Artykuły w czasopismach na temat „RNases H”
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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 źródłaOHTANI, Naoto, Hiroshi YANAGAWA, Masaru TOMITA i Mitsuhiro ITAYA. "Identification of the first archaeal Type 1 RNase H gene from Halobacterium sp. NRC-1: archaeal RNase HI can cleave an RNA–DNA junction". Biochemical Journal 381, nr 3 (27.07.2004): 795–802. http://dx.doi.org/10.1042/bj20040153.
Pełny tekst źródłaStafford, Kate A., i Arthur G. Palmer III. "Evidence from molecular dynamics simulations of conformational preorganization in the ribonuclease H active site". F1000Research 3 (7.03.2014): 67. http://dx.doi.org/10.12688/f1000research.3605.1.
Pełny tekst źródłaSchultz, Sharon J., Miaohua Zhang i James J. Champoux. "Recognition of Internal Cleavage Sites by Retroviral RNases H". Journal of Molecular Biology 344, nr 3 (listopad 2004): 635–52. http://dx.doi.org/10.1016/j.jmb.2004.09.081.
Pełny tekst źródłaOhtani, Naoto, Masaru Tomita i Mitsuhiro Itaya. "Junction ribonuclease: a ribonuclease HII orthologue from Thermus thermophilus HB8 prefers the RNA–DNA junction to the RNA/DNA heteroduplex". Biochemical Journal 412, nr 3 (28.05.2008): 517–26. http://dx.doi.org/10.1042/bj20080140.
Pełny tekst źródłaLim, David, G. Glenn Gregorio, Craig Bingman, Erik Martinez-Hackert, Wayne A. Hendrickson i Stephen P. Goff. "Crystal Structure of the Moloney Murine Leukemia Virus RNase H Domain". Journal of Virology 80, nr 17 (1.09.2006): 8379–89. http://dx.doi.org/10.1128/jvi.00750-06.
Pełny tekst źródłaZimmer, Anjali D., i Douglas Koshland. "Differential roles of the RNases H in preventing chromosome instability". Proceedings of the National Academy of Sciences 113, nr 43 (10.10.2016): 12220–25. http://dx.doi.org/10.1073/pnas.1613448113.
Pełny tekst źródłaGood-Avila, S. V., D. Majumder, H. Amos i A. G. Stephenson. "Characterization of self-incompatibility in Campanula rapunculoides (Campanulaceae) through genetic analyses and microscopy". Botany 86, nr 1 (styczeń 2008): 1–13. http://dx.doi.org/10.1139/b07-100.
Pełny tekst źródłaNowotny, Marcin, Sergei Gaidamakov, Robert J. Crouch i Wei Yang. "Structural studies of RNases H and their complexes with RNA/DNA hybrids". Acta Crystallographica Section A Foundations of Crystallography 65, a1 (16.08.2009): s138. http://dx.doi.org/10.1107/s0108767309097232.
Pełny tekst źródłaOhtani, Naoto, Mitsuru Haruki, Masaaki Morikawa, Robert J. Crouch, Mitsuhiro Itaya i Shigenori Kanaya. "Identification of the Genes Encoding Mn2+-Dependent RNase HII and Mg2+-Dependent RNase HIII fromBacillus subtilis: Classification of RNases H into Three Families†". Biochemistry 38, nr 2 (styczeń 1999): 605–18. http://dx.doi.org/10.1021/bi982207z.
Pełny tekst źródłaAn Lim, Shion, Kathryn M. Hart, Michael J. Harms i Susan Marqusee. "An Evolutionary Trend towards Kinetic Stability in the Folding Trajectory of RNases H". Biophysical Journal 112, nr 3 (luty 2017): 59a—60a. http://dx.doi.org/10.1016/j.bpj.2016.11.359.
Pełny tekst źródłaPermanasari, Etin-Diah, Kiyoshi Yasukawa i Shigenori Kanaya. "Enzymatic Activities of RNase H Domains of HIV-1 Reverse Transcriptase with Substrate Binding Domains of Bacterial RNases H1 and H2". Molecular Biotechnology 57, nr 6 (12.02.2015): 526–38. http://dx.doi.org/10.1007/s12033-015-9846-5.
