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The end of the message: multiple protein–RNA interactions define the mRNA polyadenylation site
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The key RNA sequence elements and protein factors necessary for 3′ processing of polyadenylated mRNA precursors are well known. Recent studies, however, have significantly reshaped current models for the protein–RNA interactions involved in poly(A) site recognition, painting a picture more complex than previously envisioned and also providing new insights into regulation of this important step in gene expression. Here we review the recent advances in this area and provide a perspective for future studies.
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“recent studies of Mbnl1/2 dKOs have highlighted MBNL activity in controlling alternative polyadenylation events105,107,108.”
From The neurogenetics of alternative splicing (2016) · cites this paper as [108]
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Cites
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
Mayr, C., & Bartel, D. P. (2009) · Cell · doi:10.1016/j.cell.2009.06.016 · Cited by 1,613
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×
“For example, NOVA proteins, which are known splicing regulators in the brain (Jensen et al. 2000), were shown to regulate APA by binding to sites in 3′ UTRs and repress or enhance PAS usage in a position-dependent manner (Licatalosi et al. 2008).”
BackgroundSandberg, R., Neilson, J. R., Sarma, A., Sharp, P. A., & Burge, C. B. (2008) · Science · doi:10.1126/science.1155390 · Cited by 1,349
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
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
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
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
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 992
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
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Items 101–200 of 249
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Al-Husini, N., Medler, S., & Ansari, A. (2020) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2020.194657 · Cited by 28
Splicing regulation and dysregulation of cholinergic genes expressed at the neuromuscular junction
Ohno, K., Rahman, M. A., Nazim, M., Nasrin, F., Lin, Y., Takeda, J., & Masuda, A. (2017) · Journal of Neurochemistry · doi:10.1111/jnc.13954 · Cited by 28
Therapeutic targeting of CPSF3-dependent transcriptional termination in ovarian cancer
Shen, P., Ye, K., Xiang, H., Zhang, Z., He, Q., Zhang, X., Cai, M., Chen, J., Sun, Y., Lin, L., et al. (2023) · Science Advances · doi:10.1126/sciadv.adj0123 · Cited by 25
Mariella, E., Marotta, F., Grassi, E., Gilotto, S., & Provero, P. (2019) · Frontiers in Genetics · doi:10.3389/fgene.2019.00714 · Cited by 25
Chen, X., Lloyd, S. M., Kweon, J., Gamalong, G. M., & Bao, X. (2021) · Nature Communications · doi:10.1038/s41467-020-20674-3 · Cited by 27
Structural basis of mRNA maturation: Time to put it together
Vorländer, M. K., Pacheco-Fiallos, B., & Plaschka, C. (2022) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2022.102431 · Cited by 30
Sun, R., Wei, T., Ding, D., Zhang, J., Chen, S., He, H. H., Wang, L., & Huang, H. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2205509119 · Cited by 26
Poly(A) code analyses reveal key determinants for tissue-specific mRNA alternative polyadenylation
Weng, L., Li, Y., Xie, X. S., & Shi, Y. (2016) · RNA · doi:10.1261/rna.055681.115 · Cited by 25
Self-citationMarsollier, A.-C., Joubert, R., Mariot, V., & Dumonceaux, J. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19051347 · Cited by 26
