The end of the message: multiple protein–RNA interactions define the mRNA polyadenylation site

The Spliceosome: Design Principles of a Dynamic RNP Machine

Wahl, M. C., Will, C. L., & Lührmann, R. (2009) · Cell · doi:10.1016/j.cell.2009.02.009 · Cited by 2,665 · see citing works

Widespread Shortening of 3′UTRs by Alternative Cleavage and Polyadenylation Activates Oncogenes in Cancer Cells

Mayr, C., & Bartel, D. P. (2009) · Cell · doi:10.1016/j.cell.2009.06.016 · Cited by 1,613 · see citing works

HITS-CLIP yields genome-wide insights into brain alternative RNA processing

Licatalosi, D. D., Mele, A., Fak, J. J., Ule, J., Kayikci, M., Chi, S. W., Clark, T. A., Schweitzer, A. C., Blume, J. E., Wang, X., et al. (2008) · Nature · doi:10.1038/nature07488 · Cited by 1,352 · cited 1× · see citing works

Proliferating Cells Express mRNAs with Shortened 3' Untranslated Regions and Fewer MicroRNA Target Sites

Sandberg, R., Neilson, J. R., Sarma, A., Sharp, P. A., & Burge, C. B. (2008) · Science · doi:10.1126/science.1155390 · Cited by 1,349 · see citing works

IFITM Proteins Mediate the Innate Immune Response to Influenza A H1N1 Virus, West Nile Virus and Dengue Virus

Brass, A., Huang, I.-C., Benita, Y., John, S., Krishnan, M. N., Feeley, E., Ryan, B., Weyer, J., van der Weyden, L., Fikrig, E., et al. (2009) · Cell · doi:10.1016/j.cell.2009.12.017 · Cited by 1,292 · see citing works

Integrating mRNA Processing with Transcription

Proudfoot, N. J., Furger, A., & Dye, M. J. (2002) · Cell · doi:10.1016/s0092-8674(02)00617-7 · Cited by 1,084 · see citing works

Context-dependent control of alternative splicing by RNA-binding proteins

Fu, X.-D., & Ares, M. (2014) · Nature Reviews Genetics · doi:10.1038/nrg3778 · Cited by 1,044 · see citing works

Formation of mRNA 3′ Ends in Eukaryotes: Mechanism, Regulation, and Interrelationships with Other Steps in mRNA Synthesis

Zhao, J., Hyman, L. E., & Moore, C. L. (1999) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.63.2.405-445.1999 · Cited by 1,024 · see citing works

Large-Scale Proteomic Analysis of the Human SpliceosomePreprint

Rappsilber, J., Ryder, U., Lamond, A. I., & Mann, M. (2002) · Genome Research · doi:10.1101/gr.473902 · Cited by 945 · see citing works

The General Transcription Machinery and General Cofactors

Thomas, M. C., & Chiang, C. (2006) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230600648736 · Cited by 923 · see citing works

Comprehensive proteomic analysis of the human spliceosome

Zhou, Z., Licklider, L. J., Gygi, S. P., & Reed, R. (2002) · Nature · doi:10.1038/nature01031 · Cited by 884 · see citing works

Alternative cleavage and polyadenylation: extent, regulation and function

Elkon, R., Ugalde, A. P., & Agami, R. (2013) · Nature Reviews Genetics · doi:10.1038/nrg3482 · Cited by 805 · see citing works

Mechanism and regulation of mRNA polyadenylation

Colgan, D. F., & Manley, J. L. (1997) · Genes & Development · doi:10.1101/gad.11.21.2755 · Cited by 784 · see citing works

Metabolism and regulation of canonical histone mRNAs: life without a poly(A) tail

Marzluff, W. F., Wagner, E. J., & Duronio, R. J. (2008) · Nature Reviews Genetics · doi:10.1038/nrg2438 · Cited by 768 · see citing works

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 · see citing works

Patterns of Variant Polyadenylation Signal Usage in Human GenesPreprint

Beaudoing, E., Freier, S. M., Wyatt, J. R., Claverie, J., & Gautheret, D. (2000) · Genome Research · doi:10.1101/gr.10.7.1001 · Cited by 676 · see citing works

SR proteins and splicing control.Preprint

Manley, J. L., & Tacke, R. (1996) · Genes & Development · doi:10.1101/gad.10.13.1569 · Cited by 673 · see citing works

U1 snRNP protects pre-mRNAs from premature cleavage and polyadenylation

Kaida, D., Berg, M. G., Younis, I., Kasim, M., Singh, L. N., Wan, L., & Dreyfuss, G. (2010) · Nature · doi:10.1038/nature09479 · Cited by 638 · see citing works

Influenza Virus NS1 Protein Interacts with the Cellular 30 kDa Subunit of CPSF and Inhibits 3′ End Formation of Cellular Pre-mRNAs

Nemeroff, M. E., Barabino, S. M. L., Li, Y., Keller, W., & Krug, R. M. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80099-4 · Cited by 623 · see citing works

Ending the message: poly(A) signals then and nowPreprint

Proudfoot, N. J. (2011) · Genes & Development · doi:10.1101/gad.17268411 · Cited by 607 · see citing works

Progressive lengthening of 3′ untranslated regions of mRNAs by alternative polyadenylation during mouse embryonic development

Ji, Z., Lee, J. Y., Pan, Z., Jiang, B., & Tian, B. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900028106 · Cited by 595 · see citing works

RNA polymerase II and the integration of nuclear eventsPreprint

Hirose, Y., & Manley, J. L. (2000) · Genes & Development · doi:10.1101/gad.14.12.1415 · Cited by 575 · see citing works

Molecular Architecture of the Human Pre-mRNA 3′ Processing Complex

Shi, Y., Giammartino, D. C. D., Taylor, D. J., Sarkeshik, A., Rice, W. J., Yates, J. R., Frank, J., & Manley, J. L. (2009) · Molecular Cell · doi:10.1016/j.molcel.2008.12.028 · Cited by 560 · see citing works

Rules of engagement: co-transcriptional recruitment of pre-mRNA processing factors

Bentley, D. L. (2005) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2005.04.006 · Cited by 489 · see citing works

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 464 · see citing works

CFIm25 links alternative polyadenylation to glioblastoma tumour suppression

Masamha, C. P., Xia, Z., Yang, J., Albrecht, T. R., Li, M., Shyu, A., Li, W., & Wagner, E. J. (2014) · Nature · doi:10.1038/nature13261 · Cited by 449 · see citing works

Genome-Wide Analysis of MEF2 Transcriptional Program Reveals Synaptic Target Genes and Neuronal Activity-Dependent Polyadenylation Site Selection

Flavell, S. W., Kim, T.-K., Gray, J. M., Harmin, D. A., Hemberg, M., Hong, E. J., Markenscoff-Papadimitriou, E., Bear, D. M., & Greenberg, M. E. (2008) · Neuron · doi:10.1016/j.neuron.2008.11.029 · Cited by 440 · see citing works

Complex and dynamic landscape of RNA polyadenylation revealed by PAS-Seq

Shepard, P. J., Choi, E., Lu, J., Flanagan, L. A., Hertel, K. J., & Shi, Y. (2011) · RNA · doi:10.1261/rna.2581711 · Cited by 432 · see citing works

Nova-1 Regulates Neuron-Specific Alternative Splicing and Is Essential for Neuronal Viability

Jensen, K. B., Dredge, B. K., Stefani, G., Zhong, R., Buckanovich, R. J., Okano, H. J., Yang, Y. Y. L., & Darnell, R. B. (2000) · Neuron · doi:10.1016/s0896-6273(00)80900-9 · Cited by 426 · see citing works

