Cited by 414

The DOI matches its Crossref record; 107 of the 107 references it cites were found in a registry or an index.

The pathobiology of splicing

Open access

Ward, Amanda J, Cooper, Thomas A·2010·The Journal of Pathology

Open this paper in CoChat — free account

Abstract

Ninety‐four percent of human genes are discontinuous, such that segments expressed as mRNA are contained within exons and separated by intervening segments, called introns. Following transcription, genes are expressed as precursor mRNAs (pre‐mRNAs), which are spliced co‐transcriptionally, and the flanking exons are joined together to form a continuous mRNA. One advantage of this architecture is that it allows alternative splicing by differential use of exons to generate multiple mRNAs from individual genes. Regulatory elements located within introns and exons guide the splicing complex, the spliceosome, and auxiliary RNA binding proteins to the correct sites for intron removal and exon joining. Misregulation of splicing and alternative splicing can result from mutations in cis‐regulatory elements within the affected gene or from mutations that affect the activities of trans‐acting factors that are components of the splicing machinery. Mutations that affect splicing can cause disease directly or contribute to the susceptibility or severity of disease. An understanding of the role of splicing in disease expands potential opportunities for therapeutic intervention by either directly addressing the cause or by providing novel approaches to circumvent disease processes. Copyright © 2009 Pathological Society of Great Britain and Ireland. Published by John Wiley & Sons, Ltd.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1002/path.2649

