A day in the life of the spliceosome

Expansion of the eukaryotic proteome by alternative splicing

Nilsen, T. W., & Graveley, B. R. (2010) · Nature · doi:10.1038/nature08909 · Cited by 2,172 · see citing works

CRM1 Is an Export Receptor for Leucine-Rich Nuclear Export Signals

Fornerod, M. W. J., Ohno, M., Yoshida, M., & Mattaj, I. W. (1997) · Cell · doi:10.1016/s0092-8674(00)80371-2 · Cited by 2,086 · see citing works

Frequent pathway mutations of splicing machinery in myelodysplasia

Yoshida, K., Sanada, M., Shiraishi, Y., Nowak, D., Nagata, Y., Yamamoto, R., Sato, Y., Sato-Otsubo, A., Kon, A., Nagasaki, M., et al. (2011) · Nature · doi:10.1038/nature10496 · Cited by 2,029 · see citing works

Spliceosome Structure and Function

Will, C. L., & Luhrmann, R. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a003707 · Cited by 1,829 · see citing works

A single nucleotide in the SMN gene regulates splicing and is responsible for spinal muscular atrophy

Lorson, C. L., Hahnen, E., Androphy, E. J., & Wirth, B. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.11.6307 · Cited by 1,536 · see citing works

Spliced segments at the 5′ terminus of adenovirus 2 late mRNA

Berget, S. M., Moore, C. L., & Sharp, P. A. (1977) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.74.8.3171 · Cited by 1,424 · see citing works

Understanding alternative splicing: towards a cellular code

Matlin, A. J., Clark, F., & Smith, C. W. J. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1645 · Cited by 1,299 · see citing works

An amazing sequence arrangement at the 5′ ends of adenovirus 2 messenger RNA

Chow, L. T., Gelinas, R. E., Broker, T. R., & Roberts, R. J. (1977) · Cell · doi:10.1016/0092-8674(77)90180-5 · Cited by 1,234 · see citing works

Are snRNPs involved in splicing?

Lerner, M. R., Boyle, J. A., Mount, S. M., Wolin, S. L., & STEITZ, J. A. (1980) · Nature · doi:10.1038/283220a0 · Cited by 1,192 · see citing works

Splicing regulation: From a parts list of regulatory elements to an integrated splicing code

Wang, Z., & Burge, C. B. (2008) · RNA · doi:10.1261/rna.876308 · Cited by 1,076 · see citing works

Nuclear speckles: a model for nuclear organelles

Lamond, A. I., & Spector, D. L. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1172 · Cited by 1,002 · see citing works

Pre-mRNA Splicing

Jurica, M. S., & Moore, M. J. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00270-3 · Cited by 963 · see citing works

Deciphering the splicing code

Barash, Y., Calarco, J. A., Gao, W., Pan, Q., Wang, X., Ofer Shai, A., Blencowe, B. J., & Frey, B. J. (2010) · Nature · doi:10.1038/nature09000 · Cited by 891 · 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 splicing: a pivotal step between eukaryotic transcription and translation

Kornblihtt, A. R., Schor, I. E., Alló, M., Dujardin, G., Petrillo, E., & Muñoz, M. J. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3525 · Cited by 851 · see citing works

Nuclear SpecklesPreprint

Spector, D. L., & Lamond, A. I. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a000646 · Cited by 842 · see citing works

Non-coding RNAs: lessons from the small nuclear and small nucleolar RNAs

Matera, A. G., Terns, R. M., & Terns, M. P. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2124 · Cited by 752 · see citing works

Systematic Identification and Analysis of Exonic Splicing Silencers

Wang, Z., Rolish, M. E., Yeo, G. W.-M., Tung, V., Mawson, M., & Burge, C. B. (2004) · Cell · doi:10.1016/j.cell.2004.11.010 · Cited by 678 · see citing works

Inactivation of the survival motor neuron gene, a candidate gene for human spinal muscular atrophy, leads to massive cell death in early mouse embryos

Schrank, B., Götz, R., Gunnersen, J. M., Ure, J., Toyka, K. V., Smith, A. G., & Sendtner, M. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.18.9920 · Cited by 661 · see citing works

The SMN–SIP1 Complex Has an Essential Role in Spliceosomal snRNP Biogenesis

Fischer, U., Liu, Q., & Dreyfuss, G. (1997) · Cell · doi:10.1016/s0092-8674(00)80368-2 · Cited by 657 · see citing works

The Spinal Muscular Atrophy Disease Gene Product, SMN, and Its Associated Protein SIP1 Are in a Complex with Spliceosomal snRNP Proteins

Liu, Q., Fischer, U., Wang, F., & Dreyfuss, G. (1997) · Cell · doi:10.1016/s0092-8674(00)80367-0 · Cited by 657 · 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

A post-transcriptional regulatory switch in polypyrimidine tract-binding proteins reprograms alternative splicing in developing neurons

Boutz, P. L., Stoilov, P., Li, Q., Lin, C.-H., Chawla, G., Ostrow, K., Shiue, L., Ares, M., & Black, D. L. (2007) · Genes & Development · doi:10.1101/gad.1558107 · Cited by 577 · see citing works

Integrator, a Multiprotein Mediator of Small Nuclear RNA Processing, Associates with the C-Terminal Repeat of RNA Polymerase II

Baillat, D., Hakimi, M., Näär, A. M., Shilatifard, A., Cooch, N. S., & Shiekhattar, R. (2005) · Cell · doi:10.1016/j.cell.2005.08.019 · Cited by 548 · see citing works

Essential Role for the SMN Complex in the Specificity of snRNP Assembly

Pellizzoni, L., Yong, J., & Dreyfuss, G. (2002) · Science · doi:10.1126/science.1074962 · Cited by 544 · see citing works

An RNA map predicting Nova-dependent splicing regulation

Ule, J., Stefani, G., Mele, A., Ruggiu, M., Wang, X., Taneri, B., Gaasterland, T., Blencowe, B. J., & Darnell, R. B. (2006) · Nature · doi:10.1038/nature05304 · Cited by 528 · see citing works

A nuclear cap binding protein complex involved in pre-mRNA splicing

Izaurralde, E., Lewis, J., McGuigan, C., Jankowska, M., Darzynkiewicz, E., & Mattaj, I. W. (1994) · Cell · doi:10.1016/0092-8674(94)90530-4 · Cited by 517 · see citing works

SMN oligomerization defect correlates with spinal muscular atrophy severity

Lorson, C. L., Strasswimmer, J., Yao, J.-M., Baleja, J., Hahnen, E., Wirth, B., Le, T. T., Burghes, A. H. M., & Androphy, E. J. (1998) · Nature Genetics · doi:10.1038/ng0598-63 · Cited by 500 · see citing works

Crystal Structure of a Self-Spliced Group II Intron

Toor, N., Keating, K. S., Taylor, S. D., & Pyle, A. M. (2008) · Science · doi:10.1126/science.1153803 · Cited by 498 · see citing works

Mass spectrometry and EST-database searching allows characterization of the multi-protein spliceosome complex

Neubauer, G., King, A., Rappsilber, J., Calvio, C., Watson, M. A., Ajuh, P., Sleeman, J., Lamond, A. I., & Mann, M. (1998) · Nature Genetics · doi:10.1038/1700 · Cited by 478 · see citing works

Crystal Structures of Two Sm Protein Complexes and Their Implications for the Assembly of the Spliceosomal snRNPs

Kambach, C., Walke, S., Young, R., Avis, J. M., Fortelle, E. D. L., Raker, V. A., Lührmann, R., Li, J., & Nagai, K. (1999) · Cell · doi:10.1016/s0092-8674(00)80550-4 · Cited by 475 · 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

Polyadenylation factor CPSF-73 is the pre-mRNA 3'-end-processing endonuclease

Mandel, C. R., Kaneko, S., Zhang, H., Gebauer, D., Vethantham, V., Manley, J. L., & Tong, L. (2006) · Nature · doi:10.1038/nature05363 · Cited by 458 · see citing works

Pre-mRNA splicing in disease and therapeutics

Singh, R. K., & Cooper, T. A. (2012) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2012.06.006 · Cited by 456 · see citing works

Identifying specific protein interaction partners using quantitative mass spectrometry and bead proteomes

Trinkle‐Mulcahy, L., Boulon, S., Lam, Y. W., Urcia, R., Boisvert, F., Vandermoere, F., MORRICE, N. A., Swift, S., Rothbauer, U., Leonhardt, H., et al. (2008) · The Journal of Cell Biology · doi:10.1083/jcb.200805092 · Cited by 446 · see citing works

Dynamic Protein-Protein Interaction Wiring of the Human Spliceosome

Hegele, A., Kamburov, A., Großmann, A., Sourlis, C., Wowro, S. J., Weimann, M., Will, C. L., Peña, V., Lührmann, R., & Stelzl, U. (2012) · Molecular Cell · doi:10.1016/j.molcel.2011.12.034 · Cited by 414 · see citing works

The Methylosome, a 20S Complex Containing JBP1 and pICln, Produces Dimethylarginine-Modified Sm Proteins

Friesen, W. J., Paushkin, S. V., Wyce, A., Massenet, S., Pesiridis, G. S., Duyne, G. D. V., Rappsilber, J., Mann, M., & Dreyfuss, G. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.24.8289-8300.2001 · Cited by 412 · see citing works

Promoter directionality is controlled by U1 snRNP and polyadenylation signals

Almada, A. E., Wu, X., Kriz, A. J., Burge, C. B., & Sharp, P. A. (2013) · Nature · doi:10.1038/nature12349 · Cited by 406 · see citing works

Isolation of an active step I spliceosome and composition of its RNP core

Bessonov, S., Anokhina, M. M., Will, C. L., Urlaub, H., & Lührmann, R. (2008) · Nature · doi:10.1038/nature06842 · Cited by 390 · see citing works

The spliceosome: the most complex macromolecular machine in the cell?