Recognition of the mRNA AU-rich element by the zinc finger domain of TIS11d

Hudson, B. P., Martinez‐Yamout, M. A., Dyson, H. J., & Wright, P. E. (2004) · Nature Structural & Molecular Biology · doi:10.1038/nsmb738 · Cited by 367 · see citing works

Genome-wide Analysis of Pre-mRNA 3′ End Processing Reveals a Decisive Role of Human Cleavage Factor I in the Regulation of 3′ UTR Length

Martin, G., Gruber, A. R., Keller, W., & Zavolan, M. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.05.003 · Cited by 361 · see citing works

The Poly(A)-Binding Protein Nuclear 1 Suppresses Alternative Cleavage and Polyadenylation Sites

Jenal, M., Elkon, R., Loayza‐Puch, F., van Haaften, G. W., Kühn, U., Menzies, F. M., Vrielink, J. A. F. O., Bos, A., Drost, J., Rooijers, K., et al. (2012) · Cell · doi:10.1016/j.cell.2012.03.022 · Cited by 338 · see citing works

Alternative cleavage and polyadenylation: the long and short of it

Tian, B., & Manley, J. L. (2013) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2013.03.005 · Cited by 307 · see citing works

Loss of MBNL Leads to Disruption of Developmentally Regulated Alternative Polyadenylation in RNA-Mediated Disease

Batra, R., Charizanis, K., Manchanda, M., Mohan, A., Li, M., Finn, D. J., Goodwin, M., Zhang, C., Sobczak, K., Thornton, C. A., et al. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.08.027 · Cited by 292 · see citing works

U1 snRNP Inhibits Pre-mRNA Polyadenylation through a Direct Interaction between U1 70K and Poly(A) Polymerase

Gunderson, S., Polycarpou‐Schwarz, M., & Mattaj, I. W. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80026-x · Cited by 279 · see citing works

Gene-specific requirement for P-TEFb activity and RNA polymerase II phosphorylation within the p53 transcriptional programPreprint

Gomes, N. P., Bjerke, G. A., Llorente, B., Szostek, S. A., Emerson, B. M., & Espinosa, J. M. (2006) · Genes & Development · doi:10.1101/gad.1398206 · Cited by 266 · see citing works

Human Fip1 is a subunit of CPSF that binds to U‐rich RNA elements and stimulates poly(A) polymerase

Kaufmann, I., Martin, G., Friedlein, A., Langen, H., & Keller, W. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600070 · Cited by 257 · see citing works

The 160-kD subunit of human cleavage-polyadenylation specificity factor coordinates pre-mRNA 3'-end formation.Preprint

Murthy, K. G. K., & Manley, J. L. (1995) · Genes & Development · doi:10.1101/gad.9.21.2672 · Cited by 254 · see citing works

Bioinformatic identification of candidate cis-regulatory elements involved in human mRNA polyadenylation

HU, J., Lutz, C. S., Wilusz, J., & Tian, B. (2005) · RNA · doi:10.1261/rna.2107305 · Cited by 249 · see citing works

Complex Protein Interactions within the Human Polyadenylation Machinery Identify a Novel Component

Takagaki, Y., & Manley, J. L. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.5.1515-1525.2000 · Cited by 248 · see citing works

Signals for pre‐mRNA cleavage and polyadenylation

Tian, B., & Graber, J. H. (2011) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.116 · Cited by 237 · see citing works

The 64-kilodalton subunit of the CstF polyadenylation factor binds to pre-mRNAs downstream of the cleavage site and influences cleavage site location.

MacDonald, C. C., Wilusz, J., & Shenk, T. E. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.10.6647 · Cited by 234 · see citing works

A multisubunit factor, CstF, is required for polyadenylation of mammalian pre-mRNAs.Preprint

Takagaki, Y., Manley, J. L., MacDonald, C. C., Wilusz, J., & Shenk, T. E. (1990) · Genes & Development · doi:10.1101/gad.4.12a.2112 · Cited by 232 · 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

A Mechanism for the Regulation of Pre-mRNA 3′ Processing by Human Cleavage Factor Im

Brown, K. M., & Gilmartin, G. M. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00453-2 · Cited by 226 · see citing works

Position-dependent splicing activation and repression by SR and hnRNP proteins rely on common mechanisms

Erkelenz, S., Mueller, W. F., Evans, M. S., Busch, A., Schöneweis, K., Hertel, K. J., & Schaal, H. (2012) · RNA · doi:10.1261/rna.037044.112 · Cited by 226 · see citing works

CPSF30 and Wdr33 directly bind to AAUAAA in mammalian mRNA 3′ processingPreprint

Chan, S. L., Huppertz, I., Yao, C., Weng, L., Moresco, J. J., Yates, J. R., Ule, J., Manley, J. L., & Shi, Y. (2014) · Genes & Development · doi:10.1101/gad.250993.114 · Cited by 225 · see citing works

Four factors are required for 3'-end cleavage of pre-mRNAs.Preprint

Takagaki, Y., Ryner, L. C., & Manley, J. L. (1989) · Genes & Development · doi:10.1101/gad.3.11.1711 · Cited by 223 · see citing works

The BARD1-CstF-50 Interaction Links mRNA 3′ End Formation to DNA Damage and Tumor Suppression

Kleiman, F. E., & Manley, J. L. (2001) · Cell · doi:10.1016/s0092-8674(01)00270-7 · Cited by 215 · see citing works

Reconstitution of CPSF active in polyadenylation: recognition of the polyadenylation signal by WDR33Preprint

Schönemann, L., Kühn, U., Martin, G., Schäfer, P., Gruber, A. R., Keller, W., Zavolan, M., & Wahle, E. (2014) · Genes & Development · doi:10.1101/gad.250985.114 · Cited by 215 · see citing works

Alternative polyadenylation: New insights from global analyses

Shi, Y. (2012) · RNA · doi:10.1261/rna.035899.112 · Cited by 212 · see citing works

Purification and Characterization of Human Cleavage Factor Im Involved in the 3′ End Processing of Messenger RNA Precursors

Rüegsegger, U., Beyer, K., & Keller, W. D. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.11.6107 · Cited by 210 · see citing works

Transcriptome-wide analyses of CstF64–RNA interactions in global regulation of mRNA alternative polyadenylation

Yao, C., Biesinger, J., Wan, J., Weng, L., Xing, Y., Xie, X. S., & Shi, Y. (2012) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1211101109 · Cited by 209 · see citing works

3′ cleavage and polyadenylation of mRNA precursors in vitro requires a poly(A) polymerase, a cleavage factor, and a snRNP

Christofori, G., & Keller, W. D. (1988) · Cell · doi:10.1016/s0092-8674(88)91263-9 · Cited by 206 · see citing works

RNA Recognition by the Human Polyadenylation Factor CstF

Takagaki, Y., & Manley, J. L. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.7.3907 · Cited by 205 · see citing works

Autoregulation of TDP-43 mRNA levels involves interplay between transcription, splicing, and alternative polyA site selectionPreprint

Avendaño-Vázquez, S. E., Dhir, A., Bembich, S., Buratti, E., Proudfoot, N. J., & Baralle, F. E. (2012) · Genes & Development · doi:10.1101/gad.194829.112 · Cited by 205 · see citing works

An interaction between U2AF 65 and CF Im links the splicing and 3′ end processing machineries

Millevoi, S., Loulergue, C., Dettwiler, S., Karaa, Z. S., Keller, W., Antoniou, M. N., & Vagner, S. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601331 · Cited by 203 · see citing works

Cleavage and polyadenylation factor CPF specifically interacts with the pre‐mRNA 3′ processing signal AAUAAA.

