Artículos de revistas sobre el tema "SF2 helicase"
Crea una cita precisa en los estilos APA, MLA, Chicago, Harvard y otros
Consulte los 50 mejores artículos de revistas para su investigación sobre el tema "SF2 helicase".
Junto a cada fuente en la lista de referencias hay un botón "Agregar a la bibliografía". Pulsa este botón, y generaremos automáticamente la referencia bibliográfica para la obra elegida en el estilo de cita que necesites: APA, MLA, Harvard, Vancouver, Chicago, etc.
También puede descargar el texto completo de la publicación académica en formato pdf y leer en línea su resumen siempre que esté disponible en los metadatos.
Explore artículos de revistas sobre una amplia variedad de disciplinas y organice su bibliografía correctamente.
Gilman, Benjamin, Pilar Tijerina y Rick Russell. "Distinct RNA-unwinding mechanisms of DEAD-box and DEAH-box RNA helicase proteins in remodeling structured RNAs and RNPs". Biochemical Society Transactions 45, n.º 6 (17 de noviembre de 2017): 1313–21. http://dx.doi.org/10.1042/bst20170095.
Texto completoSeybert, Anja, Leonie C. van Dinten, Eric J. Snijder y John Ziebuhr. "Biochemical Characterization of the Equine Arteritis Virus Helicase Suggests a Close Functional Relationship between Arterivirus and Coronavirus Helicases". Journal of Virology 74, n.º 20 (15 de octubre de 2000): 9586–93. http://dx.doi.org/10.1128/jvi.74.20.9586-9593.2000.
Texto completoFan, Li y Kevin T. DuPrez. "XPB: An unconventional SF2 DNA helicase". Progress in Biophysics and Molecular Biology 117, n.º 2-3 (marzo de 2015): 174–81. http://dx.doi.org/10.1016/j.pbiomolbio.2014.12.005.
Texto completoWoodman, Isabel L. y Edward L. Bolt. "Molecular biology of Hel308 helicase in archaea". Biochemical Society Transactions 37, n.º 1 (20 de enero de 2009): 74–78. http://dx.doi.org/10.1042/bst0370074.
Texto completoDu Pont, Kelly E., Russell B. Davidson, Martin McCullagh y Brian J. Geiss. "Motif V regulates energy transduction between the flavivirus NS3 ATPase and RNA-binding cleft". Journal of Biological Chemistry 295, n.º 6 (30 de diciembre de 2019): 1551–64. http://dx.doi.org/10.1074/jbc.ra119.011922.
Texto completoMoukhtar, Mirna, Wafi Chaar, Ziad Abdel-Razzak, Mohamad Khalil, Samir Taha y Hala Chamieh. "ARCPHdb: A comprehensive protein database for SF1 and SF2 helicase from archaea". Computers in Biology and Medicine 80 (enero de 2017): 185–89. http://dx.doi.org/10.1016/j.compbiomed.2016.12.004.
Texto completoKawaoka, Jane, Eckhard Jankowsky y Anna Marie Pyle. "Backbone tracking by the SF2 helicase NPH-II". Nature Structural & Molecular Biology 11, n.º 6 (16 de mayo de 2004): 526–30. http://dx.doi.org/10.1038/nsmb771.
Texto completoHalgasova, Nora, Radka Matuskova, Daniel Kraus, Adela Tkacova, Lenka Balusikova y Gabriela Bukovska. "Gp41, a superfamily SF2 helicase from bacteriophage BFK20". Virus Research 245 (febrero de 2018): 7–16. http://dx.doi.org/10.1016/j.virusres.2017.12.005.
Texto completoRomero, Zachary J., Stefanie H. Chen, Thomas Armstrong, Elizabeth A. Wood, Antoine van Oijen, Andrew Robinson y Michael M. Cox. "Resolving Toxic DNA repair intermediates in every E. coli replication cycle: critical roles for RecG, Uup and RadD". Nucleic Acids Research 48, n.º 15 (9 de julio de 2020): 8445–60. http://dx.doi.org/10.1093/nar/gkaa579.
Texto completoHajj, Mirna, Petra Langendijk-Genevaux, Manon Batista, Yves Quentin, Sébastien Laurent, Régine Capeyrou, Ziad Abdel-Razzak et al. "Phylogenetic Diversity of Lhr Proteins and Biochemical Activities of the Thermococcales aLhr2 DNA/RNA Helicase". Biomolecules 11, n.º 7 (26 de junio de 2021): 950. http://dx.doi.org/10.3390/biom11070950.