Cites

107 of 107 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Ubiquitinated TDP-43 in Frontotemporal Lobar Degeneration and Amyotrophic Lateral Sclerosis
Neumann, M., Sampathu, D. M., Kwong, L. K., Truax, A. C., Micsenyi, M. C., Chou, T. T., Bruce, J., Schuck, T., Grossman, M., Clark, C. M., et al. (2006) · Science · doi:10.1126/science.1134108 · Cited by 6,576
Alternative isoform regulation in human tissue transcriptomes
Wang, E. T., Sandberg, R., Luo, S., Khrebtukova, I., Zhang, L., Mayr, C., Kingsmore, S. F., Schroth, G. P., & Burge, C. B. (2008) · Nature · doi:10.1038/nature07509 · Cited by 5,181
Deep surveying of alternative splicing complexity in the human transcriptome by high-throughput sequencing
Pan, Q., Shai, O., Lee, L. J., Frey, B. J., & Blencowe, B. J. (2008) · Nature Genetics · doi:10.1038/ng.259 · Cited by 3,951
bcl-x, a bcl-2-related gene that functions as a dominant regulator of apoptotic cell death
Boise, L. H., González-García, M., Postema, C. E., Ding, L., Lindsten, T., Turka, L. A., Mao, X., Nuñez, G., & Thompson, C. B. (1993) · Cell · doi:10.1016/0092-8674(93)90508-n · Cited by 3,087
TDP-43 is a component of ubiquitin-positive tau-negative inclusions in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
Arai, T., Hasegawa, M., Akiyama, H., Ikeda, K., Nonaka, T., Mori, H., Mann, D., Tsuchiya, K., Yoshida, M., Hashizume, Y., et al. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.10.093 · Cited by 2,732
The Spliceosome: Design Principles of a Dynamic RNP Machine
Wahl, M. C., Will, C. L., & Lührmann, R. (2009) · Cell · doi:10.1016/j.cell.2009.02.009 · Cited by 2,665
Mutations in FUS, an RNA Processing Protein, Cause Familial Amyotrophic Lateral Sclerosis Type 6
Vance, C., Rogelj, B., Hortobágyi, T., De Vos, K. J., Nishimura, A. L., Sreedharan, J., Hu, X., Smith, B., Ruddy, D., Wright, P., et al. (2009) · Science · doi:10.1126/science.1165942 · Cited by 2,564
Mutations in the FUS/TLS Gene on Chromosome 16 Cause Familial Amyotrophic Lateral Sclerosis
Kwiatkowski, T. J., Bosco, D. A., LeClerc, A. L., Tamrazian, E., Vanderburg, C. R., Russ, C., Davis, A., Gilchrist, J., Kasarskis, E. J., Munsat, T., et al. (2009) · Science · doi:10.1126/science.1166066 · Cited by 2,553
Myotonic Dystrophy Mutation: an Unstable CTG Repeat in the 3′ Untranslated region of the Gene
Mahadevan, M., Tsilfidis, C., Sabourin, L., Shutler, G., Amemiya, C., Jansen, G., Neville, C., Narang, M., Barceló, J., O'Hoy, K., et al. (1992) · Science · doi:10.1126/science.1546325 · Cited by 1,660
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 1,532
The multifaceted roles of glycogen synthase kinase 3β in cellular signaling
Grimes, C. A., & Jope, R. S. (2001) · Progress in Neurobiology · doi:10.1016/s0301-0082(01)00011-9 · Cited by 1,423
Isolation of a candidate gene for Menkes disease and evidence that it encodes a copper–transporting ATPase
Vulpe, C., Levinson, B., Whitney, S., Packman, S., & Gitschier, J. (1993) · Nature Genetics · doi:10.1038/ng0193-7 · Cited by 1,418
The mutational spectrum of single base-pair substitutions in mRNA splice junctions of human genes: Causes and consequences
Krawczak, M., Reiss, J., & Cooper, D. (1992) · Human Genetics · doi:10.1007/bf00210743 · Cited by 1,324
Pre-mRNA splicing and human disease
Faustino, N. A., & Cooper, T. A. (2003) · Genes & Development · doi:10.1101/gad.1048803 · Cited by 1,256
Self-citation
Myotonic Dystrophy Type 2 Caused by a CCTG Expansion in Intron 1 of ZNF9
Liquori, C. L., Ricker, K., Moseley, M. L., Jacobsen, J. F., Kress, W., Naylor, S. L., Day, J. W., & Ranum, L. P. W. (2001) · Science · doi:10.1126/science.1062125 · Cited by 1,231
RNA and Disease
Cooper, T. A., Wan, L., & Dreyfuss, G. (2009) · Cell · doi:10.1016/j.cell.2009.02.011 · Cited by 1,159
Self-citation
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 1,086
Splicing in disease: disruption of the splicing code and the decoding machinery
Wang, G.-S., & Cooper, T. A. (2007) · Nature Reviews Genetics · doi:10.1038/nrg2164 · Cited by 1,050
Self-citation
Pathways of apoptotic and non-apoptotic death in tumour cells
Okada, H., & Mak, T. W. (2004) · Nature Reviews Cancer · doi:10.1038/nrc1412 · Cited by 1,044
Antisense technologies: Improvement through novel chemical modifications