Keller, W., Bienroth, S., Lang, K. M., & Christofori, G. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb05002.x · Cited by 202 · see citing works

Direct Interactions between Subunits of CPSF and the U2 snRNP Contribute to the Coupling of Pre-mRNA 3′ End Processing and Splicing

Kyburz, A., Friedlein, A., Langen, H., & Keller, W. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.05.037 · Cited by 198 · see citing works

Human Pre-mRNA Cleavage Factor Im Is Related to Spliceosomal SR Proteins and Can Be Reconstituted In Vitro from Recombinant Subunits

Rüegsegger, U., Blank, D., & Keller, W. D. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80025-8 · Cited by 183 · see citing works

Essential role for the interaction between hnRNP H/F and a G quadruplex in maintaining p53 pre-mRNA 3′-end processing and function during DNA damagePreprint

Decorsière, A., Cayrel, A., Vagner, S., & Millevoi, S. (2011) · Genes & Development · doi:10.1101/gad.607011 · Cited by 178 · see citing works

The CPSF30 Binding Site on the NS1A Protein of Influenza A Virus Is a Potential Antiviral Target

Twu, K. Y., Noah, D. L., Rao, P., Kuo, R.-L., & Krug, R. M. (2006) · Journal of Virology · doi:10.1128/jvi.80.8.3957-3965.2006 · Cited by 174 · see citing works

Characterization of the multisubunit cleavage-polyadenylation specificity factor from calf thymus.

Murthy, K. G. K., & Manley, J. L. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42111-4 · Cited by 169 · see citing works

The 30-kD subunit of mammalian cleavage and polyadenylation specificity factor and its yeast homolog are RNA-binding zinc finger proteins.Preprint

Barabino, S. M. L., Hübner, W., Jenny, A., Minvielle-Sébastia, L., & Keller, W. (1997) · Genes & Development · doi:10.1101/gad.11.13.1703 · Cited by 169 · see citing works

Purification of the cleavage and polyadenylation factor involved in the 3'-processing of messenger RNA precursors.

Bienroth, S., Wahle, E., Suter‐Crazzolara, C., & Keller, W. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)55058-4 · Cited by 168 · see citing works

Fip1 regulates mRNA alternative polyadenylation to promote stem cell self‐renewal

Lackford, B. L., Yao, C., Charles, G. M., Weng, L., Zheng, X., Choi, E., Xie, X. S., Wan, J., Xing, Y., Freudenberg, J., et al. (2014) · The EMBO Journal · doi:10.1002/embj.201386537 · Cited by 166 · see citing works

CPEB1 coordinates alternative 3′-UTR formation with translational regulation

Bava, F.-A., Eliscovich, C., Ferreira, P. G., Miñana, B., Ben-Dov, C., Guigó, R., Valcárcel, J., & Méndez, R. (2013) · Nature · doi:10.1038/nature11901 · Cited by 164 · see citing works

Recognition of GU‐rich polyadenylation regulatory elements by human CstF‐64 protein

Pérez‐Cañadillas, J. M., & Varani, G. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg259 · Cited by 163 · see citing works

Polypyrimidine Tract Binding Protein Modulates Efficiency of Polyadenylation

Castelo‐Branco, P., Furger, A., Wollerton, M., Smith, C. W. J., Moreira, A., & Proudfoot, N. J. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.10.4174-4183.2004 · Cited by 162 · see citing works

Downstream elements of mammalian pre-mRNA polyadenylation signals: primary, secondary and higher-order structures

Zarudnaya, M. I. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg241 · Cited by 162 · see citing works

Intronic splicing enhancers, cognate splicing factors and context-dependent regulation rules

Wang, Y., Ma, M., Xiao, X. G., & Wang, Z. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2377 · Cited by 159 · see citing works

Crystal Structure of a Human Cleavage Factor CFIm25/CFIm68/RNA Complex Provides an Insight into Poly(A) Site Recognition and RNA Looping

Yang, Q., Coseno, M., Gilmartin, G. M., & Doublié, S. (2011) · Structure · doi:10.1016/j.str.2010.12.021 · Cited by 158 · see citing works

Cleavage factor Imis a key regulator of 3′ UTR length

Gruber, A. R., Martin, G., Keller, W., & Zavolan, M. (2012) · RNA Biology · doi:10.4161/rna.22570 · Cited by 156 · see citing works

Structural basis of UGUA recognition by the Nudix protein CFI m 25 and implications for a regulatory role in mRNA 3′ processing

Yang, Q., Gilmartin, G. M., & Doublié, S. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1000848107 · Cited by 154 · see citing works

Pre‐mRNA 3′‐end processing complex assembly and function

Chan, S., Choi, E., & Shi, Y. (2011) · WIREs RNA · doi:10.1002/wrna.54 · Cited by 147 · see citing works

Yhh1p/Cft1p directly links poly(A) site recognition and RNA polymerase II transcription termination

Dichtl, B., Blank, D., Sadowski, M., Hübner, W., Weiser, S., & Keller, W. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf390 · Cited by 134 · see citing works

Hu Proteins Regulate Polyadenylation by Blocking Sites Containing U-rich Sequences

Zhu, H., Zhou, H.-L., Hasman, R. A., & Lou, H. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m609349200 · Cited by 131 · see citing works

A Core Complex of CPSF73, CPSF100, and Symplekin May Form Two Different Cleavage Factors for Processing of Poly(A) and Histone mRNAs

Sullivan, K. D., Steiniger, M., & Marzluff, W. F. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.04.024 · Cited by 130 · see citing works

Involvement of the carboxyl terminus of vertebrate poly(A) polymerase in U1A autoregulation and in the coupling of splicing and polyadenylation.Preprint

Gunderson, S., Vagner, S., Polycarpou‐Schwarz, M., & Mattaj, I. W. (1997) · Genes & Development · doi:10.1101/gad.11.6.761 · Cited by 130 · see citing works

PACT is a negative regulator of p53 and essential for cell growth and embryonic development

Li, L., Deng, B., Xing, G., Teng, Y., Tian, C., Cheng, X., Yin, X., Yang, J., Gao, X. J., Zhu, Y., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0701916104 · Cited by 113 · see citing works

Two distinct forms of the 64,000 M r protein of the cleavage stimulation factor are expressed in mouse male germ cells

Wallace, A. M., Dass, B., Ravnik, S. E., Tonk, V. S., Jenkins, N. A., Gilbert, D. J., Copeland, N. G., & MacDonald, C. C. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.12.6763 · Cited by 113 · see citing works

Molecular analyses of two poly(A) site-processing factors that determine the recognition and efficiency of cleavage of the pre-mRNA.

