Статті в журналах з теми "RGG-motif Protein"
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Ознайомтеся з топ-44 статей у журналах для дослідження на тему "RGG-motif Protein".
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Bhatter, Nupur, Rajan Iyyappan, and Purusharth I. Rajyaguru. "Characterizing mutations in and genetic interactions of RGG-motif translation repressor Sbp1." Wellcome Open Research 3 (August 22, 2018): 102. http://dx.doi.org/10.12688/wellcomeopenres.14709.1.
Повний текст джерелаCorley, Susan M., and Jill E. Gready. "Identification of the RGG Box Motif in Shadoo: RNA-Binding and Signaling Roles?" Bioinformatics and Biology Insights 2 (January 2008): BBI.S1075. http://dx.doi.org/10.4137/bbi.s1075.
Повний текст джерелаYun, Chi Y., and 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, no. 4 (August 21, 2000): 707–18. http://dx.doi.org/10.1083/jcb.150.4.707.
Повний текст джерелаVasilyev, Nikita, Anna Polonskaia, Jennifer C. Darnell, Robert B. Darnell, Dinshaw J. Patel та 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, № 39 (15 вересня 2015): E5391—E5400. http://dx.doi.org/10.1073/pnas.1515737112.
Повний текст джерелаBhatter, Nupur, Rajan Iyyappan, Gayatri Mohanan, and 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 (September 17, 2021): 102. http://dx.doi.org/10.12688/wellcomeopenres.14709.3.
Повний текст джерелаWang, Yi-Chun, Shang-Hsuan Huang, Chien-Ping Chang, and Chuan Li. "Identification and Characterization of Glycine- and Arginine-Rich Motifs in Proteins by a Novel GAR Motif Finder Program." Genes 14, no. 2 (January 27, 2023): 330. http://dx.doi.org/10.3390/genes14020330.
Повний текст джерелаKrüger, Timothy, Mario Hofweber, and 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, no. 13 (July 2013): 2098–111. http://dx.doi.org/10.1091/mbc.e13-01-0068.
Повний текст джерелаBhatter, Nupur, Rajan Iyyappan, and 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 (February 6, 2020): 102. http://dx.doi.org/10.12688/wellcomeopenres.14709.2.
Повний текст джерелаKoukiali, Anastasia, Makrina Daniilidou, Ilias Mylonis, Thomas Giannakouros, and Eleni Nikolakaki. "SR Protein Kinase 1 Inhibition by TAF15." Cells 12, no. 1 (December 28, 2022): 126. http://dx.doi.org/10.3390/cells12010126.
Повний текст джерелаPoornima, Gopalakrishna, Ravishankar Mythili, Priyabrata Nag, Sabnam Parbin, Praveen Kumar Verma, Tanweer Hussain, and Purusharth I. Rajyaguru. "RGG-motif self-association regulates eIF4G-binding translation repressor protein Scd6." RNA Biology 16, no. 9 (June 12, 2019): 1215–27. http://dx.doi.org/10.1080/15476286.2019.1621623.
Повний текст джерелаCorbin-Lickfett, Kara A., Stuart K. Souki, Melanie J. Cocco, and 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, no. 13 (April 21, 2010): 6367–76. http://dx.doi.org/10.1128/jvi.00509-10.
Повний текст джерелаRuiz-Jarabo, Carmen M., Noemí Sevilla, Mercedes Dávila, Gema Gómez-Mariano, Eric Baranowski, and Esteban Domingo. "Antigenic properties and population stability of a foot-and-mouth disease virus with an altered Arg-Gly-Asp receptor-recognition motif." Journal of General Virology 80, no. 8 (August 1, 1999): 1899–909. http://dx.doi.org/10.1099/0022-1317-80-8-1899.
Повний текст джерелаBoulila, Younes, Stanislas Tomavo, and Mathieu Gissot. "A RGG motif protein is involved in Toxoplasma gondii stress-mediated response." Molecular and Biochemical Parasitology 196, no. 1 (August 2014): 1–8. http://dx.doi.org/10.1016/j.molbiopara.2014.07.009.
Повний текст джерелаSiomi, H., and G. Dreyfuss. "A nuclear localization domain in the hnRNP A1 protein." Journal of Cell Biology 129, no. 3 (May 1, 1995): 551–60. http://dx.doi.org/10.1083/jcb.129.3.551.
Повний текст джерелаYin, Ziwei, Maki Kobayashi, Wenjun Hu, Koichi Higashi, Nasim A. Begum, Ken Kurokawa, and Tasuku Honjo. "RNA-binding motifs of hnRNP K are critical for induction of antibody diversification by activation-induced cytidine deaminase." Proceedings of the National Academy of Sciences 117, no. 21 (May 8, 2020): 11624–35. http://dx.doi.org/10.1073/pnas.1921115117.