Nilsen, T. W. (2003) · BioEssays · doi:10.1002/bies.10394 · Cited by 378 · see citing works

PHAX, a Mediator of U snRNA Nuclear Export Whose Activity Is Regulated by Phosphorylation

Ohno, M., Segref, A., Bachi, A., Wilm, M. S., & Mattaj, I. W. (2000) · Cell · doi:10.1016/s0092-8674(00)80829-6 · Cited by 374 · see citing works

Methylation of Sm proteins by a complex containing PRMT5 and the putative U snRNP assembly factor pICln

Meister, G., Eggert, C., Bühler, D., Brahms, H., Kambach, C., & Fischer, U. (2001) · Current Biology · doi:10.1016/s0960-9822(01)00592-9 · Cited by 373 · see citing works

Regulation of Fas Alternative Splicing by Antagonistic Effects of TIA-1 and PTB on Exon Definition

Izquierdo, J. M., Oró, N. M., Bonnal, S., Martínez, C., Castelo, R., Guigó, R., Bilbao, D., & Valcárcel, J. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.06.015 · Cited by 364 · see citing works

Dynamic RNA-RNA interactions in the spliceosome

Madhani, H. D., & Guthrie, C. (1994) · Annual Review of Genetics · doi:10.1146/annurev.ge.28.120194.000245 · Cited by 357 · see citing works

RNA catalyses nuclear pre-mRNA splicing

Fica, S. M., Tuttle, N., Novak, T., Li, N., Lu, J., Koodathingal, P., Dai, Q., Staley, J. P., & Piccirilli, J. A. (2013) · Nature · doi:10.1038/nature12734 · Cited by 348 · see citing works

Exon and intron definition in pre‐mRNA splicing

Conti, L. D., Baralle, M., & Buratti, E. (2012) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1140 · Cited by 331 · see citing works

SMN tudor domain structure and its interaction with the Sm proteins.

Sattler, M., Selenko, P., Sprangers, R., Stier, G., Bühler, D., & Fischer, U. (2001) · Nature Structural Biology · doi:10.1038/83014 · Cited by 324 · see citing works

RNA unwinding in U4/U6 snRNPs requires ATP hydrolysis and the DEIH-box splicing factor Brr2

Raghunathan, P. L., & Guthrie, C. (1998) · Current Biology · doi:10.1016/s0960-9822(07)00345-4 · Cited by 318 · see citing works

Ribonucleoprotein Assembly Defects Correlate with Spinal Muscular Atrophy Severity and Preferentially Affect a Subset of Spliceosomal snRNPs

Gabanella, F., Butchbach, M. E. R., Saieva, L., Carissimi, C., Burghes, A. H. M., & Pellizzoni, L. (2007) · PLoS ONE · doi:10.1371/journal.pone.0000921 · Cited by 315 · see citing works

The Evolutionarily Conserved Core Design of the Catalytic Activation Step of the Yeast Spliceosome

Fabrizio, P., Dannenberg, J., Dube, P., Kastner, B., Stark, H., Urlaub, H., & Lührmann, R. (2009) · Molecular Cell · doi:10.1016/j.molcel.2009.09.040 · Cited by 313 · see citing works

Crossregulation and Functional Redundancy between the Splicing Regulator PTB and Its Paralogs nPTB and ROD1

Spellman, R., Llorian, M., & Smith, C. W. J. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.06.016 · Cited by 313 · see citing works

A multiprotein complex mediates the ATP-dependent assembly of spliceosomal U snRNPs

Meister, G., Bühler, D., Pillai, R. S., Lottspeich, F., & Fischer, U. (2001) · Nature Cell Biology · doi:10.1038/ncb1101-945 · Cited by 307 · see citing works

Mutually Exclusive Splicing of the Insect Dscam Pre-mRNA Directed by Competing Intronic RNA Secondary Structures

Graveley, B. R. (2005) · Cell · doi:10.1016/j.cell.2005.07.028 · Cited by 295 · 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

Post-transcriptional spliceosomes are retained in nuclear speckles until splicing completion

Girard, C., Will, C. L., Peng, J., Makarov, E. M., Kastner, B., Lemm, I., Urlaub, H., Hartmuth, K., & Lührmann, R. (2012) · Nature Communications · doi:10.1038/ncomms1998 · Cited by 287 · see citing works

Cotranscriptional Spliceosome Assembly Occurs in a Stepwise Fashion and Requires the Cap Binding Complex

Görnemann, J., Kotovic, K. M., Hujer, K., & Neugebauer, K. M. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.05.007 · Cited by 285 · 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

Ordered and Dynamic Assembly of Single Spliceosomes

Hoskins, A. A., Friedman, L. J., Gallagher, S. S., Crawford, D. J., Anderson, E. G., Wombacher, R., Ramirez, N., Cornish, V. W., Gelles, J., & Moore, M. J. (2011) · Science · doi:10.1126/science.1198830 · Cited by 279 · see citing works

Snurportin1, an m3G‐cap‐specific nuclear import receptor with a novel domain structure

Huber, J., Cronshagen, U., Kadokura, M., Marshallsay, C., Wada, T., Sekine, M., & Lührmann, R. (1998) · The EMBO Journal · doi:10.1093/emboj/17.14.4114 · Cited by 277 · see citing works

Composition and Functional Characterization of the Yeast Spliceosomal Penta-snRNP

Stevens, S. W., Ryan, D. E., Ge, H. Y., Moore, R. E., Young, M. K., Lee, T. D., & Abelson, J. N. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00436-7 · Cited by 273 · see citing works

Advances in RNA structure analysis by chemical probing

Weeks, K. M. (2010) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2010.04.001 · Cited by 270 · see citing works

The architecture of pre-mRNAs affects mechanisms of splice-site pairing

Fox-Walsh, K. L., Dou, Y., Lam, B. J., Hung, S., Baldi, P., & Hertel, K. J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508489102 · Cited by 267 · see citing works

SR proteins promote the first specific recognition of Pre-mRNA and are present together with the U1 small nuclear ribonucleoprotein particle in a general splicing enhancer complex.

Staknis, D., & Reed, R. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.11.7670 · Cited by 265 · see citing works

Mutations in U4atac snRNA, a Component of the Minor Spliceosome, in the Developmental Disorder MOPD I

He, H., Liyanarachchi, S., Akagi, K., Nagy, R. S., Li, J., Dietrich, R. C., Li, W., Sebastian, N., Wen, B., Xin, B., et al. (2011) · Science · doi:10.1126/science.1200587 · Cited by 262 · see citing works

The nucleolus: structure/function relationship in RNA metabolism

Hernandez‐Verdun, D., Roussel, P., Thiry, M., Sirri, V., & Lafontaine, D. L. J. (2010) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.39 · Cited by 261 · see citing works

Essential Role for the Tudor Domain of SMN in Spliceosomal U snRNP Assembly: Implications for Spinal Muscular Atrophy

Buhler, D., Raker, V., Luhrmann, R., & Fischer, U. (1999) · Human Molecular Genetics · doi:10.1093/hmg/8.13.2351 · Cited by 257 · see citing works

Formation of the 3′ end of U1 snRNA requires compatible snRNA promoter elements

Hernandez, N., & Weiner, A. M. (1986) · Cell · doi:10.1016/0092-8674(86)90447-2 · Cited by 256 · see citing works

Modification of Sm small nuclear RNAs occurs in the nucleoplasmic Cajal body following import from the cytoplasm

Jády, B. E., Darzacq, X., Tucker, K. E., Matera, A. G., Bertrand, É., & Kiss, T. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg187 · Cited by 252 · see citing works

hnRNP H Is a Component of a Splicing Enhancer Complex That Activates a c- src Alternative Exon in Neuronal Cells

Chou, M., Rooke, N., Turck, C. W., & Black, D. L. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.1.69 · Cited by 251 · see citing works

The snRNP core assembly pathway: identification of stable core protein heteromeric complexes and an snRNP subcore particle in vitro.

Raker, V. A., Plessel, G., & Lührmann, R. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00579.x · Cited by 250 · see citing works

Nascent-seq indicates widespread cotranscriptional pre-mRNA splicing in <i>Drosophila</i>

Khodor, Y. L., Rodriguez, J., Abruzzi, K. C., Tang, C.-H. A., Marr, M. T., & Rosbash, M. (2011) · Genes &amp; Development · doi:10.1101/gad.178962.111 · Cited by 250 · see citing works

Newly assembled snRNPs associate with coiled bodies before speckles, suggesting a nuclear snRNP maturation pathway

Sleeman, J., & Lamond, A. I. (1999) · Current Biology · doi:10.1016/s0960-9822(99)80475-8 · Cited by 247 · see citing works

SMN mutants of spinal muscular atrophy patients are defective in binding to snRNP proteins

Pellizzoni, L., Charroux, B., & Dreyfuss, G. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.20.11167 · Cited by 246 · see citing works

Molecular anatomy of a speckle

Hall, L. L., Smith, K. P., Byron, M., & Lawrence, J. B. (2006) · The Anatomical Record Part A Discoveries in Molecular Cellular and Evolutionary Biology · doi:10.1002/ar.a.20336 · Cited by 246 · see citing works

Prp22, a DExH‐box RNA helicase, plays two distinct roles in yeast pre‐mRNA splicing

Schwer, B., & Gross, C. H. (1998) · The EMBO Journal · doi:10.1093/emboj/17.7.2086 · Cited by 239 · see citing works

Global impact of RNA polymerase II elongation inhibition on alternative splicing regulationPreprint

Ip, J. Y. Y., Schmidt, D., Pan, Q., Ramani, A. K., Fraser, A. G., Odom, D. T., & Blencowe, B. J. (2010) · Genome Research · doi:10.1101/gr.111070.110 · Cited by 237 · see citing works

Interaction between the RNA binding domains of Ser-Arg splicing factor 1 and U1-70K snRNP protein determines early spliceosome assembly

Cho, S., Hoang, A., Sinha, R., Zhong, X.-Y., Fu, X., Krainer, A. R., & Ghosh, G. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1017700108 · Cited by 236 · see citing works

An Essential Signaling Role for the m 3 G Cap in the Transport of U1 snRNP to the Nucleus

Fischer, U., & Lührmann, R. (1990) · Science · doi:10.1126/science.2143847 · Cited by 235 · see citing works

An Assembly Chaperone Collaborates with the SMN Complex to Generate Spliceosomal SnRNPs

