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Coupling mRNA processing with transcription in time and space
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Maturation of mRNA precursors often occurs simultaneously with their synthesis by RNA polymerase II (Pol II). The co-transcriptional nature of mRNA processing has permitted the evolution of coupling mechanisms that coordinate transcription with mRNA capping, splicing, editing and 3' end formation. Recent experiments using sophisticated new methods for analysis of nascent RNA have provided important insights into the relative amount of co-transcriptional and post-transcriptional processing, the relationship between mRNA elongation and processing, and the role of the Pol II carboxy-terminal domain (CTD) in regulating these processes.
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“In addition, these different pre‐mRNA processing steps are functionally coupled to transcription. Indeed, all these steps are initiated co‐transcriptionally, thereby allowing the connection of transcription with mRNA maturation in time and space (Bentley, 2014).”
From RNA polymerase II speed: a key player in controlling and adapting transcriptome composition (2021) · cites this paper as Bentley, 2014
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Cites
Expansion of the eukaryotic proteome by alternative splicing
Nilsen, T. W., & Graveley, B. R. (2010) · Nature · doi:10.1038/nature08909 · Cited by 2,270
Nascent RNA Sequencing Reveals Widespread Pausing and Divergent Initiation at Human Promoters
Core, L. J., Waterfall, J. J., & Lis, J. T. (2008) · Science · doi:10.1126/science.1162228 · Cited by 1,986
Mayr, C., & Bartel, D. P. (2009) · Cell · doi:10.1016/j.cell.2009.06.016 · Cited by 1,613
Structural Basis of Transcription: RNA Polymerase II at 2.8 Ångstrom Resolution
Cramer, P., Bushnell, D. A., & Kornberg, R. D. (2001) · Science · doi:10.1126/science.1059493 · Cited by 1,247
Regulation of Alternative Splicing by Histone Modifications
Luco, R. F., Pan, Q., Tominaga, K., Blencowe, B. J., Pereira‐Smith, O. M., & Misteli, T. (2010) · Science · doi:10.1126/science.1184208 · Cited by 1,099
Komarnitsky, P. B., Cho, E., & Buratowski, S. (2000) · Genes & Development · doi:10.1101/gad.824700 · Cited by 1,098
R Loops: From Transcription Byproducts to Threats to Genome Stability
Aguilera, A., & García‐Muse, T. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.04.009 · Cited by 1,029
DNA sequence required for efficient transcription termination in yeast
Zaret, K. S., & Sherman, F. (1982) · Cell · doi:10.1016/0092-8674(82)90211-2 · Cited by 988
CTCF-promoted RNA polymerase II pausing links DNA methylation to splicing
Shukla, S., Kavak, E., Gregory, M., Imashimizu, M., Shutinoski, B., Kashlev, M., Oberdoerffer, P., Sandberg, R., & Oberdoerffer, S. (2011) · Nature · doi:10.1038/nature10442 · Cited by 973
The C-terminal domain of RNA polymerase II couples mRNA processing to transcription
McCracken, S. A., Fong, N., Yankulov, K., Ballantyne, S. M., Pan, G., Greenblatt, J., Patterson, S. D., Wickens, M., & Bentley, D. L. (1997) · Nature · doi:10.1038/385357a0 · Cited by 925
Self-citationPrecise Maps of RNA Polymerase Reveal How Promoters Direct Initiation and Pausing
Kwak, H., Fuda, N. J., Core, L. J., & Lis, J. T. (2013) · Science · doi:10.1126/science.1229386 · Cited by 849
Nascent transcript sequencing visualizes transcription at nucleotide resolution
Churchman, L. S., & Weissman, J. S. (2011) · Nature · doi:10.1038/nature09652 · Cited by 823
Progression through the RNA Polymerase II CTD Cycle
Buratowski, S. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.10.019 · Cited by 777
RNA processing and its regulation: global insights into biological networks
Licatalosi, D. D., & Darnell, R. B. (2009) · Nature Reviews Genetics · doi:10.1038/nrg2673 · Cited by 777
Mechanisms and Consequences of Alternative Polyadenylation
Di Giammartino, D. C., Nishida, K., & Manley, J. L. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.08.017 · Cited by 737
The RNA polymerase II CTD coordinates transcription and RNA processingPreprint
Hsin, J.-P., & Manley, J. L. (2012) · Genes & Development · doi:10.1101/gad.200303.112 · Cited by 728
Differential chromatin marking of introns and expressed exons by H3K36me3
Kolasinska-Zwierz, P., Down, T. A., Latorre, I. J., Liu, T., Liu, X. S., & Ahringer, J. (2009) · Nature Genetics · doi:10.1038/ng.322 · Cited by 699
A Slow RNA Polymerase II Affects Alternative Splicing In Vivo
de la Mata, M., Alonso, C. R., Kadener, S., Fededa, J. P., Blaustein, M., Pelisch, F., Cramer, P., Bentley, D., & Kornblihtt, A. R. (2003) · Molecular Cell · doi:10.1016/j.molcel.2003.08.001 · Cited by 683
Self-citationReal-Time Observation of Transcription Initiation and Elongation on an Endogenous Yeast Gene
Larson, D. R., Zenklusen, D., Wu, B., Chao, J. A., & Singer, R. H. (2011) · Science · doi:10.1126/science.1202142 · Cited by 680
In vivo dynamics of RNA polymerase II transcription
Darzacq, X., Shav-Tal, Y., de Turris, V., Brody, Y., Shenoy, S. M., Phair, R. D., & Singer, R. H. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1280 · Cited by 665
Chromatin organization marks exon-intron structure
Schwartz, S., Meshorer, E., & Ast, G. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1659 · Cited by 638