Structural transitions in poly(A), poly(C), poly(U), and poly(G) and their possible biological roles
Zarudnaya, M. I., Kolomiets, I. N., Potyahaylo, A. L., & Hovorun, D. М. (2018) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2018.1503972 · Cited by 24
Dynamic mRNP Remodeling in Response to Internal and External Stimuli
Zarnack, K., Balasubramanian, S., Gantier, M. P., Kunetsky, V., Kracht, M., Schmitz, M. L., & Sträßer, K. (2020) · Biomolecules · doi:10.3390/biom10091310 · Cited by 24
Regulation of neuronal RNA signatures by ELAV /Hu proteins
Hilgers, V. (2022) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1733 · Cited by 26
Fujiwara, R., Zhai, S.-N., Liang, D., Shah, A. P., Tracey, M. P., Ma, X.-K., Fields, C. J., Mendoza-Figueroa, M. S., Meline, M. C., Tatomer, D. C., et al. (2023) · Molecular Cell · doi:10.1016/j.molcel.2023.10.035 · Cited by 22
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Kainov, Y. A., & Makeyev, E. V. (2020) · Nature Communications · doi:10.1038/s41467-019-14204-z · Cited by 22
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Heinrich, S., Hondele, M., Marchand, D., Derrer, C. P., Zedan, M., Oswald, A., Malinovska, L., Uliana, F., Khawaja, S., Mancini, R., et al. (2023) · Cell Reports · doi:10.1016/j.celrep.2023.113593 · Cited by 22
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Duek, L., Barkai, O., Elran, R., Adawi, I., & Choder, M. (2018) · PLoS ONE · doi:10.1371/journal.pone.0206161 · Cited by 22
Biophysical characterizations of the recognition of the AAUAAA polyadenylation signal
Hamilton, K., Sun, Y., & Tong, L. (2019) · RNA · doi:10.1261/rna.070870.119 · Cited by 22
CRISPR-iPAS: a novel dCAS13-based method for alternative polyadenylation interference
Tian, S., Zhang, B., He, Y., Sun, Z., Li, J., Li, Y., Yi, H., Zhao, Y., Zou, X., Li, Y., et al. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac108 · Cited by 21
Mukherjee, S., Graber, J. H., & Moore, C. L. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1091403 · Cited by 21
The emerging theme of 3′UTR mRNA isoform regulation in reprogramming of cell metabolism
Zhang, Q., & Tian, B. (2023) · Biochemical Society Transactions · doi:10.1042/bst20221128 · Cited by 21
RNA recognition by Roquin in posttranscriptional gene regulation
Schlundt, A., Niessing, D., Heissmeyer, V., & Sattler, M. (2016) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1333 · Cited by 20
snoRNAs associate with mRNA 3′ processing complex: New wine in old bottles
Shi, J., Huang, C., Huang, S., & Yao, C. (2017) · RNA Biology · doi:10.1080/15476286.2017.1416278 · Cited by 22
Tränkner, C., Lemnian, I., Emrani, N., Pfeiffer, N., Tiwari, S. P., Kopisch-Obuch, F., Vogt, S. H., MÜLLER, A. E., Schilhabel, M. B., Jung, C., et al. (2016) · Frontiers in Plant Science · doi:10.3389/fpls.2016.01662 · Cited by 21
Connections between 3′ end processing and DNA damage response: Ten years later
Murphy, M. R., & Kleiman, F. E. (2019) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1571 · Cited by 21
Small Nucleolar RNAs: Biological Functions and Diseases
Wang, Y., Fu, M., Zheng, Z., Feng, J., & Zhang, C. (2025) · MedComm · doi:10.1002/mco2.70257 · Cited by 23
Alahmari, A. A., Chaubey, A. H., Jonnakuti, V. S., Tisdale, A. A., Schwarz, C., Cornwell, A. C., Maraszek, K. E., Paterson, E. J., Kim, M., Venkat, S., et al. (2024) · RNA · doi:10.1261/rna.079931.123 · Cited by 19
Wang, B., Chai, H., Zhong, Y., Shen, Y., Yang, W., Chen, J., Xin, Z., & Shi, H. (2019) · Journal of Experimental Botany · doi:10.1093/jxb/erz523 · Cited by 20
