A Combinatorial Regulatory Platform Determines Expression of RNA Polymerase III Subunit RPC7α (<i>POLR3G</i>) in Cancer by Ruiying Cheng, Sihang Zhou, Rajendra K C, Simon Lizarazo, Leela Mouli, Anshita Jayanth, Qing Liu, Kevin Van Bortle

“…RNA polymerase III (Pol III) subunit RPC7α, which is encoded by <i>POLR3G</i> in humans, has been linked to both tumor growth and metastasis. …”
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Human RNA polymerase II-association factor 1 (hPaf1/PD2) regulates histone methylation and chromatin remodeling in pancreatic cancer. by Parama Dey, Moorthy P Ponnusamy, Shonali Deb, Surinder K Batra

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Pharmacophore-Model-Based Drug Repurposing for the Identification of the Potential Inhibitors Targeting the Allosteric Site in Dengue Virus NS5 RNA-Dependent RNA Polymerase by Sanjay Kumar, Leena H. Bajrai, Arwa A. Faizo, Aiah M. Khateb, Areej A. Alkhaldy, Rashmi Rana, Esam I. Azhar, Vivek Dhar Dwivedi

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AATF/Che-1 RNA polymerase II binding protein overexpression reduces the anti-tumor NK-cell cytotoxicity through activating receptors modulation by Matteo Caforio, Nicola Tumino, Cristina Sorino, Isabella Manni, Stefano Di Giovenale, Giulia Piaggio, Simona Iezzi, Georgios Strimpakos, Elisabetta Mattei, Lorenzo Moretta, M. Fanciulli, Paola Vacca, Franco Locatelli, Franco Locatelli, Valentina Folgiero

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qSR: a quantitative super-resolution analysis tool reveals the cell-cycle dependent organization of RNA Polymerase I in live human cells by Andrews, James Owen, Conway, W., Cho, Won-ki, Narayanan, Arjun, Spille, Jan Hendrik, Jayanth, Namrata, Inoue, Takuma, Thaler, Jesse, Cisse, Ibrahim I, Mullen, Susan

“…First, we illustrate qSR using a sample live cell data of RNA Polymerase II (Pol II) as an example of highly dynamic sub-diffractive clusters. …”
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A Purified Adenovirus 289-Amino-Acid ElA Protein Activates RNA Polymerase III Transcription In Vitro and Alters Transcription Factor TFIIIC by HARTER, MARIAN L., WANG, DUEN-MEI, SOONG, CHU-JING, DATTA, SHOUMEN

Subjects: “…Transcription, E1A, Adenovirus, in vitro assay, RNA polymerase, transcription factor, TFIIIC…”
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Chikungunya virus nsP4 RNA-dependent RNA polymerase core domain displays detergent-sensitive primer extension and terminal adenylyltransferase activities by Chen, Ming Wei, Tan, Yaw Bia, Zheng, Jie, Zhao, Yongqian, Lim, Bee Ting, Cornvik, Tobias, Lescar, Julien, Ng, Lisa Fong Poh, Luo, Dahai

“…The viral enzyme non-structural protein 4 (nsP4), as RNA-dependent RNA polymerase (RdRP), catalyzes the formation of negative-sense, genomic and subgenomic viral RNAs. …”
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Quantitation of RNA polymerase II and its transcription factors in an HeLa cell: little soluble holoenzyme but significant amounts of polymerases attached to the nuclear substructure. by Kimura, H, Tao, Y, Roeder, R, Cook, P

“…Various complexes that contain the core subunits of RNA polymerase II associated with different transcription factors have been isolated from eukaryotes; their precise molecular constitution depends on the purification procedure. …”

Nuclear IGF1R interacts with regulatory regions of chromatin to promote RNA Polymerase II recruitment and gene expression associated with advanced tumor stage by Aleksic, T, Gray, N, Wu, X, Rieunier, G, Osher, E, Mills, J, Verrill, C, Bryant, R, Han, C, Hutchinson, K, Lambert, A, Kumar, R, Hamdy, F, Weyer-Czernilofsky, U, Sanderson, M, Bogenrieder, T, Taylor, S, Macaulay, V

“…Using ChIP-seq to assess global chromatin occupancy, we identified IGF1R-binding sites at or near transcription start sites of genes including JUN and FAM21, most sites coinciding with occupancy by RNA polymerase II (RNAPol2) and histone marks of active enhancers/promoters. …”

RNA-free and ribonucleoprotein-associated influenza virus polymerases directly bind the serine-5 phosphorylated carboxyl-terminal domain of host RNA polymerase II by Fodor, E, Hengrung, N, Martinez-Alonso, M

“…Ongoing transcription by cellular RNA polymerase II (Pol II) is required for viral mRNA synthesis. …”