Gilmartin, G. M., & Nevins, J. R. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.5.2432 · Cited by 112 · see citing works

Gemin5-snRNA interaction reveals an RNA binding function for WD repeat domains

Lau, C.-K., Bachorik, J. L., & Dreyfuss, G. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1584 · Cited by 104 · see citing works

The 64-Kilodalton Subunit of the CstF Polyadenylation Factor Binds to Pre-mRNAs Downstream of the Cleavage Site and Influences Cleavage Site Location

MacDonald, C. C., Wilusz, J., & Shenk, T. E. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.10.6647-6654.1994 · Cited by 97 · see citing works

RBBP6 isoforms regulate the human polyadenylation machinery and modulate expression of mRNAs with AU-rich 3′ UTRsPreprint

Giammartino, D. C. D., Li, W., Ogami, K., Yashinskie, J. J., Hoque, M., Tian, B., & Manley, J. L. (2014) · Genes & Development · doi:10.1101/gad.245787.114 · Cited by 95 · see citing works

PACT: cloning and characterization of a cellular p53 binding protein that interacts with Rb

Simons, A., Melamed‐Bessudo, C., Wolkowicz, R., Sperling, J. M., Sperling, R., Eisenbach, L., & Rotter, V. (1997) · Oncogene · doi:10.1038/sj.onc.1200825 · Cited by 93 · see citing works

ELAV Links Paused Pol II to Alternative Polyadenylation in the Drosophila Nervous System

Oktaba, K., Zhang, W., Lotz, T. S., Jun, D. J., Lemke, S. B., Ng, S., Esposito, E., Levine, M., & Hilgers, V. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.11.024 · Cited by 92 · see citing works

Developmental regulation of transcription initiation: more than just changing the actors

Müller, F., Zaucker, A., & Tora, L. (2010) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2010.06.004 · Cited by 89 · see citing works

Recent advances in understanding the structure and function of general transcription factor TFIID

Cler, É., Pápai, G., Schultz, P., & Davidson, I. (2009) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-009-0009-3 · Cited by 88 · see citing works

Crystal Structure of Murine CstF-77: Dimeric Association and Implications for Polyadenylation of mRNA Precursors

Bai, Y., Aupérin, T. C., Chou, C., Chang, G., Manley, J. L., & Tong, L. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.01.034 · Cited by 88 · 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

The RBBP6/ZBTB38/MCM10 Axis Regulates DNA Replication and Common Fragile Site Stability

Miotto, B., Chibi, M., Xie, P., Koundrioukoff, S., Moolman-Smook, H., Pugh, D. J. R., Debatisse, M., He, F.-C., Zhang, L., & Defossez, P. (2014) · Cell Reports · doi:10.1016/j.celrep.2014.03.030 · Cited by 74 · see citing works

cDNA Sequence and Chromosomal Localization of a Novel Human Protein, RBQ-1 (RBBP6), That Binds to the Retinoblastoma Gene Product

Sakai, Y., Saijo, M., Coelho, K. E. F. A., Kishino, T., Niikawa, N., & Taya, Y. (1995) · Genomics · doi:10.1006/geno.1995.0017 · Cited by 72 · see citing works

Mpe1, a Zinc Knuckle Protein, Is an Essential Component of Yeast Cleavage and Polyadenylation Factor Required for the Cleavage and Polyadenylation of mRNA

Vo, L. T. A., Minét, M., Schmitter, J., Lacroute, F., & Wyers, F. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.24.8346-8356.2001 · Cited by 69 · see citing works

Overlapping and distinct functions of CstF64 and CstF64τ in mammalian mRNA 3′ processing

Yao, C., Choi, E., Weng, L., Xie, X. S., Wan, J., Xing, Y., Moresco, J. J., Tu, P. G., Yates, J. R., & Shi, Y. (2013) · RNA · doi:10.1261/rna.042317.113 · Cited by 65 · see citing works

A novel function for the U2AF 65 splicing factor in promoting pre‐mRNA 3′‐end processing

Millevoi, S., Geraghty, F., Idowu, B. D., Tam, J. L. Y., Antoniou, M. N., & Vagner, S. (2002) · EMBO Reports · doi:10.1093/embo-reports/kvf173 · Cited by 65 · see citing works

Cleavage Factor II of Saccharomyces cerevisiaeContains Homologues to Subunits of the Mammalian Cleavage/ Polyadenylation Specificity Factor and Exhibits Sequence-specific, ATP-dependent Interaction with Precursor RNA

Zhao, J., Kessler, M. M., & Moore, C. L. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.16.10831 · Cited by 60 · see citing works

The structure of human Cleavage Factor Imhints at functions beyond UGUA-specific RNA binding

Yang, Q., Gilmartin, G. M., & Doublié, S. (2011) · RNA Biology · doi:10.4161/rna.8.5.16040 · Cited by 59 · see citing works

DNA damage induces targeted, genome-wide variation of poly(A) sites in budding yeastPreprint

Graber, J. H., Nazeer, F. I., Yeh, P.-C., Kuehner, J. N., Borikar, S., Hoskinson, D. C., & Moore, C. L. (2013) · Genome Research · doi:10.1101/gr.144964.112 · Cited by 53 · see citing works

Molecular Analyses of Two Poly(A) Site-Processing Factors That Determine the Recognition and Efficiency of Cleavage of the Pre-mRNA

Gilmartin, G. M., & Nevins, J. R. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.5.2432-2438.1991 · Cited by 49 · see citing works

Drosophila Sex‐lethal protein mediates polyadenylation switching in the female germline

Gawande, B. N., Robida, M. D., Rahn, A., & Singh, R. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601022 · Cited by 48 · see citing works

De-regulation of the RBBP6 isoform 3/DWNN in human cancers

Mbita, Z., Meyer, M., Skepu, A., Hosie, M. J., Rees, D. J. G., & Dlamini, Z. (2011) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-011-1150-5 · Cited by 40 · see citing works

Overexpression of RBBP6, Alone or Combined with Mutant TP53, Is Predictive of Poor Prognosis in Colon Cancer

Chen, J., Tang, H., Wu, Z., Zhou, C., Jiang, T., Xue, Y., Huang, G., Yan, D., & Peng, Z. (2013) · PLoS ONE · doi:10.1371/journal.pone.0066524 · Cited by 38 · see citing works

Functional dissection of the zinc finger and flanking domains of the Yth1 cleavage/polyadenylation factor

Tacahashi, Y. (2003) · Nucleic Acids Research · doi:10.1093/nar/gkg265 · Cited by 37 · see citing works

Molecular Cloning of a Human Protein That Binds to the Retinoblastoma Protein and Chromosomal Mapping

Saijo, M., Sakai, Y., Kishino, T., Niikawa, N., Matsuura, Y., Morino, K., Tamai, K., & Taya, Y. (1995) · Genomics · doi:10.1006/geno.1995.1084 · Cited by 36 · see citing works

All's well that ends well: alternative polyadenylation and its implications for stem cell biology

Mueller, A. A., Cheung, T. H., & Rando, T. A. (2013) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2012.12.008 · Cited by 32 · see citing works

A family of splice variants of CstF-64 expressed in vertebrate nervous systems

Shankarling, G. S., Coates, P. W., Dass, B., & MacDonald, C. C. (2009) · BMC Molecular Biology · doi:10.1186/1471-2199-10-22 · Cited by 29 · see citing works

Efficient mRNA Polyadenylation Requires a Ubiquitin-Like Domain, a Zinc Knuckle, and a RING Finger Domain, All Contained in the Mpe1 Protein

Lee, S. D., & Moore, C. L. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.00077-14 · Cited by 25 · see citing works

Polyadenylation proteins CstF-64 and τCstF-64 exhibit differential binding affinities for RNA polymers

Monarez, R. R., MacDonald, C. C., & Dass, B. (2007) · Biochemical Journal · doi:10.1042/bj20061097 · Cited by 22 · see citing works

Hexameric architecture of CstF supported by CstF-50 homodimerization domain structure

Moreno‐Morcillo, M., Minvielle-Sébastia, L., Mackereth, C. D., & Fribourg, S. (2011) · RNA · doi:10.1261/rna.2481011 · Cited by 22 · see citing works

