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Artykuły w czasopismach na temat "RNases H"
Allen, S. J. W., S. H. Krawczyk, L. R. McGee, N. Bischofberger, A. S. Mulato i J. M. Cherrington. "Inhibition of HIV-1 RNase H Activity by Nucleotide Dimers and Monomers". Antiviral Chemistry and Chemotherapy 7, nr 1 (luty 1996): 37–45. http://dx.doi.org/10.1177/095632029600700107.
Pełny tekst źródłaLeich, Franziska, Nadine Stöhr, Anne Rietz, Renate Ulbrich-Hofmann i Ulrich Arnold. "Endocytotic Internalization as a Crucial Factor for the Cytotoxicity of Ribonucleases". Journal of Biological Chemistry 282, nr 38 (17.07.2007): 27640–46. http://dx.doi.org/10.1074/jbc.m702240200.
Pełny tekst źródłaWatkins, Harriet A., i Edward N. Baker. "Structural and Functional Characterization of an RNase HI Domain from the Bifunctional Protein Rv2228c from Mycobacterium tuberculosis". Journal of Bacteriology 192, nr 11 (2.04.2010): 2878–86. http://dx.doi.org/10.1128/jb.01615-09.
Pełny tekst źródłaOhtani, Naoto, Mitsuru Haruki, Masaaki Morikawa i Shigenori Kanaya. "Molecular diversities of RNases H". Journal of Bioscience and Bioengineering 88, nr 1 (styczeń 1999): 12–19. http://dx.doi.org/10.1016/s1389-1723(99)80168-6.
Pełny tekst źródłaHyjek, Malwina, Małgorzata Figiel i Marcin Nowotny. "RNases H: Structure and mechanism". DNA Repair 84 (grudzień 2019): 102672. http://dx.doi.org/10.1016/j.dnarep.2019.102672.
Pełny tekst źródłaGoulian, Mehran, i Cheryl J. Heard. "Discrimination between mammalian RNases H-1 and H-2". Analytical Biochemistry 192, nr 2 (luty 1991): 398–402. http://dx.doi.org/10.1016/0003-2697(91)90555-8.
Pełny tekst źródłaLim, Shion A., Kathryn M. Hart, Michael J. Harms i Susan Marqusee. "Evolutionary trend toward kinetic stability in the folding trajectory of RNases H". Proceedings of the National Academy of Sciences 113, nr 46 (31.10.2016): 13045–50. http://dx.doi.org/10.1073/pnas.1611781113.
Pełny tekst źródłaHiller, Bjoern, Martin Achleitner, Silke Glage, Ronald Naumann, Rayk Behrendt i Axel Roers. "Mammalian RNase H2 removes ribonucleotides from DNA to maintain genome integrity". Journal of Experimental Medicine 209, nr 8 (16.07.2012): 1419–26. http://dx.doi.org/10.1084/jem.20120876.
Pełny tekst źródłaKirby, Karen A., Bruno Marchand, Yee Tsuey Ong, Tanyaradzwa P. Ndongwe, Atsuko Hachiya, Eleftherios Michailidis, Maxwell D. Leslie i in. "Structural and Inhibition Studies of the RNase H Function of Xenotropic Murine Leukemia Virus-Related Virus Reverse Transcriptase". Antimicrobial Agents and Chemotherapy 56, nr 4 (17.01.2012): 2048–61. http://dx.doi.org/10.1128/aac.06000-11.
Pełny tekst źródłaCerritelli, Susana M., i Robert J. Crouch. "RNases H: Multiple roles in maintaining genome integrity". DNA Repair 84 (grudzień 2019): 102742. http://dx.doi.org/10.1016/j.dnarep.2019.102742.
Pełny tekst źródłaRozprawy doktorskie na temat "RNases H"
Pileur, Frédéric. "Les RNases H eucaryotes : étude comparative sur des substrats modèles et obtention d'inhibiteurs aptamétriques sélectifs". Bordeaux 2, 2001. http://www.theses.fr/2001BOR28843.
Pełny tekst źródłaRNases H are ubiquitous enzymes that hydrolyse the RNA of a DNA/RNA hybrid. They are found in all kingdoms. They participate in the removal of RNA primers of Okazaki fragments. A role in transcription also suspected. RNases H are divided in two classes : class I and class II. RNases HI are nuclear whereasRNases HII are cytoplasmic and mitochondrial. RNases H are also known to be implicated in antisens effects of oligodeoxyribonucleotides. To help in designing new antisens molecules and to possess a new classification criterion, we have analysed the first cuts of these enzymes on various hybrids of 20 nucleotides in length. The tested RNases HI (from bovine and human origin) prefers the 3' end of the RNA engaged in a hybrid whereas RNases HII cut preferentially at 6 and 8 nucleotides from the 5' end of the same RNAs. Moreover informations on mitochondrial localisation of RNases HII has been obtained using this new classification criterion. After this, we have attempted to clone an RNase HII gene from the protozoan Leishmania mexicana amazonensis. This attempt did not succeed. Nowadays, only a few inhibitors of the RNase H activity are known. A good mean to obtain such inhibitors is to use SELEX strategies. We have made an in vitro selection of single stranded DNA aptamers against human recombinant RNase HII. One, b33 inhibited RNaseHII with an IC50 value of 120 nM. This inhibition was specific for eukaryotic RNases HII. B33 could fold into an imperfect stem-loop structure. The second aptamer, b12 poorly inhibited human RNase HII. Moreover several structures could be formed implicating G-quartet formation
Kemiha, Samira. "Étude du rôle des protéines Ribonucléases H dans la réponse cellulaire au stress réplicatif". Electronic Thesis or Diss., Université de Montpellier (2022-....), 2022. http://www.theses.fr/2022UMONT020.