Turner, R. E., Henneken, L. M., Liem-Weits, M., Harrison, P. F., Swaminathan, A., Vary, R., Nikolić, I., Simpson, K. J., Powell, D., Beilharz, T. H., et al. (2020) · RNA · doi:10.1261/rna.075226.120 · Cited by 20
Grozdanov, P. N., Masoumzadeh, E., Kalscheuer, V. M., Bienvenu, T., Billuart, P., Delrue, M., Latham, M. P., & MacDonald, C. C. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa689 · Cited by 23
Ni, Z., Ahmed, N., Nabeel‐Shah, S., Guo, X., Pu, S., Song, J., Marcon, E., Burke, G. L., Tong, A. H. Y., Chan, K., et al. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae240 · Cited by 20
Liu, L., Yu, A. M., Wang, X., Soles, L. V., Teng, X., Chen, Y.-L., Yoon, Y., Sarkan, K. S. K., Valdez, M. C., Linder, J., et al. (2023) · Nature Structural & Molecular Biology · doi:10.1038/s41594-023-01161-x · Cited by 17
Self-citationAlemasova, E. E., & Lavrik, O. I. (2017) · Acta Naturae · doi:10.32607/20758251-2017-9-2-4-16 · Cited by 20
Fütterer, A., Gutiérrez, A., Pons, T., de Celis, J., Gutiérrez, J., Plaza, V. D., & Martínez‐A, C. (2021) · Cell Death and Disease · doi:10.1038/s41419-021-03906-2 · Cited by 18
Generation of Drosophila sisRNAs by Independent Transcription from Cognate Introns
Ng, S. S. J., Zheng, R. T., Osman, I., & Pek, J. W. (2018) · iScience · doi:10.1016/j.isci.2018.05.010 · Cited by 18
Yu, Z., Wang, J., Zhang, C., Zhan, Q., Shi, L., Song, B., Han, D., Jiang, J., Huang, J., Ou, X., et al. (2024) · Molecular Plant · doi:10.1016/j.molp.2024.07.011 · Cited by 17
Domiński, Z., & Tong, L. (2021) · Biochemical Society Transactions · doi:10.1042/bst20210323 · Cited by 17
Krzysztoń, M., & Kufel, J. (2022) · Scientific Reports · doi:10.1038/s41598-022-05574-4 · Cited by 17
Wu, J., Ma, L., & Cao, Y. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24054727 · Cited by 18
Danckwardt, S., Trégouët, D., & Castoldi, E. (2023) · Cardiovascular Research · doi:10.1093/cvr/cvad046 · Cited by 17
Deng, Z., Zhang, S., Gu, S., Ni, X., Zeng, W., & Li, X. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19010279 · Cited by 15
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Shin, J., Ding, Q., Wang, L., Cui, Y., Baljinnyam, E., Güvenek, A., & Tian, B. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab519 · Cited by 19
PQBP1: The Key to Intellectual Disability, Neurodegenerative Diseases, and Innate Immunity
Tanaka, H., & Okazawa, H. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23116227 · Cited by 18
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Hamilton, K., & Tong, L. (2020) · Genes & Development · doi:10.1101/gad.343814.120 · Cited by 16
Polyploid giant cancer cells: Underlying Mechanisms, Signaling Pathways, and Therapeutic Strategies.
Temaj, G., Saha, S., Chichiarelli, S., Telkoparan-Akillilar, P., Nuhii, N., Hadziselimovic, R., & Saso, L. (2025) · Critical reviews in oncology/hematology · doi:10.1016/j.critrevonc.2025.104802 · Cited by 16
Zhou, Y., Yang, J., Huang, L., Liu, C., Yu, M., Chen, R., & Zhou, Q. (2024) · iScience · doi:10.1016/j.isci.2024.108822 · Cited by 17
Khajuria, D. K., Nowak, I., Leung, M., Karuppagounder, V., Kawasawa, Y. I., Norbury, C. C., Kamal, F., & Elbarbary, R. A. (2023) · Bone Research · doi:10.1038/s41413-022-00236-7 · Cited by 15
Distinct roles of Pcf11 zinc-binding domains in pre-mRNA 3′-end processing
Guéguéniat, J., Dupin, A. F., Stojko, J., Beaurepaire, L., Cianférani, S., Mackereth, C. D., Minvielle-Sébastia, L., & Fribourg, S. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx674 · Cited by 15
Liu, W., Deng, L., Wang, M., Liu, X., Ouyang, X., Wang, Y., Miao, N., Luo, X., Wu, X., Lu, X., et al. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.01.023 · Cited by 14