Alternative polyadenylation of mRNA precursors

Tian, B., & Manley, J. L. (2017) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.116 · Cited by 1,179 · see citing works

RNA G-Quadruplexes in Biology: Principles and Molecular Mechanisms

Fay, M. M., Lyons, S. M., & Ivanov, P. V. (2017) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.05.017 · Cited by 448 · see citing works

The Output of Protein-Coding Genes Shifts to Circular RNAs When the Pre-mRNA Processing Machinery Is Limiting

Liang, D., Tatomer, D. C., Luo, Z., Wu, H., Yang, L. C., Chen, L., Cherry, S. R., & Wilusz, J. E. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.10.034 · Cited by 435 · 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

m6A-LAIC-seq reveals the census and complexity of the m6A epitranscriptome

Molinié, B., Wang, J., Lim, K. S., Hillebrand, R., Lu, Z., Wittenberghe, N. V., Howard, B. D., Daneshvar, K., Mullen, A. C., Dedon, P. C., et al. (2016) · Nature Methods · doi:10.1038/nmeth.3898 · Cited by 401 · see citing works

The neurogenetics of alternative splicing

Vuong, C. K., Black, D. L., & Zheng, S. (2016) · Nature Reviews Neuroscience · doi:10.1038/nrn.2016.27 · Cited by 340 · see citing works

Codon Usage and 3′ UTR Length Determine Maternal mRNA Stability in Zebrafish

Mishima, Y., & Tomari, Y. (2016) · Molecular Cell · doi:10.1016/j.molcel.2016.02.027 · Cited by 295 · see citing works

Functional diversity of small nucleolar RNAs

Bratkovič, T., Božič, J., & Rogelj, B. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkz1140 · Cited by 272 · see citing works

Emerging Roles of Disordered Sequences in RNA-Binding Proteins

Calabretta, S., & Richard, S. (2015) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.08.012 · Cited by 240 · see citing works

The pathogenic exon 1 HTT protein is produced by incomplete splicing in Huntington’s disease patients

Neueder, A., Landles, C., Ghosh, R., Howland, D., Myers, R. H., Faull, R. L. M., Tabrizi, S. J., & Bates, G. P. (2017) · Scientific Reports · doi:10.1038/s41598-017-01510-z · Cited by 235 · see citing works

Molecular Mechanisms for CFIm-Mediated Regulation of mRNA Alternative Polyadenylation

Zhu, Y., Wang, X., Forouzmand, E., Jeong, J., Qiao, F., Sowd, G. A., Engelman, A., Xie, X. S., Hertel, K. J., & Shi, Y. (2017) · Molecular Cell · doi:10.1016/j.molcel.2017.11.031 · Cited by 221 · see citing works

The roles of RNA processing in translating genotype to phenotype

Manning, K. S., & Cooper, T. A. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.139 · Cited by 206 · see citing works

Small Nucleolar RNAs Tell a Different Tale

Kufel, J., & Grzechnik, P. (2018) · Trends in Genetics · doi:10.1016/j.tig.2018.11.005 · Cited by 184 · see citing works

Properties and biological impact of RNA G-quadruplexes: from order to turmoil and back

Kharel, P., Becker, G., Цветков, В. Б., & Ivanov, P. V. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa1126 · Cited by 163 · see citing works

CPSF30-L-mediated recognition of mRNA m6A modification controls alternative polyadenylation of nitrate signaling-related gene transcripts in Arabidopsis

Hou, Y., Sun, J., Wu, B., Gao, Y., Nie, H., Nie, Z., Quan, S., Wang, Y., Cao, X., & Li, S. (2021) · Molecular Plant · doi:10.1016/j.molp.2021.01.013 · Cited by 159 · see citing works

Transcriptional Control by Premature Termination: A Forgotten Mechanism

Kamieniarz-Gdula, K., & Proudfoot, N. J. (2019) · Trends in Genetics · doi:10.1016/j.tig.2019.05.005 · Cited by 158 · see citing works

Molecular basis for the recognition of the human AAUAAA polyadenylation signal

Sun, Y., Zhang, Y., Hamilton, K., Manley, J. L., Shi, Y., Walz, T., & Tong, L. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1718723115 · Cited by 154 · see citing works

Selective Roles of Vertebrate PCF11 in Premature and Full-Length Transcript Termination

Kamieniarz-Gdula, K., Gdula, M. R., Panser, K., Nojima, T., Monks, J., Wiśniewski, J. R., Riepsaame, J., Brockdorff, N., Pauli, A., & Proudfoot, N. J. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.01.027 · Cited by 141 · see citing works

The Composition of the Arabidopsis RNA Polymerase II Transcript Elongation Complex Reveals the Interplay between Elongation and mRNA Processing Factors

Antosz, W., Pfab, A., Ehrnsberger, H. F., Holzinger, P., Köllen, K., Mortensen, S. A., Bruckmann, A., Schubert, T. E. O., Längst, G., Griesenbeck, J., et al. (2017) · The Plant Cell · doi:10.1105/tpc.16.00735 · Cited by 147 · see citing works

Translation initiation by cap‐dependent ribosome recruitment: Recent insights and open questions

Shirokikh, N. E., & Preiß, T. (2018) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1473 · Cited by 143 · see citing works

The Untranslated Regions of mRNAs in Cancer

Schuster, S. L., & Hsieh, A. C. (2019) · Trends in cancer · doi:10.1016/j.trecan.2019.02.011 · Cited by 138 · see citing works

A Polyadenylation-Dependent 3′ End Maturation Pathway Is Required for the Synthesis of the Human Telomerase RNA

Nguyen, D., St-Sauveur, V. G., Bergeron, D., Dupuis‐Sandoval, F., Scott, M. S., & Bachand, F. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.11.003 · Cited by 121 · see citing works

Structural basis of AAUAAA polyadenylation signal recognition by the human CPSF complex

Clerici, M., Faini, M., Muckenfuss, L. M., Aebersold, R. H., & Jínek, M. (2018) · Nature Structural & Molecular Biology · doi:10.1038/s41594-017-0020-6 · Cited by 119 · see citing works

U1 snRNP telescripting regulates a size–function-stratified human genome

Oh, J., Di, C., Venters, C. C., Guo, J., Arai, C., So, B. R., Pinto, A. M., Zhang, Z., Wan, L., Younis, I., et al. (2017) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.3473 · Cited by 118 · see citing works

Alternative Splicing as a Regulator of Early Plant Development

Szakonyi, D., & Duque, P. (2018) · Frontiers in Plant Science · doi:10.3389/fpls.2018.01174 · Cited by 117 · see citing works

A Complex of U1 snRNP with Cleavage and Polyadenylation Factors Controls Telescripting, Regulating mRNA Transcription in Human Cells

So, B. R., Di, C., Cai, Z., Venters, C. C., Guo, J., Oh, J., Arai, C., & Dreyfuss, G. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.08.007 · Cited by 116 · see citing works

The Chemical Biology of Human Metallo-β-Lactamase Fold Proteins

Pettinati, I., Brem, J., Lee, S. Y., McHugh, P. J., & Schofield, C. J. (2016) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.12.007 · Cited by 114 · see citing works

A snoRNA modulates mRNA 3′ end processing and regulates the expression of a subset of mRNAs

Huang, C., Shi, J., Guo, Y., Huang, W., Huang, S., Ming, S., Wu, X., Zhang, R., Ding, J., Zhao, W., et al. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx651 · Cited by 113 · see citing works

Rules and tools to predict the splicing effects of exonic and intronic mutations

Ohno, K., Takeda, J.-I., & Masuda, A. (2018) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1451 · Cited by 106 · see citing works

