The code and beyond: transcription regulation by the RNA polymerase II carboxy-terminal domain
Abstract
The carboxy-terminal domain (CTD) extends from the largest subunit of RNA polymerase II (Pol II) as a long, repetitive and largely unstructured polypeptide chain. Throughout the transcription process, the CTD is dynamically modified by post-translational modifications, many of which facilitate or hinder the recruitment of key regulatory factors of Pol II that collectively constitute the 'CTD code'. Recent studies have revealed how the physicochemical properties of the CTD promote phase separation in the presence of other low-complexity domains. Here, we discuss the intricacies of the CTD code and how the newly characterized physicochemical properties of the CTD expand the function of the CTD beyond the code.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
CDK8 inhibition by MSC2530818 did not alter the phosphorylation profile of RBP1, indicating the treatment did not affect basal transcriptional programs.
“CDK8 inhibition by MSC2530818 did not alter the phosphorylation profile of RBP1, suggesting that our treatment did not affect basal transcriptional programs (Sup. Figure 9B)”
From CDK8 fine-tunes IL-6 transcriptional activities by limiting STAT3 resident time at the gene loci (2020) · cites this paper as Harlen and Churchman, 2017
Cites
Liquid-Liquid Phase Separation in Biology
Hyman, A. A., Weber, C. A., & Jülicher, F. (2014) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev-cellbio-100913-013325 · Cited by 3,155 · see citing works
A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation
Patel, A., Lee, H. O., Jawerth, L. M., Maharana, S., Jahnel, M., Hein, M. Y., Stoynov, S., Mahamid, J., Saha, S., Franzmann, T. M., et al. (2015) · Cell · doi:10.1016/j.cell.2015.07.047 · Cited by 2,927 · see citing works
Widespread transcription at neuronal activity-regulated enhancers
Kim, T.-K., Hemberg, M., Gray, J. M., Costa, A. M., Bear, D. M., Wu, J., Harmin, D. A., Laptewicz, M., Barbara-Haley, K., Kuersten, S., et al. (2010) · Nature · doi:10.1038/nature09033 · Cited by 2,450 · see citing works
The economics of ribosome biosynthesis in yeast
Warner, J. R. (1999) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01460-7 · Cited by 1,933 · see citing works
Promoter-proximal pausing of RNA polymerase II: emerging roles in metazoans
Adelman, K., & Lis, J. T. (2012) · Nature Reviews Genetics · doi:10.1038/nrg3293 · Cited by 1,186 · see citing works
Controlling the elongation phase of transcription with P-TEFb
Peterlin, B. M., & Price, D. H. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.06.014 · Cited by 1,144 · see citing works
Komarnitsky, P. B., Cho, E., & Buratowski, S. (2000) · Genes & Development · doi:10.1101/gad.824700 · Cited by 1,098 · see citing works
Ng, H., Robert, F., Young, R. A., & Struhl, K. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00092-3 · Cited by 1,097 · see citing works
Histone exchange, chromatin structure and the regulation of transcription
Venkatesh, S., & Workman, J. L. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3941 · Cited by 940 · see citing works
Burke, K. A., Janke, A. M., Rhine, C. L., & Fawzi, N. L. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.09.006 · Cited by 932 · see citing works
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 · see citing works
Divergent transcription from active promoters
Seila, A. C., Calabrese, J. M., Levine, S., Yeo, G. W., Rahl, P., Flynn, R. A., Young, R., & Sharp, P. (2008) · Science · doi:10.1126/science.1162253 · Cited by 923 · see citing works
Getting up to speed with transcription elongation by RNA polymerase II
Jonkers, I., & Lis, J. T. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3953 · Cited by 876 · see citing works
Coupling mRNA processing with transcription in time and space
Bentley, D. L. (2014) · Nature Reviews Genetics · doi:10.1038/nrg3662 · Cited by 828 · see citing works
Progression through the RNA Polymerase II CTD Cycle
Buratowski, S. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.10.019 · Cited by 777 · see citing works
Phase separation in biology; functional organization of a higher order
Mitrea, D. M., & Kriwacki, R. W. (2016) · Cell Communication and Signaling · doi:10.1186/s12964-015-0125-7 · Cited by 723 · see citing works
Krogan, N. J., Dover, J., Wood, A., Schneider, J., Heidt, J. W., Boateng, M. A., Dean, K., Ryan, O. W., Golshani, A., Johnston, M., et al. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00091-1 · Cited by 706 · see citing works
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 696 · see citing works
Krogan, N. J., Kim, M., Tong, A. H. Y., Golshani, A., Cagney, G., Canadien, V., Richards, D. P., Beattie, B. K., Emili, A., Boone, C. M., et al. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.12.4207-4218.2003 · Cited by 680 · see citing works
Alberti, S. (2017) · Current Biology · doi:10.1016/j.cub.2017.08.069 · Cited by 654 · see citing works
Jonkers, I., Kwak, H., & Lis, J. T. (2014) · eLife · doi:10.7554/elife.02407 · Cited by 581 · see citing works
Liquid demixing of intrinsically disordered proteins is seeded by poly(ADP-ribose)
Altmeyer, M., Neelsen, K. J., Teloni, F., Pozdnyakova, I., Pellegrino, S., Grøfte, M., Rask, M., Streicher, W. W., Jungmichel, S., Nielsen, M. L., et al. (2015) · Nature Communications · doi:10.1038/ncomms9088 · Cited by 581 · see citing works
Mammalian NET-Seq Reveals Genome-wide Nascent Transcription Coupled to RNA Processing
Nojima, T., Gomes, T., Grosso, A. R. F., Kimura, H., Dye, M. J., Dhir, S., Carmo-Fonseca, M., & Proudfoot, N. J. (2015) · Cell · doi:10.1016/j.cell.2015.03.027 · Cited by 562 · see citing works
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 · see citing works
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 · see citing works
Phosphorylation-Regulated Binding of RNA Polymerase II to Fibrous Polymers of Low-Complexity Domains
Kwon, I., Kato, M., Xiang, S., Wu, L. C., Theodoropoulos, P., Mirzaei, H., Han, T. W., Xie, S., Corden, J. L., & McKnight, S. L. (2013) · Cell · doi:10.1016/j.cell.2013.10.033 · Cited by 541 · see citing works
Blazek, D., Kohoutek, J., Bartholomeeusen, K., Johansen, E., Hulinkova, P., Luo, Z., Cimermancic, P., Ule, J., & Peterlin, B. M. (2011) · Genes & Development · doi:10.1101/gad.16962311 · Cited by 522 · see citing works
Ahn, S., Kim, M., & Buratowski, S. (2004) · Molecular Cell · doi:10.1016/s1097-2765(03)00492-1 · Cited by 517 · see citing works
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 · see citing works
RNA transcription modulates phase transition-driven nuclear body assembly
Berry, J., Weber, S. C., Vaidya, N., Haataja, M., & Brangwynne, C. P. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1509317112 · Cited by 501 · see citing works