Kurreck, J. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03555.x · Cited by 1,006
Mutation-Specific Functional Impairments in Distinct Tau Isoforms of Hereditary FTDP-17
Hong, M. (1998) · Science · doi:10.1126/science.282.5395.1914 · Cited by 1,003
A single nucleotide difference that alters splicing patterns distinguishes the SMA gene SMN1 from the copy gene SMN2
Monani, U. R. (1999) · Human Molecular Genetics · doi:10.1093/hmg/8.7.1177 · Cited by 954
The gene encoding the splicing factor SF2/ASF is a proto-oncogene
Karni, R., de Stanchina, E., Lowe, S. W., Sinha, R., Mu, D., & Krainer, A. R. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1209 · Cited by 934
Transcriptome sequencing to detect gene fusions in cancer
Maher, C. A., Kumar-Sinha, C., Cao, X., Kalyana-Sundaram, S., Han, B., Jing, X., Sam, L., Barrette, T., Palanisamy, N., & Chinnaiyan, A. M. (2009) · Nature · doi:10.1038/nature07638 · Cited by 900
Alternative pre-mRNA splicing: the logic of combinatorial control
Smith, C. W. J., & Valcárcel, J. (2000) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01604-2 · Cited by 896
Aberrant regulation of insulin receptor alternative splicing is associated with insulin resistance in myotonic dystrophy
Savkur, R. S., Philips, A. V., & Cooper, T. A. (2001) · Nature Genetics · doi:10.1038/ng704 · Cited by 795
Self-citation
Diseases of Unstable Repeat Expansion: Mechanisms and Common Principles
Gatchel, J. R., & Zoghbi, H. Y. (2005) · Nature Reviews Genetics · doi:10.1038/nrg1691 · Cited by 794
A Muscleblind Knockout Model for Myotonic Dystrophy
Kanadia, R. N., Johnstone, K. A., Mankodi, A., Lungu, C., Thornton, C. A., Esson, D., Timmers, A. M., Hauswirth, W. W., & Swanson, M. S. (2003) · Science · doi:10.1126/science.1088583 · Cited by 743
Disruption of an SF2/ASF-dependent exonic splicing enhancer in SMN2 causes spinal muscular atrophy in the absence of SMN1
Cartegni, L., & Krainer, A. R. (2002) · Nature Genetics · doi:10.1038/ng854 · Cited by 730
Isolation of a candidate gene for Menkes disease that encodes a potential heavy metal binding protein
Chelly, J., Tümer, Z., Tønnesen, T., Petterson, A., Ishikawa-Brush, Y., Tommerup, N., Horn, N., & Monaco, A. P. (1993) · Nature Genetics · doi:10.1038/ng0193-14 · Cited by 726
Isolation of a partial candidate gene for Menkes disease by positional cloning
Mercer, J. F. B., Livingston, J., Hall, B., Paynter, J. A., Begy, C., Chandrasekharappa, S., Lockhart, P., Grimes, A., Bhave, M., Siemieniak, D., et al. (1993) · Nature Genetics · doi:10.1038/ng0193-20 · Cited by 696
Expanded CUG Repeats Trigger Aberrant Splicing of ClC-1 Chloride Channel Pre-mRNA and Hyperexcitability of Skeletal Muscle in Myotonic Dystrophy
Mankodi, A., Takahashi, M. P., Jiang, H., Beck, C. L., Bowers, W. J., Moxley, R. T., Cannon, S. C., & Thornton, C. A. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00563-4 · Cited by 672
Nuclear factor TDP-43 and SR proteins promote in vitro and in vivo CFTR exon 9 skipping
Buratti, E. (2001) · The EMBO Journal · doi:10.1093/emboj/20.7.1774 · Cited by 631
Loss of the Muscle-Specific Chloride Channel in Type 1 Myotonic Dystrophy Due to Misregulated Alternative Splicing
Charlet-B., N., Savkur, R. S., Singh, G., Philips, A. V., Grice, E. A., & Cooper, T. A. (2002) · Molecular Cell · doi:10.1016/s1097-2765(02)00572-5 · Cited by 619
Self-citation
SMN Deficiency Causes Tissue-Specific Perturbations in the Repertoire of snRNAs and Widespread Defects in Splicing
Zhang, Z., Lotti, F., Dittmar, K., Younis, I., Wan, L., Kasim, M., & Dreyfuss, G. (2008) · Cell · doi:10.1016/j.cell.2008.03.031 · Cited by 617
Immunohistochemical analysis of bcl-2, bax, bcl-X, and mcl-1 expression in prostate cancers.
Krajewska, M., Krajewski, S., Epstein, J. I., Shabaik, A. S., Sauvageot, J., Song, K. B., Kitada, S., & Reed, J. C. (1996) · Europe PMC (PubMed Central) · Cited by 593
Tissue-Specific Expression of a Splicing Mutation in the Gene Causes Familial Dysautonomia
Slaugenhaupt, S. A., Blumenfeld, A., Gill, S. P., Leyne, M., Mull, J., Cuajungco, M. P., Liebert, C. B., Chadwick, B., Idelson, M., Reznik, L., et al. (2001) · The American Journal of Human Genetics · doi:10.1086/318810 · Cited by 591
Rethinking ALS: The FUS about TDP-43
