Littérature scientifique sur le sujet « Phi29 DNA Polymerase »

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Articles de revues sur le sujet "Phi29 DNA Polymerase"

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del Prado, Santos, Lázaro, Salas, and de Vega. "The Loop of the TPR1 Subdomain of Phi29 DNA Polymerase Plays a Pivotal Role in Primer-Terminus Stabilization at the Polymerization Active Site." Biomolecules 9, no. 11 (2019): 648. http://dx.doi.org/10.3390/biom9110648.

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Bacteriophage Phi29 DNA polymerase belongs to the protein-primed subgroup of family B DNA polymerases that use a terminal protein (TP) as a primer to initiate genome replication. The resolution of the crystallographic structure showed that it consists of an N-terminal domain with the exonuclease activity and a C-terminal polymerization domain. It also has two subdomains specific of the protein-primed DNA polymerases; the TP Regions 1 (TPR1) that interacts with TP and DNA, and 2 (TPR2), that couples both processivity and strand displacement to the enzyme. The superimposition of the structures o
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Sakatani, Yoshihiro, Ryo Mizuuchi, and Norikazu Ichihashi. "In vitro evolution of phi29 DNA polymerases through compartmentalized gene expression and rolling-circle replication." Protein Engineering, Design and Selection 32, no. 11 (2019): 481–87. http://dx.doi.org/10.1093/protein/gzaa011.

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Abstract Phi29 DNA polymerase is widely used for DNA amplification through rolling-circle replication or multiple displacement amplification. Here, we performed completely in vitro artificial evolution of phi29 DNA polymerase by combining the in vitro compartmentalization and the gene expression-coupled rolling-circle replication of a circular DNA encoding the polymerase. We conducted the experiments in six different conditions composed of three different levels of inhibitor concentrations with two different DNA labeling methods. One of the experiments was performed in our previous study and t
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Kamtekar, Satwik. "Phi29 DNA polymerase: structure and sequencing." Acta Crystallographica Section A Foundations and Advances 75, a1 (2019): a139. http://dx.doi.org/10.1107/s010876731909860x.

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Krzywkowski, Tomasz, Malte Kühnemund, Di Wu, and Mats Nilsson. "Limited reverse transcriptase activity of phi29 DNA polymerase." Nucleic Acids Research 46, no. 7 (2018): 3625–32. http://dx.doi.org/10.1093/nar/gky190.

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Tenaglia, Enrico, Yuki Imaizumi, Yuji Miyahara, and Carlotta Guiducci. "Isothermal multiple displacement amplification of DNA templates in minimally buffered conditions using phi29 polymerase." Chemical Communications 54, no. 17 (2018): 2158–61. http://dx.doi.org/10.1039/c7cc09609g.

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Torres, Leticia L., and Vitor B. Pinheiro. "Xenobiotic Nucleic Acid (XNA) Synthesis by Phi29 DNA Polymerase." Current Protocols in Chemical Biology 10, no. 2 (2018): e41. http://dx.doi.org/10.1002/cpch.41.

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Li, Shasha, Su Liu, Yicheng Xu, et al. "Robust and highly specific fluorescence sensing of Salmonella typhimurium based on dual-functional phi29 DNA polymerase-mediated isothermal circular strand displacement polymerization." Analyst 144, no. 16 (2019): 4795–802. http://dx.doi.org/10.1039/c9an00843h.

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A simple and robust fluorescence sensing strategy has been developed for the detection of pathogenic bacteria by the combination of the dual functionality of phi29 DNA polymerase with isothermal circular strand displacement polymerization (ICSDP).
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Xu, Yun, Simon Gao, John F. Bruno, Benjamin J. Luft, and John J. Dunn. "Rapid detection and identification of a pathogen’s DNA using Phi29 DNA polymerase." Biochemical and Biophysical Research Communications 375, no. 4 (2008): 522–25. http://dx.doi.org/10.1016/j.bbrc.2008.08.082.

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Johne, Reimar, Hermann Müller, Annabel Rector, Marc van Ranst, and Hans Stevens. "Rolling-circle amplification of viral DNA genomes using phi29 polymerase." Trends in Microbiology 17, no. 5 (2009): 205–11. http://dx.doi.org/10.1016/j.tim.2009.02.004.

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Kesici, Merve-Zeynep, Philip Tinnefeld, and Andrés Manuel Vera. "A simple and general approach to generate photoactivatable DNA processing enzymes." Nucleic Acids Research 50, no. 6 (2021): e31-e31. http://dx.doi.org/10.1093/nar/gkab1212.

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Abstract DNA processing enzymes, such as DNA polymerases and endonucleases, have found many applications in biotechnology, molecular diagnostics, and synthetic biology, among others. The development of enzymes with controllable activity, such as hot-start or light-activatable versions, has boosted their applications and improved the sensitivity and specificity of the existing ones. However, current approaches to produce controllable enzymes are experimentally demanding to develop and case-specific. Here, we introduce a simple and general method to design light-start DNA processing enzymes. In
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