RNA Polymerase II Elongation Control
Zhou, Q., Li, T., & Price, D. H. (2012) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-052610-095910 · Cited by 590
Sims, R. J., Millhouse, S., Chen, C.-F., Lewis, B. A., Erdjument‐Bromage, H., Tempst, P., Manley, J. L., & Reinberg, D. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.11.010 · Cited by 581
Lin, C., Smith, E. R., Takahashi, H., Lai, K. C., Martin‐Brown, S., Florens, L. A., Washburn, M. P., Conaway, J. W., Conaway, R. C., & Shilatifard, A. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.01.026 · Cited by 574
The yeast Rat1 exonuclease promotes transcription termination by RNA polymerase II
Kim, M., Krogan, N. J., Vasiljeva, L., Rando, O. J., Nedea, E. C., Greenblatt, J., & Buratowski, S. (2004) · Nature · doi:10.1038/nature03041 · Cited by 557
McCracken, S. A., Fong, N., Rosonina, E., Yankulov, K., Brothers, G. M., Siderovski, D. P., Hessel, A., Foster, S., Program, A. E., Shuman, S., et al. (1997) · Genes & Development · doi:10.1101/gad.11.24.3306 · Cited by 548
Self-citationSplice site selection, rate of splicing, and alternative splicing on nascent transcripts.Preprint
Beyer, A. L., & Osheim, Y. N. (1988) · Genes & Development · doi:10.1101/gad.2.6.754 · Cited by 535
Ahn, S., Kim, M., & Buratowski, S. (2004) · Molecular Cell · doi:10.1016/s1097-2765(03)00492-1 · Cited by 517
Kizer, K. O., Phatnani, H. P., Shibata, Y., Hall, H., Greenleaf, A. L., & Strahl, B. D. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.8.3305-3316.2005 · Cited by 511
Rates of in situ transcription and splicing in large human genes
Singh, J., & Padgett, R. A. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1666 · Cited by 487
Tilgner, H., Knowles, D. G., Johnson, R., Davis, C., Chakrabortty, S. K., Djebali, S., Curado, J., Snyder, M. P., Gingeras, T., & Guigó, R. (2012) · Genome Research · doi:10.1101/gr.134445.111 · Cited by 486
U1 snRNP Determines mRNA Length and Regulates Isoform Expression
Berg, M. G., Singh, L. N., Younis, I., Liu, Q., Pinto, A. M., Kaida, D., Zhang, Z., Cho, S., Sherrill-Mix, S. A., Wan, L., et al. (2012) · Cell · doi:10.1016/j.cell.2012.05.029 · Cited by 482
Cho, E., Takagi, T., Moore, C. R., & Buratowski, S. (1997) · Genes & Development · doi:10.1101/gad.11.24.3319 · Cited by 478
The human SWI/SNF subunit Brm is a regulator of alternative splicing
Batsché, E., Yaniv, M., & Muchardt, C. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1030 · Cited by 471
Bhatt, D. M., Pandya‐Jones, A., Tong, A.-J., Barozzi, I., Lissner, M. M., Natoli, G., Black, D. L., & Smale, S. T. (2012) · Cell · doi:10.1016/j.cell.2012.05.043 · Cited by 447
Uniform transitions of the general RNA polymerase II transcription complex
Mayer, A., Lidschreiber, M., Siebert, M., Leike, K., Söding, J., & Cramer, P. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1903 · Cited by 446
The MO15 cell cycle kinase is associated with the TFIIH transcription-DNA repair factor
Roy, R., Adamczewski, J. P., Seroz, T., Vermeulen, W., Tassan, J., Schaeffer, L., Nigg, E. A., Hoeijmakers, J. H. J., & Egly, J. (1994) · Cell · doi:10.1016/0092-8674(94)90039-6 · Cited by 439
Post-transcriptional processing generates a diversity of 5′-modified long and short RNAs
Tóth, K. F., Sotirova, V. N., Sachidanandam, R., Gordon, A., Hannon, G. J., Gingeras, T., Kapranov, P., Foissac, S., Willingham, A. T., Duttagupta, R., et al. (2009) · Nature · doi:10.1038/nature07759 · Cited by 428
Cracking the RNA polymerase II CTD code
Egloff, S., & Murphy, S. (2008) · Trends in Genetics · doi:10.1016/j.tig.2008.03.008 · Cited by 423
Primary microRNA transcripts are processed co-transcriptionally
Morlando, M., Ballarino, M., Gromak, N., Pagano, F., Bozzoni, I., & Proudfoot, N. J. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1475 · Cited by 408
CDK12 is a transcription elongation-associated CTD kinase, the metazoan ortholog of yeast Ctk1Preprint
Bartkowiak, B., Liu, P., Phatnani, H. P., Fuda, N. J., Cooper, J. J., Price, D. H., Adelman, K., Lis, J. T., & Greenleaf, A. L. (2010) · Genes & Development · doi:10.1101/gad.1968210 · Cited by 404
Ubiquitously transcribed genes use alternative polyadenylation to achieve tissue-specific expressionPreprint
Lianoglou, S., Garg, V., Yang, J. L., Leslie, C. S., & Mayr, C. (2013) · Genes & Development · doi:10.1101/gad.229328.113 · Cited by 402
Direct Coupling of Transcription and mRNA Processing through the Thermogenic Coactivator PGC-1
Monsalve, M., Wu, Z., Adelmant, G., Puigserver, P., Fan, M., & Spiegelman, B. M. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00031-9 · Cited by 395
Dynamic association of capping enzymes with transcribing RNA polymerase IIPreprint
Schroeder, S. C., Schwer, B., Shuman, S., & Bentley, D. L. (2000) · Genes & Development · doi:10.1101/gad.836300 · Cited by 387
Self-citationConnelly, S., & Manley, J. L. (1988) · Genes & Development · doi:10.1101/gad.2.4.440 · Cited by 377
Mili, S., & STEITZ, J. A. (2004) · RNA · doi:10.1261/rna.7151404 · Cited by 372
“Cotranscriptionality”: The Transcription Elongation Complex as a Nexus for Nuclear Transactions
Perales, R., & Bentley, D. L. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.09.018 · Cited by 369
Self-citationIn vivo transcriptional pausing and cap formation on three Drosophila heat shock genes.