Lagier-Tourenne, C., & Cleveland, D. W. (2009) · Cell · doi:10.1016/j.cell.2009.03.006 · Cited by 588
A negative element in SMN2 exon 7 inhibits splicing in spinal muscular atrophy
Kashima, T., & Manley, J. L. (2003) · Nature Genetics · doi:10.1038/ng1207 · Cited by 546
Alternative splicing and disease
Tazi, J., Bakkour, N., & Stamm, S. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2008.09.017 · Cited by 540
Missense and silent tau gene mutations cause frontotemporal dementia with parkinsonism-chromosome 17 type, by affecting multiple alternative RNA splicing regulatory elements
D’Souza, I., Poorkaj, P., Hong, M., Nochlin, D., Lee, V. M.-Y., Bird, T. D., & Schellenberg, G. D. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.10.5598 · Cited by 515
Failure of MBNL1-dependent post-natal splicing transitions in myotonic dystrophy
Lin, X., Miller, J. W., Mankodi, A., Kanadia, R. N., Yuan, Y., Moxley, R. T., Swanson, M. S., & Thornton, C. A. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl132 · Cited by 510 · cited 1×
“The alternative splicing regulator MBNL1 has a high affinity for expanded CUG- and CCUG-repeat RNA and colocalizes with the nuclear foci, depleting MBNL1 from the nucleoplasm [74].”
Background
Nova regulates brain-specific splicing to shape the synapse
Ule, J., Ule, A., Spencer, J., Williams, A., Hu, J.-S., Cline, M., Wang, H., Clark, T., Fraser, C., Ruggiu, M., et al. (2005) · Nature Genetics · doi:10.1038/ng1610 · Cited by 509
A postnatal switch of CELF and MBNL proteins reprograms alternative splicing in the developing heart
Kalsotra, A., Xiao, X., Ward, A. J., Castle, J. C., Johnson, J. M., Burge, C. B., & Cooper, T. A. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0809045105 · Cited by 508
Self-citation
Elongator, a Multisubunit Component of a Novel RNA Polymerase II Holoenzyme for Transcriptional Elongation
Otero, G., Fellows, J., Li, Y., de Bizemont, T., Dirac, A. M. G., Gustafsson, C. M., Erdjument-Bromage, H., Tempst, P., & Svejstrup, J. Q. (1999) · Molecular Cell · doi:10.1016/s1097-2765(00)80179-3 · Cited by 482
Expansion of a CUG trinucleotide repeat in the 3′ untranslated region of myotonic dystrophy protein kinase transcripts results in nuclear retention of transcripts
Davis, B. M., McCurrach, M. E., Taneja, K. L., Singer, R. H., & Housman, D. E. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.14.7388 · Cited by 470
Increased Steady-State Levels of CUGBP1 in Myotonic Dystrophy 1 Are Due to PKC-Mediated Hyperphosphorylation
Kuyumcu-Martinez, N. M., Wang, G.-S., & Cooper, T. A. (2007) · Molecular Cell · doi:10.1016/j.molcel.2007.07.027 · Cited by 445
Self-citation
KLF6 , a Candidate Tumor Suppressor Gene Mutated in Prostate Cancer
Narla, G., Heath, K. E., Reeves, H. L., Li, D., Giono, L. E., Kimmelman, A. C., Glucksman, M. J., Narla, J., Eng, F. J., Chan, A. M., et al. (2001) · Science · doi:10.1126/science.1066326 · Cited by 442
An exonic enhancer is required for inclusion of an essential exon in the SMA-determining gene SMN
Lorson, C. L. (2000) · Human Molecular Genetics · doi:10.1093/hmg/9.2.259 · Cited by 435
Mitochondrial Fatty-Acid Oxidation Disorders
Kompare, M., & Rizzo, W. B. (2008) · Seminars in Pediatric Neurology · doi:10.1016/j.spen.2008.05.008 · Cited by 429
Familial Dysautonomia Is Caused by Mutations of the IKAP Gene
Anderson, S. L., Coli, R., Daly, I. W., Kichula, E. A., Rork, M. J., Volpi, S. A., Ekstein, J., & Rubin, B. Y. (2001) · The American Journal of Human Genetics · doi:10.1086/318808 · Cited by 428
Are splicing mutations the most frequent cause of hereditary disease?
López-Bigas, N., Audit, B., Ouzounis, C., Parra, G., & Guigó, R. (2005) · FEBS Letters · doi:10.1016/j.febslet.2005.02.047 · Cited by 412
Molecular pathogenesis of Wilson and Menkes disease: correlation of mutations with molecular defects and disease phenotypes
de Bie, P., Muller, P., Wijmenga, C., & Klomp, L. W. J. (2007) · Journal of Medical Genetics · doi:10.1136/jmg.2007.052746 · Cited by 390
Cell Motility Is Controlled by SF2/ASF through Alternative Splicing of the Ron Protooncogene
Ghigna, C., Giordano, S., Shen, H., Benvenuto, F., Castiglioni, F., Comoglio, P. M., Green, M. R., Riva, S., & Biamonti, G. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.10.026 · Cited by 389