Pełny tekst źródłaDuring S phase, DNA replication starts at multiple origins distributed throughout the genome. As the replication machinery (or replisome) progresses throughout the DNA, it often encounters obstacles such as DNA secondary structures or transcription complexes, thereby generating what is called replication stress. Stalled replisomes are fragile structures that can give rise to chromosome breaks and trigger genome instability. When RNA polymerases stall, the nascent RNA can potentially anneal with the template DNA strand, creating a three-strand structure called R-loop. Coordination between replication and transcription in S phase limits the risks of collisions between the replisome and RNA polymerases. Even though, physiological transcription level and R-loops accumulation lead to recombination events in S phase. Type 1 and 2 ribonucleases H (RNase H) are specific proteins involved R-loops’ resolution through the degradation of the RNA strand within the RNA:DNA duplex. In the absence of RNases H, cells accumulate R-loops and are extremely sensitive to different replication stress-inducing genotoxic agents (e.g. MMS: methyl methanesulfonate or HU: hydroxyurea).The goal of my PhD project was to assess the roles of RNases H in the cellular response to replication stress. Using two cellular models, the budding yeast S. cerevisiae and mammalian cells, we demonstrated that RNases H mutations induce HU- and MMS-stalled replication forks processing and restart defects. Analysis of separation-of-function RNase H2 mutants suggests that it is the RNA:DNA hybrids removal activity of RNase H2 that is important for the correct processing of stalled forks experiencing replication stress. Indeed, quantification of RNA:DNA hybrids during the cell cycle reveals a higher level of hybrids in S phase in the presence of exogenous replication stress in both wild-type and RNases H-depleted cells. Moreover, our results demonstrate that the inhibition of transcrip tion or the overexpression of the RNA:DNA helicase Senataxin restore stalled replication fork processing and restart upon MMS treatment when cells lack RNase H2 activities. Altogether, our data indicate that Ribonucleases H1 and 2 and Senataxin helicase cooperate to resolve RNA polymerases and/or RNA:DNA hybrids interferences with replication
Pâtureau, Bénédicte Marie. "Induction of rnase H activity by arabinose-peptide nucleic acids". Thesis, McGill University, 2005. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=98763.
Pełny tekst źródłaThis thesis highlights the synthesis of the 5'-amino nucleoside analogue required for the incorporation of the peptide nucleic acid in both 2'-fluoroarabinonucleic acid (2'F-ANA) and DNA. Circular dichroism experiments afforded information on the hybrid conformation in solution, whereas UV thermal melting studies provided a measure of the thermal stability of such hybrid duplexes. Finally, ability of various linker modified AON/RNA hybrids to activate the RNase H enzyme was evaluated in parallel with the corresponding native unmodified DNA/RNA hybrids.
Incorporation of a PNA residue within DNA or 2'-FANA did not afford improvement in neither thermal stability nor enzymatic cleavage (except for homopolymeric sequences vs DNA) as compared to control or butyl-sequences.
Yang, Taehwan. "Understanding the relation between RNase H and retrotransposition activity in the context of the Aicardi-Goutieres syndrome". Thesis, Georgia Institute of Technology, 2014. http://hdl.handle.net/1853/53997.
Pełny tekst źródłaCORONA, ANGELA. "Characterization of the mechanism of action of new HIV-1 reverse transcriptase-associated ribonuclease H inhibitors". Doctoral thesis, Università degli Studi di Cagliari, 2014. http://hdl.handle.net/11584/266462.
Pełny tekst źródłaAcosta-Hoyos, Antonio J. "Relationship Between RNase H and Excision Activities of HIV-1 Reverse Transcriptase (RT)". Scholarly Repository, 2010. http://scholarlyrepository.miami.edu/oa_dissertations/458.
Pełny tekst źródłaLeo, Berit [Verfasser], i Birgitta [Akademischer Betreuer] Wöhrl. "Foamy Virus RNase H - Aktivität, Struktur und Funktion / Berit Leo. Betreuer: Birgitta Wöhrl". Bayreuth : Universität Bayreuth, 2013. http://d-nb.info/1059352982/34.