Chari, A., Golas, M. M., Klingenhäger, M., Neuenkirchen, N., Sander, B. O., Englbrecht, C., Sickmann, A., Stark, H., & Fischer, U. (2008) · Cell · doi:10.1016/j.cell.2008.09.020 · Cited by 232 · see citing works

Crystal structure of Prp8 reveals active site cavity of the spliceosome

Galej, W. P., Oubridge, C., Newman, A. J., & Nagai, K. (2013) · Nature · doi:10.1038/nature11843 · Cited by 231 · see citing works

Residual Cajal bodies in coilin knockout mice fail to recruit Sm snRNPs and SMN, the spinal muscular atrophy gene product

Tucker, K. E., Berciano, M. T., Jacobs, E. Y., LePage, D. F., Shpargel, K. B., Rossire, J. J., Chan, E. K. L., Lafarga, M., Conlon, R. A., & Matera, A. G. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.200104083 · Cited by 228 · see citing works

The Long Unwinding Road of RNA Helicases

Bleichert, F., & Baserga, S. J. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.07.014 · Cited by 228 · see citing works

Alternative Splicing Events Are a Late Feature of Pathology in a Mouse Model of Spinal Muscular Atrophy

Bäumer, D., Lee, S., Nicholson, G., Davies, J. L., Parkinson, N., Murray, L. M., Gillingwater, T. H., Ansorge, O., Davies, K. E., & Talbot, K. (2009) · PLoS Genetics · doi:10.1371/journal.pgen.1000773 · Cited by 227 · see citing works

G Triplets Located throughout a Class of Small Vertebrate Introns Enforce Intron Borders and Regulate Splice Site Selection

McCullough, A. J., & Berget, S. M. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.8.4562 · Cited by 223 · see citing works

A new type of mutation causes a splicing defect in ATM

Pagani, F., Buratti, E., Stuani, C., Bendix, R., Dörk, T., & Baralle, F. E. (2002) · Nature Genetics · doi:10.1038/ng858 · Cited by 217 · see citing works

Multiple Splicing Defects in an Intronic False Exon

Sun, H., & Chasin, L. A. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.17.6414-6425.2000 · Cited by 209 · see citing works

Determination of the RNA Binding Specificity of the Heterogeneous Nuclear Ribonucleoprotein (hnRNP) H/H′/F/2H9 Family

Caputi, M., & Zahler, A. M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102861200 · Cited by 206 · see citing works

Gemin proteins are required for efficient assembly of Sm-class ribonucleoproteins

Shpargel, K. B., & Matera, A. G. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0508947102 · Cited by 205 · see citing works

Nuclear RNA export

Cullen, B. R. (2003) · Journal of Cell Science · doi:10.1242/jcs.00268 · Cited by 203 · see citing works

Binding of hnRNP H to an exonic splicing silencer is involved in the regulation of alternative splicing of the rat beta -tropomyosin genePreprint

Chen, C. D., Kobayashi, R., & Helfman, D. M. (1999) · Genes & Development · doi:10.1101/gad.13.5.593 · 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

Co-transcriptional commitment to alternative splice site selection

Roberts, G. P. (1998) · Nucleic Acids Research · doi:10.1093/nar/26.24.5568 · Cited by 198 · see citing works

The EF-G-like GTPase Snu114p Regulates Spliceosome Dynamics Mediated by Brr2p, a DExD/H Box ATPase

Small, E. C., Leggett, S. R., Winans, A. A., & Staley, J. P. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.05.043 · Cited by 194 · see citing works

A novel U2-U6 snRNA structure is necessary for mammalian mRNA splicing.Preprint

Sun, J., & Manley, J. L. (1995) · Genes & Development · doi:10.1101/gad.9.7.843 · Cited by 193 · see citing works

hnRNP C Tetramer Measures RNA Length to Classify RNA Polymerase II Transcripts for Export

McCloskey, A., Taniguchi, I., Shinmyozu, K., & Ohno, M. (2012) · Science · doi:10.1126/science.1218469 · Cited by 191 · see citing works

Trans -Splicing in Trypanosomes: Machinery and Its Impact on the Parasite Transcriptome

Michaeli, S. (2011) · Future Microbiology · doi:10.2217/fmb.11.20 · Cited by 191 · see citing works

Nuclear Bodies: Random Aggregates of Sticky Proteins or Crucibles of Macromolecular Assembly?

Matera, A. G., Izaguire-Sierra, M., Praveen, K., & Rajendra, T. K. (2009) · Developmental Cell · doi:10.1016/j.devcel.2009.10.017 · Cited by 186 · see citing works

Architectural limits on split genes

Sterner, D. A., Carlo, T., & Berget, S. M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.26.15081 · Cited by 185 · see citing works

Nucleo‐cytoplasmic transport of U snRNPs: definition of a nuclear location signal in the Sm core domain that binds a transport receptor independently of the m3G cap.

Fischer, U., Sumpter, V. G., SEKINE, M., Satoh, T., & Lührmann, R. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb05689.x · Cited by 185 · see citing works

New connections between splicing and human disease

Padgett, R. A. (2012) · Trends in Genetics · doi:10.1016/j.tig.2012.01.001 · Cited by 183 · see citing works

Ongoing U snRNP Biogenesis Is Required for the Integrity of Cajal Bodies

Lemm, I., Girard, C., Kuhn, A. N., Watkins, N. J., Schneider, M., Bordonné, R., & Lührmann, R. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e06-03-0247 · Cited by 182 · see citing works

Coilin-dependent snRNP assembly is essential for zebrafish embryogenesis

Strzelecka, M., Trowitzsch, S., Weber, G., Lührmann, R., Oates, A. C., & Neugebauer, K. M. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1783 · Cited by 179 · see citing works

Polypyrimidine tract binding protein controls the transition from exon definition to an intron defined spliceosome

Sharma, S., Kohlstaedt, L. A., Damianov, A., Rio, D. C., & Black, D. L. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1375 · Cited by 177 · see citing works

RBM5/Luca-15/H37 Regulates Fas Alternative Splice Site Pairing after Exon Definition

Bonnal, S., Martínez, C., Förch, P., Bachi, A., Wilm, M. S., & Valcárcel, J. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.08.008 · Cited by 176 · see citing works

Conservation of the Protein Composition and Electron Microscopy Structure of Drosophila melanogaster and Human Spliceosomal Complexes

Herold, N., Will, C. L., Wolf, E., Kastner, B., Urlaub, H., & Lührmann, R. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01415-08 · Cited by 176 · see citing works

Visualizing Group II Intron Catalysis through the Stages of Splicing

Marcia, M., & Pyle, A. M. (2012) · Cell · doi:10.1016/j.cell.2012.09.033 · Cited by 176 · see citing works

PHAX and CRM1 Are Required Sequentially to Transport U3 snoRNA to Nucleoli

Boulon, S., Verheggen, C., Jády, B. E., Girard, C., Begon‐Pescia, C., Paul, C., Ospina, J. K., Kiss, T., Matera, A. G., Bordonné, R., et al. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.11.013 · Cited by 175 · see citing works

The U1 snRNP protein U1C recognizes the 5′ splice site in the absence of base pairing

Du, H., & Rosbash, M. (2002) · Nature · doi:10.1038/nature00947 · Cited by 169 · see citing works

RNAi knockdown of hPrp31 leads to an accumulation of U4/U6 di‐snRNPs in Cajal bodies

Schaffert, N., Hoßbach, M., Heintzmann, R., Achsel, T., & Lührmann, R. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600296 · Cited by 167 · see citing works

PRPF mutations are associated with generalized defects in spliceosome formation and pre-mRNA splicing in patients with retinitis pigmentosa

Tanačković, G., Ransijn, A., Thibault, P., Elela, S. A., Klinck, R., Berson, E. L., Chabot, B., & Rivolta, C. (2011) · Human Molecular Genetics · doi:10.1093/hmg/ddr094 · 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

CBC–ARS2 stimulates 3′-end maturation of multiple RNA families and favors cap-proximal processing

Hallais, M., Pontvianne, F., Andersen, P. R., Clerici, M., Lener, D., Benbahouche, N. E. H., Gostan, T., Vandermoere, F., Robert, M.-C., Cusack, S., et al. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2720 · Cited by 159 · see citing works

A Drosophila melanogaster model of spinal muscular atrophy reveals a function for SMN in striated muscle

Rajendra, T. K., Gonsalvez, G. B., Walker, M. P., Shpargel, K. B., Salz, H. K., & Matera, A. G. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200610053 · Cited by 158 · see citing works

The Cajal body: a meeting place for spliceosomal snRNPs in the nuclear maze

Staněk, D., & Neugebauer, K. M. (2006) · Chromosoma · doi:10.1007/s00412-006-0056-6 · Cited by 158 · see citing works

Biologic and clinical significance of somatic mutations of SF3B1 in myeloid and lymphoid neoplasms

Cazzola, M., Rossi, M., & Malcovati, L. (2012) · Blood · doi:10.1182/blood-2012-09-399725 · Cited by 151 · see citing works

Trans ‐splicing

Lasda, E. L., & Blumenthal, T. (2011) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.71 · Cited by 146 · see citing works

Coilin Is Essential for Cajal Body Organization in Drosophila melanogaster

Liu, J., Wu, Z., Nizami, Z. F., Deryusheva, S., Rajendra, T. K., Beumer, K. J., Gao, H., Matera, A. G., Carroll, D., & Gall, J. G. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-05-0525 · Cited by 144 · see citing works

Coupled In Vitro Import of U snRNPs and SMN, the Spinal Muscular Atrophy Protein

Narayanan, U., Achsel, T., Lührmann, R., & Matera, A. G. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.09.024 · Cited by 143 · see citing works

Nuclear import of U snRNPs requires importin β

Palacios, I. M., Hetzer, M., Adam, S. A., & Mattaj, I. W. (1997) · The EMBO Journal · doi:10.1093/emboj/16.22.6783 · Cited by 142 · see citing works

Gemin5 Delivers snRNA Precursors to the SMN Complex for snRNP Biogenesis

Yong, J., Kasim, M., Bachorik, J. L., Wan, L., & Dreyfuss, G. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.03.014 · Cited by 141 · see citing works

E Pluribus Unum: 3′ End Formation of Polyadenylated mRNAs, Histone mRNAs, and U snRNAs