Reversal of RNA Dominance by Displacement of Protein Sequestered on Triplet Repeat RNA
Wheeler, T. M., Sobczak, K., Lueck, J. D., Osborne, R. J., Lin, X., Dirksen, R. T., & Thornton, C. A. (2009) · Science · doi:10.1126/science.1173110 · Cited by 387
Single base-pair substitutions in exon-intron junctions of human genes: nature, distribution, and consequences for mRNA splicing
Krawczak, M., Thomas, N. S. T., Hundrieser, B., Mort, M., Wittig, M., Hampe, J., & Cooper, D. N. (2007) · Human Mutation · doi:10.1002/humu.20400 · Cited by 374
The connection between splicing and cancer
Srebrow, A., & Kornblihtt, A. R. (2006) · Journal of Cell Science · doi:10.1242/jcs.03053 · Cited by 335
Tau exon 10 alternative splicing and tauopathies
Liu, F., & Gong, C.-X. (2008) · Molecular Neurodegeneration · doi:10.1186/1750-1326-3-8 · Cited by 323
Determinants of Exon 7 Splicing in the Spinal Muscular Atrophy Genes, SMN1 and SMN2
Cartegni, L., Hastings, M. L., Calarco, J. A., de Stanchina, E., & Krainer, A. R. (2006) · The American Journal of Human Genetics · doi:10.1086/498853 · Cited by 306
Unbalanced alternative splicing and its significance in cancer
Venables, J. P. (2006) · BioEssays · doi:10.1002/bies.20390 · Cited by 299
Somatic reversion/suppression of the mouse mdx phenotype in vivo
Hoffman, E. P., Morgan, J. E., Watkins, S. C., & Partridge, T. A. (1990) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(90)90195-s · Cited by 277
Antisense-mediated exon skipping: A versatile tool with therapeutic and research applications
Aartsma-Rus, A., & van Ommen, G.-J. B. (2007) · RNA · doi:10.1261/rna.653607 · Cited by 267
Occipital horn syndrome and a mild Menkes phenotype associated with splice site mutations at the MNK locus
Kaler, S. G., Gallo, L. K., Proud, V. K., Percy, A. K., Mark, Y., Segal, N. A., Goldstein, D. S., Holmes, C. S., & Gahl, W. A. (1994) · Nature Genetics · doi:10.1038/ng1094-195 · Cited by 264
Triplet-repeat oligonucleotide-mediated reversal of RNA toxicity in myotonic dystrophy
Mulders, S. A. M., van den Broek, W. J. A. A., Wheeler, T. M., Croes, H. J. E., van Kuik-Romeijn, P., de Kimpe, S. J., Furling, D., Platenburg, G. J., Gourdon, G., Thornton, C. A., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0905780106 · Cited by 257
Correction of ClC-1 splicing eliminates chloride channelopathy and myotonia in mouse models of myotonic dystrophy
Wheeler, T. M., Lueck, J. D., Swanson, M. S., Dirksen, R. T., & Thornton, C. A. (2007) · Journal of Clinical Investigation · doi:10.1172/jci33355 · Cited by 256
Regulation of Alternative Splicing by Reversible Protein Phosphorylation
Stamm, S. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r700034200 · Cited by 251
Purification and Characterization of the Human Elongator Complex
Hawkes, N. A., Otero, G., Winkler, G. S., Marshall, N., Dahmus, M. E., Krappmann, D., Scheidereit, C., Thomas, C. L., Schiavo, G., Erdjument-Bromage, H., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110445200 · Cited by 246
BCL-X expression in multiple myeloma: possible indicator of chemoresistance.
Tu, Y., Renner, S., Xu, F., Fleishman, A. N., Taylor, J. M. G., Weisz, J., Vescio, R. A., Rettig, M. B., Berenson, J., Krajewski, S., et al. (1998) · PubMed · Cited by 222
A Germline DNA Polymorphism Enhances Alternative Splicing of the KLF6 Tumor Suppressor Gene and Is Associated with Increased Prostate Cancer Risk
Narla, G., DiFeo, A., Reeves, H. L., Schaid, D. J., Hirshfeld, J., Hod, E., Katz, A., Isaacs, W. B., Hebbring, S., Komiya, A., et al. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-4249 · Cited by 214
MBNL1 Is the Primary Determinant of Focus Formation and Aberrant Insulin Receptor Splicing in DM1
Dansithong, W., Paul, S., Comai, L., & Reddy, S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m410781200 · Cited by 212
hnRNP A1 functions with specificity in repression of SMN2 exon 7 splicing
Kashima, T., Rao, N., David, C. J., & Manley, J. L. (2007) · Human Molecular Genetics · doi:10.1093/hmg/ddm276 · Cited by 212
Transcription Impairment and Cell Migration Defects in Elongator-Depleted Cells: Implication for Familial Dysautonomia
Close, P., Hawkes, N., Cornez, I., Creppe, C., Lambert, C. A., Rogister, B., Siebenlist, U., Merville, M.-P., Slaugenhaupt, S. A., Bours, V., et al. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.04.017 · Cited by 211