Real-Time Dynamics of RNA Polymerase II Clustering in Live Human Cells
Cissé, I. I., Izeddin, I., Causse, S., Boudarène, L., Senecal, A., Mureşan, L., Dugast‐Darzacq, C., Hajj, B., Dahan, M., & Darzacq, X. (2013) · Science · doi:10.1126/science.1239053 · Cited by 489 · see citing works
The RNA Polymerase II Carboxy-Terminal Domain (CTD) Code
Eick, D., & Geyer, M. (2013) · Chemical Reviews · doi:10.1021/cr400071f · Cited by 470 · see citing works
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 · see citing works
Topoisomerases facilitate transcription of long genes linked to autism
King, I. F. G., Yandava, C., Mabb, A. M., Hsiao, J. S., Huang, H., Pearson, B. L., Calabrese, J. M., Starmer, J., Parker, J. S., Magnuson, T., et al. (2013) · Nature · doi:10.1038/nature12504 · Cited by 430 · see citing works
Phosphorylation of RNA polymerase II CTD regulates H3 methylation in yeastPreprint
Xiao, T., Hall, H., Kizer, K. O., Shibata, Y., Hall, M. C., Borchers, C. H., & Strahl, B. D. (2003) · Genes & Development · doi:10.1101/gad.1055503 · Cited by 411 · see citing works
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 408 · see citing works
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 · see citing works
Cap and cap‐binding proteins in the control of gene expression
Topisirović, I., Svitkin, Y. V., Sonenberg, N., & Shatkin, A. J. (2010) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.52 · Cited by 402 · see citing works
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 · see citing works
Devaiah, B. N., Lewis, B. A., Cherman, N., Hewitt, M. C., Albrecht, B. K., Robey, P. G., Ozato, K., Sims, R. J., & Singer, D. S. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1120422109 · Cited by 379 · see citing works
Li, B., Howe, L. J., Anderson, S., Yates, J. R., & Workman, J. L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212134200 · Cited by 371 · see citing works
Mayer, A., di Iulio, J., Maleri, S., Eser, U., Vierstra, J., Reynolds, A., Sandstrom, R., Stamatoyannopoulos, J. A., & Churchman, L. S. (2015) · Cell · doi:10.1016/j.cell.2015.03.010 · Cited by 367 · see citing works
Self-citationHahn, S., & Young, E. T. (2011) · Genetics · doi:10.1534/genetics.111.127019 · Cited by 341 · see citing works
Ho, C. K., & Shuman, S. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80468-2 · Cited by 338 · see citing works
Buratowski, S. (2003) · Nature Structural & Molecular Biology · doi:10.1038/nsb0903-679 · Cited by 334 · see citing works
The Med proteins of yeast and their function through the RNA polymerase II carboxy-terminal domain.Preprint
Myers, L., Gustafsson, C., Bushnell, D., Lui, M., Erdjument-Bromage, H., Tempst, P., & Kornberg, R. (1998) · Genes & Development · doi:10.1101/gad.12.1.45 · Cited by 329 · see citing works
Lu, H., Flores, O. A., Weinmann, R. S., & Reinberg, D. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.22.10004 · Cited by 325 · see citing works
Transcribing RNA Polymerase II Is Phosphorylated at CTD Residue Serine-7
Chapman, R. D., Heidemann, M., Albert, T., Mailhammer, R., Flatley, A., Meisterernst, M., Kremmer, E., & Eick, D. (2007) · Science · doi:10.1126/science.1145977 · Cited by 323 · see citing works
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 · see citing works
Recognition 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 · see citing works
Transcription termination and the control of the transcriptome: why, where and how to stop
Porrúa, O., & Libri, D. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3943 · Cited by 314 · see citing works
NELF and DSIF cause promoter proximal pausing on thehsp70promoter inDrosophilaPreprint
Wu, C.-H., Yamaguchi, Y., Benjamin, L. R., Horvat‐Gordon, M., Washinsky, J., Enerly, E., Larsson, J., Lambertsson, A., Handa, H., & Gilmour, D. S. (2003) · Genes & Development · doi:10.1101/gad.1091403 · Cited by 314 · see citing works
RNA Polymerase II Regulates Topoisomerase 1 Activity to Favor Efficient Transcription
Baranello, L., Wójtowicz, D., Cui, K., Devaiah, B. N., Chung, H., Chan-Salis, K. Y., Guha, R., Wilson, K. M., Zhang, X., Zhang, H., et al. (2016) · Cell · doi:10.1016/j.cell.2016.02.036 · Cited by 306 · see citing works
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 · see citing works
Xiang, S., Kato, M., Wu, L. C., Lin, Y., Ding, M., Zhang, Y., Yu, Y., & McKnight, S. L. (2015) · Cell · doi:10.1016/j.cell.2015.10.040 · Cited by 299 · see citing works
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 · see citing works
Cadena, D. L., & Dahmus, M. E. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)45229-5 · Cited by 293 · see citing works
Vasiljeva, L., Kim, M., Mutschler, H., Buratowski, S., & Meinhart, A. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1468 · Cited by 290 · see citing works
Courchaine, E. M., Lü, A., & Neugebauer, K. M. (2016) · The EMBO Journal · doi:10.15252/embj.201593517 · Cited by 289 · see citing works
Regulation of RNA polymerase II activation by histone acetylation in single living cells
Stasevich, T. J., Hayashi‐Takanaka, Y., Sato, Y., Maehara, K., Ohkawa, Y., Sakata-Sogawa, K., Tokunaga, M., Nagase, T., Nozaki, N., McNally, J. G., et al. (2014) · Nature · doi:10.1038/nature13714 · Cited by 287 · see citing works
RNA Polymerase II cluster dynamics predict mRNA output in living cells
Cho, W., Jayanth, N., English, B. P., Inoue, T., Andrews, J. O., Conway, W., Grimm, J. B., Spille, J.-H., Lavis, L. D., Lionnet, T., et al. (2016) · eLife · doi:10.7554/elife.13617 · Cited by 280 · see citing works
Li, J., Moazed, D., & Gygi, S. P. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m209294200 · Cited by 273 · see citing works
Nonet, M. L., & Young, R. A. (1989) · Genetics · doi:10.1093/genetics/123.4.715 · Cited by 259 · see citing works
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 · see citing works
Termination of Cryptic Unstable Transcripts Is Directed by Yeast RNA-Binding Proteins Nrd1 and Nab3
Arigo, J. T., Eyler, D. E., Carroll, K. L., & Corden, J. L. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.07.024 · Cited by 257 · see citing works
The Spt6 SH2 domain binds Ser2-P RNAPII to direct Iws1-dependent mRNA splicing and exportPreprint
Yoh, S. M., Cho, H. K., Pickle, L., Evans, R. M., & Jones, K. A. (2007) · Genes & Development · doi:10.1101/gad.1503107 · Cited by 257 · see citing works
PAF1, a Molecular Regulator of Promoter-Proximal Pausing by RNA Polymerase II
Chen, F., Woodfin, A. R., Gardini, A., Rickels, R. A., Marshall, S. A., Smith, E. R., Shiekhattar, R., & Shilatifard, A. (2015) · Cell · doi:10.1016/j.cell.2015.07.042 · Cited by 253 · see citing works
Construction and analysis of yeast RNA polymerase II CTD deletion and substitution mutations.