Rasmussen, E. B., & Lis, J. T. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.17.7923 · Cited by 369
Pradeepa, M. M., Sutherland, H. G. E., Ule, J., Grimes, G. R., & Bickmore, W. A. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002717 · Cited by 365
Quality control of mRNA 3′-end processing is linked to the nuclear exosome
Hilleren, P. J., McCarthy, T., Rosbash, M., Parker, R., & Jensen, T. H. (2001) · Nature · doi:10.1038/35097110 · Cited by 364
The splicing factor SC35 has an active role in transcriptional elongation
Lin, S., Coutinho-Mansfield, G., Wang, D., Pandit, S., & Fu, X. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1461 · Cited by 363
Sequence requirements for splicing of higher eukaryotic nuclear pre-mRNA
Aebi, M., Hornig, H., Padgett, R. A., Reiser, J., & Weissmann, C. (1986) · Cell · doi:10.1016/0092-8674(86)90620-3 · Cited by 362
RNA polymerase II is an essential mRNA polyadenylation factor
Hirose, Y., & Manley, J. L. (1998) · Nature · doi:10.1038/25786 · Cited by 359
A unique structure at the carboxyl terminus of the largest subunit of eukaryotic RNA polymerase II.
Corden, J. L., Cadena, D. L., Ahearn, J. M., & Dahmus, M. E. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.23.7934 · Cited by 354
Buratowski, S. (2003) · Nature Structural & Molecular Biology · doi:10.1038/nsb0903-679 · Cited by 350
SR Proteins Collaborate with 7SK and Promoter-Associated Nascent RNA to Release Paused Polymerase
Ji, X., Zhou, Y., Pandit, S., Huang, J. S., Li, H., Lin, C. Y., Xiao, R., Burge, C. B., & Fu, X. (2013) · Cell · doi:10.1016/j.cell.2013.04.028 · Cited by 348
SR Proteins Function in Coupling RNAP II Transcription to Pre-mRNA Splicing
Das, R., Yu, J., Zhang, Z., Gygi, M. P., Krainer, A. R., Gygi, S. P., & Reed, R. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.05.036 · Cited by 346
Functional association between promoter structure and transcript alternative splicing
Cramer, P., Pesce, C. G., Baralle, F. E., & Kornblihtt, A. R. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.21.11456 · Cited by 344
Ho, C. K., & Shuman, S. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80468-2 · Cited by 343
RNA polymerase II pauses and associates with pre-mRNA processing factors at both ends of genes
Glover-Cutter, K. M., Kim, S., Espinosa, J. M., & Bentley, D. L. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1352 · Cited by 343
Self-citationCross-Intron Bridging Interactions in the Yeast Commitment Complex Are Conserved in Mammals
Abovich, N., & Rosbash, M. (1997) · Cell · doi:10.1016/s0092-8674(00)80221-4 · Cited by 341
Danko, C. G., Hah, N., Luo, X., Martins, A. L., Core, L., Lis, J. T., Siepel, A., & Kraus, W. L. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.02.015 · Cited by 333
Listerman, I., Sapra, A. K., & Neugebauer, K. M. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1135 · Cited by 324
Ameur, A., Zaghlool, A., Halvardson, J., Wetterbom, A., Gyllensten, U., Cavelier, L., & Feuk, L. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2143 · Cited by 323
Functional Interaction of Yeast Pre-mRNA 3′ End Processing Factors with RNA Polymerase II
Licatalosi, D. D., Geiger, G., Minet, M., Schroeder, S. C., Cilli, K., McNeil, J. B., & Bentley, D. L. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00518-x · Cited by 316
Self-citationRecognition of RNA polymerase II carboxy-terminal domain by 3′-RNA-processing factors
Meinhart, A., & Cramer, P. (2004) · Nature · doi:10.1038/nature02679 · Cited by 315
In vitro polyadenylation is stimulated by the presence of an upstream intron.Preprint
Niwa, M., Rose, S. D., & Berget, S. M. (1990) · Genes & Development · doi:10.1101/gad.4.9.1552 · Cited by 314
Bitoun, E., Oliver, P. L., & Davies, K. E. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl444 · Cited by 311
DNA Damage Regulates Alternative Splicing through Inhibition of RNA Polymerase II Elongation
Muñoz, M. J., Perez-Santángelo, S., Paronetto, M. P., de la Mata, M., Pelisch, F., Boireau, S., Glover-Cutter, K. M., Ben-Dov, C., Blaustein, M., Lozano, J. J., et al. (2009) · Cell · doi:10.1016/j.cell.2009.03.010 · Cited by 310
Self-citationTFIIH Kinase Places Bivalent Marks on the Carboxy-Terminal Domain of RNA Polymerase II
Akhtar, M. S., Heidemann, M., Tietjen, J. R., Zhang, D. W., Chapman, R. D., Eick, D., & Ansari, A. Z. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.04.016 · Cited by 310
Dynamic phosphorylation patterns of RNA polymerase II CTD during transcription
Heidemann, M., Hintermair, C., Voß, K., & Eick, D. (2012) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2012.08.013 · Cited by 300