A compendium of conserved cleavage and polyadenylation events in mammalian genesPreprint

Wang, R., Zheng, D., Yehia, G., & Tian, B. (2018) · Genome Research · doi:10.1101/gr.237826.118 · Cited by 111 · see citing works

Regulation of Intronic Polyadenylation by PCF11 Impacts mRNA Expression of Long Genes

Wang, R., Zheng, D., Lü, W., Ding, Q., & Tian, B. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.02.049 · Cited by 105 · see citing works

Herpes simplex virus blocks host transcription termination via the bimodal activities of ICP27

Wang, X., Hennig, T., Whisnant, A. W., Erhard, F., Prusty, B. K., Friedel, C. C., Forouzmand, E., Hu, W. K., Erber, L. N., Chen, Y., et al. (2020) · Nature Communications · doi:10.1038/s41467-019-14109-x · Cited by 99 · see citing works

Activation of the Endonuclease that Defines mRNA 3′ Ends Requires Incorporation into an 8-Subunit Core Cleavage and Polyadenylation Factor Complex

Hill, C. H., Boreikaitė, V., Kumar, A., Casañal, A., Kubík, P., Degliesposti, G., Maslen, S., Mariani, A., von Loeffelholz, O., Girbig, M., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2018.12.023 · Cited by 98 · see citing works

Alternative Polyadenylation: a new frontier in post transcriptional regulation

Ren, F., Zhang, N., Zhang, L., Miller, E. W., & Pu, J. J. (2020) · Biomarker Research · doi:10.1186/s40364-020-00249-6 · Cited by 89 · see citing works

Structural insights into the assembly and polyA signal recognition mechanism of the human CPSF complex

Clerici, M., Faini, M., Aebersold, R. H., & Jínek, M. (2017) · eLife · doi:10.7554/elife.33111 · Cited by 87 · see citing works

Transcription and splicing: A two‐way street

Tellier, M., Maudlin, I., & Murphy, S. (2020) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1593 · Cited by 82 · see citing works

Alternative cleavage and polyadenylation in spermatogenesis connects chromatin regulation with post-transcriptional control

Li, W., Park, J. Y., Zheng, D., Hoque, M., Yehia, G., & Tian, B. (2016) · BMC Biology · doi:10.1186/s12915-016-0229-6 · Cited by 84 · see citing works

Structural Insights into the Human Pre-mRNA 3′-End Processing Machinery

Zhang, Y., Sun, Y., Shi, Y., Walz, T., & Tong, L. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.11.005 · Cited by 78 · see citing works

PAF Complex Plays Novel Subunit-Specific Roles in Alternative Cleavage and Polyadenylation

Yang, Y., Li, W., Hoque, M., Hou, L., Shen, S., Tian, B., & Dynlacht, B. D. (2016) · PLoS Genetics · doi:10.1371/journal.pgen.1005794 · Cited by 80 · see citing works

U1 snRNP Telescripting: Suppression of Premature Transcription Termination in Introns as a New Layer of Gene RegulationPreprint

Venters, C. C., Oh, J., Di, C., So, B. R., & Dreyfuss, G. (2019) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a032235 · Cited by 72 · see citing works

RNA-dependent chromatin association of transcription elongation factors and Pol II CTD kinases

Battaglia, S., Lidschreiber, M., Baejen, C., Torkler, P., Vos, S. M., & Cramer, P. (2017) · eLife · doi:10.7554/elife.25637 · Cited by 75 · see citing works

Activity-Dependent Regulation of Alternative Cleavage and Polyadenylation During Hippocampal Long-Term Potentiation

Fontes, M. M., Güvenek, A., Kawaguchi, R., Zheng, D., Huang, A., Ho, V. M., Chen, P. B., Liu, X., O’Dell, T. J., Coppola, G., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-17407-w · Cited by 72 · see citing works

Alternative polyadenylation drives oncogenic gene expression in pancreatic ductal adenocarcinomaPreprint

Venkat, S., Tisdale, A. A., Schwarz, J. R., Alahmari, A. A., Maurer, H. C., Olive, K. P., Eng, K. H., & Feigin, M. E. (2020) · Genome Research · doi:10.1101/gr.257550.119 · Cited by 72 · see citing works

Recent molecular insights into canonical pre-mRNA 3’-end processing

Sun, Y., Hamilton, K., & Tong, L. (2020) · Transcription · doi:10.1080/21541264.2020.1777047 · Cited by 69 · see citing works

Codon usage biases co-evolve with transcription termination machinery to suppress premature cleavage and polyadenylation

Zhou, Z., Dang, Y., Zhou, M., Yuan, H., & Liu, Y. (2018) · eLife · doi:10.7554/elife.33569 · Cited by 69 · see citing works

Transcription elongation rate has a tissue-specific impact on alternative cleavage and polyadenylation in <i>Drosophila melanogaster</i>

Liu, X., Freitas, J., Zheng, D., Oliveira, M. S., Hoque, M., Martins, T., Henriques, T., Tian, B., & Moreira, A. (2017) · RNA · doi:10.1261/rna.062661.117 · Cited by 67 · see citing works

The landscape of alternative polyadenylation in single cells of the developing mouse embryo

Agarwal, V., Lopez-Darwin, S. L., Kelley, D. R., & Shendure, J. (2021) · Nature Communications · doi:10.1038/s41467-021-25388-8 · Cited by 64 · see citing works

Transcriptome Analyses of FY Mutants Reveal Its Role in mRNA Alternative Polyadenylation

Yu, Z., Lin, J., & Li, Q. Q. (2019) · The Plant Cell · doi:10.1105/tpc.18.00545 · Cited by 67 · see citing works

CDK11 in TREX/THOC Regulates HIV mRNA 3′ End Processing

Pak, V., Eifler, T., Jäger, S., Krogan, N. J., Fujinaga, K., & Peterlin, B. M. (2015) · Cell Host & Microbe · doi:10.1016/j.chom.2015.10.012 · Cited by 63 · see citing works

The m6A pathway protects the transcriptome integrity by restricting RNA chimera formation in plants

Pontier, D., Picart, C., Baidouri, M. E., Roudier, F., Xu, T., Lahmy, S., Llauro, C., Azevedo, J., Laudié, M., Attina, A., et al. (2019) · Life Science Alliance · doi:10.26508/lsa.201900393 · Cited by 64 · see citing works

Widespread transcript shortening through alternative polyadenylation in secretory cell differentiation

Cheng, L. C., Zheng, D., Baljinnyam, E., Sun, F., Ogami, K., Yeung, P. L., Hoque, M., Lu, C.-W., Manley, J. L., & Tian, B. (2020) · Nature Communications · doi:10.1038/s41467-020-16959-2 · Cited by 63 · see citing works

Alternative polyadenylation by sequential activation of distal and proximal PolyA sites

Tang, P., Yang, Y., Li, G., Huang, L., Wen, M., Ruan, W., Guo, X., Zhang, C., Zuo, X., Luo, D., et al. (2022) · Nature Structural & Molecular Biology · doi:10.1038/s41594-021-00709-z · Cited by 63 · see citing works

Transcript isoform sequencing reveals widespread promoter-proximal transcriptional termination in Arabidopsis

Thomas, Q. A., Ard, R., Liu, J., Li, B., Wang, J., Pelechano, V., & Marquardt, S. (2020) · Nature Communications · doi:10.1038/s41467-020-16390-7 · Cited by 63 · see citing works