West, M. L., & Corden, J. L. (1995) · Genetics · doi:10.1093/genetics/140.4.1223 · Cited by 245 · see citing works
3D imaging of Sox2 enhancer clusters in embryonic stem cells
Liu, Z. J., Legant, W. R., Chen, B., Li, L., Grimm, J. B., Lavis, L. D., Betzig, E., & Tjian, R. (2014) · eLife · doi:10.7554/elife.04236 · Cited by 245 · see citing works
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 · see citing works
Yu, M., Yang, W., Ni, T., Tang, Z., Nakadai, T., Zhu, J., & Roeder, R. G. (2015) · Science · doi:10.1126/science.aad2338 · Cited by 241 · see citing works
Thiebaut, M., Kisseleva-Romanova, E., Rougemaille, M., Boulay, J., & Libri, D. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.07.029 · Cited by 241 · see citing works
Payne, J., Laybourn, P. J., & Dahmus, M. E. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)47159-7 · Cited by 240 · see citing works
Wong, K. H., Jin, Y., & Struhl, K. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.03.024 · Cited by 240 · see citing works
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 · see citing works
Yoh, S. M., Lucas, J., & Jones, K. A. (2008) · Genes & Development · doi:10.1101/gad.1720008 · Cited by 238 · see citing works
Gcn5 Promotes Acetylation, Eviction, and Methylation of Nucleosomes in Transcribed Coding Regions
Govind, C. K., Zhang, F., Qiu, H., Hofmeyer, K., & Hinnebusch, A. G. (2007) · Molecular Cell · doi:10.1016/j.molcel.2006.11.020 · Cited by 238 · see citing works
Structure of a Complete Mediator-RNA Polymerase II Pre-Initiation Complex
Robinson, P. J. J., Trnka, M. J., Bushnell, D. A., Davis, R., Matteï, P., Burlingame, A. L., & Kornberg, R. D. (2016) · Cell · doi:10.1016/j.cell.2016.08.050 · Cited by 238 · see citing works
SMN and symmetric arginine dimethylation of RNA polymerase II C-terminal domain control termination
Zhao, D. Y., Gish, G. D., Braunschweig, U., Li, Y., Ni, Z., Schmitges, F. W., Zhong, G., Liu, K., Li, W., Moffat, J., et al. (2015) · Nature · doi:10.1038/nature16469 · Cited by 238 · see citing works
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 · see citing works
The C-Terminal Domain of RNA Polymerase II Is Modified by Site-Specific Methylation
Sims, R. J., Rojas, L. A., Beck, D. B., Bonasio, R., Schüller, R., Drury, W. J., Eick, D., & Reinberg, D. (2011) · Science · doi:10.1126/science.1202663 · Cited by 228 · see citing works
Participation of the nuclear cap binding complex in pre-mRNA 3′ processing
Flaherty, S. M., Fortes, P., Izaurralde, E., Mattaj, I. W., & Gilmartin, G. M. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.22.11893 · Cited by 227 · see citing works
The pol II CTD: new twists in the tail
Zaborowska, J., Egloff, S., & Murphy, S. (2016) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3285 · Cited by 227 · see citing works
Bataille, A. R., Jerónimo, C., Jacques, P., Laramée, L., Fortin, M.-È., Forest, A., Bergeron, M., Hanes, S. D., & Robert, F. (2012) · Molecular Cell · doi:10.1016/j.molcel.2011.11.024 · Cited by 220 · see citing works
Lee, J., & Skalnik, D. G. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01356-07 · Cited by 218 · see citing works
Splicing of Nascent RNA Coincides with Intron Exit from RNA Polymerase II
Oesterreich, F. C., Herzel, L., Straube, K., Hujer, K., Howard, J., & Neugebauer, K. M. (2016) · Cell · doi:10.1016/j.cell.2016.02.045 · Cited by 218 · see citing works
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 · see citing works
Low-complexity regions within protein sequences have position-dependent roles
Coletta, A., Pinney, J. W., Solís, D. W., Marsh, J., Pettifer, S. R., & Attwood, T. K. (2010) · BMC Systems Biology · doi:10.1186/1752-0509-4-43 · Cited by 209 · see citing works
The maintenance of chromosome structure: positioning and functioning of SMC complexes
Jeppsson, K. E., Kanno, T., Shirahige, K., & Sjögren, C. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3857 · Cited by 206 · see citing works
Transcription-associated histone modifications and cryptic transcription
Smolle, M. M., & Workman, J. L. (2012) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2012.08.008 · Cited by 203 · see citing works
The Splicing Factor, Prp40, Binds the Phosphorylated Carboxyl-terminal Domain of RNA Polymerase II
Morris, D. P., & Greenleaf, A. L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m004118200 · Cited by 198 · see citing works
Liang, K., Gao, X., Gilmore, J. M., Florens, L. A., Washburn, M. P., Smith, E. R., & Shilatifard, A. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.01426-14 · Cited by 194 · see citing works
David, C. J., Boyne, A. R., Millhouse, S., & Manley, J. L. (2011) · Genes & Development · doi:10.1101/gad.2038011 · Cited by 191 · see citing works
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 · see citing works
The structure and substrate specificity of human Cdk12/Cyclin K
Bösken, C. A., Farnung, L., Hintermair, C., Merzel Schachter, M., Vogel-Bachmayr, K., Blazek, D., Anand, K., Fisher, R. P., Eick, D., & Geyer, M. (2014) · Nature Communications · doi:10.1038/ncomms4505 · Cited by 191 · see citing works
RNA Polymerase II C-Terminal Domain: Tethering Transcription to Transcript and Template
Corden, J. L. (2013) · Chemical Reviews · doi:10.1021/cr400158h · Cited by 184 · see citing works
The histone 3 lysine 36 methyltransferase, SET2, is involved in transcriptional elongation
Schaft, D. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg372 · Cited by 180 · see citing works
RNAP II CTD Phosphorylated on Threonine-4 Is Required for Histone mRNA 3′ End Processing
Hsin, J.-P., Sheth, A., & Manley, J. L. (2011) · Science · doi:10.1126/science.1206034 · Cited by 168 · see citing works
Molecular evolution of the RNA polymerase II CTD
Chapman, R. D., Heidemann, M., Hintermair, C., & Eick, D. (2008) · Trends in Genetics · doi:10.1016/j.tig.2008.03.010 · Cited by 165 · see citing works
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 · see citing works
Hintermair, C., Heidemann, M., Koch, F., Descostes, N., Gut, M., Gut, I. G., Fenouil, R., Ferrier, P., Flatley, A., Kremmer, E., et al. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.123 · Cited by 161 · see citing works
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 160 · see citing works
P-TEFb Is Critical for the Maturation of RNA Polymerase II into Productive Elongation In Vivo
Ni, Z., Saunders, A., Fuda, N. J., Yao, J., Suárez, J.-R., Webb, W. W., & Lis, J. T. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01859-07 · Cited by 157 · see citing works
Kin28 regulates the transient association of Mediator with core promoters
Jerónimo, C., & Robert, F. (2014) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2810 · Cited by 156 · see citing works