Identification and analysis of alternative splicing events conserved in human and mouse
Yeo, G. W.-M., Nostrand, E. L. V., Holste, D., Poggio, T., & Burge, C. B. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409742102 · Cited by 299
Co-transcriptional splicing of constitutive and alternative exons
Pandya‐Jones, A., & Black, D. L. (2009) · RNA · doi:10.1261/rna.1714509 · Cited by 297
Serine-7 of the RNA Polymerase II CTD Is Specifically Required for snRNA Gene Expression
Egloff, S., O’Reilly, D., Chapman, R. D., Taylor, A., Tanzhaus, K., Pitts, L., Eick, D., & Murphy, S. (2007) · Science · doi:10.1126/science.1145989 · Cited by 294
Vasiljeva, L., Kim, M., Mutschler, H., Buratowski, S., & Meinhart, A. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1468 · Cited by 290
Post-transcriptional spliceosomes are retained in nuclear speckles until splicing completion
Girard, C., Will, C. L., Peng, J., Makarov, E. M., Kastner, B., Lemm, I., Urlaub, H., Hartmuth, K., & Lührmann, R. (2012) · Nature Communications · doi:10.1038/ncomms1998 · Cited by 287
Ordered and Dynamic Assembly of Single Spliceosomes
Hoskins, A. A., Friedman, L. J., Gallagher, S. S., Crawford, D. J., Anderson, E. G., Wombacher, R., Ramirez, N., Cornish, V. W., Gelles, J., & Moore, M. J. (2011) · Science · doi:10.1126/science.1198830 · Cited by 279
Histone H3 lysine 9 trimethylation and HP1γ favor inclusion of alternative exons
Saint-André, V., Batsché, E., Rachez, C., & Muchardt, C. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1995 · Cited by 278
Splicing of Balbiani ring 1 gene pre-mRNA occurs simultaneously with transcription
Baurén, G., & Wieslander, L. (1994) · Cell · doi:10.1016/0092-8674(94)90182-1 · Cited by 278
Eperon, L. P., Graham, I. R., Griffiths, A. D., & Eperon, I. C. (1988) · Cell · doi:10.1016/0092-8674(88)90202-4 · Cited by 275
Schor, I. E., Rascovan, N., Pelisch, F., Alló, M., & Kornblihtt, A. R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0810666106 · Cited by 270
Logan, J., Falck-Pedersen, E., Darnell, J. E., & Shenk, T. (1987) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.84.23.8306 · Cited by 261
CTD Tyrosine Phosphorylation Impairs Termination Factor Recruitment to RNA Polymerase II
Mayer, A., Heidemann, M., Lidschreiber, M., Schreieck, A., Sun, M., Hintermair, C., Kremmer, E., Eick, D., & Cramer, P. (2012) · Science · doi:10.1126/science.1219651 · Cited by 257
Splicing-Dependent RNA Polymerase Pausing in Yeast
Alexander, R. D., Innocente, S. A., Barrass, J. D., & Beggs, J. D. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.11.005 · Cited by 251
Nascent-seq indicates widespread cotranscriptional pre-mRNA splicing in Drosophila
Khodor, Y. L., Rodriguez, J., Abruzzi, K. C., Tang, C.-H. A., Marr, M. T., & Rosbash, M. (2011) · Genes & Development · doi:10.1101/gad.178962.111 · Cited by 250
Splicing enhances recruitment of methyltransferase HYPB/Setd2 and methylation of histone H3 Lys36
de Almeida, S. F., Grosso, A. R., Koch, F., Fenouil, R., Carvalho, S., Andrade, J., Levezinho, H. I. D. S. P., Gut, M., Eick, D., Gut, I. G., et al. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2123 · Cited by 247
RNA FOLDING DURING TRANSCRIPTION
Pan, T., & Sosnick, T. R. (2006) · Annual Review of Biophysics and Biomolecular Structure · doi:10.1146/annurev.biophys.35.040405.102053 · Cited by 244
Global Analysis of Nascent RNA Reveals Transcriptional Pausing in Terminal Exons
Oesterreich, F. C., Preibisch, S., & Neugebauer, K. M. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.11.004 · Cited by 244
Phosphorylated RNA polymerase II stimulates pre-mRNA splicingPreprint
Hirose, Y., Tacke, R., & Manley, J. L. (1999) · Genes & Development · doi:10.1101/gad.13.10.1234 · Cited by 241
Payne, J., Laybourn, P. J., & Dahmus, M. E. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)47159-7 · Cited by 240
FUS binds the CTD of RNA polymerase II and regulates its phosphorylation at Ser2Preprint
Schwartz, J. C., Ebmeier, C. C., Podell, E. R., Heimiller, J., Taatjes, D. J., & Cech, T. R. (2012) · Genes & Development · doi:10.1101/gad.204602.112 · Cited by 240
Single-Molecule Imaging of Transcriptionally Coupled and Uncoupled Splicing
Vargas, D. Y., Shah, K. N., Batish, M., Levandoski, M., Sinha, S., Marras, S. A. E., Schedl, P. D., & Tyagi, S. (2011) · Cell · doi:10.1016/j.cell.2011.10.024 · Cited by 239
Whitelaw, E., & Proudfoot, N. J. (1986) · The EMBO Journal · doi:10.1002/j.1460-2075.1986.tb04587.x · Cited by 237
Gene-specific RNA polymerase II phosphorylation and the CTD code
Kim, H., Erickson, B., Luo, W., Seward, D. J., Graber, J. H., Pollock, D. D., Megee, P. C., & Bentley, D. L. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1913 · Cited by 235