Texto completoPugh, Robert A., Masayoshi Honda, Haley Leesley, Alvin Thomas, Yuyen Lin, Mark J. Nilges, Isaac K. O. Cann y Maria Spies. "The Iron-containing Domain Is Essential in Rad3 Helicases for Coupling of ATP Hydrolysis to DNA Translocation and for Targeting the Helicase to the Single-stranded DNA-Double-stranded DNA Junction". Journal of Biological Chemistry 283, n.º 3 (20 de noviembre de 2007): 1732–43. http://dx.doi.org/10.1074/jbc.m707064200.
Texto completoBonde, Nina J., Zachary J. Romero, Sindhu Chitteni-Pattu y Michael M. Cox. "RadD is a RecA-dependent accessory protein that accelerates DNA strand exchange". Nucleic Acids Research 50, n.º 4 (12 de febrero de 2022): 2201–10. http://dx.doi.org/10.1093/nar/gkac041.
Texto completoSmith, Corey L. y Craig L. Peterson. "A Conserved Swi2/Snf2 ATPase Motif Couples ATP Hydrolysis to Chromatin Remodeling". Molecular and Cellular Biology 25, n.º 14 (julio de 2005): 5880–92. http://dx.doi.org/10.1128/mcb.25.14.5880-5892.2005.
Texto completoMasterson, Philip J., Margaret A. Stanley, Alan P. Lewis y Michael A. Romanos. "A C-Terminal Helicase Domain of the Human Papillomavirus E1 Protein Binds E2 and the DNA Polymerase α-Primase p68 Subunit". Journal of Virology 72, n.º 9 (1 de septiembre de 1998): 7407–19. http://dx.doi.org/10.1128/jvi.72.9.7407-7419.1998.
Texto completoJangra, Rohit K., MinKyung Yi y Stanley M. Lemon. "DDX6 (Rck/p54) Is Required for Efficient Hepatitis C Virus Replication but Not for Internal Ribosome Entry Site-Directed Translation". Journal of Virology 84, n.º 13 (14 de abril de 2010): 6810–24. http://dx.doi.org/10.1128/jvi.00397-10.
Texto completoCHINO, MAKOTO, KIYOHIRO NISHIKAWA, RYUICHI SAWA, MASA HAMADA, HIROSHI NAGANAWA, TSUTOMU SAWA y TOMIO TAKEUCHI. "Heliquinomycin, a New Inhibitor of DNA Helicase, Produced by Streptomyces sp. MJ929-SF2. III. Biosynthesis." Journal of Antibiotics 50, n.º 9 (1997): 781–84. http://dx.doi.org/10.7164/antibiotics.50.781.
Texto completoMackeldanz, Petra, Jürgen Alves, Elisabeth Möncke-Buchner, Karol H. Wyszomirski, Detlev H. Krüger y Monika Reuter. "Functional consequences of mutating conserved SF2 helicase motifs in the Type III restriction endonuclease EcoP15I translocase domain". Biochimie 95, n.º 4 (abril de 2013): 817–23. http://dx.doi.org/10.1016/j.biochi.2012.11.014.
Texto completoCHINO, MAKOTO, KIYOHIRO NISHIKAWA, TOSHIO TSUCHIDA, RYUICHI SAWA, HIKARU NAKAMURA, KAZUO T. NAKAMURA, YASUHIKO MURAOKA et al. "Heliquinomycin, a New Inhibitor of DNA Helicase, Produced by Streptomyces sp. MJ929-SF2.II. Structure Determination of Heliquinomycin." Journal of Antibiotics 50, n.º 2 (1997): 143–46. http://dx.doi.org/10.7164/antibiotics.50.143.
Texto completoGajewski, Stefan, Michael R. Webb, Vitold Galkin, Edward H. Egelman, Kenneth N. Kreuzer y Stephen W. White. "Crystal Structure of the Phage T4 Recombinase UvsX and Its Functional Interaction with the T4 SF2 Helicase UvsW". Journal of Molecular Biology 405, n.º 1 (enero de 2011): 65–76. http://dx.doi.org/10.1016/j.jmb.2010.10.004.
