Статті в журналах з теми "SF2 helicase"
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Ознайомтеся з топ-50 статей у журналах для дослідження на тему "SF2 helicase".
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Gilman, Benjamin, Pilar Tijerina, and 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, no. 6 (November 17, 2017): 1313–21. http://dx.doi.org/10.1042/bst20170095.
Повний текст джерелаSeybert, Anja, Leonie C. van Dinten, Eric J. Snijder, and John Ziebuhr. "Biochemical Characterization of the Equine Arteritis Virus Helicase Suggests a Close Functional Relationship between Arterivirus and Coronavirus Helicases." Journal of Virology 74, no. 20 (October 15, 2000): 9586–93. http://dx.doi.org/10.1128/jvi.74.20.9586-9593.2000.
Повний текст джерелаFan, Li, and Kevin T. DuPrez. "XPB: An unconventional SF2 DNA helicase." Progress in Biophysics and Molecular Biology 117, no. 2-3 (March 2015): 174–81. http://dx.doi.org/10.1016/j.pbiomolbio.2014.12.005.
Повний текст джерелаWoodman, Isabel L., and Edward L. Bolt. "Molecular biology of Hel308 helicase in archaea." Biochemical Society Transactions 37, no. 1 (January 20, 2009): 74–78. http://dx.doi.org/10.1042/bst0370074.
Повний текст джерелаDu Pont, Kelly E., Russell B. Davidson, Martin McCullagh, and Brian J. Geiss. "Motif V regulates energy transduction between the flavivirus NS3 ATPase and RNA-binding cleft." Journal of Biological Chemistry 295, no. 6 (December 30, 2019): 1551–64. http://dx.doi.org/10.1074/jbc.ra119.011922.
Повний текст джерелаMoukhtar, Mirna, Wafi Chaar, Ziad Abdel-Razzak, Mohamad Khalil, Samir Taha, and Hala Chamieh. "ARCPHdb: A comprehensive protein database for SF1 and SF2 helicase from archaea." Computers in Biology and Medicine 80 (January 2017): 185–89. http://dx.doi.org/10.1016/j.compbiomed.2016.12.004.
Повний текст джерелаKawaoka, Jane, Eckhard Jankowsky, and Anna Marie Pyle. "Backbone tracking by the SF2 helicase NPH-II." Nature Structural & Molecular Biology 11, no. 6 (May 16, 2004): 526–30. http://dx.doi.org/10.1038/nsmb771.
Повний текст джерелаHalgasova, Nora, Radka Matuskova, Daniel Kraus, Adela Tkacova, Lenka Balusikova, and Gabriela Bukovska. "Gp41, a superfamily SF2 helicase from bacteriophage BFK20." Virus Research 245 (February 2018): 7–16. http://dx.doi.org/10.1016/j.virusres.2017.12.005.
Повний текст джерелаRomero, Zachary J., Stefanie H. Chen, Thomas Armstrong, Elizabeth A. Wood, Antoine van Oijen, Andrew Robinson, and 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, no. 15 (July 9, 2020): 8445–60. http://dx.doi.org/10.1093/nar/gkaa579.
Повний текст джерелаHajj, 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, no. 7 (June 26, 2021): 950. http://dx.doi.org/10.3390/biom11070950.
Повний текст джерелаPugh, Robert A., Masayoshi Honda, Haley Leesley, Alvin Thomas, Yuyen Lin, Mark J. Nilges, Isaac K. O. Cann, and 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, no. 3 (November 20, 2007): 1732–43. http://dx.doi.org/10.1074/jbc.m707064200.
Повний текст джерелаBonde, Nina J., Zachary J. Romero, Sindhu Chitteni-Pattu, and Michael M. Cox. "RadD is a RecA-dependent accessory protein that accelerates DNA strand exchange." Nucleic Acids Research 50, no. 4 (February 12, 2022): 2201–10. http://dx.doi.org/10.1093/nar/gkac041.
