrobiology, 673. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-662-44185-5_5176.

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Peretó, Juli. "RNA Polymerase." In Encyclopedia of Astrobiology, 2194. Berlin, Heidelberg: Springer Berlin Heidelberg, 2015. http://dx.doi.org/10.1007/978-3-662-44185-5_5177.

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Conference papers on the topic "Polymerasa"

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Knight, Bryce M., Marco P. Schoen, and Alba Perez-Gracia. "Distributed Actuation and Shape Control of Ionic Polymer Metal Composites." In ASME 2006 International Mechanical Engineering Congress and Exposition. ASMEDC, 2006. http://dx.doi.org/10.1115/imece2006-15826.

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Ionic polymer metal composites (IPMC) present great potential as future actuators and sensors in a variety of fields including aerospace and biomedical engineering. The benefits of using IPMCs are based on the material's large bending deformation capabilities, low power consumption, light weight and compact size. However, before this novel material can be exploited, a better understanding of its electromechanical properties and a higher level of controllability must be obtained. This paper presents the results of experimental research with these goals in mind. The actuation of these electro active polymers is achieved by using geometrically defined actuation points on the polymer's surface. The input voltage is spatially controlled to achieve faster response times as well as increased control of the shape of the polymer's surface. The experimental work is carried out under a constant humidity and uses vision based sensing to detect the various shapes generated by these electro active polymers. The experimental outcomes are compared against a dynamical model. The results demonstrate the ability for increased control of the shape generated by the surface. A good match of the dynamical model to predict the displacement of the polymer at instances in time is found. In addition, the proposed approach improves the response time of an IPMC through the application of distributed voltage sources over the surface of the material.
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Chen, Pin-Chuan, Hong Wang, Daniel S. Park, Sunggook Park, Dimitris E. Nikitopoulos, Steven A. Soper, and Michael C. Murphy. "Protein Adsorption in a Continuous Flow Microchannel Environment." In ASME 2008 International Mechanical Engineering Congress and Exposition. ASMEDC, 2008. http://dx.doi.org/10.1115/imece2008-68094.

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Protein adsorption is a critical issue in microfluidic devices especially for those reactions depending on proteins like the polymerase chain reaction (PCR). Understanding protein absorption phenomena in different geometry microchannels and evaluating the efficiency of dynamic coating, which has been using as a method to prevent protein adsorption, are important tasks. Two different sets of microchannels were designed and fabricated on polymers. Bovine serum albumin (BSA) was used as a model protein for quantification of and monitoring the protein loss in different microchannel geometries. Up to 58% of the BSA was lost after flowing a 2030 mm long microchannel. The BSA adsorption rate changed along the microchannel. Smaller microchannels required a longer time to achieve protein saturation point. Dynamic coating was shown to be a time consuming and inefficient method to prevent protein adsorption in a continuous flow environment.
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"OFD - Polymers." In 2005 Optical Fiber Communications Conference Technical Digest. IEEE, 2005. http://dx.doi.org/10.1109/ofc.2005.193084.

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Tuichiev, Sh, V. Rashidov, and A. Esfidary. "Magnetic Polymers." In Proceedings of the Symposium F. WORLD SCIENTIFIC, 2003. http://dx.doi.org/10.1142/9789812704344_0042.

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Vaníková, Zuzana, and Michal Hocek. "Polymerase synthesis of new photocaged DNA." In XVIth Symposium on Chemistry of Nucleic Acid Components. Prague: Institute of Organic Chemistry and Biochemistry, Academy of Sciences of the Czech Republic, 2014. http://dx.doi.org/10.1135/css201414392.

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Persat, Alexandre, Tomoyuki Morita, and Juan G. Santiago. "On-Chip Isothermal Polymerase Chain Reaction." In ASME 2007 International Mechanical Engineering Congress and Exposition. ASMEDC, 2007. http://dx.doi.org/10.1115/imece2007-43070.

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Abstract:
We present a novel technique for on-chip PCR where temperature is held constant and uniform in the reactor. Specific chemicals, known as denaturants, have the ability to melt DNA. A flow control scheme establishes spatio-temporal fluctuations in the concentration of denaturants along a microchannel, while electromigration drives DNA through this spatially varying denaturant concentration field. Preliminary results show denaturation and extension of a 200 base pairs (bp) DNA template.
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Fuentes-Hernandez, Canek, Jayan Thomas, Roberto Termine, Muhsin Eralp, Michiharu Yamamoto, Kevin Cammack, Kenji Matsumoto, et al. "Photorefractive polymers based on bis-triarylamine side-chain polymers." In Optical Science and Technology, SPIE's 48th Annual Meeting, edited by Klaus Meerholz. SPIE, 2003. http://dx.doi.org/10.1117/12.506490.

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Shirk, James S., Guy Beadie, Richard S. Lepkowicz, Y. Jin, E. Baer, and A. Hiltner. "Biomimetic Optical Polymers." In CLEO 2007. IEEE, 2007. http://dx.doi.org/10.1109/cleo.2007.4452707.

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Masi, James V. "New magnetic polymers." In 2007 Electrical Insulation Conference and Electrical Manufacturing Expo (EIC/EME). IEEE, 2007. http://dx.doi.org/10.1109/eeic.2007.4562641.

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DAOUD, M. "POLYMERS AND FRAGMENTATION." In Proceedings of the Workshop. WORLD SCIENTIFIC, 1995. http://dx.doi.org/10.1142/9789814447089_0009.

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Reports on the topic "Polymerasa"

1

Bohnert, G. W. Conductive Polymers. Office of Scientific and Technical Information (OSTI), November 2002. http://dx.doi.org/10.2172/804936.

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Kuchta, Robert D. Fidelity Mechanisms of DNA Polymerase Alpha. Fort Belvoir, VA: Defense Technical Information Center, July 2008. http://dx.doi.org/10.21236/ada499543.

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Hecht, Sidney M. Inhibition of Malarial DNA Polymerase Alpha. Fort Belvoir, VA: Defense Technical Information Center, November 1990. http://dx.doi.org/10.21236/adb151470.

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Pang, Yi. Exploring novel silicon-containing polymers---From preceramic polymers to conducting polymers with nonlinear optical properties. Office of Scientific and Technical Information (OSTI), October 1991. http://dx.doi.org/10.2172/5097635.

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Russell, Thomas P. Interfacial Behavior of Polymers: Using Interfaces to Manipulate Polymers. Office of Scientific and Technical Information (OSTI), February 2015. http://dx.doi.org/10.2172/1171152.

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Kempel, Leo, and Shanker Balasubramaniam. RF Polymers II. Fort Belvoir, VA: Defense Technical Information Center, March 2009. http://dx.doi.org/10.21236/ada495291.

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Calvert, Paul D., H. K. Hall, and Jr. Intelligent Synthetic Polymers. Fort Belvoir, VA: Defense Technical Information Center, January 1995. http://dx.doi.org/10.21236/ada292905.

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Phillips, Shawn H., Timothy S. Haddad, Rusty L. Blanski, Andre Y. Lee, and Richard A. Vaia. Molecularly Reinforced Polymers. Fort Belvoir, VA: Defense Technical Information Center, June 2001. http://dx.doi.org/10.21236/ada409917.

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Tirrell, David A. Protein-Based Polymers. Fort Belvoir, VA: Defense Technical Information Center, November 1995. http://dx.doi.org/10.21236/ada302424.

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Gordon, III, Runt Bernard, Painter James P., and Paul C. New Conducting Polymers. Fort Belvoir, VA: Defense Technical Information Center, June 1988. http://dx.doi.org/10.21236/ada197009.

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