Texto completoCHINO, M., K. NISHIKAWA, R. SAWA, M. HAMADA, H. NAGANAWA, T. SAWA y T. TAKEUCHI. "ChemInform Abstract: Heliquinomycin, a New Inhibitor of DNA Helicase, Produced by Streptomyces sp. MJ929-SF2. Part 3. Biosynthesis." ChemInform 29, n.º 9 (23 de junio de 2010): no. http://dx.doi.org/10.1002/chin.199809242.
Texto completoCHINO, M., K. NISHIKAWA, T. TSUCHIDA, R. SAWA, H. NAKAMURA, K. T. NAKAMURA, Y. MURAOKA et al. "ChemInform Abstract: Heliquinomycin, a New Inhibitor of DNA Helicase, Produced by Streptomyces Sp. MJ929-SF2. Part 2. Structure Determination of Heliquinomycin." ChemInform 28, n.º 30 (3 de agosto de 2010): no. http://dx.doi.org/10.1002/chin.199730221.
Texto completoZhang, Xianduo, Jianbo Song, Liping Wang, Zhi Min Yang y Di Sun. "Identification of a DEAD-Box RNA Helicase BnRH6 Reveals Its Involvement in Salt Stress Response in Rapeseed (Brassica napus)". International Journal of Molecular Sciences 24, n.º 1 (20 de diciembre de 2022): 2. http://dx.doi.org/10.3390/ijms24010002.
Texto completoFairman-Williams, Margaret E., Ulf-Peter Guenther y Eckhard Jankowsky. "SF1 and SF2 helicases: family matters". Current Opinion in Structural Biology 20, n.º 3 (junio de 2010): 313–24. http://dx.doi.org/10.1016/j.sbi.2010.03.011.
Texto completoThomas, Christopher A., Jonathan M. Craig, Shuichi Hoshika, Andrew H. Laszlo, Jesse R. Huang, Sarah J. Abell, Hwanhee C. Kim et al. "C-Glycoside DNA bases from an artificially expanded genetic information system reduce processivity in a SF2 helicase as revealed by nanopore tweezers". Biophysical Journal 121, n.º 3 (febrero de 2022): 209a—210a. http://dx.doi.org/10.1016/j.bpj.2021.11.1671.
Texto completoCHINO, MAKOTO, KIYOHIRO NISHIKAWA, MAYA UMEKITA, CHIGUSA HAYASHI, TAKAKO YAMAZAKI, TOSHIO TSUCHIDA, TSUTOMU SAWA, MASA HAMADA y TOMIO TAKEUCHI. "Heliquinomycin, a New Inhibitor of DNA Helicase, Produced by Streptomyces sp. MJ929-SF2. I. Taxonomy, Production, Isolation, Physico-chemical Properties and Biological Activities." Journal of Antibiotics 49, n.º 8 (1996): 752–57. http://dx.doi.org/10.7164/antibiotics.49.752.
Texto completoCHINO, M., K. NISHIKAWA, M. UMEKITA, C. HAYASHI, T. YAMAZAKI, T. TSUCHIDA, T. SAWA, M. HAMADA y T. TAKEUCHI. "ChemInform Abstract: Heliquinomycin, a New Inhibitor of DNA Helicase, Produced by Streptomyces sp. MJ929-SF2. Part 1. Taxonomy, Production, Isolation, Physico-Chemical Properties and Biological Activities". ChemInform 28, n.º 6 (4 de agosto de 2010): no. http://dx.doi.org/10.1002/chin.199706230.
Texto completoChamieh, Hala, Hiba Ibrahim y Juliana Kozah. "Genome-wide identification of SF1 and SF2 helicases from archaea". Gene 576, n.º 1 (enero de 2016): 214–28. http://dx.doi.org/10.1016/j.gene.2015.10.007.
Texto completoHanet, Aoife, Felix Räsch, Ramona Weber, Vincenzo Ruscica, Maria Fauser, Tobias Raisch, Duygu Kuzuoğlu-Öztürk et al. "HELZ directly interacts with CCR4–NOT and causes decay of bound mRNAs". Life Science Alliance 2, n.º 5 (30 de septiembre de 2019): e201900405. http://dx.doi.org/10.26508/lsa.201900405.
Texto completoChaar, Wafi, Hiba Ibrahim, Juliana Kozah y Hala Chamieh. "Comparative analysis data of SF1 and SF2 helicases from three domains of life". Data in Brief 11 (abril de 2017): 510–16. http://dx.doi.org/10.1016/j.dib.2017.02.047.