Повний текст джерелаSmith, Corey L., and Craig L. Peterson. "A Conserved Swi2/Snf2 ATPase Motif Couples ATP Hydrolysis to Chromatin Remodeling." Molecular and Cellular Biology 25, no. 14 (July 2005): 5880–92. http://dx.doi.org/10.1128/mcb.25.14.5880-5892.2005.
Повний текст джерелаMasterson, Philip J., Margaret A. Stanley, Alan P. Lewis та 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, № 9 (1 вересня 1998): 7407–19. http://dx.doi.org/10.1128/jvi.72.9.7407-7419.1998.
Повний текст джерелаJangra, Rohit K., MinKyung Yi, and 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, no. 13 (April 14, 2010): 6810–24. http://dx.doi.org/10.1128/jvi.00397-10.
Повний текст джерелаCHINO, MAKOTO, KIYOHIRO NISHIKAWA, RYUICHI SAWA, MASA HAMADA, HIROSHI NAGANAWA, TSUTOMU SAWA, and TOMIO TAKEUCHI. "Heliquinomycin, a New Inhibitor of DNA Helicase, Produced by Streptomyces sp. MJ929-SF2. III. Biosynthesis." Journal of Antibiotics 50, no. 9 (1997): 781–84. http://dx.doi.org/10.7164/antibiotics.50.781.
Повний текст джерелаMackeldanz, Petra, Jürgen Alves, Elisabeth Möncke-Buchner, Karol H. Wyszomirski, Detlev H. Krüger, and Monika Reuter. "Functional consequences of mutating conserved SF2 helicase motifs in the Type III restriction endonuclease EcoP15I translocase domain." Biochimie 95, no. 4 (April 2013): 817–23. http://dx.doi.org/10.1016/j.biochi.2012.11.014.
Повний текст джерелаCHINO, 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, no. 2 (1997): 143–46. http://dx.doi.org/10.7164/antibiotics.50.143.
Повний текст джерелаGajewski, Stefan, Michael R. Webb, Vitold Galkin, Edward H. Egelman, Kenneth N. Kreuzer, and 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, no. 1 (January 2011): 65–76. http://dx.doi.org/10.1016/j.jmb.2010.10.004.
Повний текст джерелаCHINO, M., K. NISHIKAWA, R. SAWA, M. HAMADA, H. NAGANAWA, T. SAWA, and T. TAKEUCHI. "ChemInform Abstract: Heliquinomycin, a New Inhibitor of DNA Helicase, Produced by Streptomyces sp. MJ929-SF2. Part 3. Biosynthesis." ChemInform 29, no. 9 (June 23, 2010): no. http://dx.doi.org/10.1002/chin.199809242.
Повний текст джерелаCHINO, 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, no. 30 (August 3, 2010): no. http://dx.doi.org/10.1002/chin.199730221.
Повний текст джерелаZhang, Xianduo, Jianbo Song, Liping Wang, Zhi Min Yang, and 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, no. 1 (December 20, 2022): 2. http://dx.doi.org/10.3390/ijms24010002.
Повний текст джерелаFairman-Williams, Margaret E., Ulf-Peter Guenther, and Eckhard Jankowsky. "SF1 and SF2 helicases: family matters." Current Opinion in Structural Biology 20, no. 3 (June 2010): 313–24. http://dx.doi.org/10.1016/j.sbi.2010.03.011.
Повний текст джерелаThomas, 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, no. 3 (February 2022): 209a—210a. http://dx.doi.org/10.1016/j.bpj.2021.11.1671.
Повний текст джерелаCHINO, MAKOTO, KIYOHIRO NISHIKAWA, MAYA UMEKITA, CHIGUSA HAYASHI, TAKAKO YAMAZAKI, TOSHIO TSUCHIDA, TSUTOMU SAWA, MASA HAMADA, and 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, no. 8 (1996): 752–57. http://dx.doi.org/10.7164/antibiotics.49.752.
