Artículos de revistas sobre el tema "RGG-motif Proteins"
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Rajyaguru, Purusharth y Roy Parker. "RGG motif proteins: Modulators of mRNA functional states". Cell Cycle 11, n.º 14 (15 de enero de 2012): 2594–99. http://dx.doi.org/10.4161/cc.20716.
Texto completoWang, Yi-Chun, Shang-Hsuan Huang, Chien-Ping Chang y Chuan Li. "Identification and Characterization of Glycine- and Arginine-Rich Motifs in Proteins by a Novel GAR Motif Finder Program". Genes 14, n.º 2 (27 de enero de 2023): 330. http://dx.doi.org/10.3390/genes14020330.
Texto completoCorley, Susan M. y Jill E. Gready. "Identification of the RGG Box Motif in Shadoo: RNA-Binding and Signaling Roles?" Bioinformatics and Biology Insights 2 (enero de 2008): BBI.S1075. http://dx.doi.org/10.4137/bbi.s1075.
Texto completoChaussee, Michael S., Gail L. Sylva, Daniel E. Sturdevant, Laura M. Smoot, Morag R. Graham, Robert O. Watson y James M. Musser. "Rgg Influences the Expression of Multiple Regulatory Loci To Coregulate Virulence Factor Expression in Streptococcus pyogenes". Infection and Immunity 70, n.º 2 (febrero de 2002): 762–70. http://dx.doi.org/10.1128/iai.70.2.762-770.2002.
Texto completoVasilyev, Nikita, Anna Polonskaia, Jennifer C. Darnell, Robert B. Darnell, Dinshaw J. Patel y Alexander Serganov. "Crystal structure reveals specific recognition of a G-quadruplex RNA by a β-turn in the RGG motif of FMRP". Proceedings of the National Academy of Sciences 112, n.º 39 (15 de septiembre de 2015): E5391—E5400. http://dx.doi.org/10.1073/pnas.1515737112.
Texto completoYun, Chi Y. y Xiang-Dong Fu. "Conserved Sr Protein Kinase Functions in Nuclear Import and Its Action Is Counteracted by Arginine Methylation in Saccharomyces cerevisiae". Journal of Cell Biology 150, n.º 4 (21 de agosto de 2000): 707–18. http://dx.doi.org/10.1083/jcb.150.4.707.
Texto completoKrüger, Timothy, Mario Hofweber y Susanne Kramer. "SCD6 induces ribonucleoprotein granule formation in trypanosomes in a translation-independent manner, regulated by its Lsm and RGG domains". Molecular Biology of the Cell 24, n.º 13 (julio de 2013): 2098–111. http://dx.doi.org/10.1091/mbc.e13-01-0068.
Texto completoBhatter, Nupur, Rajan Iyyappan, Gayatri Mohanan y Purusharth I. Rajyaguru. "Exploring the role of RRM domains and conserved aromatic residues in RGG motif of eIF4G-binding translation repressor protein Sbp1". Wellcome Open Research 3 (17 de septiembre de 2021): 102. http://dx.doi.org/10.12688/wellcomeopenres.14709.3.
Texto completoKoukiali, Anastasia, Makrina Daniilidou, Ilias Mylonis, Thomas Giannakouros y Eleni Nikolakaki. "SR Protein Kinase 1 Inhibition by TAF15". Cells 12, n.º 1 (28 de diciembre de 2022): 126. http://dx.doi.org/10.3390/cells12010126.
Texto completoRajyaguru, Purusharth, Meipei She y Roy Parker. "Scd6 Targets eIF4G to Repress Translation: RGG Motif Proteins as a Class of eIF4G-Binding Proteins". Molecular Cell 45, n.º 2 (enero de 2012): 244–54. http://dx.doi.org/10.1016/j.molcel.2011.11.026.
Texto completoCorbin-Lickfett, Kara A., Stuart K. Souki, Melanie J. Cocco y Rozanne M. Sandri-Goldin. "Three Arginine Residues within the RGG Box Are Crucial for ICP27 Binding to Herpes Simplex Virus 1 GC-Rich Sequences and for Efficient Viral RNA Export". Journal of Virology 84, n.º 13 (21 de abril de 2010): 6367–76. http://dx.doi.org/10.1128/jvi.00509-10.