Texto completoPugh, Robert A., Colin G. Wu y Maria Spies. "Regulation of translocation polarity by helicase domain 1 in SF2B helicases". EMBO Journal 31, n.º 2 (11 de noviembre de 2011): 503–14. http://dx.doi.org/10.1038/emboj.2011.412.
Texto completoKorolev, Sergey, Timothy M. Lohman, Gabriel Waksman, Nanhua Yao y Patricia C. Weber. "Comparisons between the structures of HCV and Rep helicases reveal structural similarities between SF1 and SF2 super-families of helicases". Protein Science 7, n.º 3 (marzo de 1998): 605–10. http://dx.doi.org/10.1002/pro.5560070309.
Texto completoJedrzejczak, Robert, Jiawei Wang, Miroslawa Dauter, Roman J. Szczesny, Piotr P. Stepien y Zbigniew Dauter. "Human Suv3 protein reveals unique features among SF2 helicases". Acta Crystallographica Section D Biological Crystallography 67, n.º 11 (19 de octubre de 2011): 988–96. http://dx.doi.org/10.1107/s0907444911040248.
Texto completoSèle, Céleste, Frank Gabel, Irina Gutsche, Ivan Ivanov, Wim P. Burmeister, Frédéric Iseni y Nicolas Tarbouriech. "Low-Resolution Structure of Vaccinia Virus DNA Replication Machinery". Journal of Virology 87, n.º 3 (21 de noviembre de 2012): 1679–89. http://dx.doi.org/10.1128/jvi.01533-12.
Texto completoHickman, Alison Burgess y Fred Dyda. "Binding and unwinding: SF3 viral helicases". Current Opinion in Structural Biology 15, n.º 1 (febrero de 2005): 77–85. http://dx.doi.org/10.1016/j.sbi.2004.12.001.
Texto completoStopp, Marius, Philipp A. Steinmetz y Gottfried Unden. "Properties of transmembrane helix TM1 of the DcuS sensor kinase of Escherichia coli, the stator for TM2 piston signaling". Biological Chemistry 402, n.º 10 (6 de agosto de 2021): 1239–46. http://dx.doi.org/10.1515/hsz-2021-0254.
Texto completoRuben, George C. y W. H. Stockmayer. "Evidence for helical structures in poly(l-olefin sulfones) by TEM". Proceedings, annual meeting, Electron Microscopy Society of America 50, n.º 1 (agosto de 1992): 276–77. http://dx.doi.org/10.1017/s0424820100121788.
Texto completoVAN DER KNAAP, Jan A., Vincent VAN DEN BOOM, Jeroen KUIPERS, Michiel J. T. VAN EIJK, Peter C. VAN DER VLIET y H. Th Marc TIMMERS. "The gene for human TATA-binding-protein-associated factor (TAFII) 170: structure, promoter and chromosomal localization". Biochemical Journal 345, n.º 3 (25 de enero de 2000): 521–27. http://dx.doi.org/10.1042/bj3450521.
Texto completoBöttcher, P. y H. Buchkremer-Hermanns. "Darstellung und Kristallstruktur des Bis(2-amino-1-ammonioethan)hexasulfids [H3N-(CH2)2-NH2]2S6 /Synthesis and Crystal Structure of Bis(2-amino-1-ammonioethan)hexasulfide, [H3N—(CH2)2-NH2]2S6". Zeitschrift für Naturforschung B 42, n.º 3 (1 de marzo de 1987): 267–71. http://dx.doi.org/10.1515/znb-1987-0303.
Texto completoPROUX-GILLARDEAUX, Véronique, Thierry GALLI, Isabelle CALLEBAUT, Anatoly MIKHAILIK, Georges CALOTHY y Maria MARX. "D53 is a novel endosomal SNARE-binding protein that enhances interaction of syntaxin 1 with the synaptobrevin 2 complex in vitro". Biochemical Journal 370, n.º 1 (15 de febrero de 2003): 213–21. http://dx.doi.org/10.1042/bj20021309.
Texto completoJames, J. Anson, Carlos R. Escalante, Miran Yoon-Robarts, Thomas A. Edwards, R. Michael Linden y Aneel K. Aggarwal. "Crystal Structure of the SF3 Helicase from Adeno-Associated Virus Type 2". Structure 11, n.º 8 (agosto de 2003): 1025–35. http://dx.doi.org/10.1016/s0969-2126(03)00152-7.