The SARS-coronavirus nsp7+nsp8 complex is a unique multimeric RNA polymerase capable of both de novo initiation and primer extension. by te Velthuis, A, van den Worm, S, Snijder, E

“…Uniquely among RNA viruses, replication of the ~30-kb SARS-coronavirus genome is believed to involve two RNA-dependent RNA polymerase (RdRp) activities. The first is primer-dependent and associated with the 106-kDa non-structural protein 12 (nsp12), whereas the second is catalysed by the 22-kDa nsp8. …”

Noncatalytic ions direct the RNA-dependent RNA polymerase of bacterial double-stranded RNA virus ϕ6 from de novo initiation to elongation. by Wright, S, Poranen, M, Bamford, D, Stuart, D, Grimes, J

“…RNA-dependent RNA polymerases (RdRps) are key to the replication of RNA viruses. …”

Footprints of a trypanosomatid RNA world: pre-small subunit rRNA processing by spliced leader addition trans-splicing by Mario Gustavo Mayer, Marcos Gonzaga dos Santos, Maria Fernanda Laranjeira da Silva, Lucile Maria Floeter-Winter

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The IQA Energy Partition in a Drug Design Setting: A Hepatitis C Virus RNA-Dependent RNA Polymerase (NS5B) Case Study by César A. Zapata-Acevedo, Paul L. A. Popelier

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Identification of novel SARS-CoV-2 RNA dependent RNA polymerase (RdRp) inhibitors: From in silico screening to experimentally validated inhibitory activity by Tanaporn Uengwetwanit, Nopporn Chutiwitoonchai, Kanin Wichapong, Nitsara Karoonuthaisiri

“…Due to its vital role in viral replication, RNA-dependent RNA polymerase (RdRp) is a promising therapeutic target. …”
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The F-Actin-Binding MPRIP Forms Phase-Separated Condensates and Associates with PI(4,5)P2 and Active RNA Polymerase II in the Cell Nucleus by Can Balaban, Martin Sztacho, Michaela Blažíková, Pavel Hozák

“…We identified MPRIP as a component of RNA Polymerase II/Nuclear Myosin 1 complex and showed that MPRIP forms phase-separated condensates which are able to bind nuclear F-actin fibers. …”
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Remdesivir Strongly Binds to RNA-Dependent RNA Polymerase, Membrane Protein, and Main Protease of SARS-CoV-2: Indication From Molecular Modeling and Simulations by Faez Iqbal Khan, Tongzhou Kang, Haider Ali, Dakun Lai

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Loss of RNA-dependent RNA polymerase 2 (RDR2) function causes widespread and unexpected changes in the expression of transposons, genes, and 24-nt small RNAs. by Yi Jia, Damon R Lisch, Kazuhiro Ohtsu, Michael J Scanlon, Daniel Nettleton, Patrick S Schnable

“…Transposable elements (TEs) comprise a substantial portion of many eukaryotic genomes and are typically transcriptionally silenced. RNA-dependent RNA polymerase 2 (RDR2) is a component of the RNA-directed DNA methylation (RdDM) silencing pathway. …”
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Epstein-Barr virus-encoded EBNA1 enhances RNA polymerase III-dependent EBER expression through induction of EBER-associated cellular transcription factors by Owen Thomas J, O'Neil John D, Dawson Christopher W, Hu Chunfang, Chen Xiaoyi, Yao Yunhong, Wood Victoria HJ, Mitchell Louise E, White Robert J, Young Lawrence S, Arrand John R

“…<p>Abstract</p> <p>Background</p> <p>Epstein-Barr Virus (EBV)-encoded RNAs (EBERs) are non-polyadenylated RNA molecules transcribed from the EBV genome by RNA polymerase III (pol III). EBERs are the most abundant viral latent gene products, although the precise mechanisms by which EBV is able to achieve such high levels of EBER expression are not fully understood. …”
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Identification of 6ω-cyclohexyl-2-(phenylamino carbonylmethylthio)pyrimidin-4(3H)-ones targeting the ZIKV NS5 RNA dependent RNA polymerase by Guang-Feng Zhou, Guang-Feng Zhou, Cong-Qiang Xie, Jian-Xia Xue, Jian-Xia Xue, Jing-Bo Wang, Yu-Zhuo Yang, Chang-Bo Zheng, Rong-Hua Luo, Ren-Hua Yang, Wen Chen, Liu-Meng Yang, Yue-Ping Wang, Hong-Bin Zhang, Yan-Ping He, Yong-Tang Zheng

“…Here, we discovered 4w targeted on the ZIKV NS5 RNA -dependent RNA polymerase (RdRp), which exhibited good in vitro antiviral activity without cell species specificity, both at the protein level and at the RNA level can significantly inhibit ZIKV replication. …”
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