Self-citationWuarin, J., & Schibler, U. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.11.7219 · Cited by 233
Venkataraman, K., Brown, K. M., & Gilmartin, G. M. (2005) · Genes & Development · doi:10.1101/gad.1298605 · Cited by 223
Govind, C. K., Qiu, H., Ginsburg, D. S., Ruan, C., Hofmeyer, K., Hu, C., Venkatesh, S., Workman, J. L., Li, B., & Hinnebusch, A. G. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.07.003 · Cited by 216
Transcription elongation factor hSPT5 stimulates mRNA cappingPreprint
Wen, Y., & Shatkin, A. J. (1999) · Genes & Development · doi:10.1101/gad.13.14.1774 · Cited by 210
The In Vivo Kinetics of RNA Polymerase II Elongation during Co-Transcriptional Splicing
Brody, Y., Neufeld, N., Bieberstein, N. I., Causse, S., Böhnlein, E.-M., Neugebauer, K. M., Darzacq, X., & Shav‐Tal, Y. (2011) · PLoS Biology · doi:10.1371/journal.pbio.1000573 · Cited by 205
Brannan, K. W., Kim, H., Erickson, B., Glover-Cutter, K. M., Kim, S., Fong, N., Kiemele, L., Hansen, K. C., Davis, R. E., Lykke‐Andersen, J., et al. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.03.006 · Cited by 205
Self-citationNiwa, M., & Berget, S. M. (1991) · Genes & Development · doi:10.1101/gad.5.11.2086 · Cited by 205
Pre-mRNA splicing is a determinant of histone H3K36 methylation
Kim, S., Kim, H., Fong, N., Erickson, B., & Bentley, D. L. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1109475108 · Cited by 198
Self-citationNucleosomal Elements that Control the Topography of the Barrier to Transcription
Bintu, L., Ishibashi, T., Dangkulwanich, M., Wu, Y.-Y., Lubkowska, L., Kashlev, M., & Bustamante, C. (2012) · Cell · doi:10.1016/j.cell.2012.10.009 · Cited by 192
David, C. J., Boyne, A. R., Millhouse, S., & Manley, J. L. (2011) · Genes & Development · doi:10.1101/gad.2038011 · Cited by 191
Serine-7 but not serine-5 phosphorylation primes RNA polymerase II CTD for P-TEFb recognition
Czudnochowski, N., Bösken, C. A., & Geyer, M. (2012) · Nature Communications · doi:10.1038/ncomms1846 · Cited by 191
Mandal, S. S., Chu, C., Wada, T., Handa, H., Shatkin, A. J., & Reinberg, D. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0401493101 · Cited by 191
First Exon Length Controls Active Chromatin Signatures and Transcription
Bieberstein, N. I., Oesterreich, F. C., Straube, K., & Neugebauer, K. M. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.05.019 · Cited by 191
The transcriptional cycle of HIV-1 in real-time and live cells
Boireau, S., Maiuri, P., Basyuk, E., de la Mata, M., Knezevich, A., Pradet-Balade, B., Bäcker, V., Kornblihtt, A., Marcello, A., & Bertrand, E. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200706018 · Cited by 191
Intronic delay is essential for oscillatory expression in the segmentation clock
Takashima, Y., Ohtsuka, T., González, A., Miyachi, H., & Kageyama, R. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1014418108 · Cited by 182
Updating the RNA polymerase CTD code: adding gene-specific layers
Egloff, S., Dienstbier, M., & Murphy, S. (2012) · Trends in Genetics · doi:10.1016/j.tig.2012.03.007 · Cited by 177
Identification of a quality-control mechanism for mRNA 5′-end capping
Jiao, X., Xiang, S., Oh, C., Martin, C. E., Tong, L., & Kiledjian, M. (2010) · Nature · doi:10.1038/nature09338 · Cited by 176
Lee, J. M., & Greenleaf, A. L. (1991) · PubMed · Cited by 176
Mediator Complex Regulates Alternative mRNA Processing via the MED23 Subunit
Huang, Y., Li, W., Xiao, Y., Lin, Q.-J., Yin, J., Liang, Y., Heiner, M., Tian, B., Hui, J., & Wang, G. (2012) · Molecular Cell · doi:10.1016/j.molcel.2011.12.022 · Cited by 172
Crystal structure of the human symplekin–Ssu72–CTD phosphopeptide complex
Xiang, K., Nagaike, T., Xiang, S., Kilic, T., Beh, M. M., Manley, J. L., & Tong, L. (2010) · Nature · doi:10.1038/nature09391 · Cited by 171
Jiao, X., Chang, J. H., Kilic, T., Tong, L., & Kiledjian, M. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.02.017 · Cited by 171
Interactions between Fission Yeast mRNA Capping Enzymes and Elongation Factor Spt5
Pei, Y., & Shuman, S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200015200 · Cited by 168
Ranuncolo, S. M., Ghosh, S. K., Hanover, J. A., Hart, G. W., & Lewis, B. A. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.330910 · Cited by 164
Analysis of the stimulatory effect of splicing on mRNA production and utilization in mammalian cells
Lu, S., & Cullen, B. R. (2003) · RNA · doi:10.1261/rna.5260303 · Cited by 163