Structure of the catalytic core of the Integrator complex

Pfleiderer, M. M., & Galej, W. P. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.01.005 · Cited by 63 · see citing works

The mRNA Export Receptor NXF1 Coordinates Transcriptional Dynamics, Alternative Polyadenylation, and mRNA Export

Chen, S., Wang, R., Zheng, D., Zhang, H., Chang, X., Wang, K., Li, W., Fan, J., Tian, B., & Cheng, H. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.01.026 · Cited by 59 · see citing works

Integrated structural biology to unravel molecular mechanisms of protein-RNA recognition

Schlundt, A., Tants, J., & Sattler, M. (2017) · Methods · doi:10.1016/j.ymeth.2017.03.015 · Cited by 58 · see citing works

The Nrd1-like protein Seb1 coordinates cotranscriptional 3′ end processing and polyadenylation site selectionPreprint

Lemay, J., Marguerat, S., Larochelle, M., Liu, X., van Nues, R. W., Hunyadkürti, J., Hoque, M., Tian, B., Granneman, S., Bähler, J., et al. (2016) · Genes & Development · doi:10.1101/gad.280222.116 · Cited by 58 · see citing works

ALYREF links 3′‐end processing to nuclear export of non‐polyadenylated mRNAs

Fan, J., Wang, K., Du, X., Wang, J., Chen, S., Wang, Y., Shi, M. Y., Zhang, L., Wu, X., Zheng, D., et al. (2019) · The EMBO Journal · doi:10.15252/embj.201899910 · Cited by 56 · see citing works

The G-Quadruplex-Specific RNA Helicase DHX36 Regulates p53 Pre-mRNA 3′-End Processing Following UV-Induced DNA Damage

Newman, M., Sfaxi, R., Saha, A., Monchaud, D., Teulade‐Fichou, M., & Vagner, S. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.11.033 · Cited by 55 · 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

Comparative analysis of alternative polyadenylation in S. cerevisiae and S. pombePreprint

Liu, X., Hoque, M., Larochelle, M., Lemay, J., Yurko, N., Manley, J., Bachand, F., & Tian, B. (2017) · Genome Research · doi:10.1101/gr.222331.117 · Cited by 56 · see citing works

Reconstitution of mammalian cleavage factor II involved in 3′ processing of mRNA precursors

Schafer, P. H., Tüting, C., Schönemann, L., Kühn, U., Treiber, T., Treiber, N., Ihling, C. H., Graber, A., Keller, W., Meister, G., et al. (2018) · RNA · doi:10.1261/rna.068056.118 · Cited by 54 · see citing works

Cleavage and polyadenylation specificity factor 30: An RNA-binding zinc-finger protein with an unexpected 2Fe–2S cluster

Shimberg, G. D., Michalek, J. L., Oluyadi, A. A., Rodrigues, A. V., Zucconi, B. E., Neu, H. M., Ghosh, S., Sureschandra, K., Wilson, G. M., Stemmler, T. L., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1517620113 · Cited by 53 · see citing works

Common mechanism of transcription termination at coding and noncoding RNA genes in fission yeast

Larochelle, M., Robert, M.-A., Hébert, J.-N., Liu, X., Matteau, D., Rodrigue, S., Tian, B., Jacques, P., & Bachand, F. (2018) · Nature Communications · doi:10.1038/s41467-018-06546-x · Cited by 53 · see citing works

Competitive regulation of alternative splicing and alternative polyadenylation by hnRNP H and CstF64 determines acetylcholinesterase isoforms

Nazim, M., Masuda, A., Rahman, M. A., Nasrin, F., Takeda, J., Ohe, K., Ohkawara, B., Ito, M., & Ohno, K. (2016) · Nucleic Acids Research · doi:10.1093/nar/gkw823 · Cited by 52 · see citing works

Plant 3’ Regulatory Regions From mRNA-Encoding Genes and Their Uses to Modulate Expression

Bernardes, W. S., & Menossi, M. (2020) · Frontiers in Plant Science · doi:10.3389/fpls.2020.01252 · Cited by 50 · see citing works

The polyadenylation factor FIP1 is important for plant development and root responses to abiotic stresses

Téllez‐Robledo, B., Manzano, C., Saéz, Á., Navarro‐Neila, S., Silva‐Navas, J., de Lorenzo, L., González‐García, M. P., Toribio, R., Hunt, A. G., Baigorri, R., et al. (2019) · The Plant Journal · doi:10.1111/tpj.14416 · Cited by 51 · see citing works

The Ins and Outs of Messenger RNA Electroporation for Physical Gene Delivery in Immune Cell-Based Therapy

Campillo-Davó, D., Laere, M. D., Roex, G., Versteven, M., Flumens, D., Berneman, Z. N., Tendeloo, V. F. V., Anguille, S., & Lion, E. (2021) · Pharmaceutics · doi:10.3390/pharmaceutics13030396 · Cited by 50 · see citing works

RNA Binding Protein CELF2 Regulates Signal-Induced Alternative Polyadenylation by Competing with Enhancers of the Polyadenylation Machinery

Chatrikhi, R., Mallory, M. J., Gazzara, M. R., Agosto, L. M., Zhu, W. S., Litterman, A. J., Ansel, K. M., & Lynch, K. W. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.08.022 · Cited by 47 · see citing works

mRNA Editing, Processing and Quality Control in Caenorhabditis elegans

Arribere, J. A., Kuroyanagi, H., & Hundley, H. A. (2020) · Genetics · doi:10.1534/genetics.119.301807 · Cited by 46 · see citing works

Codon usage bias regulates gene expression and protein conformation in yeast expression system P. pastoris

Xu, Y., Liu, K., Han, Y., Xing, Y., Zhang, Y., Yang, Q., & Zhou, M. (2021) · Microbial Cell Factories · doi:10.1186/s12934-021-01580-9 · Cited by 48 · see citing works

Screening thousands of transcribed coding and non-coding regions reveals sequence determinants of RNA polymerase II elongation potential

Vlaming, H., Mimoso, C. A., Field, A. R., Martin, B. J. E., & Adelman, K. (2022) · Nature Structural & Molecular Biology · doi:10.1038/s41594-022-00785-9 · Cited by 49 · see citing works

LABRAT reveals association of alternative polyadenylation with transcript localization, RNA binding protein expression, transcription speed, and cancer survival

Goering, R., Engel, K. L., Gillen, A. E., Fong, N., Bentley, D. L., & Taliaferro, J. M. (2021) · BMC Genomics · doi:10.1186/s12864-021-07781-1 · Cited by 44 · see citing works

The three as: Alternative splicing, alternative polyadenylation and their impact on apoptosis in immune function

Blake, D., & Lynch, K. W. (2021) · Immunological Reviews · doi:10.1111/imr.13018 · Cited by 49 · see citing works

CPF Recruitment to Non-canonical Transcription Termination Sites Triggers Heterochromatin Assembly and Gene Silencing

Vo, T. V., Dhakshnamoorthy, J., Larkin, M., Zofall, M., Thillainadesan, G., Balachandran, V., Holla, S., Wheeler, D. L., & Grewal, S. I. S. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.05.107 · Cited by 47 · see citing works

Alternative polyadenylation factors link cell cycle to migration

Mitra, M., Johnson, E. L., Swamy, V. S., Nersesian, L., Corney, D. C., Robinson, D. G., Taylor, D. G., Ambrus, A., Jelínek, D., Wang, W., et al. (2018) · Genome biology · doi:10.1186/s13059-018-1551-9 · Cited by 45 · see citing works

The reciprocal regulation between splicing and 3′‐end processing

Kaida, D. (2016) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1348 · Cited by 44 · see citing works