Повний текст джерелаHuang, Zhou-Li, Jing Dai, Wen-Hua Luo, Xiang-Gui Wang, Jia-Heng Tan, Shuo-Bin Chen, and Zhi-Shu Huang. "Identification of G-Quadruplex-Binding Protein from the Exploration of RGG Motif/G-Quadruplex Interactions." Journal of the American Chemical Society 140, no. 51 (December 5, 2018): 17945–55. http://dx.doi.org/10.1021/jacs.8b09329.
Повний текст джерелаVolná, Adriana, Martin Bartas, Jakub Nezval, Vladimír Špunda, Petr Pečinka, and Jiří Červeň. "Searching for G-Quadruplex-Binding Proteins in Plants: New Insight into Possible G-Quadruplex Regulation." BioTech 10, no. 4 (September 22, 2021): 20. http://dx.doi.org/10.3390/biotech10040020.
Повний текст джерелаAnderson, J. T., S. M. Wilson, K. V. Datar, and M. S. Swanson. "NAB2: a yeast nuclear polyadenylated RNA-binding protein essential for cell viability." Molecular and Cellular Biology 13, no. 5 (May 1993): 2730–41. http://dx.doi.org/10.1128/mcb.13.5.2730-2741.1993.
Повний текст джерелаAnderson, J. T., S. M. Wilson, K. V. Datar, and M. S. Swanson. "NAB2: a yeast nuclear polyadenylated RNA-binding protein essential for cell viability." Molecular and Cellular Biology 13, no. 5 (May 1993): 2730–41. http://dx.doi.org/10.1128/mcb.13.5.2730.
Повний текст джерелаIacovides, Demetris C., Clodagh C. O'Shea, Juan Oses-Prieto, Alma Burlingame, and Frank McCormick. "Critical Role for Arginine Methylation in Adenovirus-Infected Cells." Journal of Virology 81, no. 23 (August 8, 2007): 13209–17. http://dx.doi.org/10.1128/jvi.01415-06.
Повний текст джерелаLiu, Q., and G. Dreyfuss. "In vivo and in vitro arginine methylation of RNA-binding proteins." Molecular and Cellular Biology 15, no. 5 (May 1995): 2800–2808. http://dx.doi.org/10.1128/mcb.15.5.2800.
Повний текст джерелаSolomon, Samuel, Yaoxian Xu, Bin Wang, Muriel D. David, Peter Schubert, Derek Kennedy та 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, № 6 (8 січня 2007): 2324–42. http://dx.doi.org/10.1128/mcb.02300-06.
Повний текст джерелаFreischmidt, 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, no. 4 (April 1, 2021): 1214–29. http://dx.doi.org/10.1093/brain/awab018.
Повний текст джерелаYan, Qiuxia, Peng Zeng, Xiuqin Zhou, Xiaoying Zhao, Runqiang Chen, Jing Qiao, Ling Feng, Zhenjie Zhu, Guozhi Zhang, and Cairong Chen. "RBMX suppresses tumorigenicity and progression of bladder cancer by interacting with the hnRNP A1 protein to regulate PKM alternative splicing." Oncogene 40, no. 15 (February 9, 2021): 2635–50. http://dx.doi.org/10.1038/s41388-021-01666-z.
Повний текст джерелаLorković, Z. J., R. G. Herrmann, and R. Oelmüller. "PRH75, a new nucleus-localized member of the DEAD-box protein family from higher plants." Molecular and Cellular Biology 17, no. 4 (April 1997): 2257–65. http://dx.doi.org/10.1128/mcb.17.4.2257.
Повний текст джерелаMears, W. E., and S. A. Rice. "The RGG box motif of the herpes simplex virus ICP27 protein mediates an RNA-binding activity and determines in vivo methylation." Journal of virology 70, no. 11 (1996): 7445–53. http://dx.doi.org/10.1128/jvi.70.11.7445-7453.1996.
Повний текст джерелаNakamoto, Meagan Y., Nickolaus C. Lammer, Robert T. Batey, and Deborah S. Wuttke. "hnRNPK recognition of the B motif of Xist and other biological RNAs." Nucleic Acids Research 48, no. 16 (August 19, 2020): 9320–35. http://dx.doi.org/10.1093/nar/gkaa677.
Повний текст джерелаZinszner, H., J. Sok, D. Immanuel, Y. Yin, and D. Ron. "TLS (FUS) binds RNA in vivo and engages in nucleo-cytoplasmic shuttling." Journal of Cell Science 110, no. 15 (August 1, 1997): 1741–50. http://dx.doi.org/10.1242/jcs.110.15.1741.