Canonical and noncanonical RNA polyadenylation
Ustyantsev, I. G., Golubchikova, J. S., Borodulina, O. R., & Kramerov, D. A. (2017) · Molecular Biology · doi:10.1134/s0026893317010186 · Cited by 14
Peart, N. J., & Wagner, E. J. (2017) · Human Genetics · doi:10.1007/s00439-017-1813-8 · Cited by 14
Rodríguez‐Romero, J., Marconi, M., Ortega‐Campayo, V., Demuez, M., Wilkinson, M. D., & Sesma, A. (2018) · New Phytologist · doi:10.1111/nph.15405 · Cited by 16
Elton, T. S., Hernandez, V. A., Carvajal‐Moreno, J., Wang, X., Ipinmoroti, D., & Yalowich, J. C. (2022) · Cancers · doi:10.3390/cancers14133148 · Cited by 15
Suboptimal RNA–RNA interaction limits U1 snRNP inhibition of canonical mRNA 3’ processing
Shi, J., Deng, Y., Huang, S., Huang, C., Wang, J., Xiang, A. P., & Yao, C. (2019) · RNA Biology · doi:10.1080/15476286.2019.1636596 · Cited by 14
Alternative mRNA polyadenylation regulates macrophage hyperactivation via the autophagy pathway
Chen, Y., Chen, B., Li, J., Li, H., Wang, G., Cai, X., Zhang, Q., Liu, X., Chen, K., Wang, Z., et al. (2024) · Cellular and Molecular Immunology · doi:10.1038/s41423-024-01237-8 · Cited by 13
Ma, H., Lin, J., Mei, F., Mao, H., & Li, Q. Q. (2023) · The Plant Journal · doi:10.1111/tpj.16150 · Cited by 13
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Lavi, E., & Carmel, L. (2018) · RNA Biology · doi:10.1080/15476286.2018.1429880 · Cited by 13
Mohibi, S., Zhang, J., & Chen, X. (2020) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2020.03.942 · Cited by 13
Sequential Polyadenylation to Enable Alternative mRNA 3’ End Formation
Hao, Y., Cai, T., Liu, C., Zhang, X., & Fu, X. (2023) · Molecules and Cells · doi:10.14348/molcells.2023.2176 · Cited by 12
Effect of CFIm25 knockout on RNA polymerase II transcription
Tellier, M., Hardy, J. G., Norbury, C. J., & Murphy, S. (2018) · BMC Research Notes · doi:10.1186/s13104-018-4006-1 · Cited by 12
Ouyang, Z., Duan, H., Mi, L., Hu, W., Chen, J., Li, X., & Zhong, B. (2019) · Journal of the American Society for Horticultural Science · doi:10.21273/jashs04567-18 · Cited by 12
Thr 4 phosphorylation on RNA Pol II occurs at early transcription regulating 3′-end processing
Moreno, R. Y., Panina, S., Irani, S., Hardtke, H. A., Stephenson, R., Floyd, B. M., Marcotte, E. M., Zhang, Q., & Zhang, Y. (2024) · Science Advances · doi:10.1126/sciadv.adq0350 · Cited by 11
RNA interference and turnover in plants -a complex partnership
Krzysztoń, M., Kufel, J., & Zakrzewska‐Placzek, M. (2025) · Frontiers in Plant Science · doi:10.3389/fpls.2025.1608888 · Cited by 11
Ustyantsev, I. G., Borodulina, O. R., & Kramerov, D. A. (2020) · RNA Biology · doi:10.1080/15476286.2020.1857942 · Cited by 11
Said, M. A., Bejjani, F., Abdouni, A., Ségéral, E., & Emiliani, S. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2313356120 · Cited by 10
Lee, S. D., Liu, H., Graber, J. H., Heller-Trulli, D., Michaels, K. K., Cerezo, J. F., & Moore, C. L. (2020) · RNA Biology · doi:10.1080/15476286.2020.1724717 · Cited by 10
Alternative polyadenylated mRNAs behave as asynchronous rhythmic transcription in Arabidopsis
Lin, J., Yu, Z., Ye, C., Hong, L., Chu, Y., Shen, Y., & Li, Q. Q. (2021) · RNA Biology · doi:10.1080/15476286.2021.1933732 · Cited by 12
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Gutierrez, P. A., Baughman, K. M., Sun, Y., & Tong, L. (2021) · RNA · doi:10.1261/rna.078764.121 · Cited by 11
Zhang, Y., Li, X., Goodrich, J., Wu, C., Wei, H., Yang, S., & Feng, X. (2016) · Plant Molecular Biology · doi:10.1007/s11103-016-0487-2 · Cited by 10
Ma, X.-X., Qiu, Y., Chang, Z., Gao, J., Jiang, R.-R., Li, C.-L., Wang, C., & Chang, Q. (2021) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2021.779259 · Cited by 10