Pełny tekst źródłaHafkemeyer, Peter, Klaus Neftel, Reinhard Hobi, Andreas Pfaltz, Hans Lutz, Kersten Lüthi, Federico Focher, Silvio Spadari i Ulrich Hübscher. "HP 0.35, a cephalosporin degradation product is a specific inhibitor of lentiviral RNAses H". Nucleic Acids Research 19, nr 15 (1991): 4059–65. http://dx.doi.org/10.1093/nar/19.15.4059.
Pełny tekst źródłaRosen, Laura E., i Susan Marqusee. "Autonomously Folding Protein Fragments Reveal Differences in the Energy Landscapes of Homologous RNases H". PLOS ONE 10, nr 3 (24.03.2015): e0119640. http://dx.doi.org/10.1371/journal.pone.0119640.
Pełny tekst źródłaStaroseletz, Yaroslav, Svetlana Gaponova, Olga Patutina, Elena Bichenkova, Bahareh Amirloo, Thomas Heyman, Daria Chiglintseva i Marina Zenkova. "Site-Selective Artificial Ribonucleases: Renaissance of Oligonucleotide Conjugates for Irreversible Cleavage of RNA Sequences". Molecules 26, nr 6 (19.03.2021): 1732. http://dx.doi.org/10.3390/molecules26061732.
Pełny tekst źródłaSmith, Robert M., Cherie M. Walton, Catherine H. Wu i George Y. Wu. "Secondary Structure and Hybridization Accessibility of Hepatitis C Virus 3′-Terminal Sequences". Journal of Virology 76, nr 19 (1.10.2002): 9563–74. http://dx.doi.org/10.1128/jvi.76.19.9563-9574.2002.
Pełny tekst źródłaSchultz, Sharon J., Miaohua Zhang i James J. Champoux. "Sequence, Distance, and Accessibility Are Determinants of 5′-End-directed Cleavages by Retroviral RNases H". Journal of Biological Chemistry 281, nr 4 (22.11.2005): 1943–55. http://dx.doi.org/10.1074/jbc.m510504200.
Pełny tekst źródłaShen, Ying, Kyung Duk Koh, Bernard Weiss i Francesca Storici. "Mispaired rNMPs in DNA are mutagenic and are targets of mismatch repair and RNases H". Nature Structural & Molecular Biology 19, nr 1 (4.12.2011): 98–104. http://dx.doi.org/10.1038/nsmb.2176.
Pełny tekst źródłaMeng, Wenzhao, i Allen W. Nicholson. "Heterodimer-based analysis of subunit and domain contributions to double-stranded RNA processing by Escherichia coli RNase III in vitro". Biochemical Journal 410, nr 1 (29.01.2008): 39–48. http://dx.doi.org/10.1042/bj20071047.
Pełny tekst źródłaLi, Chang, Mengqi Lu, Junqin Zhou, Sen Wang, Yi Long, Yan Xu i Xiaofeng Tan. "Transcriptome Analysis of the Late-Acting Self-Incompatibility Associated with RNase T2 Family in Camellia oleifera". Plants 12, nr 10 (9.05.2023): 1932. http://dx.doi.org/10.3390/plants12101932.
Pełny tekst źródłaSchultz, Sharon J., Miaohua Zhang i James J. Champoux. "Multiple Nucleotide Preferences Determine Cleavage-Site Recognition by the HIV-1 and M-MuLV RNases H". Journal of Molecular Biology 397, nr 1 (marzec 2010): 161–78. http://dx.doi.org/10.1016/j.jmb.2010.01.059.
Pełny tekst źródłaSchultz, Sharon J., Miaohua Zhang i James J. Champoux. "Preferred Sequences within a Defined Cleavage Window Specify DNA 3′ End-directed Cleavages by Retroviral RNases H". Journal of Biological Chemistry 284, nr 47 (24.09.2009): 32225–38. http://dx.doi.org/10.1074/jbc.m109.043158.