Weiner, A. M. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.10.009 · Cited by 139 · see citing works

Structure of a Key Intermediate of the SMN Complex Reveals Gemin2's Crucial Function in snRNP Assembly

Zhang, R., So, B. R., Li, P., Yong, J., Glisovic, T., Wan, L., & Dreyfuss, G. (2011) · Cell · doi:10.1016/j.cell.2011.06.043 · Cited by 137 · see citing works

Inhibition of RNA Helicase Brr2 by the C-Terminal Tail of the Spliceosomal Protein Prp8

Mozaffari‐Jovin, S., Wandersleben, T., Santos, K. F., Will, C. L., Lührmann, R., & Wahl, M. C. (2013) · Science · doi:10.1126/science.1237515 · Cited by 136 · see citing works

Structure of a Multipartite Protein-Protein Interaction Domain in Splicing Factor Prp8 and Its Link to Retinitis Pigmentosa

Peña, V., Liu, S., Bujnicki, J. M., Lührmann, R., & Wahl, M. C. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.01.023 · Cited by 132 · see citing works

Structure of the spliceosomal U4 snRNP core domain and its implication for snRNP biogenesis

Leung, A., Nagai, K., & Li, J. (2011) · Nature · doi:10.1038/nature09956 · Cited by 132 · see citing works

The SMN Complex Is Associated with snRNPs throughout Their Cytoplasmic Assembly Pathway

Massenet, S., Pellizzoni, L., Paushkin, S. V., Mattaj, I. W., & Dreyfuss, G. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.18.6533-6541.2002 · Cited by 131 · see citing works

Regulation of Alternative Splicing by the ATP-Dependent DEAD-Box RNA Helicase p72

Hönig, A., Auboeuf, D., Parker, M. M., O’Malley, B. W., & Berget, S. M. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.16.5698-5707.2002 · Cited by 130 · see citing works

Dynamic Regulation of Alternative Splicing by Silencers that Modulate 5′ Splice Site Competition

Yu, Y., Maroney, P. A., Denker, J. A., Zhang, X. H.-F., Dybkov, O., Lührmann, R., Jankowsky, E., Chasin, L. A., & Nilsen, T. W. (2008) · Cell · doi:10.1016/j.cell.2008.10.046 · Cited by 129 · see citing works

SMN, the spinal muscular atrophy protein, forms a pre-import snRNP complex with snurportin1 and importin beta

Narayanan, U. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.15.1785 · Cited by 119 · see citing works

Targeting of U4/U6 small nuclear RNP assembly factor SART3/p110 to Cajal bodies

Staněk, D., Rader, S. D., Klingauf, M., & Neugebauer, K. M. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200210087 · Cited by 118 · see citing works

The Integrator Complex Recognizes a New Double Mark on the RNA Polymerase II Carboxyl-terminal Domain

Egloff, S., Szczepaniak, S. A., Dienstbier, M., Taylor, A., Knight, S., & Murphy, S. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.132530 · Cited by 117 · see citing works

Interaction between the small‐nuclear‐RNA cap hypermethylase and the spinal muscular atrophy protein, survival of motor neuron

Mouaikel, J., Narayanan, U., Verheggen, C., Matera, A. G., Bertrand, É., Tazi, J., & Bordonné, R. (2003) · EMBO Reports · doi:10.1038/sj.embor.embor863 · Cited by 114 · see citing works

Both Catalytic Steps of Nuclear Pre-mRNA Splicing Are Reversible

Tseng, C. K., & Cheng, S.-C. (2008) · Science · doi:10.1126/science.1158993 · Cited by 112 · see citing works

Stabilization of the Tau Exon 10 Stem Loop Alters Pre-mRNA Splicing

Donahue, C. P., Muratore, C., Wu, J. Y., Kosik, K. S., & Wolfe, M. S. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.c600143200 · Cited by 110 · see citing works

A complex network of factors with overlapping affinities represses splicing through intronic elements

Wang, Y., Xiao, X. G., Zhang, J., Choudhury, R., Robertson, A. D., Li, K., Ma, M., Burge, C. B., & Wang, Z. (2012) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2459 · Cited by 109 · see citing works

Dissection of the factor requirements for spliceosome disassembly and the elucidation of its dissociation products using a purified splicing systemPreprint

Fourmann, J., Schmitzová, J., Christian, H., Urlaub, H., Ficner, R., Boon, K.-L., Fabrizio, P., & Lührmann, R. (2013) · Genes & Development · doi:10.1101/gad.207779.112 · Cited by 109 · see citing works

Detection of snRNP assembly intermediates in Cajal bodies by fluorescence resonance energy transfer

Staněk, D., & Neugebauer, K. M. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200405160 · Cited by 109 · see citing works

Structure, function and regulation of spliceosomal RNA helicases

Cordin, O., Hahn, D., & Beggs, J. D. (2012) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2012.03.004 · Cited by 108 · see citing works

prp8 mutations that cause human retinitis pigmentosa lead to a U5 snRNP maturation defect in yeast

Boon, K.-L., Grainger, R. J. R., Ehsani, P., Barrass, J. D., Auchynnikava, T., Inglehearn, C. F., & Beggs, J. D. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1303 · Cited by 108 · see citing works

Counting on co-transcriptional splicing

Brugiolo, M., Herzel, L., & Neugebauer, K. M. (2013) · F1000Prime Reports · doi:10.12703/p5-9 · Cited by 108 · see citing works

Pumping RNA: nuclear bodybuilding along the RNP pipeline

Matera, A. G., & Shpargel, K. B. (2006) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2006.03.005 · Cited by 105 · see citing works

Exon Definition Complexes Contain the Tri-snRNP and Can Be Directly Converted into B-like Precatalytic Splicing Complexes

Schneider, M., Will, C. L., Anokhina, M. M., Tazi, J., Urlaub, H., & Lührmann, R. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.02.027 · Cited by 104 · see citing works

A Subset of Drosophila Integrator Proteins Is Essential for Efficient U7 snRNA and Spliceosomal snRNA 3′-End Formation

Ezzeddine, N., Chen, J., Waltenspiel, B., Burch, B. D., Albrecht, T. R., Zhuo, M., Warren, W., Marzluff, W. F., & Wagner, E. J. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00943-10 · Cited by 103 · see citing works

RNA-mediated interaction of Cajal bodies and U2 snRNA genes

Frey, M. R., & Matera, A. G. (2001) · The Journal of Cell Biology · doi:10.1083/jcb.200105084 · Cited by 101 · see citing works

Evolution of an RNP assembly system: A minimal SMN complex facilitates formation of UsnRNPs in Drosophila melanogaster

Kroiß, M., Schultz, J., Wiesner, J., Chari, A., Sickmann, A., & Fischer, U. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0802287105 · Cited by 100 · see citing works

RNA secondary structure in mutually exclusive splicing

Yang, Y., Zhan, L., Zhang, W., Sun, F., Wang, W., Tian, N., Bi, J., Wang, H., Shi, D., Jiang, Y., et al. (2011) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1959 · Cited by 100 · see citing works

Role of poly (A) tail as an identity element for mRNA nuclear export

Fuke, H., & Ohno, M. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm1120 · Cited by 99 · see citing works

Structural Basis of Assembly Chaperone- Mediated snRNP Formation

Grimm, C., Chari, A., Pelz, J.-P., Kuper, J., Kisker, C., Diederichs, K., Stark, H., Schindelin, H., & Fischer, U. (2013) · Molecular Cell · doi:10.1016/j.molcel.2012.12.009 · Cited by 99 · see citing works

An exonic splicing silencer represses spliceosome assembly after ATP-dependent exon recognition

House, A. E., & Lynch, K. W. (2006) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1149 · Cited by 98 · see citing works

Conformational dynamics of single pre-mRNA molecules during in vitro splicing

Abelson, J. N., Blanco, M. R., Ditzler, M. A., Fuller, F. D., Aravamudhan, P., Wood, M. L., Villa, T., Ryan, D. E., Pleiss, J. A., Maeder, C., et al. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1767 · Cited by 97 · see citing works

U1 snRNA Directly Interacts with Polypyrimidine Tract-Binding Protein during Splicing Repression

Sharma, S., Maris, C., Allain, F. H. ‐., & Black, D. L. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.02.012 · Cited by 97 · see citing works

Reduced Viability, Fertility and Fecundity in Mice Lacking the Cajal Body Marker Protein, Coilin

Walker, M. P., Tian, L., & Matera, A. G. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006171 · Cited by 93 · see citing works

The nuclear cap-binding complex interacts with the U4/U6·U5 tri-snRNP and promotes spliceosome assembly in mammalian cells

Pabiś, M., Neufeld, N., Steiner, M. C., Bojić, T., Shav‐Tal, Y., & Neugebauer, K. M. (2013) · RNA · doi:10.1261/rna.037069.112 · Cited by 93 · see citing works

The Little Elongation Complex Regulates Small Nuclear RNA Transcription

Smith, E. R., Lin, C., Garrett, A. S., Thornton, J., Mohaghegh, N., Hu, D., Jackson, J., Saraf, A. P., Swanson, S. K., Seidel, C. W., et al. (2011) · Molecular Cell · doi:10.1016/j.molcel.2011.12.008 · Cited by 91 · see citing works

Specific trans-acting proteins interact with auxiliary RNA polyadenylation elements in the COX-2 3′-UTR

Hall‐Pogar, T., Liang, S., Hague, L. K., & Lutz, C. S. (2007) · RNA · doi:10.1261/rna.577707 · Cited by 90 · see citing works

A role for Cajal bodies in the final steps of U2 snRNP biogenesis

Nešić, D., Tanačković, G., & Krämer, A. (2004) · Journal of Cell Science · doi:10.1242/jcs.01308 · Cited by 90 · see citing works

Spliced leader RNAs from lower eukaryotes are trans- spliced in mammalian cells

Bruzik, J. P., & Maniatis, T. (1992) · Nature · doi:10.1038/360692a0 · Cited by 86 · see citing works

RNA length defines RNA export pathwayPreprint

Masuyama, K., Taniguchi, I., Kataoka, N., & Ohno, M. (2004) · Genes & Development · doi:10.1101/gad.1216204 · Cited by 86 · see citing works