Characterization of heterogeneous nuclear RNA-protein complexes in vivo with monoclonal antibodies.
Dreyfuss, G., Choi, Y. D., & Adam, S. A. (1984) · Molecular and Cellular Biology · doi:10.1128/mcb.4.6.1104 · Cited by 206
X-Linked Cutis Laxa: Defective Cross-Link Formation in Collagen Due to Decreased Lysyl Oxidase Activity
Byers, P. H., Siegel, R. C., Holbrook, K. A., Narayanan, A. S., Bornstein, P., & Hall, J. G. (1980) · New England Journal of Medicine · doi:10.1056/nejm198007103030201 · Cited by 206
Overexpression of BCL-x protein in primary breast cancer is associated with high tumor grade and nodal metastases.
Olopade, O. I., Adeyanju, M., Safa, A. R., Hagos, F., Mick, R., Thompson, C. B., & Recant, W. M. (1997) · PubMed · Cited by 203
Comparative analysis detects dependencies among the 5′ splice-site positions
CARMEL, I., TAL, S., VIG, I., & AST, G. (2004) · RNA · doi:10.1261/rna.5196404 · Cited by 198
Mechanism for elimination of a tumor suppressor: Aberrant splicing of a brain-specific exon causes loss of function of Bin1 in melanoma
Ge, K., DuHadaway, J., Du, W., Herlyn, M., Rodeck, U., & Prendergast, G. C. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.17.9689 · Cited by 195
Overexpression of Bcl-XS sensitizes MCF-7 cells to chemotherapy-induced apoptosis.
Sumantran, V. N., Ealovega, M. W., Núñez, G., Clarke, M. F., & Wicha, M. S. (1995) · PubMed · Cited by 195
The emerging role of splicing factors in cancer
Grosso, A. R., Martins, S., & Carmo‐Fonseca, M. (2008) · EMBO reports · doi:10.1038/embor.2008.189 · Cited by 179
Functional integration of transcriptional and RNA processing machineries
Pandit, S., Wang, D., & Fu, X.-D. (2008) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2008.03.001 · Cited by 173
Current-generation high-throughput sequencing: deepening insights into mammalian transcriptomes
Blencowe, B. J., Ahmad, S., & Lee, L. J. (2009) · Genes & Development · doi:10.1101/gad.1788009 · Cited by 168
Targeted Inhibition of the KLF6 Splice Variant, KLF6 SV1, Suppresses Prostate Cancer Cell Growth and Spread
Narla, G., DiFeo, A., Yao, S., Banno, A., Hod, E., Reeves, H. L., Qiao, R. F., Camacho-Vanegas, O., Levine, A., Kirschenbaum, A., et al. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-0217 · Cited by 166
Cyclin-Dependent Kinase Inhibition by the KLF6 Tumor Suppressor Protein through Interaction with Cyclin D1
Benzeno, S., Narla, G., Allina, J., Cheng, G. Z., Reeves, H. L., Banck, M. S., Odin, J. A., Diehl, J. A., Germain, D., & Friedman, S. L. (2004) · Cancer Research · doi:10.1158/0008-5472.can-03-2818 · Cited by 154
Alternative splicing of Bcl-2-related genes: functional consequences and potential therapeutic applications
Akgül, C., MOULDING, D. A., & Edwards, S. W. (2004) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-004-4001-7 · Cited by 149
Seemingly Neutral Polymorphic Variants May Confer Immunity to Splicing-Inactivating Mutations: A Synonymous SNP in Exon 5 of MCAD Protects from Deleterious Mutations in a Flanking Exonic Splicing Enhancer
Nielsen, K. B., Sørensen, S., Cartegni, L., Corydon, T. J., Doktor, T. K., Schroeder, L. D., Reinert, L. S., Elpeleg, O. N., Krainer, A. R., Gregersen, N., et al. (2007) · The American Journal of Human Genetics · doi:10.1086/511992 · Cited by 147
The role of KLF6 and its splice variants in cancer therapy
DiFeo, A. V., Martignetti, J. A., & Narla, G. (2008) · Drug Resistance Updates · doi:10.1016/j.drup.2008.11.001 · Cited by 141
Glycogen Synthase Kinase-3 Plays a Crucial Role in Tau Exon 10 Splicing and Intranuclear Distribution of SC35
Hernández, F., Pérez, M., Lucas, J. J., Mata, A. M., Bhat, R. V., & Ávila, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m311512200 · Cited by 140
Kruppel-Like Factor 6 Is Frequently Down-Regulated and Induces Apoptosis in Non-Small Cell Lung Cancer Cells
Ito, G., Uchiyama, M., Kondo, M., Mori, S., Usami, N., Maeda, O., Kawabe, T., Hasegawa, Y., Shimokata, K., & Sekido, Y. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-0185 · Cited by 136
Tissue-Specific Reduction in Splicing Efficiency of IKBKAP Due to the Major Mutation Associated with Familial Dysautonomia