Pełny tekst źródłaGugliotti, Lina A., Kiran B. Sakhuja, Hongsheng Wang, Julia Pinkhasov, Paul E. Love, Susana M. Cerritelli, Herbert Morse i Robert J. Crouch. "Constitutive Lymphoid Expression of the Nuclear Form of RNase H1 Is Associated with a Developmental Bottleneck at the Pro-B Cell Stage of B Cell Differentiation." Blood 114, nr 22 (20.11.2009): 4702. http://dx.doi.org/10.1182/blood.v114.22.4702.4702.
Pełny tekst źródłaGuo, Yan, Jie Wu, Shilin Zhao, Fei Ye, Yinghao Su, Travis Clark, Quanhu Sheng, Brian Lehmann, Xiao-ou Shu i Qiuyin Cai. "RNA Sequencing of Formalin-Fixed, Paraffin-Embedded Specimens for Gene Expression Quantification and Data Mining". International Journal of Genomics 2016 (2016): 1–10. http://dx.doi.org/10.1155/2016/9837310.
Pełny tekst źródłaMorris, Shannon, i Jonathan Leis. "Changes in Rous Sarcoma Virus RNA Secondary Structure near the Primer Binding Site upon tRNATrpPrimer Annealing". Journal of Virology 73, nr 8 (1.08.1999): 6307–18. http://dx.doi.org/10.1128/jvi.73.8.6307-6318.1999.
Pełny tekst źródłaDharap, Ashuthosh, Kellie Bowen, Robert Place, Long-Cheng Li i Raghu Vemuganti. "Transient Focal Ischemia Induces Extensive Temporal Changes in Rat Cerebral MicroRNAome". Journal of Cerebral Blood Flow & Metabolism 29, nr 4 (14.01.2009): 675–87. http://dx.doi.org/10.1038/jcbfm.2008.157.
Pełny tekst źródłaGruber, Cornelia, Torsten Gursinsky, Selma Gago-Zachert, Vitantonio Pantaleo i Sven-Erik Behrens. "Effective Antiviral Application of Antisense in Plants by Exploiting Accessible Sites in the Target RNA". International Journal of Molecular Sciences 24, nr 24 (5.12.2023): 17153. http://dx.doi.org/10.3390/ijms242417153.
Pełny tekst źródłaLu, Gaofeng, Elena Lomonosova, Xiaohong Cheng, Eileen A. Moran, Marvin J. Meyers, Stuart F. J. Le Grice, Craig J. Thomas i in. "Hydroxylated Tropolones Inhibit Hepatitis B Virus Replication by Blocking Viral Ribonuclease H Activity". Antimicrobial Agents and Chemotherapy 59, nr 2 (1.12.2014): 1070–79. http://dx.doi.org/10.1128/aac.04617-14.
Pełny tekst źródłaArudchandran, Arulvathani, Susana Cerritelli, Scott Narimatsu, Mitsuhiro Itaya, Deug-Yong Shin, Yuji Shimada i Robert Crouch. "The absence of ribonuclease H1 or H2 alters the sensitivity of Saccharomyces cerevisiae to hydroxyurea, caffeine and ethyl methanesulphonate: implications for roles of RNases H in DNA replication and repair". Genes to Cells 5, nr 10 (październik 2000): 789–802. http://dx.doi.org/10.1046/j.1365-2443.2000.00373.x.
Pełny tekst źródłaSharma, Vasudha, Prachi Thakore i Sharmistha Majumdar. "THAP9 Transposase Cleaves DNA via Conserved Acidic Residues in an RNaseH-Like Domain". Cells 10, nr 6 (29.05.2021): 1351. http://dx.doi.org/10.3390/cells10061351.
Pełny tekst źródłaCorona, Angela, Anna Schneider, Kristian Schweimer, Paul Rösch, Birgitta M. Wöhrl i Enzo Tramontano. "Inhibition of Foamy Virus Reverse Transcriptase by Human Immunodeficiency Virus Type 1 RNase H Inhibitors". Antimicrobial Agents and Chemotherapy 58, nr 7 (5.05.2014): 4086–93. http://dx.doi.org/10.1128/aac.00056-14.