Max, T., Søgaard, M., & Svejstrup, J. Q. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m701345200 · Cited by 150 · see citing works
Heptad-Specific Phosphorylation of RNA Polymerase II CTD
Schüller, R., Forné, I., Straub, T., Schreieck, A., Texier, Y., Shah, N., Decker, T.-M., Cramer, P., Imhof, A., & Eick, D. (2016) · Molecular Cell · doi:10.1016/j.molcel.2015.12.003 · Cited by 150 · see citing works
Harlen, K. M., Trotta, K. L., Smith, E. E., Mosaheb, M. M., Fuchs, S. M., & Churchman, L. S. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.05.010 · Cited by 150 · see citing works
Self-citationPhosphorylation of the Yeast Rpb1 C-terminal Domain at Serines 2, 5, and 7
Kim, M., Suh, H., Cho, E., & Buratowski, S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.028993 · Cited by 149 · see citing works
Chemical-genomic dissection of the CTD code
Tietjen, J. R., Zhang, D. W., Rodríguez‐Molina, J. B., White, B. E., Akhtar, M. S., Heidemann, M., Li, X., Chapman, R. D., Shokat, K. M., Keleş, S., et al. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1900 · Cited by 148 · see citing works
Drouin, S., Laramée, L., Jacques, P., Forest, A., Bergeron, M., & Robert, F. (2010) · PLoS Genetics · doi:10.1371/journal.pgen.1001173 · Cited by 141 · see citing works
The RNA Polymerase II CTD: The Increasing Complexity of a Low-Complexity Protein Domain
Jerónimo, C., Collin, P., & Robert, F. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.02.006 · Cited by 136 · see citing works
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 · see citing works
Recruitment Timing and Dynamics of Transcription Factors at the Hsp70 Loci in Living Cells
Zobeck, K. L., Buckley, M. S., Zipfel, W. R., & Lis, J. T. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.11.022 · Cited by 131 · see citing works
Interaction of yeast RNA-binding proteins Nrd1 and Nab3 with RNA polymerase II terminator elements
Carroll, K. L., Ghirlando, R., Ames, J. M., & Corden, J. L. (2007) · RNA · doi:10.1261/rna.338407 · Cited by 130 · see citing works
Structure of the Mediator Head module bound to the carboxy-terminal domain of RNA polymerase II
Robinson, P. J. J., Bushnell, D. A., Trnka, M. J., Burlingame, A. L., & Kornberg, R. D. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1215241109 · Cited by 121 · see citing works
Direct Analysis of Phosphorylation Sites on the Rpb1 C-Terminal Domain of RNA Polymerase II
Suh, H., Ficarro, S. B., Kang, U., Chun, Y., Marto, J. A., & Buratowski, S. (2016) · Molecular Cell · doi:10.1016/j.molcel.2015.12.021 · Cited by 121 · see citing works
Schröder, S., Herker, E., Itzen, F., He, D. X., Thomas, S., Gilchrist, D. A., Kaehlcke, K., Cho, S., Pollard, K. S., Capra, J. A., et al. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.10.009 · Cited by 115 · see citing works
Gu, B., Eick, D., & Bensaude, O. (2012) · Nucleic Acids Research · doi:10.1093/nar/gks1327 · Cited by 114 · see citing works
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 114 · see citing works
The Writers, Readers, and Functions of the RNA Polymerase II C-Terminal Domain Code
Jerónimo, C., Bataille, A. R., & Robert, F. (2013) · Chemical Reviews · doi:10.1021/cr4001397 · Cited by 114 · see citing works
Ginsburg, D. S., Govind, C. K., & Hinnebusch, A. G. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01033-09 · Cited by 113 · see citing works
Intranuclear Distribution and Local Dynamics of RNA Polymerase II during Transcription Activation
Yao, J., Ardehali, M. B., Fecko, C. J., Webb, W. W., & Lis, J. T. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.10.017 · Cited by 111 · see citing works
Vojnic, E., Simon, B., Strahl, B. D., Sattler, M., & Cramer, P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500423200 · Cited by 99 · see citing works
Descostes, N., Heidemann, M., Spinelli, L., Schüller, R., Maqbool, M. A., Fenouil, R., Koch, F., Innocenti, C., Gut, M., Gut, I. G., et al. (2014) · eLife · doi:10.7554/elife.02105 · Cited by 92 · see citing works
Li, H., Zhang, Z., Wang, B., Zhang, J., Zhao, Y., & Jin, Y. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01667-06 · Cited by 87 · see citing works
Sun, M., Larivière, L., Dengl, S., Mayer, A., & Cramer, P. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.144568 · Cited by 87 · see citing works
Dissecting the role of low-complexity regions in the evolution of vertebrate proteins
Radó-Trilla, N., & Albà, M. M. (2012) · BMC Evolutionary Biology · doi:10.1186/1471-2148-12-155 · Cited by 86 · see citing works
Pol II CTD kinases Bur1 and Kin28 promote Spt5 CTR‐independent recruitment of Paf1 complex
Qiu, H., Hu, C., Gaur, N. A., & Hinnebusch, A. G. (2012) · The EMBO Journal · doi:10.1038/emboj.2012.188 · Cited by 82 · see citing works
Functional Unit of the RNA Polymerase II C-Terminal Domain Lies within Heptapeptide Pairs
Stiller, J. W., & Cook, M. S. (2004) · Eukaryotic Cell · doi:10.1128/ec.3.3.735-740.2004 · Cited by 79 · see citing works
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 · see citing works
The Cap and the 3′ Splice Site Similarly Affect Polyadenylation Efficiency
Cooke, C., & Alwine, J. C. (1996) · Molecular and Cellular Biology · doi:10.1128/mcb.16.6.2579 · Cited by 76 · see citing works
Rodríguez‐Molina, J. B., Tseng, S. C., Simonett, S. P., Taunton, J., & Ansari, A. Z. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.06.036 · Cited by 74 · see citing works
Moore, M. J., Schwartzfarb, E. M., Silver, P. A., & Yu, M. C. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.12.006 · Cited by 70 · see citing works
Kanagaraj, R., Hühn, D., MacKellar, A. L., Menigatti, M., Zheng, L., Urban, V., Shevelev, I., Greenleaf, A. L., & Janščák, P. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq697 · Cited by 70 · see citing works
Islam, M. N., Fox, D., Guo, R., Enomoto, T., & Wang, W. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.01583-09 · Cited by 69 · see citing works
H3K4 Trimethylation by Set1 Promotes Efficient Termination by the Nrd1-Nab3-Sen1 Pathway
Çizmecioğlu, N. T., Churchman, L. S., Vasiljeva, L., Weissman, J. S., & Buratowski, S. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.05590-11 · Cited by 69 · see citing works
Self-citationProtein modifications in transcription elongation
Fuchs, S. M., Laribee, R. N., & Strahl, B. D. (2008) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2008.07.008 · Cited by 65 · see citing works
DNA topology and transcription
Kouzine, F., Levens, D., & Baranello, L. (2014) · Nucleus · doi:10.4161/nucl.28909 · Cited by 65 · see citing works
Schwer, B., Bitton, D. A., Sánchez, A. M., Bähler, J., & Shuman, S. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1321842111 · Cited by 62 · see citing works
Conditional inactivation of mRNA capping enzyme affects yeast pre-mRNA splicing in vivo.