Solution Structure and Ligand Recognition of the WW Domain Pair of the Yeast Splicing Factor Prp40

Wiesner, S., Stier, G., Sattler, M., & Macías, M. J. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)01145-2 · Cited by 84 · see citing works

SNAP19 mediates the assembly of a functional core promoter complex (SNAPc) shared by RNA polymerases II and IIIPreprint

Henry, R. W., Mittal, V., Ma, B., Kobayashi, R., & Hernandez, N. (1998) · Genes & Development · doi:10.1101/gad.12.17.2664 · Cited by 84 · see citing works

Identity Elements Used in Export of mRNAs

Ohno, M., Segref, A., Kuersten, S., & Mattaj, I. W. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00454-9 · Cited by 80 · see citing works

In vivo kinetics of U4/U6·U5 tri-snRNP formation in Cajal bodies

Novotný, I., Blažíková, M., Staněk, D., Heřman, P., & Malínský, J. (2010) · Molecular Biology of the Cell · doi:10.1091/mbc.e10-07-0560 · Cited by 79 · see citing works

Protein-free small nuclear RNAs catalyze a two-step splicing reaction

Valadkhan, S., Mohammadi, A., Jaladat, Y., & Geisler, S. J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0902020106 · Cited by 76 · see citing works

A Drosophila Model of Spinal Muscular Atrophy Uncouples snRNP Biogenesis Functions of Survival Motor Neuron from Locomotion and Viability Defects

Praveen, K., Wen, Y., & Matera, A. G. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.05.014 · Cited by 76 · see citing works

The Survival Motor Neuron Protein Forms Soluble Glycine Zipper Oligomers

Martin, R. S., Gupta, K., Ninan, N. S., Perry, K., & Duyne, G. D. V. (2012) · Structure · doi:10.1016/j.str.2012.08.024 · Cited by 74 · see citing works

An RNAi screen identifies additional members of the Drosophila Integrator complex and a requirement for cyclin C/Cdk8 in snRNA 3′-end formation

Chen, J., Ezzeddine, N., Waltenspiel, B., Albrecht, T. R., Warren, W., Marzluff, W. F., & Wagner, E. J. (2012) · RNA · doi:10.1261/rna.035725.112 · Cited by 74 · see citing works

HnRNP L and HnRNP A1 Induce Extended U1 snRNA Interactions with an Exon to Repress Spliceosome Assembly

Chiou, N.-T., Shankarling, G. S., & Lynch, K. W. (2013) · Molecular Cell · doi:10.1016/j.molcel.2012.12.025 · Cited by 73 · see citing works

The Schizosaccharomyces pombe protein Yab8p and a novel factor, Yip1p, share structural and functional similarity with the spinal muscular atrophy-associated proteins SMN and SIP1

Hannus, S. (2000) · Human Molecular Genetics · doi:10.1093/hmg/9.5.663 · Cited by 70 · see citing works

Molecular dissection of step 2 catalysis of yeast pre-mRNA splicing investigated in a purified system

Ohrt, T., Odenwälder, P., Dannenberg, J., Prior, M., Warkocki, Z., Schmitzová, J., Karaduman, R., Gregor, I., Enderlein, J., Fabrizio, P., et al. (2013) · RNA · doi:10.1261/rna.039024.113 · Cited by 67 · see citing works

Dynamic control of Cajal body number during zebrafish embryogenesis

Strzelecka, M., Oates, A. C., & Neugebauer, K. M. (2010) · Nucleus · doi:10.4161/nucl.1.1.10680 · Cited by 64 · see citing works

Structural insights into RNA splicing

Toor, N., Keating, K. S., & Pyle, A. M. (2009) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2009.04.002 · Cited by 61 · see citing works

Interactions of U2 Gene Loci and Their Nuclear Transcripts with Cajal (Coiled) Bodies: Evidence for PreU2 within Cajal Bodies

Smith, K. P., & Lawrence, J. B. (2000) · Molecular Biology of the Cell · doi:10.1091/mbc.11.9.2987 · Cited by 61 · see citing works

Coevolutionary networks of splicing cis -regulatory elements

Xiao, X. G., Wang, Z., Jang, M., & Burge, C. B. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0707349104 · Cited by 61 · see citing works

The U1 snRNP Base Pairs with the 5′ Splice Site within a Penta-snRNP Complex

Malca, H., Shomron, N., & Ast, G. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.10.3442-3455.2003 · Cited by 59 · see citing works

Splicing proofreading at 5′ splice sites by ATPase Prp28p

Yang, F., Wang, X., Zhang, Z.-M., Pu, J., Fan, Y., Zhou, J., Query, C. C., & Xu, Y. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt149 · Cited by 52 · see citing works

The Conserved Intronic Cleavage and Polyadenylation Site of CstF-77 Gene Imparts Control of 3′ End Processing Activity through Feedback Autoregulation and by U1 snRNP

Luo, W., Ji, Z., Pan, Z., You, B., Hoque, M., Li, W., Gunderson, S., & Tian, B. (2013) · PLoS Genetics · doi:10.1371/journal.pgen.1003613 · Cited by 51 · see citing works

Rearrangements within human spliceosomes captured after exon ligation

Ilagan, J. O., Chalkley, R. J., Burlingame, A. L., & Jurica, M. S. (2013) · RNA · doi:10.1261/rna.034223.112 · Cited by 49 · see citing works

Role of the snRNAs in spliceosomal active site

Valadkhan, S. (2010) · RNA Biology · doi:10.4161/rna.7.3.12089 · Cited by 48 · see citing works

Protein-free spliceosomal snRNAs catalyze a reaction that resembles the first step of splicing

Valadkhan, S., Mohammadi, A., Wachtel, C., & Manley, J. L. (2007) · RNA · doi:10.1261/rna.626207 · Cited by 47 · see citing works

RH70, a Bidirectional RNA Helicase, Co-purifies with U1snRNP

Lee, C.-G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200337200 · Cited by 46 · see citing works

Developmental arrest of Drosophila survival motor neuron (Smn) mutants accounts for differences in expression of minor intron-containing genes

Garcia, E. L., Lu, Z., Meers, M. P., Praveen, K., & Matera, A. G. (2013) · RNA · doi:10.1261/rna.038919.113 · Cited by 46 · see citing works

Cajal body surveillance of U snRNA export complex assembly

Suzuki, T., Izumi, H., & Ohno, M. (2010) · The Journal of Cell Biology · doi:10.1083/jcb.201004109 · Cited by 45 · see citing works

SMN-assisted assembly of snRNP-specific Sm cores in trypanosomesPreprint

Pálfi, Z., Jaé, N., Preußer, C., Kaminska, K. H., Bujnicki, J. M., Lee, J. H., Günzl, A., Kambach, C., Urlaub, H., & Bindereif, A. (2009) · Genes & Development · doi:10.1101/gad.526109 · Cited by 42 · see citing works

The integrator complex is required for integrity of Cajal bodies

Takata, H., Nishijima, H., Maeshima, K., & Shibahara, K. (2012) · Journal of Cell Science · doi:10.1242/jcs.090837 · Cited by 42 · see citing works

Identification of novel snRNA-specific Sm proteins that bind selectively to U2 and U4 snRNAs in Trypanosoma brucei

Tkacz, I. D., Lustig, Y., Stern, M. Z., Biton, M., Salmon‐Divon, M., Das, A., Bellofatto, V., & Michaeli, S. (2006) · RNA · doi:10.1261/rna.174307 · Cited by 40 · see citing works

The intronic splicing code: multiple factors involved in ATM pseudoexon definition

Dhir, A., Buratti, E., van Santen, M. A., Lührmann, R., & Baralle, F. E. (2010) · The EMBO Journal · doi:10.1038/emboj.2009.397 · Cited by 40 · see citing works

A Compartmentalized Phosphorylation/Dephosphorylation System That Regulates U snRNA Export from the Nucleus

Kitao, S., Segref, A., Kast, J., Wilm, M. S., Mattaj, I. W., & Ohno, M. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01189-07 · Cited by 39 · see citing works

A conformational switch in PRP8 mediates metal ion coordination that promotes pre-mRNA exon ligation

Schellenberg, M. J., Wu, T., Ritchie, D. B., Fica, S. M., Staley, J. P., Atta, K. A., LaPointe, P., & MacMillan, A. M. (2013) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.2556 · Cited by 39 · see citing works

Cross-Talk between Snurportin1 Subdomains

Ospina, J. K., Gonsalvez, G. B., Bednenko, J., Darżynkiewicz, E., Gerace, L., & Matera, A. G. (2005) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-04-0316 · Cited by 38 · see citing works

An RNA architectural locus control region involved in Dscam mutually exclusive splicing

Wang, X., Li, G., Yang, Y., Wang, W., Zhang, W., Pan, H., Zhang, P., Yue, Y., Lin, H., Liu, B., et al. (2012) · Nature Communications · doi:10.1038/ncomms2269 · Cited by 38 · see citing works

Functional spliceosomal A complexes can be assembled in vitro in the absence of a penta-snRNP

Behzadnia, N., Hartmuth, K., Will, C. L., & Lührmann, R. (2006) · RNA · doi:10.1261/rna.120606 · Cited by 38 · see citing works

Drosophila hnRNP A1 homologs Hrp36/Hrp38 enhance U2-type versus U12-type splicing to regulate alternative splicing of the prospero twintron

Borah, S., Wong, A. C., & STEITZ, J. A. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812826106 · Cited by 36 · see citing works

Cotranscriptional spliceosome assembly and splicing are independent of the Prp40p WW domain

Görnemann, J., Barrandon, C., Hujer, K., Rutz, B., Rigaut, G., Kotovic, K. M., Faux, C., Neugebauer, K. M., & Séraphin, B. (2011) · RNA · doi:10.1261/rna.02646811 · Cited by 33 · see citing works

Regulation of snRNA gene expression by the Drosophila melanogaster small nuclear RNA activating protein complex (DmSNAPc)

Hung, K., & Stumph, W. E. (2010) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2010.518136 · Cited by 33 · see citing works

The Yeast Splicing Factor Prp40p Contains Functional Leucine-Rich Nuclear Export Signals That Are Essential for Splicing