Cuajungco, M. P., Leyne, M., Mull, J., Gill, S., Lu, W., Zagzag, D., Axelrod, F. B., Maayan, C., Gusella, J. F., & Slaugenhaupt, S. A. (2003) · The American Journal of Human Genetics · doi:10.1086/368263 · Cited by 135
Similar splicing mutations of the Menkes/mottled copper-transporting ATPase gene in occipital horn syndrome and the blotchy mouse.
Das, S., Levinson, B., Vulpe, C. D., Whitney, S., Gitschier, J. M., & Packman, S. (1995) · PubMed · Cited by 132
Similar Splice-Site Mutations of the ATP7A Gene Lead to Different Phenotypes: Classical Menkes Disease or Occipital Horn Syndrome
Møller, L. B., Tümer, Z., Lund, C., Petersen, C., Cole, T. R. P., Hanusch, R., Seidel, J. J., Jensen, L. R., & Horn, N. (2000) · The American Journal of Human Genetics · doi:10.1086/302857 · Cited by 130
Krüppel-like factor 6 is frequently down-regulated and induces apoptosis in non-small cell lung cancer cells
伊藤, 源. (2005) · 名古屋大学 eBooks · Cited by 119
KLF6-SV1 overexpression accelerates human and mouse prostate cancer progression and metastasis
Narla, G., DiFeo, A. V., Fernández, Y., Dhanasekaran, S. M., Huang, F., Sangodkar, J., Hod, E. A., Leake, D., Friedman, S. L., Hall, S. J., et al. (2008) · Journal of Clinical Investigation · doi:10.1172/jci34780 · Cited by 112
Expression of splicing factors in human ovarian cancer
Fischer, D., Noack, K., Runnebaum, I. B., Watermann, D. O., Kieback, D., Stamm, S., & Stickeler, E. (2004) · Oncology Reports · doi:10.3892/or.11.5.1085 · Cited by 106
A profile of alternative RNA splicing and transcript variation of CACNA1H, a human T-channel gene candidate for idiopathic generalized epilepsies
Zhong, X., Liu, J. R., Kyle, J. W., Hanck, D. A., & Agnew, W. S. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl068 · Cited by 97
Exon skipping and translation in patients with frameshift deletions in the dystrophin gene.
Sherratt, T. G., Vulliamy, T., Dubowitz, V., Sewry, C. A., & Strong, P. N. (1993) · Europe PMC (PubMed Central) · Cited by 92
A new role for the Krüppel-like transcription factor KLF6 as an inhibitor of c-Jun proto-oncoprotein function
Slavin, D. A., Koritschoner, N. P., Prieto, C. C., López-Díaz, F. J., Chatton, B., & Bocco, J. L. (2004) · Oncogene · doi:10.1038/sj.onc.1208020 · Cited by 92
Expression of apoptosis-regulatory genes in lung tumour cell lines: relationship to p53 expression and relevance to acquired drug resistance
Reeve, J. G., Xiong, J., Morgan, J., & Bleehen, N. M. (1996) · British Journal of Cancer · doi:10.1038/bjc.1996.230 · Cited by 88
Melanoma and genetics
Nelson, A. A., & Tsao, H. (2008) · Clinics in Dermatology · doi:10.1016/j.clindermatol.2008.09.005 · Cited by 84
Global analysis of mRNA splicing
Moore, M. J., & Silver, P. A. (2007) · RNA · doi:10.1261/rna.868008 · Cited by 79
CDKN2A germline splicing mutation affecting both p16ink4 and p14arf RNA processing in a melanoma/neurofibroma kindred
Petronzelli, F., Sollima, D., Coppola, G., Martini‐Neri, M. E., Neri, G., & Genuardi, M. (2001) · Genes Chromosomes and Cancer · doi:10.1002/gcc.1159 · Cited by 75
Substances that can change alternative splice-site selection
Sumanasekera, C., Watt, D. S., & Stamm, S. (2008) · Biochemical Society Transactions · doi:10.1042/bst0360483 · Cited by 61
RNA-Based Therapeutics: Ready for Delivery?
Bonetta, L. P. (2009) · Cell · doi:10.1016/j.cell.2009.02.010 · Cited by 57
Genome-wide survey of allele-specific splicing in humans
Nembaware, V., Lupindo, B., Schouest, K. R., Spillane, C., Scheffler, K., & Seoighe, C. (2008) · BMC Genomics · doi:10.1186/1471-2164-9-265 · Cited by 49
Weak definition ofIKBKAPexon 20 leads to aberrant splicing in familial dysautonomia
Ibrahim, E. C., Hims, M. M., Shomron, N., Burge, C. B., Slaugenhaupt, S. A., & Reed, R. (2006) · Human Mutation · doi:10.1002/humu.20401 · Cited by 46
A mutation-created novel intra-exonic pre-mRNA splice site causes constitutive activation of KIT in human gastrointestinal stromal tumors
Chen, L. L., Sabripour, M., Wu, E. F., Prieto, V. G., Fuller, G. N., & Frazier, M. L. (2005) · Oncogene · doi:10.1038/sj.onc.1208587 · Cited by 46
The Molecular Basis of Familial Dysautonomia: Overview, New Discoveries and Implications for Directed Therapies
Rubin, B. Y., & Anderson, S. L. (2007) · NeuroMolecular Medicine · doi:10.1007/s12017-007-8019-5 · Cited by 44