Schwer, B., & Shuman, S. (1996) · PubMed Central · Cited by 55 · see citing works
RNAP II CTD tyrosine 1 performs diverse functions in vertebrate cells
Hsin, J.-P., Li, W., Hoque, M., Tian, B., & Manley, J. L. (2014) · eLife · doi:10.7554/elife.02112 · Cited by 53 · see citing works
Strand‐specific, high‐resolution mapping of modified RNA polymerase II
Milligan, L., Huynh‐Thu, V. A., Delan‐Forino, C., Tuck, A., Petfalski, E., Lombraña, R., Sanguinetti, G., Kudla, G. R., & Tollervey, D. W. (2016) · Molecular Systems Biology · doi:10.15252/msb.20166869 · Cited by 52 · see citing works
Zhou, Y., Xia, X., & Lingle, C. J. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1500953112 · Cited by 50 · see citing works
Punctuation 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 · see citing works
Li, M., Xu, X., & Liu, Y. (2011) · Molecular and Cellular Biology · doi:10.1128/mcb.01137-10 · Cited by 48 · see citing works
Engineering an analog-sensitive CDK12 cell line using CRISPR/Cas
Bartkowiak, B., Yan, C. M., & Greenleaf, A. L. (2015) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2015.07.010 · Cited by 46 · see citing works
Chapman, A., & Agabian, N. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)37608-1 · Cited by 43 · see citing works
Mapping RNA exit channel on transcribing RNA polymerase II by FRET analysis
Chen, C., Chang, C., Yen, C., Chiu, M. T.-K., & Chang, W. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0811689106 · Cited by 42 · see citing works
Dias, J. D., Rito, T., Triglia, E. T., Kukalev, A., Ferrai, C., Chotalia, M., Brookes, E., Kimurâ, H., & Pombo, A. (2015) · eLife · doi:10.7554/elife.11215 · Cited by 38 · see citing works
Distributive O-GlcNAcylation on the Highly Repetitive C-Terminal Domain of RNA Polymerase II
Lü, L., Fan, D., Hu, C., Worth, M., Ma, Z., & Jiang, J. (2016) · Biochemistry · doi:10.1021/acs.biochem.5b01280 · Cited by 34 · see citing works
Topoisomerases, chromatin and transcription termination
Durand‐Dubief, M., Svensson, J. P., Persson, J., & Ekwall, K. (2011) · Transcription · doi:10.4161/trns.2.2.14411 · Cited by 34 · see citing works
Rosonina, E., Yurko, N., Li, W., Hoque, M., Tian, B., & Manley, J. L. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1412802111 · Cited by 33 · see citing works
Voß, K., Forné, I., Descostes, N., Hintermair, C., Schüller, R., Maqbool, M. A., Heidemann, M., Flatley, A., Imhof, A., Gut, M., et al. (2015) · Transcription · doi:10.1080/21541264.2015.1114983 · Cited by 28 · see citing works
The C-Terminal Domain of Rpb1 Functions on Other RNA Polymerase II Subunits
Suh, H., Hazelbaker, D. Z., Soares, L. M., & Buratowski, S. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.08.015 · Cited by 23 · see citing works
Liu, J., Fan, S., Lee, C., Greenleaf, A. L., & Zhou, P. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.460238 · Cited by 23 · see citing works
Hintermair, C., Voß, K., Forné, I., Heidemann, M., Flatley, A., Kremmer, E., Imhof, A., & Eick, D. (2016) · Scientific Reports · doi:10.1038/srep27401 · Cited by 23 · see citing works
Distinct requirement of RNA polymerase II CTD phosphorylations in budding and fission yeast
Cassart, C., Drogat, J., Migeot, V., & Hermand, D. (2012) · Transcription · doi:10.4161/trns.21066 · Cited by 23 · see citing works
Getting Access to Low-Complexity Domain Modifications
Schüller, R., & Eick, D. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2016.05.010 · Cited by 12 · see citing works
DNA Instability Maintains the Repeat Length of the Yeast RNA Polymerase II C-terminal Domain
Morrill, S., Exner, A. E., Babokhov, M., Reinfeld, B. I., & Fuchs, S. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.696252 · Cited by 9 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
Organizational principles of 3D genome architecture
Rowley, M. J., & Corces, V. G. (2018) · Nature Reviews Genetics · doi:10.1038/s41576-018-0060-8 · Cited by 1,171 · see citing works
The molecular language of membraneless organelles
Gomes, E., & Shorter, J. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.tm118.001192 · Cited by 763 · see citing works
Pol II phosphorylation regulates a switch between transcriptional and splicing condensates
Guo, Y. E., Manteiga, J. C., Henninger, J. E., Sabari, B. R., Dall’Agnese, A., Hannett, N. M., Spille, J.-H., Afeyan, L. K., Zamudio, A. V., Shrinivas, K., et al. (2019) · Nature · doi:10.1038/s41586-019-1464-0 · Cited by 676 · see citing works
Phase-separation mechanism for C-terminal hyperphosphorylation of RNA polymerase II
Lu, H., Yu, D., Hansen, A. S., Ganguly, S., Liu, R., Heckert, A. B., Darzacq, X., & Zhou, Q. (2018) · Nature · doi:10.1038/s41586-018-0174-3 · Cited by 576 · see citing works
Born to run: control of transcription elongation by RNA polymerase II
Chen, F. X., Smith, E. R., & Shilatifard, A. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0010-5 · Cited by 447 · see citing works
Mechanisms of lncRNA biogenesis as revealed by nascent transcriptomics
Nojima, T., & Proudfoot, N. J. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-021-00447-6 · Cited by 424 · see citing works
Regulation of Co-transcriptional Pre-mRNA Splicing by m6A through the Low-Complexity Protein hnRNPG
Zhou, K. I., Shi, H., Lyu, R., Wylder, A. C., Matuszek, Ż., Pan, J. N., He, C., Parisien, M., & Pan, T. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.07.005 · Cited by 385 · see citing works
Splicing and transcription touch base: co-transcriptional spliceosome assembly and function
Herzel, L., Ottoz, D. S. M., Alpert, T., & Neugebauer, K. M. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.63 · Cited by 356 · see citing works
Phase separation of ligand-activated enhancers licenses cooperative chromosomal enhancer assembly
Nair, S. J., Lu, Y., Meluzzi, D., Oh, S., Yang, F., Friedman, M. J., Wang, S. S., Suter, T., Alshareedah, I., Gamliel, A., et al. (2019) · Nature Structural & Molecular Biology · doi:10.1038/s41594-019-0190-5 · Cited by 366 · see citing works
Therapeutic Targeting of CDK12/CDK13 in Triple-Negative Breast Cancer
Quereda, V., Bayle, S., Vena, F., Frydman, S. M., Monastyrskyi, A., Roush, W. R., & Duckett, D. R. (2019) · Cancer Cell · doi:10.1016/j.ccell.2019.09.004 · Cited by 352 · see citing works
Zhang, C., Chen, L., Peng, D., Jiang, A., He, Y., Zeng, Y., Xie, C., Zhou, H., Luo, X., Liu, H., et al. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.06.017 · Cited by 333 · see citing works
Nucleated transcriptional condensates amplify gene expression
Wei, M., Chang, Y.-C., Shimobayashi, S. F., Shin, Y., Strom, A. R., & Brangwynne, C. P. (2020) · Nature Cell Biology · doi:10.1038/s41556-020-00578-6 · Cited by 330 · see citing works
Structure and mechanism of the RNA polymerase II transcription machineryPreprint
Schier, A. C., & Taatjes, D. J. (2020) · Genes & Development · doi:10.1101/gad.335679.119 · Cited by 301 · see citing works
Hidden codes in mRNA: Control of gene expression by m6A
Murakami, S., & Jaffrey, S. R. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.05.029 · Cited by 283 · see citing works
Liquid–liquid phase separation in tumor biology
Tong, X., Tang, R., Xu, J., Wang, W., Zhao, Y., Yu, X., & Shi, S. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01076-x · Cited by 256 · see citing works
Causes and consequences of RNA polymerase II stalling during transcript elongation
González, M. N., Blears, D., & Svejstrup, J. Q. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-00308-8 · Cited by 238 · see citing works
The PP2A-Integrator-CDK9 axis fine-tunes transcription and can be targeted therapeutically in cancer
Vervoort, S. J., Welsh, S. A., Devlin, J. R., Barbieri, E., Knight, D. A., Offley, S. R., Bjelosevic, S., Costacurta, M., Todorovski, I., Kearney, C. J., et al. (2021) · Cell · doi:10.1016/j.cell.2021.04.022 · Cited by 206 · see citing works
Alternative Splicing and Protein Diversity: Plants Versus Animals
Chaudhary, S., Khokhar, W., Jabre, I., Reddy, A. S. N., Byrne, L. J., Wilson, C. M., & Syed, N. H. (2019) · Frontiers in Plant Science · doi:10.3389/fpls.2019.00708 · Cited by 204 · see citing works
RNA polymerase II speed: a key player in controlling and adapting transcriptome composition
Muniz, L., Nicolas, E., & Trouche, D. (2021) · The EMBO Journal · doi:10.15252/embj.2020105740 · Cited by 203 · see citing works
“The CTD is the target of many post-translational modifications, yielding specific patterns (referred to as “the CTD code”), which are recognized by factors playing essential roles throughout the transcription cycle (Harlen & Churchman, 2017).”