Lunde, B. M., Reichow, S., Kim, M., Suh, H., Leeper, T. C., Yang, F., Mutschler, H., Buratowski, S., Meinhart, A., & Varani, G. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1893 · Cited by 159
Windhager, L., Bonfert, T., Burger, K., Ruzsics, Z., Krebs, S., Kaufmann, S., Malterer, G., L’Hernault, A., Schilhabel, M. B., Schreiber, S., et al. (2012) · Genome Research · doi:10.1101/gr.131847.111 · Cited by 152
In Vivo Kinetics of mRNA Splicing and Transport in Mammalian Cells
Audibert, A., Weil, D., & Dautry, F. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.19.6706-6718.2002 · Cited by 149
From Structure to Systems: High-Resolution, Quantitative Genetic Analysis of RNA Polymerase II
Braberg, H., Jin, H., Moehle, E. A., Chan, Y. A., Wang, S., Shales, M., Benschop, J. J., Morris, J. H., Qiu, C., Hu, F., et al. (2013) · Cell · doi:10.1016/j.cell.2013.07.033 · Cited by 143
He, X., Khan, A. U., Cheng, H.-L. M., Pappas, D. L., Hampsey, M., & Moore, C. L. (2003) · Genes & Development · doi:10.1101/gad.1075203 · Cited by 143
Tat Stimulates Cotranscriptional Capping of HIV mRNA
Chiu, Y., Ho, C. K., Saha, N., Schwer, B., Shuman, S., & Rana, T. M. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00630-5 · Cited by 140
Zhou, H.-L., Hinman, M. N., Barron, V. A., Geng, C., Zhou, G., Luo, G., Siegel, R. E., & Lou, H. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1103344108 · Cited by 136
RNA polymerase II kinetics in polo polyadenylation signal selection
Pinto, P. A. B., Henriques, T., Freitas, M. O., Martins, T., Domingues, R. G., Wyrzykowska, P. S., Coelho, P. A., Carmo, A. M., Sunkel, C. E., Proudfoot, N. J., et al. (2011) · The EMBO Journal · doi:10.1038/emboj.2011.156 · Cited by 136
Deciphering the RNA Polymerase II CTD Code in Fission Yeast
Schwer, B., & Shuman, S. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.05.024 · Cited by 135
Smale, S. T., & Tjian, R. (1985) · Molecular and Cellular Biology · doi:10.1128/mcb.5.2.352 · Cited by 134
Kinetic Competition between RNA Polymerase II and Sen1-Dependent Transcription Termination
Hazelbaker, D. Z., Marquardt, S., Wlotzka, W., & Buratowski, S. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.10.014 · Cited by 133
Identification of a Cytoplasmic Complex That Adds a Cap onto 5′-Monophosphate RNA
Otsuka, Y., Kedersha, N., & Schoenberg, D. R. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01325-08 · Cited by 128
Bird, G. A., Zorio, D. A. R., & Bentley, D. L. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.20.8963-8969.2004 · Cited by 126
Self-citationCotranscriptional splicing efficiency differs dramatically between Drosophila and mouse
Khodor, Y. L., Menet, J. S., Tolan, M., & Rosbash, M. (2012) · RNA · doi:10.1261/rna.034090.112 · Cited by 126
Mechanistic Interpretation of Promoter-Proximal Peaks and RNAPII Density Maps
Ehrensberger, A. H., Kelly, G. P., & Svejstrup, J. Q. (2013) · Cell · doi:10.1016/j.cell.2013.07.032 · Cited by 125
Phatnani, H. P., Jones, J. C., & Greenleaf, A. L. (2004) · Biochemistry · doi:10.1021/bi048364h · Cited by 123
Schmidt, U., Basyuk, E. I., Robert, M.-C., Yoshida, M., Villemin, J.-P., Auboeuf, D., Aitken, S., & Bertrand, É. (2011) · The Journal of Cell Biology · doi:10.1083/jcb.201009012 · Cited by 121
Nascent-Seq Indicates Widespread Cotranscriptional RNA Editing in Drosophila
Rodriguez, J., Menet, J. S., & Rosbash, M. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.05.002 · Cited by 119
DBIRD complex integrates alternative mRNA splicing with RNA polymerase II transcript elongation
Close, P., East, P., Dirac-Svejstrup, A. B., Hartmann, H., Heron, M., Maslen, S., Chariot, A., Söding, J., Skehel, M., & Svejstrup, J. Q. (2012) · Nature · doi:10.1038/nature10925 · Cited by 119
A Genome-Wide Analysis Indicates that Yeast Pre-mRNA Splicing Is Predominantly Posttranscriptional
Tardiff, D. F., Lacadie, S. A., & Rosbash, M. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.12.002 · Cited by 117
Nascent RNA structure modulates the transcriptional dynamics of RNA polymerases
Zamft, B., Bintu, L., Ishibashi, T., & Bustamante, C. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1205063109 · Cited by 117
Transcriptional Activators Enhance Polyadenylation of mRNA Precursors
Nagaike, T., Logan, C. J., Hotta, I., Rozenblatt–Rosen, O., Meyerson, M. M., & Manley, J. L. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.01.022 · Cited by 116
Sisodia, S. S., Sollner-Webb, B., & Cleveland, D. W. (1987) · Molecular and Cellular Biology · doi:10.1128/mcb.7.10.3602 · Cited by 115
de la Mata, M., Lafaille, C., & Kornblihtt, A. R. (2010) · RNA · doi:10.1261/rna.1993510 · Cited by 115
Positive patches and negative noodles: linking RNA processing to transcription?