Distinct regulation of alternative polyadenylation and gene expression by nuclear poly(A) polymerases

Li, W., Li, W., Laishram, R. S., Hoque, M., Ji, Z., Tian, B., & Anderson, R. A. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx560 · Cited by 44 · see citing works

A conserved RNA degradation complex required for spreading and epigenetic inheritance of heterochromatin

Shipkovenska, G. G., Durango, A., Kalocsay, M., Gygi, S. P., & Moazed, D. (2020) · eLife · doi:10.7554/elife.54341 · Cited by 44 · see citing works

Alternative polyadenylation: An enigma of transcript length variation in health and disease

Mohanan, N. K., Shaji, F., Koshre, G. R., & Laishram, R. S. (2021) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1692 · Cited by 41 · see citing works

FUS ‐mediated regulation of alternative RNA processing in neurons: insights from global transcriptome analysis

Masuda, A., Takeda, J., & Ohno, K. (2016) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1338 · Cited by 41 · see citing works

RNA regulatory processes in RNA virus biology

Cross, S. T., Michalski, D., Miller, M. R., & Wilusz, J. (2019) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1536 · Cited by 40 · see citing works

Two distinct transcription termination modes dictated by promotersPreprint

Miki, T., Carl, S. H., & Großhans, H. (2017) · Genes & Development · doi:10.1101/gad.301093.117 · Cited by 40 · see citing works

Analysis of alternative cleavage and polyadenylation in mature and differentiating neurons using RNA‐seq data

Güvenek, A., & Tian, B. (2018) · Quantitative Biology · doi:10.1007/s40484-018-0148-3 · Cited by 39 · see citing works

NAA10 polyadenylation signal variants cause syndromic microphthalmia

Johnston, J. J., Williamson, K. A., Chou, C. M., Sapp, J. C., Ansari, M., Chapman, H. M., Cooper, D. N., Dabir, T. A., Dudley, J. N., Holt, R. J., et al. (2019) · Journal of Medical Genetics · doi:10.1136/jmedgenet-2018-105836 · Cited by 37 · see citing works

Target Identification of an Antimalarial Oxaborole Identifies AN13762 as an Alternative Chemotype for Targeting CPSF3 in Apicomplexan Parasites

Bellini, V., Swale, C., Brenier‐Pinchart, M., Pézier, T., Georgeault, S., Laurent, F., Hakimi, M., & Bougdour, A. (2020) · iScience · doi:10.1016/j.isci.2020.101871 · Cited by 39 · see citing works

Prenatal maternal stress and offspring aggressive behavior: Intergenerational and transgenerational inheritance

Mbiydzenyuy, N. E., Hemmings, S. M. J., & Qulu, L. (2022) · Frontiers in Behavioral Neuroscience · doi:10.3389/fnbeh.2022.977416 · Cited by 40 · see citing works

Processing and transcriptome expansion at the mRNA 3′ end in health and disease: finding the right end

Ogorodnikov, A., Kargapolova, Y., & Danckwardt, S. (2016) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-016-1828-3 · Cited by 38 · see citing works

TENT5 cytoplasmic noncanonical poly(A) polymerases regulate the innate immune response in animals

Liudkovska, V., Krawczyk, P. S., Brouze, A., Gumińska, N., Węgierski, T., Cysewski, D., Mackiewicz, Z., Ewbank, J. J., Drabikowski, K., Mroczek, S., et al. (2022) · Science Advances · doi:10.1126/sciadv.add9468 · Cited by 34 · see citing works

The PAF1 complex promotes 3′ processing of pervasive transcripts

Liu, X., Guo, Z., Han, J., Peng, B., Zhang, B., Li, H., Hu, X., David, C. J., & Chen, M. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110519 · Cited by 35 · see citing works

Global analysis of physical and functional RNA targets of hnRNP L reveals distinct sequence and epigenetic features of repressed and enhanced exons

Cole, B. S., Tapescu, I., Allon, S. J., Mallory, M. J., Qiu, J., Lake, R. J., Fan, H.-Y., Fu, X., & Lynch, K. W. (2015) · RNA · doi:10.1261/rna.052969.115 · Cited by 34 · see citing works

Mechanism and consequences of herpes simplex virus 1-mediated regulation of host mRNA alternative polyadenylation

Wang, X., Liu, L., Whisnant, A. W., Hennig, T., Djaković, L., Haque, N., Bach, C., Sandri-Goldin, R. M., Erhard, F., Friedel, C. C., et al. (2021) · PLoS Genetics · doi:10.1371/journal.pgen.1009263 · Cited by 35 · see citing works

On the Cutting Edge: Regulation and Therapeutic Potential of the mRNA 3′ End Nuclease

Liu, H., & Moore, C. L. (2021) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2021.04.003 · Cited by 34 · see citing works

Rapid and Scalable Profiling of Nascent RNA with fastGRO

Barbieri, E., Hill, C., Quesnel-Vallières, M., Zucco, A. J., Barash, Y., & Gardini, A. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108373 · Cited by 33 · see citing works

Roles of Sumoylation in mRNA Processing and Metabolism

Richard, P., Vethantham, V., & Manley, J. L. (2017) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-50044-7_2 · Cited by 32 · see citing works

A conserved role for the ALS-linked splicing factor SFPQ in repression of pathogenic cryptic last exons

Gordon, P. M., Hamid, F., Makeyev, E. V., & Houart, C. (2021) · Nature Communications · doi:10.1038/s41467-021-22098-z · Cited by 32 · see citing works

Elevated pre-mRNA 3′ end processing activity in cancer cells renders vulnerability to inhibition of cleavage and polyadenylation

Cui, Y., Wang, L., Ding, Q., Shin, J., Cassel, J. A., Liu, Q., Salvino, J. M., & Tian, B. (2023) · Nature Communications · doi:10.1038/s41467-023-39793-8 · Cited by 31 · see citing works

Characterization of mRNA polyadenylation in the apicomplexa

Stevens, A. T., Howe, D. K., & Hunt, A. G. (2018) · PLoS ONE · doi:10.1371/journal.pone.0203317 · Cited by 31 · see citing works

A Genome-wide Study of “Non-3UTR” Polyadenylation Sites in Arabidopsis thaliana

Guo, C., Spinelli, M., Liu, M., Li, Q. Q., & Liang, C. (2016) · Scientific Reports · doi:10.1038/srep28060 · Cited by 30 · see citing works

SnoRNAs: Exploring Their Implication in Human Diseases

Chauhan, W., Sudharshan, S. J., Kafle, S., & Zennadi, R. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25137202 · Cited by 28 · see citing works

Structural biology of poly(A) site definition

Yang, Q., & Doublié, S. (2011) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.88 · Cited by 51 · see citing works

Means to an end: mechanisms of alternative polyadenylation of messenger RNA precursors

Gruber, A. R., Martin, G., Keller, W., & Zavolan, M. (2013) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1206 · Cited by 74 · see citing works

A complex protein assembly catalyzes polyadenylation of mRNA precursors

Manley, J. L. (1995) · Current Opinion in Genetics & Development · doi:10.1016/0959-437x(95)80012-3 · Cited by 89 · see citing works

Mechanistic insights into mRNA 3′-end processing

Kumar, A., Clerici, M., Muckenfuss, L. M., Passmore, L. A., & Jínek, M. (2019) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2019.08.001 · Cited by 110 · see citing works

Characterization of the Mammalian mRNA 3' Processing Complex

Chan, S. L. (2014) · eScholarship (California Digital Library)