Fujiwara, N., Shigemoto, M., Hirayama, M., Fujita, K., Seno, S., Matsuda, H., Nagahama, M., & Masuda, S. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac559 · Cited by 10
An examination of the metal ion content in the active sites of human endonucleases CPSF73 and INTS11
Huang, J. W., Liu, X., Sun, Y., Li, Z., Lin, M.-H., Hamilton, K., Mandel, C. R., Sandmeir, F., Conti, E., Oyala, P. H., et al. (2023) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2023.103047 · Cited by 10
Sun, Y., Aik, W. S., Yang, X.-C., Marzluff, W. F., Domiński, Z., & Tong, L. (2021) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2021.03.021 · Cited by 10
Emerging value of the viroid model in molecular biology and beyond
Ma, J., Mudiyanselage, S. D. D., & Wang, Y. (2022) · Virus Research · doi:10.1016/j.virusres.2022.198730 · Cited by 10
Zhang, M., & Liu, J. (2022) · Bioengineered · doi:10.1080/21655979.2022.2063100 · Cited by 9
Molecular basis for the recognition of the AUUAAA polyadenylation signal by mPSF
Gutierrez, P. A., Jia, W., Sun, Y., & Tong, L. (2022) · RNA · doi:10.1261/rna.079322.122 · Cited by 9
Restrictor slows RNAPII elongation to promote termination at noncoding RNA lociPreprint
Mimoso, C. A., Vlaming, H., Wagenaar, N. P. V.-D., Siegenfeld, A. P., & Adelman, K. (2025) · Genes & Development · doi:10.1101/gad.352654.125 · Cited by 9
Hudson, S. W., McNally, L. M., & McNally, M. T. (2016) · Virology · doi:10.1016/j.virol.2016.08.021 · Cited by 8
Feng, Q., Lin, Z., Zhao, D., Li, M., Yang, S., Xiang, A. P., Ye, C., & Yao, C. (2025) · Cell Reports · doi:10.1016/j.celrep.2025.115376 · Cited by 8
The Nrd1–Nab3–Sen1 transcription termination complex from a structural perspective
Chaves‐Arquero, B., & Pérez‐Cañadillas, J. M. (2023) · Biochemical Society Transactions · doi:10.1042/bst20221418 · Cited by 7
Ogorodnikov, A., & Danckwardt, S. (2021) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2021.03.022 · Cited by 7
In vivo discovery of RNA proximal proteins in human cells via proximity-dependent biotinylationPreprint
Lin, X., Fonseca, M. A., Corona, R. I., & Lawrenson, K. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.02.28.970442 · Cited by 7
Isoform-specific regulation of rhythmic gene expression by alternative polyadenylationPreprint
Greenwell, B. J., Beytebiere, J. R., Lamb, T. M., Bell‐Pedersen, D., Merlin, C., & Menet, J. S. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.12.12.422514 · Cited by 5
Exploring the Impact of Cleavage and Polyadenylation Factors on Pre-mRNA Splicing Across Eukaryotes
Lepennetier, G., & Catania, F. (2017) · G3 Genes Genomes Genetics · doi:10.1534/g3.117.041483 · Cited by 7
Aydin, E., Schreiner, S., Böhme, J., Keil, B., Weber, J., Žunar, B., Glatter, T., & Kilchert, C. (2024) · Nature Communications · doi:10.1038/s41467-024-51035-z · Cited by 6
Cao, Y., Guo, Y., Yu, Z., Nie, H., Yang, J., Qiu, D., Li, Q., Xu, X., Cheng, C., Li, Y., et al. (2025) · Advanced Science · doi:10.1002/advs.202504562 · Cited by 5
Overlapping and distinct functions of SPT6, PNUTS, and PCF11 in regulating transcription termination
Bejjani, F., Ségéral, E., Mosca, K., Lecourieux, A., Bakail, M., Hamoudi, M., & Emiliani, S. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf179 · Cited by 5
Gain-of-Function Reporters For Analysis of mRNA 3′-End Formation: Design and Optimization
Peart, N. J., & Wagner, E. J. (2016) · BioTechniques · doi:10.2144/000114390 · Cited by 5
Attenuation of Eukaryotic Protein-Coding Gene Expression via Premature Transcription TerminationPreprint