Greenleaf, A. L. (1993) · Trends in Biochemical Sciences · doi:10.1016/0968-0004(93)90016-g · Cited by 114
Gu, B., Eick, D., & Bensaude, O. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks1327 · Cited by 114
Meyer, M., Plass, M., Pérez‐Valle, J., Eyras, E., & Vilardell, J. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.07.030 · Cited by 113
Serine phosphorylation and proline isomerization in RNAP II CTD control recruitment of Nrd1Preprint
Kubíček, K., Cerná, H., Holub, P., Pasulka, J., Hroššová, D., Loehr, F., Hofr, C., Vaňáčová, Š., & Štefl, R. (2012) · Genes & Development · doi:10.1101/gad.192781.112 · Cited by 109
Darnell, J. E., Jr. (2013) · RNA · doi:10.1261/rna.038596.113 · Cited by 109
Counting on co-transcriptional splicing
Brugiolo, M., Herzel, L., & Neugebauer, K. M. (2013) · F1000Prime Reports · doi:10.12703/p5-9 · Cited by 108
Pandya‐Jones, A., Bhatt, D. M., Lin, C.-H., Tong, A.-J., Smale, S. T., & Black, D. L. (2013) · RNA · doi:10.1261/rna.039081.113 · Cited by 106
A pause site for RNA polymerase II is associated with termination of transcription.
Enriquez-Harris, P., Levitt, N. C., Briggs, D., & Proudfoot, N. J. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07709.x · Cited by 105
Dxo1 is a new type of eukaryotic enzyme with both decapping and 5′-3′ exoribonuclease activity
Chang, J. H., Jiao, X., Chiba, K., Oh, C., Martin, C. E., Kiledjian, M., & Tong, L. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2381 · Cited by 105
The differential interaction of snRNPs with pre-mRNA reveals splicing kinetics in living cells
Huranová, M., Ivani, I., Benda, A., Poser, I., Brody, Y., Hof, M., Shav‐Tal, Y., Neugebauer, K. M., & Staněk, D. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201004030 · Cited by 103
Structural Insights to How Mammalian Capping Enzyme Reads the CTD Code
Ghosh, A., Shuman, S., & Lima, C. D. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.06.001 · Cited by 99
Transcriptional elongation and alternative splicing
Dujardin, G., Lafaille, C., Petrillo, E., Buggiano, V., Acuña, L. I. G., Fiszbein, A., Herz, M. A. G., Moreno, N. N., Muñoz, M. J., Alló, M., et al. (2012) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2012.08.005 · Cited by 99
Conformational dynamics of single pre-mRNA molecules during in vitro splicing
Abelson, J. N., Blanco, M. R., Ditzler, M. A., Fuller, F. D., Aravamudhan, P., Wood, M. L., Villa, T., Ryan, D. E., Pleiss, J. A., Maeder, C., et al. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1767 · Cited by 97
Co‐transcriptional degradation of aberrant pre‐mRNA by Xrn2
Davidson, L., Kerr, A. R. W., & West, S. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.101 · Cited by 96
The export factor Yra1 modulates mRNA 3′ end processing
Johnson, S. A., Kim, H., Erickson, B., & Bentley, D. L. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2126 · Cited by 89
Self-citationBaurén, G., Belikov, S. V., & Wieslander, L. (1998) · Genes & Development · doi:10.1101/gad.12.17.2759 · Cited by 88
Lenasi, T., Peterlin, B. M., & Barborič, M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.235077 · Cited by 87
RNA splicing regulates the temporal order of TNF-induced gene expression
Hao, S., & Baltimore, D. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1309990110 · Cited by 86
Shen, Z., St‐Denis, A., & Chartrand, P. (2010) · Genes & Development · doi:10.1101/gad.1937510 · Cited by 84
Spliceosome assembly is coupled to RNA polymerase II dynamics at the 3′ end of human genes
Martins, S., Rino, J., Carvalho, T., Carvalho, C., Yoshida, M., Klose, J. M., de Almeida, S. F., & Carmo‐Fonseca, M. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2124 · Cited by 80
The CTD code of RNA polymerase II: a structural view
Jasnovidova, O., & Štefl, R. (2012) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1138 · Cited by 78
Gunderson, F. Q., Merkhofer, E., & Johnson, T. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1011982108 · Cited by 75
Lionnet, T., & Singer, R. H. (2012) · EMBO Reports · doi:10.1038/embor.2012.31 · Cited by 75
Batada, N. N., Westover, K. D., Bushnell, D. A., Levitt, M., & Kornberg, R. D. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0408168101 · Cited by 72
An active role for splicing in 3′‐end formation
Martinson, H. G. (2010) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.68 · Cited by 68
Functional roles of protein splicing factors
Chen, H.-C., & Cheng, S.-C. (2012) · Bioscience Reports · doi:10.1042/bsr20120007 · Cited by 67
A Function of Yeast mRNA Cap Methyltransferase, Abd1, in Transcription by RNA Polymerase II
Schroeder, S. C., Zorio, D. A. R., Schwer, B., Shuman, S., & Bentley, D. L. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00007-3 · Cited by 67