Murphy, M. W., Olson, B. L., & Siliciano, P. G. (2004) · Genetics · doi:10.1534/genetics.166.1.53 · Cited by 27 · see citing works

Functional studies on the ATM intronic splicing processing element

Lewandowska, M. A. (2005) · Nucleic Acids Research · doi:10.1093/nar/gki710 · Cited by 26 · see citing works

Autosomal Dominant Retinitis Pigmentosa Secondary to Pre-mRNA Splicing-Factor GenePRPF31(RP11): Review of Disease Mechanism and Report of a Family with a Novel 3-Base Pair Insertion

Utz, V. M., Beight, C. D., Marino, M. J., Hagstrom, S. A., & Traboulsi, E. I. (2013) · Ophthalmic Genetics · doi:10.3109/13816810.2012.762932 · Cited by 25 · see citing works

Spliceosome mutations in myelodysplastic syndromes and chronic myelomonocytic leukemia

Chesnais, V., Kosmider, O., Damm, F., Itzykson, R., Bernard, O., Solary, É., & Fontenay, M. (2012) · Oncotarget · doi:10.18632/oncotarget.749 · Cited by 24 · see citing works

The Spliceosome and Its Metal Ions

Butcher, S. E. (2011) · Royal Society of Chemistry eBooks · doi:10.1039/9781849732512-00235 · Cited by 23 · see citing works

U1 snRNP-mediated poly(A) site suppression

Langemeier, J., Radtke, M., & Bohne, J. (2013) · RNA Biology · doi:10.4161/rna.23314 · Cited by 16 · see citing works

U1 snRNP regulates cancer cell migration and invasion in vitro

Oh, J.-M., Venters, C. C., Di, C., Pinto, A. M., Wan, L., Younis, I., Cai, Z., Arai, C., So, B. R., Duan, J., et al. (2020) · Nature Communications · doi:10.1038/s41467-019-13993-7 · Cited by 7,157 · see citing works

A brave new world of RNA-binding proteins

Hentze, M. W., Castelló, A., Schwarzl, T., & Preiß, T. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.130 · Cited by 1,727 · see citing works

Robust transcriptome-wide discovery of RNA-binding protein binding sites with enhanced CLIP (eCLIP)

Van Nostrand, E. L., Pratt, G. A., Shishkin, A. A., Gelboin-Burkhart, C., Fang, M. Y., Sundararaman, B., Blue, S. M., Nguyen, T. B., Surka, C., Elkins, K., et al. (2016) · Nature Methods · doi:10.1038/nmeth.3810 · Cited by 1,397 · see citing works

Transcriptome Engineering with RNA-Targeting Type VI-D CRISPR Effectors

Konermann, S., Lotfy, P., Brideau, N. J., Oki, J., Shokhirev, M. N., & Hsu, P. D. (2018) · Cell · doi:10.1016/j.cell.2018.02.033 · Cited by 1,164 · see citing works

RNA in cancer

Goodall, G. J., & Wickramasinghe, V. O. (2020) · Nature reviews. Cancer · doi:10.1038/s41568-020-00306-0 · Cited by 1,070 · see citing works

Circular RNA and its mechanisms in disease: From the bench to the clinic

Han, B., Chao, J., & Yao, H. (2018) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2018.01.010 · Cited by 784 · see citing works

RNA splicing factors as oncoproteins and tumour suppressors

Dvinge, H., Kim, E. H., Abdel-Wahab, O. I., & Bradley, R. K. (2016) · Nature reviews. Cancer · doi:10.1038/nrc.2016.51 · Cited by 684 · see citing works

Efficient backsplicing produces translatable circular mRNAs

Wang, Y., & Wang, Z. (2014) · RNA · doi:10.1261/rna.048272.114 · Cited by 665 · see citing works

Therapeutic targeting of splicing in cancer

Lee, S. C.-W., & Abdel-Wahab, O. I. (2016) · Nature Medicine · doi:10.1038/nm.4165 · Cited by 556 · see citing works

A guide to membraneless organelles and their various roles in gene regulation

Hirose, T., Ninomiya, K., Nakagawa, S., & Yamazaki, T. (2022) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-022-00558-8 · Cited by 496 · see citing works

Aberrant RNA splicing in cancer; expression changes and driver mutations of splicing factor genes

Sveen, A., Kilpinen, S. K., Ruusulehto, A., Lothe, R. A., & Skotheim, R. I. (2015) · Oncogene · doi:10.1038/onc.2015.318 · Cited by 463 · see citing works

Cancer-Associated SF3B1 Hotspot Mutations Induce Cryptic 3′ Splice Site Selection through Use of a Different Branch Point

Darman, R. B., Seiler, M., Agrawal, A. A., Lim, K., Peng, S., Aird, D. R., Bailey, S., Bhavsar, E. B., Chan, B., Colla, S., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.09.053 · Cited by 455 · see citing works

Insights into circular RNA biology

Ebbesen, K. K., Hansen, T. B., & Kjems, J. (2016) · RNA Biology · doi:10.1080/15476286.2016.1271524 · Cited by 454 · see citing works

SMN2 splice modulators enhance U1–pre-mRNA association and rescue SMA mice

Palacino, J., Swalley, S. E., Song, C., Cheung, A. K., Shu, L., Zhang, X., Van Hoosear, M., Shin, Y., Chin, D. N., Keller, C. G., et al. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1837 · Cited by 432 · see citing works

Supermeres are functional extracellular nanoparticles replete with disease biomarkers and therapeutic targets

Zhang, Q., Jeppesen, D. K., Higginbotham, J. N., Graves‐Deal, R., Trinh, V. Q., Ramirez, M. A., Sohn, Y., Neininger, A. C., Taneja, N., McKinley, E. T., et al. (2021) · Nature Cell Biology · doi:10.1038/s41556-021-00805-8 · Cited by 423 · see citing works

Biogenesis, identification, and function of exonic circular RNAs

Chen, I., Chen, C., & Chuang, T. (2015) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1294 · Cited by 397 · see citing works

Alternative splicing and related RNA binding proteins in human health and disease

Tao, Y., Zhang, Q., Wang, H., Yang, X., & Mu, H. (2024) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-01734-2 · Cited by 342 · 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

Lessons from non-canonical splicing

Sibley, C. R., Blázquez, L., & Ule, J. (2016) · Nature Reviews Genetics · doi:10.1038/nrg.2016.46 · Cited by 312 · see citing works

The role of alternative splicing in cancer: From oncogenesis to drug resistance

Sciarrillo, R., Wojtuszkiewicz, A., Assaraf, Y. G., Jansen, G., Kaspers, G. J. L., Giovannetti, E., & Cloos, J. J. (2020) · Drug Resistance Updates · doi:10.1016/j.drup.2020.100728 · Cited by 311 · see citing works

Splicing regulation by long noncoding RNAs

Romero-Barrios, N., Legascue, M. F., Benhamed, M., Ariel, F., & Crespi, M. D. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky095 · Cited by 305 · see citing works

Circular RNAs in immune responses and immune diseases

Chen, X., Yang, T., Wang, W., Xi, W., Zhang, T., Li, Q., Yang, A., & Wang, T. (2019) · Theranostics · doi:10.7150/thno.29678 · Cited by 291 · see citing works

The powerful world of antisense oligonucleotides: From bench to bedside

Quéméner, A. M., Bachelot, L., Forestier, A., Donnou‐Fournet, E., Gilot, D., & Galibert, M. (2020) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1594 · Cited by 279 · see citing works

FTO controls reversible m6Am RNA methylation during snRNA biogenesis

Mauer, J., Sindelar, M., Despic, V., Guez, T., Hawley, B. R., Vasseur, J., Rentmeister, A., Gross, S. S., Pellizzoni, L., Debart, F., et al. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0231-8 · Cited by 270 · see citing works

Innate immune evasion strategies of SARS-CoV-2

Minkoff, J. M., & tenOever, B. R. (2023) · Nature Reviews Microbiology · doi:10.1038/s41579-022-00839-1 · Cited by 255 · see citing works

The Spliceosome: The Ultimate RNA Chaperone and Sculptor

Papasaikas, P., & Valcárcel, J. (2015) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.11.003 · Cited by 248 · see citing works

Alternative mRNA splicing in cancer immunotherapy

Frankiw, L., Baltimore, D., & Li, G. (2019) · Nature reviews. Immunology · doi:10.1038/s41577-019-0195-7 · Cited by 248 · see citing works

PRMT9 is a Type II methyltransferase that methylates the splicing factor SAP145

Yang, Y., Hadjikyriacou, A., Xia, Z., Gayatri, S., Kim, D., Zurita‐Lopez, C. I., Kelly, R. L., Guo, A., Li, W., Clarke, S. G., et al. (2015) · Nature Communications · doi:10.1038/ncomms7428 · Cited by 240 · see citing works

Control of mammalian gene expression by selective mRNA export

Wickramasinghe, V. O., & Laskey, R. A. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm4010 · Cited by 230 · see citing works

Cytoplasmic RNA decay pathways - Enzymes and mechanisms

Łabno, A., Tomecki, R., & Dziembowski, A. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.09.023 · Cited by 229 · see citing works

The role of survival motor neuron protein (SMN) in protein homeostasis

Chaytow, H., Huang, Y.-T., Gillingwater, T. H., & Faller, K. M. E. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2849-1 · Cited by 227 · see citing works

The Splicing Factor RBM4 Controls Apoptosis, Proliferation, and Migration to Suppress Tumor Progression

Wang, Y., Chen, D., Qian, H., Tsai, Y., Shao, S., Liu, Q., Dominguez, D., & Wang, Z. (2014) · Cancer Cell · doi:10.1016/j.ccr.2014.07.010 · Cited by 224 · see citing works

PRMT5 Regulates DNA Repair by Controlling the Alternative Splicing of Histone-Modifying Enzymes

Hamard, P.-J., Santiago, G. E., Liu, F., Karl, D. L., Martínez, C., Man, N., Mookhtiar, A. K., Duffort, S., Greenblatt, S. M., Verdún, R. E., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2018.08.002 · Cited by 224 · see citing works

RNA Splicing and Disease: Animal Models to Therapies

Montes, M., Sanford, B. L., Comiskey, D. F., & Chandler, D. S. (2018) · Trends in Genetics · doi:10.1016/j.tig.2018.10.002 · Cited by 214 · see citing works