Tatomer, D. C., & Wilusz, J. E. (2019) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.2019.84.039644 · Cited by 5
Reduced Usage of GLS Intronic Polyadenylation Promotes Cellular Senescence
Li, X., Li, Y., Ding, D., Xie, B., Yao, J., Chen, Y., Zhao, Z., Yu, P., Zhang, S., Fu, Y., et al. (2025) · Phenomics · doi:10.1007/s43657-024-00198-2 · Cited by 4
Yu, S., Chen, W. C., Wang, L., Jewell, S., Mammedova, A., Han, S. W., Wickramasinghe, J. M., Barash, Y., & Tian, B. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf1212 · Cited by 4
Post‐transcriptional polyadenylation site cleavage maintains 3′‐end processing upon DNA damage
Sfaxi, R., Biswas, B., Boldina, G., Cadix, M., Servant, N., Chen, H., Larson, D. R., Dutertre, M., Robert, C., & Vagner, S. (2023) · The EMBO Journal · doi:10.15252/embj.2022112358 · Cited by 4
Wachs, A. S., & Bohne, J. (2020) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1616 · Cited by 4
Liang, D., Tatomer, D. C., & Wilusz, J. E. (2021) · Methods · doi:10.1016/j.ymeth.2021.04.012 · Cited by 4
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Deykin, A. V., Tikhonov, M. V., Kalmykov, V. A., Korobko, I. V., Georgiev, P. G., & Maksimenko, O. G. (2019) · Transgenic Research · doi:10.1007/s11248-019-00122-9 · Cited by 4
Boldyreva, L. V., Yarinich, L. A., Kozhevnikova, E. N., Ivankin, A. V., Lebedev, M. O., & Pindyurin, A. V. (2021) · Molecular Biology Reports · doi:10.1007/s11033-021-06160-z · Cited by 3
Cai, Z., So, B. R., & Dreyfuss, G. (2021) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2021.04.017 · Cited by 2
An investigation into the role of ATP in the mammalian pre-mRNA 3′ cleavage reaction
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Effect of CFIm68 knockdown on RNA polymerase II transcription
Tellier, M., Hardy, J. G., Norbury, C. J., & Murphy, S. (2019) · BMC Research Notes · doi:10.1186/s13104-019-4582-8 · Cited by 3
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Molecular basis for the recognition of low-frequency polyadenylation signals by mPSF
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Metadata
- Authors
- Shi, Y., & Manley, J. L.
- Affiliations
- University of California, Irvine (US)
- Columbia University (US)
- Corresponding author
- Shi, Yongsheng
- Manley, James L.
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2015-05-01
- Volume
- 29
- Issue
- 9
- Pages
- 889-897
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- PMC
- PMC4421977
- OpenAlex
- W2056608604
- Cited by
- 249
- References
- 108
- Citations by year
- 2026: 5 · 2025: 19 · 2024: 12 · 2023: 19 · 2022: 22 · 2021: 34 · 2020: 29 · 2019: 30 · 2018: 22 · 2017: 27 · 2016: 26 · 2015: 4
- Type
- posted content
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by-nc
- Locations
- Genes & Development (publishedVersion, cc-by-nc)
- PubMed Central (publishedVersion, cc-by-nc)
- PubMed (publishedVersion)
- eScholarship (California Digital Library) (submittedVersion, cc-by)
- eScholarship (California Digital Library) (submittedVersion, cc-by-nc)
- Funders
- National Institutes of Health (GM090056, CA177651)
- American Cancer Society (RSG-12-186)
- NIH (GM28983)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA regulation and disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Keywords
- mRNA polyadenylation, RNA-protein interactions, polyadenylation factors, 3' end processing, mRNA precursors, gene expression regulation, polyadenylation signal
- MeSH terms
- Gene Expression Regulation, Protein Binding, RNA Precursors, RNA, Messenger, Conserved Sequence, Amino Acid Motifs, Polyadenylation, Cleavage And Polyadenylation Specificity Factor
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