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
Function of alternative splicing
Stamm, S., Ben-Ari, S., Rafalska, I., Tang, Y., Zhang, Z., Toiber, D., Thanaraj, T. A., & Soreq, H. (2005) · Gene · doi:10.1016/j.gene.2004.10.022 · Cited by 1,377
Function of alternative splicing
Kelemen, O., Convertini, P., Zhang, Z., Wen, Y., Shen, M., Falaleeva, M., & Stamm, S. (2013) · Gene · doi:10.1016/j.gene.2012.07.083 · Cited by 743
Splicing mutations in human genetic disorders: Examples, detection, and confirmation
Anna, A., & Monika, G. (2018) · Journal of Applied Genetics · doi:10.1007/s13353-018-0444-7 · Cited by 657
Regulation of constitutive and alternative splicing by PRMT5 reveals a role for Mdm4 pre-mRNA in sensing defects in the spliceosomal machinery
Bezzi, M., Teo, S. X., Muller, J., Mok, W. C., Sahu, S. K., Vardy, L. A., Bonday, Z. Q., & Guccione, E. (2013) · Genes & Development · doi:10.1101/gad.219899.113 · Cited by 300

See all 414

Authors: Ward, A. J., & Cooper, T. A.
Venue: The Journal of Pathology
Publisher: Wiley
Published: 2009-11-13
Volume: 220
Issue: 2
Pages: 152-163
ISSN: 0022-3417 (ISSN-L)
1096-9896
DOI: 10.1002/path.2649
OpenAlex: W2052931181
Cited by: 414
References: 107
FWCI: 10.68
Type: journal article
Language: en
Open access: green

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.

The pathobiology of splicing

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Self-check

Citations

Cites

Cited by

Metadata

Record

About these checks

Data sources