Pełny tekst źródłaBecaud, Jessica. "Towards RNase H mimics : artificial catalysts for the site specific cleavage of RNA /". [S.l.] : [s.n.], 2005. http://www.zb.unibe.ch/download/eldiss/05becaud_j.pdf.
Pełny tekst źródłaSchönewolf, Nicola. "Mutationen in der Connection und RNAse H-Domain der Reversen Transkriptase von HIV-1". Diss., lmu, 2010. http://nbn-resolving.de/urn:nbn:de:bvb:19-121176.
Pełny tekst źródłaLarrouy, Béatrice. "Effets sur la traduction d'oligonucléotides chimiquement modifiés : contribution de la RNase H, modulation post-transcriptionnelle". Bordeaux 2, 1996. http://www.theses.fr/1996BOR28413.
Pełny tekst źródłaKsiążki na temat "RNases H"
Blain, Stacy Wister. Structure-function studies of Moloney murine leukemia virus RNase H. 1995.
Znajdź pełny tekst źródłaCzęści książek na temat "RNases H"
Ponchon, Luc, Geneviève Beauvais, Sylvie Nonin-Lecomte i Frédéric Dardel. "Selective RNase H Cleavage of Target RNAs from a tRNA Scaffold". W Recombinant and In Vitro RNA Synthesis, 9–18. Totowa, NJ: Humana Press, 2012. http://dx.doi.org/10.1007/978-1-62703-113-4_2.
Pełny tekst źródłaHollis, Thomas, i Nadine M. Shaban. "Structure and Function of RNase H Enzymes". W Nucleic Acids and Molecular Biology, 299–317. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-21078-5_12.
Pełny tekst źródłaNowotny, Marcin, i Małgorzata Figiel. "The RNase H Domain: Structure, Function and Mechanism". W Human Immunodeficiency Virus Reverse Transcriptase, 53–75. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-7291-9_3.
Pełny tekst źródłaMoelling, Karin, Felix Broecker i John E. Kerrigan. "RNase H: Specificity, Mechanisms of Action, and Antiviral Target". W Methods in Molecular Biology, 71–84. Totowa, NJ: Humana Press, 2014. http://dx.doi.org/10.1007/978-1-62703-670-2_7.
Pełny tekst źródłaTachedjian, Gilda, i Nicolas Sluis-Cremer. "Role of RNase H Activity in NRTI/NNRTI Drug Resistance". W Human Immunodeficiency Virus Reverse Transcriptase, 281–303. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-7291-9_13.
Pełny tekst źródłaArvola, René M., i Aaron C. Goldstrohm. "Measuring Poly-Adenosine Tail Length of RNAs by High-Resolution Northern Blotting Coupled with RNase H Cleavage". W Methods in Molecular Biology, 93–111. New York, NY: Springer US, 2023. http://dx.doi.org/10.1007/978-1-0716-3481-3_6.
Pełny tekst źródłaSeth, Punit P., i Eric E. Swayze. "CHAPTER 3. The Medicinal Chemistry of RNase H-activating Antisense Oligonucleotides". W Drug Discovery, 32–61. Cambridge: Royal Society of Chemistry, 2019. http://dx.doi.org/10.1039/9781788015714-00032.
Pełny tekst źródłaWei, Fenju, Edeildo Ferreira da Silva-Júnior, Xinyong Liu i Peng Zhan. "HIV-1 and HBV RNase H as Metal-Chelating Inhibitors: Discovery and Medicinal Chemistry Strategies". W Human Viruses: Diseases, Treatments and Vaccines, 585–602. Cham: Springer International Publishing, 2021. http://dx.doi.org/10.1007/978-3-030-71165-8_28.
Pełny tekst źródłaMoelling, K., M. Nawrath, T. Schulze, L. Pavlitzkova, M. Soucek, K. H. Budt, L. H. Pearl, M. T. Knoop, J. Kay i V. Kruft. "Cleavage of RT/RNase H by HIV-1 Protease and Analysis of Substrate Cleavage Sites in vitro". W Retroviral Proteases, 19–29. London: Macmillan Education UK, 1990. http://dx.doi.org/10.1007/978-1-349-11907-3_4.
Pełny tekst źródłaMatthews, David A., Jay F. Davies, Zuzana Hostomska, Zdenek Hostomsky i Steven R. Jordan. "Three-dimensional structure of the RNase H domain of HIV-1 reverse transcriptase at 2. 4 Å resolution". W Peptides, 682–84. Dordrecht: Springer Netherlands, 1992. http://dx.doi.org/10.1007/978-94-011-2264-1_272.
Pełny tekst źródłaStreszczenia konferencji na temat "RNases H"
Sun, Yewei. "The role of eukaryotic RNase H in R-loop resolution". W Third International Conference on Biological Engineering and Medical Science (ICBioMed2023), redaktor Alan Wang. SPIE, 2024. http://dx.doi.org/10.1117/12.3012930.
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