Повний текст джерелаCHINO, M., K. NISHIKAWA, M. UMEKITA, C. HAYASHI, T. YAMAZAKI, T. TSUCHIDA, T. SAWA, M. HAMADA, and 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, no. 6 (August 4, 2010): no. http://dx.doi.org/10.1002/chin.199706230.
Повний текст джерелаChamieh, Hala, Hiba Ibrahim, and Juliana Kozah. "Genome-wide identification of SF1 and SF2 helicases from archaea." Gene 576, no. 1 (January 2016): 214–28. http://dx.doi.org/10.1016/j.gene.2015.10.007.
Повний текст джерелаHanet, 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, no. 5 (September 30, 2019): e201900405. http://dx.doi.org/10.26508/lsa.201900405.
Повний текст джерелаChaar, Wafi, Hiba Ibrahim, Juliana Kozah, and Hala Chamieh. "Comparative analysis data of SF1 and SF2 helicases from three domains of life." Data in Brief 11 (April 2017): 510–16. http://dx.doi.org/10.1016/j.dib.2017.02.047.
Повний текст джерелаPugh, Robert A., Colin G. Wu, and Maria Spies. "Regulation of translocation polarity by helicase domain 1 in SF2B helicases." EMBO Journal 31, no. 2 (November 11, 2011): 503–14. http://dx.doi.org/10.1038/emboj.2011.412.
Повний текст джерелаKorolev, Sergey, Timothy M. Lohman, Gabriel Waksman, Nanhua Yao, and 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, no. 3 (March 1998): 605–10. http://dx.doi.org/10.1002/pro.5560070309.
Повний текст джерелаJedrzejczak, Robert, Jiawei Wang, Miroslawa Dauter, Roman J. Szczesny, Piotr P. Stepien, and Zbigniew Dauter. "Human Suv3 protein reveals unique features among SF2 helicases." Acta Crystallographica Section D Biological Crystallography 67, no. 11 (October 19, 2011): 988–96. http://dx.doi.org/10.1107/s0907444911040248.
Повний текст джерелаSèle, Céleste, Frank Gabel, Irina Gutsche, Ivan Ivanov, Wim P. Burmeister, Frédéric Iseni, and Nicolas Tarbouriech. "Low-Resolution Structure of Vaccinia Virus DNA Replication Machinery." Journal of Virology 87, no. 3 (November 21, 2012): 1679–89. http://dx.doi.org/10.1128/jvi.01533-12.
Повний текст джерелаHickman, Alison Burgess, and Fred Dyda. "Binding and unwinding: SF3 viral helicases." Current Opinion in Structural Biology 15, no. 1 (February 2005): 77–85. http://dx.doi.org/10.1016/j.sbi.2004.12.001.
Повний текст джерелаStopp, Marius, Philipp A. Steinmetz, and Gottfried Unden. "Properties of transmembrane helix TM1 of the DcuS sensor kinase of Escherichia coli, the stator for TM2 piston signaling." Biological Chemistry 402, no. 10 (August 6, 2021): 1239–46. http://dx.doi.org/10.1515/hsz-2021-0254.
Повний текст джерелаRuben, George C., and W. H. Stockmayer. "Evidence for helical structures in poly(l-olefin sulfones) by TEM." Proceedings, annual meeting, Electron Microscopy Society of America 50, no. 1 (August 1992): 276–77. http://dx.doi.org/10.1017/s0424820100121788.
Повний текст джерелаVAN DER KNAAP, Jan A., Vincent VAN DEN BOOM, Jeroen KUIPERS, Michiel J. T. VAN EIJK, Peter C. VAN DER VLIET, and H. Th Marc TIMMERS. "The gene for human TATA-binding-protein-associated factor (TAFII) 170: structure, promoter and chromosomal localization." Biochemical Journal 345, no. 3 (January 25, 2000): 521–27. http://dx.doi.org/10.1042/bj3450521.