Повний текст джерелаJenning, 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, no. 9 (June 12, 2020): 1194–202. http://dx.doi.org/10.1136/annrheumdis-2019-216919.
Повний текст джерелаSoliman, Tarik M., and Saul J. Silverstein. "Identification of an Export Control Sequence and a Requirement for the KH Domains in ICP27 from Herpes Simplex Virus Type 1." Journal of Virology 74, no. 16 (August 15, 2000): 7600–7609. http://dx.doi.org/10.1128/jvi.74.16.7600-7609.2000.
Повний текст джерелаRajyaguru, Purusharth, and Roy Parker. "RGG motif proteins: Modulators of mRNA functional states." Cell Cycle 11, no. 14 (January 15, 2012): 2594–99. http://dx.doi.org/10.4161/cc.20716.
Повний текст джерелаChaussee, Michael S., Gail L. Sylva, Daniel E. Sturdevant, Laura M. Smoot, Morag R. Graham, Robert O. Watson, and James M. Musser. "Rgg Influences the Expression of Multiple Regulatory Loci To Coregulate Virulence Factor Expression in Streptococcus pyogenes." Infection and Immunity 70, no. 2 (February 2002): 762–70. http://dx.doi.org/10.1128/iai.70.2.762-770.2002.
Повний текст джерелаRajyaguru, Purusharth, Meipei She, and Roy Parker. "Scd6 Targets eIF4G to Repress Translation: RGG Motif Proteins as a Class of eIF4G-Binding Proteins." Molecular Cell 45, no. 2 (January 2012): 244–54. http://dx.doi.org/10.1016/j.molcel.2011.11.026.
Повний текст джерелаDammer, 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, no. 6 (June 21, 2012): e38658. http://dx.doi.org/10.1371/journal.pone.0038658.
Повний текст джерелаRoy, Raju, Gitartha Das, Ishwarya Achappa Kuttanda, Nupur Bhatter, and Purusharth I. Rajyaguru. "Low complexity RGG-motif sequence is required for Processing body (P-body) disassembly." Nature Communications 13, no. 1 (April 19, 2022). http://dx.doi.org/10.1038/s41467-022-29715-5.
Повний текст джерелаTunnicliffe, Richard B., William K. Hu, Michele Y. Wu, Colin Levy, A. Paul Mould, Edward A. McKenzie, Rozanne M. Sandri-Goldin, and Alexander P. Golovanov. "Molecular Mechanism of SR Protein Kinase 1 Inhibition by the Herpes Virus Protein ICP27." mBio 10, no. 5 (October 22, 2019). http://dx.doi.org/10.1128/mbio.02551-19.
Повний текст джерелаBonucci, A., M. G. Murrali, L. Banci, and 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, no. 1 (December 2020). http://dx.doi.org/10.1038/s41598-020-77899-x.
Повний текст джерелаde Vries, Tebbe, William Martelly, Sébastien Campagne, Kevin Sabath, Chris P. Sarnowski, Jason Wong, Alexander Leitner, Stefanie Jonas, Shalini Sharma, and 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, no. 6 (January 31, 2022). http://dx.doi.org/10.1073/pnas.2114092119.
Повний текст джерелаJohansson, Josefin, Sarah Lidéus, Carina Frykholm, Cecilia Gunnarsson, Filip Mihalic, Sanna Gudmundsson, Sara Ekvall, et al. "Gustavson syndrome is caused by an in-frame deletion in RBMX associated with potentially disturbed SH3 domain interactions." European Journal of Human Genetics, June 5, 2023. http://dx.doi.org/10.1038/s41431-023-01392-y.
Повний текст джерелаVishal, Sonali S., Denethi Wijegunawardana, Muthu Raj Salaikumaran, and Pallavi P. Gopal. "Sequence Determinants of TDP-43 Ribonucleoprotein Condensate Formation and Axonal Transport in Neurons." Frontiers in Cell and Developmental Biology 10 (May 12, 2022). http://dx.doi.org/10.3389/fcell.2022.876893.
Повний текст джерелаWu, Shan, Boon Heng Dennis Teo, Seng Yin Kelly Wee, Junjie Chen, and Jinhua Lu. "The GAR/RGG motif defines a family of nuclear alarmins." Cell Death & Disease 12, no. 5 (May 2021). http://dx.doi.org/10.1038/s41419-021-03766-w.
Повний текст джерелаGarg, Mani, Debadrita Roy, and 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, July 2022, 119327. http://dx.doi.org/10.1016/j.bbamcr.2022.119327.
Повний текст джерелаKedersha, 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, no. 7 (March 28, 2016). http://dx.doi.org/10.1083/jcb.201508028.
Повний текст джерелаThandapani, 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 (August 12, 2015). http://dx.doi.org/10.7554/elife.06234.
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