Defective control of pre–messenger RNA splicing in human disease

Chabot, B., & Shkreta, L. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201510032 · Cited by 209 · 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

Modular Assembly of the Bacterial Large Ribosomal Subunit

Davis, J. H., Tan, Y. Z., Carragher, B. O., Potter, C. S., Lyumkis, D., & Williamson, J. R. (2016) · Cell · doi:10.1016/j.cell.2016.11.020 · Cited by 203 · see citing works

The Short- and Long-Range RNA-RNA Interactome of SARS-CoV-2

Ziv, O., Price, J. L., Shalamova, L. A., Kamenova, T., Goodfellow, I., Weber, F., & Miska, E. A. (2020) · Molecular Cell · doi:10.1016/j.molcel.2020.11.004 · Cited by 203 · see citing works

Tau-mediated disruption of the spliceosome triggers cryptic rna splicing and neurodegeneration in Alzheimer's Disease

Hsieh, Y.-C., Guo, C., Yalamanchili, H. K., Abreha, M., Al-Ouran, R., Li, Y., Dammer, E. B., Lah, J. J., Levey, A. I., Bennett, D. A., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.08.104 · Cited by 196 · see citing works

Punctuated evolution of canonical genomic aberrations in uveal melanoma

Field, M. G., Durante, M. A., Anbunathan, H., CAI, L. Z., Decatur, C. L., Bowcock, A. M., Kurtenbach, S., & Harbour, J. W. (2018) · Nature Communications · doi:10.1038/s41467-017-02428-w · Cited by 195 · see citing works

Alternative Splicing in Neurogenesis and Brain Development

Su, C.-H., Dhananjaya, D., & Tarn, W. (2018) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2018.00012 · Cited by 192 · see citing works

Alternative splicing in prostate cancer

Paschalis, A., Sharp, A., Welti, J. C., Neeb, A., Raj, G. V., Luo, J., Plymate, S. R., & Bono, J. S. D. (2018) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-018-0085-0 · Cited by 190 · see citing works

Circular RNA expression in human hematopoietic cells is widespread and cell-type specific

Nicolet, B. P., Engels, S., Aglialoro, F., van den Akker, E., Lindern, M. V., & Wolkers, M. C. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky721 · Cited by 184 · see citing works

Widespread Transcriptional Scanning in the Testis Modulates Gene Evolution Rates

Xia, B., Yan, Y., Baron, M., Wagner, F., Barkley, D., Chiodin, M., Kim, S. Y., Keefe, D. L., Alukal, J. P., Boeke, J. D., et al. (2020) · Cell · doi:10.1016/j.cell.2019.12.015 · Cited by 180 · see citing works

The Many Facets of Therapy Resistance and Tumor Recurrence in Glioblastoma

Goenka, A., Tiek, D., Song, X., Huang, T., Hu, B., & Cheng, S.-Y. (2021) · Cells · doi:10.3390/cells10030484 · Cited by 169 · see citing works

The emerging role of alternative splicing in senescence and aging

Deschênes, M., & Chabot, B. (2017) · Aging Cell · doi:10.1111/acel.12646 · Cited by 167 · see citing works

Design and synthesis of analogues of natural products

Maier, M. E. (2015) · Organic & Biomolecular Chemistry · doi:10.1039/c5ob00169b · Cited by 166 · see citing works

Cajal bodies are linked to genome conformation

Wang, Q., Sawyer, I. A., Sung, M.-H., Sturgill, D., Shevtsov, S. P., Pegoraro, G., Hakim, O., Baek, S., Hager, G. L., & Dundr, M. (2016) · Nature Communications · doi:10.1038/ncomms10966 · Cited by 164 · see citing works

Diabetic neuropathy and the sensory neuron: New aspects of pathogenesis and their treatment implications

Kobayashi, M., & Zochodne, D. W. (2018) · Journal of Diabetes Investigation · doi:10.1111/jdi.12833 · Cited by 160 · see citing works

A multicolor riboswitch-based platform for imaging of RNA in live mammalian cells

Braselmann, E., Wierzba, A. J., Polaski, J. T., Chromiński, M., Holmes, Z. E., Hung, S., Batan, D., Wheeler, J. R., Parker, R., Jimenez, R., et al. (2018) · Nature Chemical Biology · doi:10.1038/s41589-018-0103-7 · Cited by 159 · see citing works

An extensive program of periodic alternative splicing linked to cell cycle progression

Dominguez, D., Tsai, Y., Weatheritt, R. J., Wang, Y., Blencowe, B. J., & Wang, Z. (2016) · eLife · doi:10.7554/elife.10288 · Cited by 156 · see citing works

The RNA Splicing Response to DNA Damage

Shkreta, L., & Chabot, B. (2015) · Biomolecules · doi:10.3390/biom5042935 · Cited by 154 · see citing works

The pathogenicity of splicing defects: mechanistic insights into pre‐mRNA processing inform novel therapeutic approaches

Daguenet, É., Dujardin, G., & Valcárcel, J. (2015) · EMBO Reports · doi:10.15252/embr.201541116 · Cited by 151 · see citing works

Altered RNA Processing in Cancer Pathogenesis and Therapy

Obeng, E. A., Stewart, C., & Abdel-Wahab, O. I. (2019) · Cancer Discovery · doi:10.1158/2159-8290.cd-19-0399 · Cited by 141 · see citing works

Splicing modulators act at the branch point adenosine binding pocket defined by the PHF5A–SF3b complex

Teng, T., Tsai, J., Puyang, X., Seiler, M., Peng, S., Prajapati, S., Aird, D. R., Buonamici, S., Caleb, B. L., Chan, B., et al. (2017) · Nature Communications · doi:10.1038/ncomms15522 · Cited by 139 · see citing works

The Glucocorticoid Receptor: Isoforms, Functions, and Contribution to Glucocorticoid Sensitivity

Lockett, J., Inder, W. J., & Clifton, V. L. (2024) · Endocrine Reviews · doi:10.1210/endrev/bnae008 · Cited by 135 · see citing works

Illuminating RNA Biology: Tools for Imaging RNA in Live Mammalian Cells

Braselmann, E., Rathbun, C. M., Richards, E. M., & Palmer, A. E. (2020) · Cell chemical biology · doi:10.1016/j.chembiol.2020.06.010 · Cited by 134 · see citing works

Decoding mechanisms by which silent codon changes influence protein biogenesis and function

Bali, V., & Bebok, Z. M. (2015) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2015.03.011 · Cited by 133 · see citing works

Alternative splicing: the pledge, the turn, and the prestige

Gallego-Paez, L. M., Bordone, M. C., Leote, A. C., Saraiva-Agostinho, N., Ascensão-Ferreira, M., & Barbosa‐Morais, N. L. (2017) · Human Genetics · doi:10.1007/s00439-017-1790-y · Cited by 133 · see citing works

Rethinking gene regulatory networks in light of alternative splicing, intrinsically disordered protein domains, and post-translational modifications

Niklas, K. J., Bondos, S. E., Dunker, A. K., & Newman, S. A. (2015) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2015.00008 · Cited by 132 · see citing works

Hypoxia-induced alternative splicing: the 11th Hallmark of Cancer

Farina, A. R., Cappabianca, L. A., Sebastiano, M., Zelli, V., Guadagni, S., & Mackay, A. R. (2020) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/s13046-020-01616-9 · Cited by 131 · see citing works

Modifications in small nuclear RNAs and their roles in spliceosome assembly and function

Bohnsack, M. T., & Sloan, K. E. (2018) · Biological Chemistry · doi:10.1515/hsz-2018-0205 · Cited by 130 · see citing works

Plant Small Non-coding RNAs and Their Roles in Biotic Stresses

Brant, E. J., & Budak, H. (2018) · Frontiers in Plant Science · doi:10.3389/fpls.2018.01038 · Cited by 127 · see citing works

RNA splicing analysis using heterogeneous and large RNA-seq datasets

Vaquero-Garcia, J., Aicher, J. K., Jewell, S., Gazzara, M. R., Radens, C. M., Jha, A., Green, C. J., Norton, S., Lahens, N. F., Grant, G. R., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36585-y · Cited by 124 · see citing works

The life of U6 small nuclear RNA, from cradle to grave

Didychuk, A. L., Butcher, S. E., & Brow, D. A. (2018) · RNA · doi:10.1261/rna.065136.117 · Cited by 123 · see citing works

SRSF1 inhibits autophagy through regulating Bcl-x splicing and interacting with PIK3C3 in lung cancer

Lv, Y., Zhang, W., Zhao, J., Sun, B., Qi, Y., Ji, H., Chen, C., Zhang, J., Sheng, J., Wang, T., et al. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00495-6 · Cited by 120 · see citing works

A mouse tissue atlas of small noncoding RNA

Isakova, A., Fehlmann, T., Keller, A., & Quake, S. R. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2002277117 · Cited by 119 · see citing works

PRMT5 Modulates Splicing for Genome Integrity and Preserves Proteostasis of Hematopoietic Stem Cells

Tan, D. Q., Li, Y., Yang, C., Li, J., Tan, S. H., Chin, D. W. L., Nakamura‐Ishizu, A., Yang, H. H., & Suda, T. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.02.001 · Cited by 116 · see citing works

Comprehensive characterization of the alternative splicing landscape in head and neck squamous cell carcinoma reveals novel events associated with tumorigenesis and the immune microenvironment

Li, Z., Zheng, Z., Wei, Z.-H., Zhang, L., Li, F., Lin, L., Liu, R., Huang, X., Lv, J., Chen, F., et al. (2019) · Theranostics · doi:10.7150/thno.36585 · Cited by 114 · see citing works

Mutations in spliceosomal proteins and retina degeneration

Rùzicková, Š., & Staněk, D. (2016) · RNA Biology · doi:10.1080/15476286.2016.1191735 · Cited by 113 · see citing works

The Role of Pontin and Reptin in Cellular Physiology and Cancer Etiology

Mao, Y.-Q., & Houry, W. A. (2017) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2017.00058 · Cited by 113 · see citing works

