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 2,270

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

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

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

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

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 1,483

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

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

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

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 1,127

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

Pre-mRNA Splicing

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

Deciphering the splicing code

Barash, Y., Calarco, J. A., Gao, W., Pan, Q., Wang, X., Shai, O., Blencowe, B. J., & Frey, B. J. (2010) · Nature · doi:10.1038/nature09000 · Cited by 925

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 899

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

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 877

Nuclear SpecklesPreprint

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

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

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 672

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

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

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

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

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 555

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

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

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

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

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

U1 snRNP Determines mRNA Length and Regulates Isoform Expression

Berg, M. G., Singh, L. N., Younis, I., Liu, Q., Pinto, A. M., Kaida, D., Zhang, Z., Cho, S., Sherrill-Mix, S. A., Wan, L., et al. (2012) · Cell · doi:10.1016/j.cell.2012.05.029 · Cited by 482

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

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 472

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

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 453

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 424

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 419

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

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 396

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., de la Fortelle, E., Raker, V. A., Lührmann, R., Li, J., & Nagai, K. (1999) · Cell · doi:10.1016/s0092-8674(00)80550-4 · Cited by 387

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

Nilsen, T. W. (2003) · BioEssays · doi:10.1002/bies.10394 · Cited by 386

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

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

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

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

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

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

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 330

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

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

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 313

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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 253

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

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

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

Nascent-seq indicates widespread cotranscriptional pre-mRNA splicing in Drosophila

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

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

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

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

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

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 236

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

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

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

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

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

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

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 226

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

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

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

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

Nuclear RNA export

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

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

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

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

New connections between splicing and human disease

Padgett, R. A. (2012) · Trends in Genetics · doi:10.1016/j.tig.2012.01.001 · Cited by 194

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

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 193

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

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 192

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

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

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

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

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

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

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

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

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

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

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 169

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 169

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

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

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 167

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

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

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 154

Trans ‐splicing

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

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

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 143

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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 112

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

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

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

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

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

Counting on co-transcriptional splicing

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

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 107

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

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

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

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

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

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

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

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 98

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

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

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

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 93

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

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

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

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

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

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

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 83

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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 50

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

Role of the snRNAs in spliceosomal active site

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

Functional studies on the ATM intronic splicing processing element

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

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

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 25

The Spliceosome and Its Metal Ions

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

snRNA-specific role of SMN in trypanosome snRNP biogenesis in vivo

Jaé, N., Preußer, C., Krüger, T., Tkacz, I. D., Engstler, M., Michaeli, S., & Bindereif, A. (2011) · RNA Biology · doi:10.4161/rna.8.1.13985 · Cited by 16

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

A brave new world of RNA-binding proteins

Hentze, M. W., Castello, A., Schwarzl, T., & Preiss, T. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2017.130 · Cited by 1,821

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

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

RNA in cancer

Goodall, G. J., & Wickramasinghe, V. O. (2020) · Nature reviews. Cancer · doi:10.1038/s41568-020-00306-0 · Cited by 1,090

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 106

RNA Splicing and Genes

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

Spliceosomes

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

The nuts and bolts of the endogenous spliceosome

Sperling, R. (2016) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1377 · Cited by 40