The Mediator Complex: At the Nexus of RNA Polymerase II Transcription
Jerónimo, C., & Robert, F. (2017) · Trends in Cell Biology · doi:10.1016/j.tcb.2017.07.001 · Cited by 189 · see citing works
Ion homeostasis for salinity tolerance in plants: a molecular approach
Amin, I., Rasool, S., Mir, M. A., Wani, W., Masoodi, K. Z., & Ahmad, P. (2020) · Physiologia Plantarum · doi:10.1111/ppl.13185 · Cited by 186 · see citing works
The cooperative action of CSB, CSA, and UVSSA target TFIIH to DNA damage-stalled RNA polymerase II
van der Weegen, Y., Golan-Berman, H., Mevissen, T. E. T., Apelt, K., González‐Prieto, R., Goedhart, J., Heilbrun, E. E., Vertegaal, A. C. O., van den Heuvel, D., Walter, J. C., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-15903-8 · Cited by 177 · see citing works
Targeting transcription cycles in cancer
Vervoort, S., Devlin, J., Kwiatkowski, N., Teng, M.-X., Gray, N., & Johnstone, R. (2021) · Nature Reviews. Cancer · doi:10.1038/s41568-021-00411-8 · Cited by 140 · see citing works
Human TFIIH Kinase CDK7 Regulates Transcription-Associated Chromatin Modifications
Ebmeier, C. C., Erickson, B., Allen, B. L., Allen, M. A., Kim, H., Fong, N., Jacobsen, J. R., Liang, K., Shilatifard, A., Dowell, R. D., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.07.021 · Cited by 157 · see citing works
RNA-modifying proteins as anticancer drug targets
Boriack‐Sjodin, P. A., Ribich, S. A., & Copeland, R. A. (2018) · Nature Reviews Drug Discovery · doi:10.1038/nrd.2018.71 · Cited by 154 · see citing works
Anshabo, A. T., Milne, R. W., Wang, S., & Albrecht, H. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.678559 · Cited by 152 · see citing works
Phase separation of RNA-binding protein promotes polymerase binding and transcription
Shao, W., Bi, X., Pan, Y., Gao, B., Wu, J. F., Yin, Y., Liu, Z., Peng, M., Zhang, W., Jiang, X., et al. (2021) · Nature Chemical Biology · doi:10.1038/s41589-021-00904-5 · Cited by 147 · see citing works
RNA polymerase II activity revealed by GRO-seq and pNET-seq in Arabidopsis
Zhu, J., Liu, M., Liu, X., & Dong, Z. (2018) · Nature Plants · doi:10.1038/s41477-018-0280-0 · Cited by 147 · see citing works
Transcriptional Control of Circadian Rhythms and Metabolism: A Matter of Time and Space
Kim, Y. H., & Lazar, M. A. (2020) · Endocrine Reviews · doi:10.1210/endrev/bnaa014 · Cited by 146 · see citing works
Samata, M., & Akhtar, A. (2018) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-062917-011816 · Cited by 143 · see citing works
Genome-wide analyses of chromatin interactions after the loss of Pol I, Pol II, and Pol III
Jiang, Y., Huang, J. S., Lun, K., Li, B., Zheng, H., Li, Y., Zhou, R., Duan, W., Wang, C., Feng, Y., et al. (2020) · Genome biology · doi:10.1186/s13059-020-02067-3 · Cited by 136 · see citing works
The essential and multifunctional TFIIH complex
Rimel, J. K., & Taatjes, D. J. (2018) · Protein Science · doi:10.1002/pro.3424 · Cited by 137 · see citing works
Stress-induced nuclear condensation of NELF drives transcriptional downregulation
Rawat, P., Boehning, M., Hummel, B., Aprile-Garcia, F., Pandit, A. S., Eisenhardt, N., Khavaran, A., Niskanen, E. A., Vos, S. M., Palvimo, J. J., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.01.016 · Cited by 137 · see citing works
CDK12 controls G1/S progression by regulating RNAPII processivity at core DNA replication genes
Manavalan, A. P. C., Pilařová, K., Kluge, M., Bartholomeeusen, K., Rájecký, M., Oppelt, J., Khirsariya, P., Paruch, K., Krejčí, L., Friedel, C. C., et al. (2019) · EMBO Reports · doi:10.15252/embr.201847592 · Cited by 110 · see citing works
Dobrinić, P., Szczurek, A., & Klose, R. J. (2021) · Nature Structural & Molecular Biology · doi:10.1038/s41594-021-00661-y · Cited by 109 · see citing works
RNA and liquid-liquid phase separation
Guo, Q., Shi, X., & Wang, X. (2021) · Non-coding RNA Research · doi:10.1016/j.ncrna.2021.04.003 · Cited by 116 · see citing works
Transcription rate strongly affects splicing fidelity and cotranscriptionality in budding yeast
Aslanzadeh, V., Huang, Y., Sanguinetti, G., & Beggs, J. D. (2018) · Genome Research · doi:10.1101/gr.225615.117 · Cited by 109 · see citing works
Tracking chromatin state changes using nanoscale photo-proximity labelling
Seath, C. P., Burton, A. J., Sun, X., Lee, G., Kleiner, R. E., MacMillan, D. W. C., & Muir, T. W. (2023) · Nature · doi:10.1038/s41586-023-05914-y · Cited by 110 · see citing works
R-Loops Enhance Polycomb Repression at a Subset of Developmental Regulator Genes
Skourti-Stathaki, K., Triglia, E. T., Warburton, M., Voigt, P., Bird, A. P., & Pombo, A. (2019) · Molecular Cell · doi:10.1016/j.molcel.2018.12.016 · Cited by 109 · see citing works
Therapeutic targeting of transcriptional cyclin-dependent kinases
Galbraith, M. D., Bender, H., & Espinosa, J. M. (2018) · Transcription · doi:10.1080/21541264.2018.1539615 · Cited by 105 · see citing works
Anticancer mechanism of coumarin-based derivatives
Yadav, A. K., Shrestha, R. M., & Yadav, P. N. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116179 · Cited by 103 · see citing works
Puget, N., Miller, K. M., & Legube, G. (2019) · DNA repair · doi:10.1016/j.dnarep.2019.102661 · Cited by 90 · see citing works
Tyrosine kinase c-Abl couples RNA polymerase II transcription to DNA double-strand breaks
Burger, K., Schlackow, M., & Gullerová, M. (2019) · Nucleic Acids Research · doi:10.1093/nar/gkz024 · Cited by 88 · see citing works
Genomic regulation of transcription and RNA processing by the multitasking Integrator complex
Welsh, S. A., & Gardini, A. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00534-2 · Cited by 86 · see citing works
BAP1 constrains pervasive H2AK119ub1 to control the transcriptional potential of the genomePreprint
Fursova, N. A., Turberfield, A. H., Blackledge, N. P., Findlater, E. L., Lastuvkova, A., Huseyin, M. K., Dobrinić, P., & Klose, R. J. (2021) · Genes & Development · doi:10.1101/gad.347005.120 · Cited by 87 · see citing works
Transcription Factor DynamicsPreprint
Lu, F., & Lionnet, T. (2021) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a040949 · Cited by 84 · see citing works
Cryo-ET reveals the macromolecular reorganization of S. pombe mitotic chromosomes in vivo
Cai, S., Chen, C., Tan, Z. Y., Huang, Y., Shi, J. R., & Gan, L. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1720476115 · Cited by 78 · see citing works
Guo, C., Che, Z., Yue, J., Xie, P., Hao, S., Xie, W., Luo, Z., & Lin, C. (2020) · Science Advances · doi:10.1126/sciadv.aay4858 · Cited by 84 · see citing works