Quantitative analysis of cryptic splicing associated with TDP-43 depletion

Humphrey, J., Emmett, W., Fratta, P., Isaacs, A. M., & Plagnol, V. (2017) · BMC Medical Genomics · doi:10.1186/s12920-017-0274-1 · Cited by 113 · see citing works

SRSF10-mediated IL1RAP alternative splicing regulates cervical cancer oncogenesis via mIL1RAP-NF-κB-CD47 axis

Liu, F., Dai, M., Xu, Q., Zhu, X., Zhou, Y., Jiang, S., Wang, Y., Ai, Z., Ma, L., Zhang, Y., et al. (2018) · Oncogene · doi:10.1038/s41388-017-0119-6 · Cited by 112 · see citing works

Rectifier of aberrant mRNA splicing recovers tRNA modification in familial dysautonomia

Yoshida, M., Kataoka, N., Miyauchi, K., Ohe, K., Iida, K., Yoshida, S., Nojima, T., Okuno, Y., Onogi, H., Usui, T., et al. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1415525112 · Cited by 111 · see citing works

Influenza virus mRNA trafficking through host nuclear speckles

Mor, A., White, A., Zhang, K., Thompson, M. G., Esparza, M. A., Muñoz-Moreno, R., Koide, K., Lynch, K. W., García‐Sastre, A., & Fontoura, B. M. A. (2016) · Nature Microbiology · doi:10.1038/nmicrobiol.2016.69 · Cited by 111 · see citing works

Dysregulation of the splicing machinery is directly associated to aggressiveness of prostate cancer

Jiménez‐Vacas, J. M., Herrero‐Aguayo, V., Montero‐Hidalgo, A. J., Gómez‐Gómez, E., Fuentes-Fayos, A. C., León‐González, A. J., Sáez-Martínez, P., Alors‐Pérez, E., Pedraza‐Arévalo, S., González-Serrano, T., et al. (2020) · EBioMedicine · doi:10.1016/j.ebiom.2019.11.008 · Cited by 111 · see citing works

A review of craniofacial disorders caused by spliceosomal defects

Lehalle, D., Wieczorek, D., Zechi‐Ceide, R. M., Passos‐Bueno, M. R., Lyonnet, S., Amiel, J., & Gordon, C. T. (2015) · Clinical Genetics · doi:10.1111/cge.12596 · Cited by 110 · see citing works

2′- O -Methylation can increase the abundance and lifetime of alternative RNA conformational states

Assi, H. A., Rangadurai, A., Shi, H., Liu, B., Clay, M. C., Erharter, K., Kreutz, C., Holley, C. L., & Al‐Hashimi, H. M. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa928 · Cited by 109 · see citing works

Alternative Splicing in Angiogenesis

Bowler, E., & Oltean, S. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20092067 · Cited by 108 · see citing works

Regulation of alternative mRNA splicing: old players and new perspectives

Dvinge, H. (2018) · FEBS Letters · doi:10.1002/1873-3468.13119 · Cited by 105 · see citing works

SAM68: Signal Transduction and RNA Metabolism in Human Cancer

Frisone, P., Pradella, D., Matteo, A. D., Belloni, E., Ghigna, C., & Paronetto, M. P. (2015) · BioMed Research International · doi:10.1155/2015/528954 · Cited by 104 · see citing works

The Coilin Interactome Identifies Hundreds of Small Noncoding RNAs that Traffic through Cajal Bodies

Machyna, M., Kehr, S., Straube, K., Kappei, D., Buchholz, F., Butter, F., Ule, J., Jana Hertel, A., Stadler, P. F., & Neugebauer, K. M. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.10.004 · Cited by 103 · see citing works

A benchmark study of ab initio gene prediction methods in diverse eukaryotic organisms

Scalzitti, N., Jeannin‐Girardon, A., Collet, P., Poch, O., & Thompson, J. (2020) · BMC Genomics · doi:10.1186/s12864-020-6707-9 · Cited by 102 · see citing works

Dyskerin: an essential pseudouridine synthase with multifaceted roles in ribosome biogenesis, splicing, and telomere maintenance

Garus, A., & Autexier, C. (2021) · RNA · doi:10.1261/rna.078953.121 · Cited by 101 · see citing works

Cyclic Nucleotide Monophosphates and Their Cyclases in Plant Signaling

Gehring, C., & Turek, I. (2017) · Frontiers in Plant Science · doi:10.3389/fpls.2017.01704 · Cited by 101 · see citing works

Alternative splicing in cancers: From aberrant regulation to new therapeutics

Song, X., Zeng, Z., Wei, H. Y., & Wang, Z. (2017) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2017.09.018 · Cited by 100 · see citing works

Physical Activity Associated Proteomics of Skeletal Muscle: Being Physically Active in Daily Life May Protect Skeletal Muscle From Aging

Ubaida‐Mohien, C., González‐Freire, M., Lyashkov, A. E., Moaddel, R., Chia, C. W., Simonsick, E. M., Sen, R., & Ferrucci, L. (2019) · Frontiers in Physiology · doi:10.3389/fphys.2019.00312 · Cited by 100 · see citing works

RNA-Binding Proteins: Splicing Factors and Disease

Fredericks, A. M., Cygan, K. J., Brown, B., & Fairbrother, W. G. (2015) · Biomolecules · doi:10.3390/biom5020893 · Cited by 100 · see citing works

The spliceosome assembly factor GEMIN2 attenuates the effects of temperature on alternative splicing and circadian rhythms

Schlaen, R. G., Mancini, E., Sánchez, S. E., Perez-Santángelo, S., Rugnone, M. L., Simpson, C. G., Brown, J. W. S., Zhang, X., Chernomoretz, A., & Yanovsky, M. J. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1504541112 · Cited by 100 · see citing works

Splicing machinery dysregulation drives glioblastoma development/aggressiveness: oncogenic role of SRSF3

Fuentes-Fayos, A. C., Vazquez-Borrego, M. C., Jiménez‐Vacas, J. M., Bejarano, L., Pedraza‐Arévalo, S., L‐López, F., Blanco-Acevedo, C., Sánchez‐Sánchez, R., Reyes, Ó., Ventura, S., et al. (2020) · Brain · doi:10.1093/brain/awaa273 · Cited by 99 · see citing works

Ribosomal Proteins Rpl22 and Rpl22l1 Control Morphogenesis by Regulating Pre-mRNA Splicing

Zhang, Y., O’Leary, M. N., Peri, S., Wang, M., Zha, J., Melov, S., Kappes, D. J., Feng, Q., Rhodes, J., Amieux, P. S., et al. (2017) · Cell Reports · doi:10.1016/j.celrep.2016.12.034 · Cited by 98 · see citing works

Splicing at the phase-separated nuclear speckle interface: a model

Liao, S. E., & Regev, O. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa1209 · Cited by 98 · see citing works

Emerging regulatory mechanisms and functions of biomolecular condensates: implications for therapeutic targets

Jeon, S., Jeon, Y., Lim, J.-Y., Kim, Y., Cha, B., & Kim, W. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02070-1 · Cited by 97 · see citing works

Extensive cryptic splicing upon loss of RBM17 and TDP43 in neurodegeneration models

Tan, Q., Yalamanchili, H. K., Park, J., Maio, A. D., Lu, H., Wan, Y., White, J. J., Bondar, V. V., Sayegh, L. S., Liu, X., et al. (2016) · Human Molecular Genetics · doi:10.1093/hmg/ddw337 · Cited by 96 · see citing works

Assembly of the U5 snRNP component PRPF8 is controlled by the HSP90/R2TP chaperones

Malinová, A., Cvačková, Z., Matějů, D., Hořejšı́, Z., Abéza, C., Vandermoere, F., Bertrand, É., Staněk, D., & Verheggen, C. (2017) · The Journal of Cell Biology · doi:10.1083/jcb.201701165 · Cited by 92 · see citing works

Spliceator: multi-species splice site prediction using convolutional neural networks

Scalzitti, N., Kress, A., Orhand, R., Weber, T., Moulinier, L., Jeannin‐Girardon, A., Collet, P., Poch, O., & Thompson, J. (2021) · BMC Bioinformatics · doi:10.1186/s12859-021-04471-3 · Cited by 92 · see citing works

Regulation of constitutive and alternative mRNA splicing across the human transcriptome by PRPF8 is determined by 5′ splice site strength

Wickramasinghe, V. O., Gonzàlez-Porta, M., Perera, D., Bartolozzi, A. R., Sibley, C. R., Hallegger, M., Ule, J., Marioni, J. C., & Venkitaraman, A. R. (2015) · Genome Biology · doi:10.1186/s13059-015-0749-3 · Cited by 91 · see citing works

Integrator: surprisingly diverse functions in gene expression

Baillat, D., & Wagner, E. J. (2015) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.03.005 · Cited by 91 · see citing works

Diversification of the muscle proteome through alternative splicing

Nakka, K. K., Ghigna, C., Gabellini, D., & Dilworth, F. J. (2018) · Skeletal Muscle · doi:10.1186/s13395-018-0152-3 · Cited by 90 · see citing works

Structural basis for DEAH-helicase activation by G-patch proteins

Studer, M. K., Ivanović, L., Weber, M. E., Marti, S., & Jonas, S. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1913880117 · Cited by 88 · see citing works

Identification and characterization of small molecule inhibitors of pre-mRNA splicing that block spliceosome assembly at novel stages

Sidarovich, A. (2016) · doi:10.53846/goediss-5520

Transcriptome-wide splicing network reveals specialized regulatory functions of the core spliceosome

Rogalska, M. E., Mancini, E., Bonnal, S., Gohr, A., Dunyak, B. M., Arecco, N., Smith, P. G., Vaillancourt, F. H., & Valcárcel, J. (2024) · Science · doi:10.1126/science.adn8105 · Cited by 102 · see citing works

RNA Splicing and Genes

Sharp, P. A. (1988) · JAMA · doi:10.1001/jama.1988.03410200091032 · Cited by 21 · see citing works

Spliceosomes

Chen, W., & Moore, M. J. (2015) · Current Biology · doi:10.1016/j.cub.2014.11.059 · Cited by 75 · see citing works

The nuts and bolts of the endogenous spliceosome

Sperling, R. (2016) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1377 · Cited by 39 · see citing works