Pełny tekst źródłaCorona, Angela, Francesco Saverio Di Leva, Sylvain Thierry, Luca Pescatori, Giuliana Cuzzucoli Crucitti, Frederic Subra, Olivier Delelis i in. "Identification of Highly Conserved Residues Involved in Inhibition of HIV-1 RNase H Function by Diketo Acid Derivatives". Antimicrobial Agents and Chemotherapy 58, nr 10 (4.08.2014): 6101–10. http://dx.doi.org/10.1128/aac.03605-14.
Pełny tekst źródłaWang, Yafang, Namin Hu, Chang Liu, Cunpeng Nie, Manman He, Juan Zhang, Qiaoqin Yu, Chuan Zhao, Tingting Chen i Xia Chu. "An RNase H-powered DNA walking machine for sensitive detection of RNase H and the screening of related inhibitors". Nanoscale 12, nr 3 (2020): 1673–79. http://dx.doi.org/10.1039/c9nr07550j.
Pełny tekst źródłaDelviks-Frankenberry, Krista A., Galina N. Nikolenko, Rebekah Barr i Vinay K. Pathak. "Mutations in Human Immunodeficiency Virus Type 1 RNase H Primer Grip Enhance 3′-Azido-3′-Deoxythymidine Resistance". Journal of Virology 81, nr 13 (11.04.2007): 6837–45. http://dx.doi.org/10.1128/jvi.02820-06.
Pełny tekst źródłaLee, Hyunjee, HyeokJin Cho, Jooyoung Kim, Sua Lee, Jungmin Yoo, Daeho Park i Gwangrog Lee. "RNase H is an exo- and endoribonuclease with asymmetric directionality, depending on the binding mode to the structural variants of RNA:DNA hybrids". Nucleic Acids Research 50, nr 4 (12.11.2021): 1801–14. http://dx.doi.org/10.1093/nar/gkab1064.
Pełny tekst źródłaFarias, Richard V., Deborah A. Vargas, Andres E. Castillo, Beatriz Valenzuela, Marie L. Coté, Monica J. Roth i Oscar Leon. "Expression of an Mg2+-Dependent HIV-1 RNase H Construct for Drug Screening". Antimicrobial Agents and Chemotherapy 55, nr 10 (18.07.2011): 4735–41. http://dx.doi.org/10.1128/aac.00658-11.
Pełny tekst źródłaBrincat, Jennifer L., Julie K. Pfeiffer i Alice Telesnitsky. "RNase H Activity Is Required for High-Frequency Repeat Deletion during Moloney Murine Leukemia Virus Replication". Journal of Virology 76, nr 1 (1.01.2002): 88–95. http://dx.doi.org/10.1128/jvi.76.1.88-95.2002.
Pełny tekst źródłaKeck, James L., Eric R. Goedken i Susan Marqusee. "Activation/Attenuation Model for RNase H". Journal of Biological Chemistry 273, nr 51 (18.12.1998): 34128–33. http://dx.doi.org/10.1074/jbc.273.51.34128.
Pełny tekst źródłaKrakowiak, Agnieszka, Alina Owczarek, Maria Koziołkiewicz i Wojciech J. Stec. "Stereochemical Course ofEscherichia coli RNase H". ChemBioChem 3, nr 12 (2.12.2002): 1242–50. http://dx.doi.org/10.1002/1439-7633(20021202)3:12<1242::aid-cbic1242>3.0.co;2-y.
Pełny tekst źródłaSu, Hua-Poo, Youwei Yan, G. Sridhar Prasad, Robert F. Smith, Christopher L. Daniels, Pravien D. Abeywickrema, John C. Reid i in. "Structural Basis for the Inhibition of RNase H Activity of HIV-1 Reverse Transcriptase by RNase H Active Site-Directed Inhibitors". Journal of Virology 84, nr 15 (19.05.2010): 7625–33. http://dx.doi.org/10.1128/jvi.00353-10.
Pełny tekst źródłaCorona, Angela, Valentina Onnis, Claudia Del Vecchio, Francesca Esposito, Yung-Chi Cheng i Enzo Tramontano. "2-(Arylamino)-6-(trifluoromethyl)nicotinic Acid Derivatives: New HIV-1 RT Dual Inhibitors Active on Viral Replication". Molecules 25, nr 6 (15.03.2020): 1338. http://dx.doi.org/10.3390/molecules25061338.
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