Suskiewicz, M. (2024) · Bioessays · doi:10.1002/bies.202300178 · Cited by 84 · see citing works
CDK12 phosphorylates 4E-BP1 to enable mTORC1-dependent translation and mitotic genome stabilityPreprint
Choi, S. H., Martinez, T. F., Kim, S., Donaldson, C. J., Shokhirev, M. N., Saghatelian, A., & Jones, K. A. (2019) · Genes & Development · doi:10.1101/gad.322339.118 · Cited by 83 · see citing works
Live-cell single particle imaging reveals the role of RNA polymerase II in histone H2A.Z eviction
Ranjan, A., Nguyen, V. Q., Liu, S., Wiśniewski, J., Kim, J. M., Tang, X., Mizuguchi, G., Elalaoui, E., Nickels, T. J., Jou, V., et al. (2020) · eLife · doi:10.7554/elife.55667 · Cited by 75 · see citing works
Nascent RNA and the Coordination of Splicing with TranscriptionPreprint
Neugebauer, K. M. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a032227 · Cited by 77 · see citing works
Chromatin dependencies in cancer and inflammation
Marazzi, I., Greenbaum, B. D., Low, D. H. P., & Guccione, E. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.113 · Cited by 80 · see citing works
RNA Targets Ribogenesis Factor WDR43 to Chromatin for Transcription and Pluripotency Control
Bi, X., Xu, Y., Li, T., Li, X., Li, W., Shao, W., Wang, K., Zhan, G., Wu, Z., Liu, W., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.05.007 · Cited by 79 · see citing works
Stochastic pausing at latent HIV-1 promoters generates transcriptional bursting
Tantale, K., García-Oliver, E., Robert, M.-C., L’Hostis, A., Yang, Y., Tsanov, N., Topno, R., Gostan, T., Kozulic-Pirher, A., Shrivastava, M. B., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24462-5 · Cited by 75 · see citing works
Ito, M., Tanaka, T., Toita, A., Uchiyama, N., Kokubo, H., Morishita, N., Klein, M. G., Zou, H., Murakami, M., Kondo, M., et al. (2018) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b00683 · Cited by 73 · see citing works
The cryoelectron microscopy structure of the human CDK-activating kinase
Greber, B. J., Perez-Bertoldi, J. M., Lim, K., Iavarone, A. T., Toso, D. B., & Nogales, E. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2009627117 · Cited by 72 · see citing works
Mechanisms of Transcription Elongation Factor DSIF (Spt4–Spt5)
Decker, T.-M. (2020) · Journal of Molecular Biology · doi:10.1016/j.jmb.2020.09.016 · Cited by 71 · see citing works
Zhang, Y., Yuan, J., Zhang, L., Chen, C., Wang, Y., Zhang, G., Li, P., Xie, S., Jiang, J., Zhu, J., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-20089-0 · Cited by 71 · see citing works
Structural Basis of Poxvirus Transcription: Vaccinia RNA Polymerase Complexes
Grimm, C., Hillen, H. S., Bedenk, K., Bartuli, J., Neyer, S., Zhang, Q., Hüttenhofer, A., Erlacher, M. D., Dienemann, C., Schlösser, A., et al. (2019) · Cell · doi:10.1016/j.cell.2019.11.024 · Cited by 69 · see citing works
Depicting HIV-1 Transcriptional Mechanisms: A Summary of What We Know
Dutilleul, A., Rodari, A., & Lint, C. M. V. (2020) · Viruses · doi:10.3390/v12121385 · Cited by 69 · see citing works
Landsverk, H. B., Sandquist, L. E., Bay, L. T. E., Steurer, B., Campsteijn, C., Landsverk, O. J. B., Marteijn, J. A. F., Petermann, E., Trinkle‐Mulcahy, L., & Syljuåsen, R. G. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108469 · Cited by 68 · see citing works
G 1 cyclin–Cdk promotes cell cycle entry through localized phosphorylation of RNA polymerase II
Kõivomägi, M., Swaffer, M. P., Turner, J. J., Marinov, G. K., & Skotheim, J. M. (2021) · Science · doi:10.1126/science.aba5186 · Cited by 67 · see citing works
Widespread and precise reprogramming of yeast protein–genome interactions in response to heat shockPreprint
Vinayachandran, V., Reja, R., Rossi, M. J., Park, B., Rieber, L., Mittal, C., Mahony, S., & Pugh, B. F. (2018) · Genome Research · doi:10.1101/gr.226761.117 · Cited by 67 · see citing works
Regulation of RAD51 at the Transcriptional and Functional Levels: What Prospects for Cancer Therapy?
Orhan, E., Velázquez, C., Tabet, I., Sardet, C., & Theillet, C. G. (2021) · Cancers · doi:10.3390/cancers13122930 · Cited by 67 · see citing works
Arginine Citrullination at the C-Terminal Domain Controls RNA Polymerase II Transcription
Sharma, P., Lioutas, A., Fernández‐Fuentes, N., Quilez, J., Carbonell‐Caballero, J., Wright, R. H. G., Vona, C. D., Dily, F. L., Schüller, R., Eick, D., et al. (2018) · Molecular Cell · doi:10.1016/j.molcel.2018.10.016 · Cited by 66 · see citing works
Influenza virus infection causes global RNAPII termination defects
Zhao, N., Sebastiano, V., Moshkina, N., Mena, I., Hultquist, J. F., Jimenez‐Morales, D., Ma, Y., Rialdi, A., Albrecht, R. A., Fenouil, R., et al. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-018-0124-7 · Cited by 61 · see citing works
Beato, M., & Sharma, P. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21041351 · Cited by 61 · see citing works
Live imaging of transcription sites using an elongating RNA polymerase II–specific probe
Uchino, S., Ito, Y., Sato, Y., Handa, T., Ohkawa, Y., Tokunaga, M., & Kimurâ, H. (2021) · The Journal of Cell Biology · doi:10.1083/jcb.202104134 · Cited by 58 · see citing works
The Integrator complex at the crossroad of coding and noncoding RNA
Kirstein, N., Santos, H. G. D., Blumenthal, E., & Shiekhattar, R. (2020) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2020.11.003 · Cited by 59 · see citing works
The Promise and Current Status of CDK12/13 Inhibition for the Treatment of Cancer
Tadesse, S., Duckett, D. R., & Monastyrskyi, A. (2020) · Future Medicinal Chemistry · doi:10.4155/fmc-2020-0240 · Cited by 59 · see citing works
Enserink, J. M., & Chymkowitch, P. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031293 · Cited by 59 · see citing works
RNA Pol II Length and Disorder Enable Cooperative Scaling of Transcriptional Bursting
Quintero-Cadena, P., Lenstra, T. L., & Sternberg, P. W. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.05.030 · Cited by 58 · see citing works
Lu, F., Portz, B., & Gilmour, D. S. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.01.008 · Cited by 57 · see citing works
Distinct patterns of histone acetyltransferase and Mediator deployment at yeast protein-coding genesPreprint
Bruzzone, M. J., Grünberg, S., Kubik, S., Zentner, G. E., & Shore, D. (2018) · Genes & Development · doi:10.1101/gad.312173.118 · Cited by 57 · see citing works
Protein kinase CK2 – diverse roles in cancer cell biology and therapeutic promise