Texto completoBéguin, Pierre, Bruno Baron, Sukhvinder Gill, Nicole Charpin y Patrick Forterre. "The SF1 helicase encoded by the archaeal plasmid pTN2 of Thermococcus nautili". Extremophiles 18, n.º 4 (3 de junio de 2014): 779–87. http://dx.doi.org/10.1007/s00792-014-0658-5.
Texto completoFradet-Turcotte, Amélie, Cary Moody, Laimonis A. Laimins y Jacques Archambault. "Nuclear Export of Human Papillomavirus Type 31 E1 Is Regulated by Cdk2 Phosphorylation and Required for Viral Genome Maintenance". Journal of Virology 84, n.º 22 (15 de septiembre de 2010): 11747–60. http://dx.doi.org/10.1128/jvi.01445-10.
Texto completoPeled-Zehavi, Hadas, J. Andrew Berglund, Michael Rosbash y Alan D. Frankel. "Recognition of RNA Branch Point Sequences by the KH Domain of Splicing Factor 1 (Mammalian Branch Point Binding Protein) in a Splicing Factor Complex". Molecular and Cellular Biology 21, n.º 15 (1 de agosto de 2001): 5232–41. http://dx.doi.org/10.1128/mcb.21.15.5232-5241.2001.
Texto completoPaul, John H., Shannon J. Williamson, Amy Long, R. Nathan Authement, David John, Anca M. Segall, Forest L. Rohwer, Matthew Androlewicz y Stacey Patterson. "Complete Genome Sequence of φHSIC, a Pseudotemperate Marine Phage of Listonella pelagia". Applied and Environmental Microbiology 71, n.º 6 (junio de 2005): 3311–20. http://dx.doi.org/10.1128/aem.71.6.3311-3320.2005.
Texto completoMüller, C. y P. Böttcher. "Darstellung und Kristallstruktur des Bis(diisobutylammonium)-heptasulfids [H2N(i-C4H9)2]2S7 / Synthesis and Crystal Structure of Bis(diisobutylammonium)-heptasulfide [H2N(i-C4H9)2]2S7". Zeitschrift für Naturforschung B 48, n.º 12 (1 de diciembre de 1993): 1732–36. http://dx.doi.org/10.1515/znb-1993-1207.
Texto completoGargantini, Pablo R., Marianela C. Serradell, Alessandro Torri y Hugo D. Lujan. "Putative SF2 helicases of the early-branching eukaryote Giardia lamblia are involved in antigenic variation and parasite differentiation into cysts". BMC Microbiology 12, n.º 1 (2012): 284. http://dx.doi.org/10.1186/1471-2180-12-284.
Texto completoMüller, C. y P. Böttcher. "Darstellung und Kristallstruktur des Bis(dicyclohexylammoniuni)-lieptasulfids [H2N(C6H11 )2]2S7/Preparation and Crystal Structure of Bis(dicyclohexylammonium )-heptasulfide [H2N(C6H11)2]2S7". Zeitschrift für Naturforschung B 48, n.º 1 (1 de enero de 1993): 90–92. http://dx.doi.org/10.1515/znb-1993-0120.
Texto completoZheng, Zheng, Minli Bao, Fengnian Wu, Christopher Van Horn, Jianchi Chen y Xiaoling Deng. "A Type 3 Prophage of ‘Candidatus Liberibacter asiaticus’ Carrying a Restriction-Modification System". Phytopathology® 108, n.º 4 (abril de 2018): 454–61. http://dx.doi.org/10.1094/phyto-08-17-0282-r.
Texto completoGeorge, Biju, Rajrani Ruhel, Mohit Mazumder, Veerendra Kumar Sharma, Swatantra Kumar Jain, Samudrala Gourinath y Supriya Chakraborty. "Mutational analysis of the helicase domain of a replication initiator protein reveals critical roles of Lys 272 of the B′ motif and Lys 289 of the β-hairpin loop in geminivirus replication". Journal of General Virology 95, n.º 7 (1 de julio de 2014): 1591–602. http://dx.doi.org/10.1099/vir.0.064923-0.
Texto completoVasilevskaya, Ekaterina Romanovna y Anastasia Gennadievna Akhremko. "Proteomic study of pig’s spleen". Potravinarstvo Slovak Journal of Food Sciences 13, n.º 1 (28 de mayo de 2019): 314–17. http://dx.doi.org/10.5219/1093.
Texto completo