Self-citationTranscriptional Activators Control Splicing and 3′-End Cleavage Levels
Rosonina, E., Bakowski, M. A., McCracken, S. A., & Blencowe, B. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307289200 · Cited by 66
Splicing-independent recruitment of U1 snRNP to a transcription unit in living cells
Spiluttini, B., Gu, B., Belagal, P., Henriques, A. S., Nguyen, V. T., Hébert, C., Schmidt, U., Bertrand, É., Darzacq, X., & Bensaude, O. (2010) · Journal of Cell Science · doi:10.1242/jcs.061358 · Cited by 63
de Almeida, S. F., García-Sacristán, A., Custódio, N., & Carmo‐Fonseca, M. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq703 · Cited by 62
Fernández-Sánchez, M. E., Gonatopoulos-Pournatzis, T., Preston, G., Lawlor, M. A., & Cowling, V. H. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00973-09 · Cited by 62
Connections between chromatin signatures and splicing
Acuña, L. I. G., Fiszbein, A., Alló, M., Schor, I. E., & Kornblihtt, A. R. (2012) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1142 · Cited by 56
Újvári, A., & Luse, D. S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409087200 · Cited by 52
Bird, G. A., Fong, N., Gatlin, J. C., Farabaugh, S., & Bentley, D. L. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.11.009 · Cited by 52
Self-citationRyman, K., Fong, N., Bratt, E., Bentley, D. L., & Öhman, M. (2007) · RNA · doi:10.1261/rna.404407 · Cited by 50
Self-citationPunctuation and syntax of the RNA polymerase II CTD code in fission yeast
Schwer, B., Sánchez, A. M., & Shuman, S. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1208995109 · Cited by 49
Cotranscriptional folding kinetics of ribonucleic acid secondary structures
Zhao, P., Zhang, W., & Chen, S. (2011) · The Journal of Chemical Physics · doi:10.1063/1.3671644 · Cited by 49
fus/TLS orchestrates splicing of developmental regulators during gastrulationPreprint
Dichmann, D. S., & Harland, R. M. (2012) · Genes & Development · doi:10.1101/gad.187278.112 · Cited by 45
Benson, M. J., Äijö, T., Chang, X., Gagnon, J. D., Pape, U. J., Anantharaman, V., Aravind, L., Pursiheimo, J., Oberdoerffer, S., Liu, X. S., et al. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1214414109 · Cited by 44
Eberle, A. B., Hessle, V., Helbig, R., Dantoft, W., Gimber, N., & Visa, N. (2010) · PLoS ONE · doi:10.1371/journal.pone.0011540 · Cited by 44
An RNA Polymerase Pause Site Is Associated with the Immunoglobulin μs Poly(A) Site
Peterson, M. L., Bertolino, S., & Davis, F. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.15.5606-5615.2002 · Cited by 40
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Andersen, P. K., Lykke‐Andersen, S., & Jensen, T. H. (2012) · Genes & Development · doi:10.1101/gad.189126.112 · Cited by 35
Rigo, F., Kazerouninia, A., Nag, A., & Martinson, H. G. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.09.026 · Cited by 34
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Suh, M.-H., Meyer, P. A., Gu, M., Ye, P., Zhang, M., Kaplan, C. D., Lima, C. D., & Fu, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.145110 · Cited by 33
Definition of RNA Polymerase II CoTC Terminator Elements in the Human Genome
Nojima, T., Dienstbier, M., Murphy, S., Proudfoot, N. J., & Dye, M. J. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.03.012 · Cited by 32
Garrido‐Lecca, A., & Blumenthal, T. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00325-10 · Cited by 20
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Metadata
- Authors
- Bentley, D. L.
- Affiliations
- University of Colorado Anschutz (US)
- Corresponding author
- Bentley, David L.
- ORCID
- Bentley, David L.
- Venue
- Nature Reviews Genetics
- Published
- 2014-02-11
- Volume
- 15
- Issue
- 3
- Pages
- 163-175
- ISSN
- 1471-0056 (ISSN-L)
- 1471-0064
- PMC
- PMC4304646
- OpenAlex
- W2040410152
- Cited by
- 828
- References
- 188
- Citations by year
- 2026: 47 · 2025: 49 · 2024: 53 · 2023: 64 · 2022: 68 · 2021: 77 · 2020: 90 · 2019: 88 · 2018: 64 · 2017: 74 · 2016: 73 · 2015: 57 · 2014: 24
- FWCI
- 7.16
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Genetics (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Cancer Research UK
- National Institutes of Health
- National Institute of General Medical Sciences (GM58163, R01GM058613, GM 063873, R01GM063873)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Keywords
- post-transcriptional processing, RNA polymerase II, C-terminal domain, mRNA capping, mRNA splicing, RNA editing, 3' end formation, nascent RNA
- MeSH terms
- RNA Caps, RNA Polymerase II, RNA Splicing, RNA, Messenger, Transcription, Genetic
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