Texto completoSiomi, H. y G. Dreyfuss. "A nuclear localization domain in the hnRNP A1 protein." Journal of Cell Biology 129, n.º 3 (1 de mayo de 1995): 551–60. http://dx.doi.org/10.1083/jcb.129.3.551.
Texto completoVolná, Adriana, Martin Bartas, Jakub Nezval, Vladimír Špunda, Petr Pečinka y Jiří Červeň. "Searching for G-Quadruplex-Binding Proteins in Plants: New Insight into Possible G-Quadruplex Regulation". BioTech 10, n.º 4 (22 de septiembre de 2021): 20. http://dx.doi.org/10.3390/biotech10040020.
Texto completoAnderson, J. T., S. M. Wilson, K. V. Datar y M. S. Swanson. "NAB2: a yeast nuclear polyadenylated RNA-binding protein essential for cell viability". Molecular and Cellular Biology 13, n.º 5 (mayo de 1993): 2730–41. http://dx.doi.org/10.1128/mcb.13.5.2730-2741.1993.
Texto completoAnderson, J. T., S. M. Wilson, K. V. Datar y M. S. Swanson. "NAB2: a yeast nuclear polyadenylated RNA-binding protein essential for cell viability." Molecular and Cellular Biology 13, n.º 5 (mayo de 1993): 2730–41. http://dx.doi.org/10.1128/mcb.13.5.2730.
Texto completoLiu, Q. y G. Dreyfuss. "In vivo and in vitro arginine methylation of RNA-binding proteins." Molecular and Cellular Biology 15, n.º 5 (mayo de 1995): 2800–2808. http://dx.doi.org/10.1128/mcb.15.5.2800.
Texto completoIacovides, Demetris C., Clodagh C. O'Shea, Juan Oses-Prieto, Alma Burlingame y Frank McCormick. "Critical Role for Arginine Methylation in Adenovirus-Infected Cells". Journal of Virology 81, n.º 23 (8 de agosto de 2007): 13209–17. http://dx.doi.org/10.1128/jvi.01415-06.
Texto completoSolomon, Samuel, Yaoxian Xu, Bin Wang, Muriel D. David, Peter Schubert, Derek Kennedy y John W. Schrader. "Distinct Structural Features ofCaprin-1 Mediate Its Interaction with G3BP-1 and Its Induction of Phosphorylation of Eukaryotic Translation InitiationFactor 2α, Entry to Cytoplasmic Stress Granules, and Selective Interaction with a Subset of mRNAs". Molecular and Cellular Biology 27, n.º 6 (8 de enero de 2007): 2324–42. http://dx.doi.org/10.1128/mcb.02300-06.
Texto completoLorković, Z. J., R. G. Herrmann y R. Oelmüller. "PRH75, a new nucleus-localized member of the DEAD-box protein family from higher plants." Molecular and Cellular Biology 17, n.º 4 (abril de 1997): 2257–65. http://dx.doi.org/10.1128/mcb.17.4.2257.
Texto completoDammer, Eric B., Claudia Fallini, Yair M. Gozal, Duc M. Duong, Wilfried Rossoll, Ping Xu, James J. Lah et al. "Coaggregation of RNA-Binding Proteins in a Model of TDP-43 Proteinopathy with Selective RGG Motif Methylation and a Role for RRM1 Ubiquitination". PLoS ONE 7, n.º 6 (21 de junio de 2012): e38658. http://dx.doi.org/10.1371/journal.pone.0038658.
Texto completoFreischmidt, Axel, Anand Goswami, Katharina Limm, Vitaly L. Zimyanin, Maria Demestre, Hannes Glaß, Karlheinz Holzmann et al. "A serum microRNA sequence reveals fragile X protein pathology in amyotrophic lateral sclerosis". Brain 144, n.º 4 (1 de abril de 2021): 1214–29. http://dx.doi.org/10.1093/brain/awab018.
Texto completoZinszner, H., J. Sok, D. Immanuel, Y. Yin y D. Ron. "TLS (FUS) binds RNA in vivo and engages in nucleo-cytoplasmic shuttling". Journal of Cell Science 110, n.º 15 (1 de agosto de 1997): 1741–50. http://dx.doi.org/10.1242/jcs.110.15.1741.