Повний текст джерелаBöttcher, P., and 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, no. 3 (March 1, 1987): 267–71. http://dx.doi.org/10.1515/znb-1987-0303.
Повний текст джерелаPROUX-GILLARDEAUX, Véronique, Thierry GALLI, Isabelle CALLEBAUT, Anatoly MIKHAILIK, Georges CALOTHY, and 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, no. 1 (February 15, 2003): 213–21. http://dx.doi.org/10.1042/bj20021309.
Повний текст джерелаJames, J. Anson, Carlos R. Escalante, Miran Yoon-Robarts, Thomas A. Edwards, R. Michael Linden, and Aneel K. Aggarwal. "Crystal Structure of the SF3 Helicase from Adeno-Associated Virus Type 2." Structure 11, no. 8 (August 2003): 1025–35. http://dx.doi.org/10.1016/s0969-2126(03)00152-7.
Повний текст джерелаBéguin, Pierre, Bruno Baron, Sukhvinder Gill, Nicole Charpin, and Patrick Forterre. "The SF1 helicase encoded by the archaeal plasmid pTN2 of Thermococcus nautili." Extremophiles 18, no. 4 (June 3, 2014): 779–87. http://dx.doi.org/10.1007/s00792-014-0658-5.
Повний текст джерелаFradet-Turcotte, Amélie, Cary Moody, Laimonis A. Laimins, and 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, no. 22 (September 15, 2010): 11747–60. http://dx.doi.org/10.1128/jvi.01445-10.
Повний текст джерелаPeled-Zehavi, Hadas, J. Andrew Berglund, Michael Rosbash, and 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, no. 15 (August 1, 2001): 5232–41. http://dx.doi.org/10.1128/mcb.21.15.5232-5241.2001.
Повний текст джерелаPaul, John H., Shannon J. Williamson, Amy Long, R. Nathan Authement, David John, Anca M. Segall, Forest L. Rohwer, Matthew Androlewicz та Stacey Patterson. "Complete Genome Sequence of φHSIC, a Pseudotemperate Marine Phage of Listonella pelagia". Applied and Environmental Microbiology 71, № 6 (червень 2005): 3311–20. http://dx.doi.org/10.1128/aem.71.6.3311-3320.2005.
Повний текст джерелаMüller, C., and 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, no. 12 (December 1, 1993): 1732–36. http://dx.doi.org/10.1515/znb-1993-1207.
Повний текст джерелаGargantini, Pablo R., Marianela C. Serradell, Alessandro Torri, and 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, no. 1 (2012): 284. http://dx.doi.org/10.1186/1471-2180-12-284.
Повний текст джерелаMüller, C., and 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, no. 1 (January 1, 1993): 90–92. http://dx.doi.org/10.1515/znb-1993-0120.
Повний текст джерелаZheng, Zheng, Minli Bao, Fengnian Wu, Christopher Van Horn, Jianchi Chen, and Xiaoling Deng. "A Type 3 Prophage of ‘Candidatus Liberibacter asiaticus’ Carrying a Restriction-Modification System." Phytopathology® 108, no. 4 (April 2018): 454–61. http://dx.doi.org/10.1094/phyto-08-17-0282-r.
Повний текст джерелаGeorge, Biju, Rajrani Ruhel, Mohit Mazumder, Veerendra Kumar Sharma, Swatantra Kumar Jain, Samudrala Gourinath та 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, № 7 (1 липня 2014): 1591–602. http://dx.doi.org/10.1099/vir.0.064923-0.
Повний текст джерелаVasilevskaya, Ekaterina Romanovna, and Anastasia Gennadievna Akhremko. "Proteomic study of pig’s spleen." Potravinarstvo Slovak Journal of Food Sciences 13, no. 1 (May 28, 2019): 314–17. http://dx.doi.org/10.5219/1093.
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