Trembley, J. H., Kren, B. T., Afzal, M., Scaria, G. S., Klein, M. A., & Ahmed, K. (2022) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-022-04558-2 · Cited by 56 · see citing works
Forero-Quintero, L. S., Raymond, W., Handa, T., Saxton, M. N., Morisaki, T., Kimurâ, H., Bertrand, É., Munsky, B. E., & Stasevich, T. J. (2021) · Nature Communications · doi:10.1038/s41467-021-23417-0 · Cited by 58 · see citing works
The Integrator Complex in Transcription and Development
Mendoza-Figueroa, M. S., Tatomer, D. C., & Wilusz, J. E. (2020) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2020.07.004 · Cited by 54 · see citing works
Angel or Devil ? - CDK8 as the new drug target
Wu, D., Zhang, Z., Chen, X., Yan, Y., & Liu, X. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.113043 · Cited by 53 · see citing works
BRD4: a general regulator of transcription elongation
Altendorfer, E., Mochalova, Y., & Mayer, A. (2022) · Transcription · doi:10.1080/21541264.2022.2108302 · Cited by 53 · see citing works
PHF3 regulates neuronal gene expression through the Pol II CTD reader domain SPOC
Appel, L.-M., Franke, V., Bruno, M., Grishkovskaya, I., Kasiliauskaitė, A., Kaufmann, T., Schoeberl, U. E., Puchinger, M. G., Kostrhon, S., Ebenwaldner, C., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-26360-2 · Cited by 53 · see citing works
Enhancer-Promoter Interaction of SELF PRUNING 5G Shapes Photoperiod Adaptation
Zhang, S., Jiao, Z., Liu, L., Wang, K., Zhong, D., Li, S., Zhao, T., Xu, X., & Cui, X. (2018) · PLANT PHYSIOLOGY · doi:10.1104/pp.18.01137 · Cited by 51 · see citing works
CDK11 is required for transcription of replication-dependent histone genes
Gajdušková, P., Mozos, I. R. D. L., Rájecký, M., Hluchý, M., Ule, J., & Blažek, D. (2020) · Nature Structural & Molecular Biology · doi:10.1038/s41594-020-0406-8 · Cited by 51 · see citing works
Coordinated Control of rRNA Processing by RNA Polymerase I
Scull, C. E., & Schneider, D. A. (2019) · Trends in Genetics · doi:10.1016/j.tig.2019.07.002 · Cited by 51 · see citing works
Cesari, E., Ciucci, A., Pieraccioli, M., Caggiano, C., Nero, C., Bonvissuto, D., Sillano, F., Buttarelli, M., Piermattei, A., Loverro, M., et al. (2023) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-023-02682-5 · Cited by 49 · see citing works
TFIIH: A multi-subunit complex at the cross-roads of transcription and DNA repair
Kolesnikova, O., Radu, L., & Poterszman, A. (2019) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2019.01.003 · Cited by 50 · see citing works
Xu, J., Li, H., Wang, X., Huang, J., Li, S., Liu, C., Dong, R., Zhu, G., Duan, C., Jiang, F., et al. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112424 · Cited by 50 · see citing works
Emerging Properties and Functional Consequences of Noncoding Transcription.
Ard, R., Allshire, R. C., & Marquardt, S. (2017) · Europe PMC (PubMed Central) · doi:10.1534/genetics.117.300095 · Cited by 46 · see citing works
RNA Polymerase II CTD Tyrosine 1 Is Required for Efficient Termination by the Nrd1-Nab3-Sen1 Pathway
Collin, P., Jerónimo, C., Poitras, C., & Robert, F. (2019) · Molecular Cell · doi:10.1016/j.molcel.2018.12.002 · Cited by 49 · see citing works
Chromatin-based mechanisms to coordinate convergent overlapping transcription
Inagaki, S., Takahashi, M. M., Takashima, K., Oya, S., & Kakutani, T. (2021) · Nature Plants · doi:10.1038/s41477-021-00868-3 · Cited by 48 · see citing works
Sousa, L. B. D. A. E., Jonkers, I. H., Syx, L., Dunkel, I., Chaumeil, J., Picard, C., Forêt, B., Chen, C., Lis, J. T., Heard, É., et al. (2019) · Genome Research · doi:10.1101/gr.245027.118 · Cited by 44 · see citing works
CDK8 Fine-Tunes IL-6 Transcriptional Activities by Limiting STAT3 Resident Time at the Gene Loci
Martínez‐Fábregas, J., Wang, L., Pöhler, E., Cozzani, A., Wilmes, S., Kazemian, M., Mitra, S., & Moraga, I. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108545 · Cited by 47 · see citing works
Naro, C., Bielli, P., & Sette, C. (2021) · FEBS Journal · doi:10.1111/febs.16057 · Cited by 47 · see citing works
Cyclin‐dependent kinases: Masters of the eukaryotic universe
Pluta, A. J., Studniarek, C., Murphy, S., & Norbury, C. J. (2023) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1816 · Cited by 45 · see citing works
Acetylation of BMAL1 by TIP60 controls BRD4-P-TEFb recruitment to circadian promoters
Petkau, N., Budak, H., Zhou, X., Oster, H., & Gregor Eichele, C. (2019) · eLife · doi:10.7554/elife.43235 · Cited by 46 · see citing works
Chromatin regulation of transcriptional enhancers and cell fate by the Sotos syndrome gene NSD1
Sun, Z., Lin, Y., Islam, M. T., Koche, R. P., Hedehus, L., Liu, D., Huang, C., Vierbuchen, T., Sawyers, C. L., & Helin, K. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.06.007 · Cited by 44 · see citing works
Structural basis of INTAC-regulated transcription
Zheng, H., Jin, Q., Wang, X., Qi, Y., Liu, W., Ren, Y., Zhao, D., Chen, F., Cheng, J., Chen, X., et al. (2023) · Protein & Cell · doi:10.1093/procel/pwad010 · Cited by 45 · see citing works
Eom, H., Park, S. J., Kim, M. K., Kim, H., Kang, H., & Lee, I. (2017) · The Plant Journal · doi:10.1111/tpj.13758 · Cited by 44 · see citing works
Pai, A. A., & Luca, F. (2018) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1503 · Cited by 47 · see citing works
Key Concepts and Challenges in Archaeal Transcription
Blombach, F., Matelska, D., Fouqueau, T., Cackett, G., & Werner, F. (2019) · Journal of Molecular Biology · doi:10.1016/j.jmb.2019.06.020 · Cited by 43 · see citing works
- Authors
- Harlen, K. M., & Churchman, L. S.
- Affiliations
- Harvard University (US)
- Corresponding author
- Churchman, L. Stirling
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2017-03-01
- Volume
- 18
- Issue
- 4
- Pages
- 263-273
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W2594707272
- Cited by
- 499
- References
- 159
- Citations by year
- 2026: 40 · 2025: 46 · 2024: 70 · 2023: 65 · 2022: 51 · 2021: 66 · 2020: 65 · 2019: 44 · 2018: 35 · 2017: 17
- FWCI
- 4.15
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Human Genome Research Institute (R01HG007173)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Keywords
- RNA polymerase II, C-terminal domain, post-translational modification, transcriptional regulation, phase separation, low-complexity domains
- MeSH terms
- Protein Domains, Gene Expression Regulation, Humans, Phosphorylation, Protein Processing, Post-Translational, RNA Polymerase II, Transcription, Genetic
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review