Texto completoJenning, Madeleine, Bianka Marklein, Jimmy Ytterberg, Roman A. Zubarev, Vijay Joshua, Dirkjan van Schaardenburg, Lotte van de Stadt et al. "Bacterial citrullinated epitopes generated by Porphyromonas gingivalis infection—a missing link for ACPA production". Annals of the Rheumatic Diseases 79, n.º 9 (12 de junio de 2020): 1194–202. http://dx.doi.org/10.1136/annrheumdis-2019-216919.
Texto completoNakamoto, Meagan Y., Nickolaus C. Lammer, Robert T. Batey y Deborah S. Wuttke. "hnRNPK recognition of the B motif of Xist and other biological RNAs". Nucleic Acids Research 48, n.º 16 (19 de agosto de 2020): 9320–35. http://dx.doi.org/10.1093/nar/gkaa677.
Texto completoWu, Shan, Boon Heng Dennis Teo, Seng Yin Kelly Wee, Junjie Chen y Jinhua Lu. "The GAR/RGG motif defines a family of nuclear alarmins". Cell Death & Disease 12, n.º 5 (mayo de 2021). http://dx.doi.org/10.1038/s41419-021-03766-w.
Texto completoRoy, Raju, Gitartha Das, Ishwarya Achappa Kuttanda, Nupur Bhatter y Purusharth I. Rajyaguru. "Low complexity RGG-motif sequence is required for Processing body (P-body) disassembly". Nature Communications 13, n.º 1 (19 de abril de 2022). http://dx.doi.org/10.1038/s41467-022-29715-5.
Texto completoBonucci, A., M. G. Murrali, L. Banci y R. Pierattelli. "A combined NMR and EPR investigation on the effect of the disordered RGG regions in the structure and the activity of the RRM domain of FUS". Scientific Reports 10, n.º 1 (diciembre de 2020). http://dx.doi.org/10.1038/s41598-020-77899-x.
Texto completoTunnicliffe, Richard B., William K. Hu, Michele Y. Wu, Colin Levy, A. Paul Mould, Edward A. McKenzie, Rozanne M. Sandri-Goldin y Alexander P. Golovanov. "Molecular Mechanism of SR Protein Kinase 1 Inhibition by the Herpes Virus Protein ICP27". mBio 10, n.º 5 (22 de octubre de 2019). http://dx.doi.org/10.1128/mbio.02551-19.
Texto completode Vries, Tebbe, William Martelly, Sébastien Campagne, Kevin Sabath, Chris P. Sarnowski, Jason Wong, Alexander Leitner, Stefanie Jonas, Shalini Sharma y Frédéric H. T. Allain. "Sequence-specific RNA recognition by an RGG motif connects U1 and U2 snRNP for spliceosome assembly". Proceedings of the National Academy of Sciences 119, n.º 6 (31 de enero de 2022). http://dx.doi.org/10.1073/pnas.2114092119.
Texto completoGarg, Mani, Debadrita Roy y Purusharth I. Rajyaguru. "Low complexity RGG-motif containing proteins Scd6 and Psp2 act as suppressors of clathrin heavy chain deficiency". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, julio de 2022, 119327. http://dx.doi.org/10.1016/j.bbamcr.2022.119327.
Texto completoKedersha, Nancy, Marc D. Panas, Christopher A. Achorn, Shawn Lyons, Sarah Tisdale, Tyler Hickman, Marshall Thomas et al. "G3BP–Caprin1–USP10 complexes mediate stress granule condensation and associate with 40S subunits". Journal of Cell Biology 212, n.º 7 (28 de marzo de 2016). http://dx.doi.org/10.1083/jcb.201508028.
Texto completoThandapani, Palaniraja, Jingwen Song, Valentina Gandin, Yutian Cai, Samuel G. Rouleau, Jean-Michel Garant, Francois-Michel Boisvert et al. "Aven recognition of RNA G-quadruplexes regulates translation of the mixed lineage leukemia protooncogenes". eLife 4 (12 de agosto de 2015). http://dx.doi.org/10.7554/elife.06234.
Texto completoVishal, Sonali S., Denethi Wijegunawardana, Muthu Raj Salaikumaran y Pallavi P. Gopal. "Sequence Determinants of TDP-43 Ribonucleoprotein Condensate Formation and Axonal Transport in Neurons". Frontiers in Cell and Developmental Biology 10 (12 de mayo de 2022). http://dx.doi.org/10.3389/fcell.2022.876893.
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