Spliceosome Structure and Function

Lysine acetylation targets protein complexes and co-regulates major cellular functions

Choudhary, C., Kumar, C., Gnad, F., Nielsen, M. L., Rehman, M., Walther, T. C., Olsen, J. V., & Mann, M. (2009) · Science · doi:10.1126/science.1175371 · Cited by 4,040

Mechanisms of Alternative Pre-Messenger RNA Splicing

Black, D. L. (2003) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.72.121801.161720 · Cited by 2,704

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

Expansion of the eukaryotic proteome by alternative splicing

Nilsen, T. W., & Graveley, B. R. (2010) · Nature · doi:10.1038/nature08909 · Cited by 2,254

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

Mechanisms of alternative splicing regulation: insights from molecular and genomics approaches

Chen, M., & Manley, J. L. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2777 · Cited by 1,284

An extensive network of coupling among gene expression machines

Maniatis, T., & Reed, R. (2002) · Nature · doi:10.1038/416499a · Cited by 1,148

Mechanical Devices of the Spliceosome: Motors, Clocks, Springs, and Things

Staley, J. P., & Guthrie, C. (1998) · Cell · doi:10.1016/s0092-8674(00)80925-3 · Cited by 1,133

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

Exon Recognition in Vertebrate Splicing

Berget, S. M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.6.2411 · Cited by 1,090

Transcription-associated cyclin-dependent kinase 12 (CDK12) as a potential target for cancer therapy

Wu, W., Yu, S., & Yu, X. (2022) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2022.188842 · Cited by 16

IARA: a complete and curated atlas of the biogenesis of spliceosome machinery during RNA splicing

Rodrigues, K. S., Petroski, L. P., Utumi, P. H., Ferrasa, A., & Herai, R. H. (2023) · Life Science Alliance · doi:10.26508/lsa.202201593 · Cited by 13

A network of DZF proteins controls alternative splicing regulation and fidelity

Haque, N., Will, A., Cook, A. G., & Hogg, J. R. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad351 · Cited by 15

Plant immunity suppressor SKRP encodes a novel RNA ‐binding protein that targets exon 3′ end of unspliced RNA

Chen, L., Xu, Z., Huang, J., Shu, H., Hui, Y., Zhu, D., Wu, Y., Dong, S., & Wu, Z. (2023) · New Phytologist · doi:10.1111/nph.19236 · Cited by 15

An ATP-independent role for Prp16 in promoting aberrant splicing

Chung, C.-S., Wai, H. L., Kao, C.-Y., & Cheng, S.-C. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad861 · Cited by 12

What is going on inside of phytochrome B photobodies?

Willige, B. C., Yoo, C. Y., & Guzmán, J. P. S. (2024) · The Plant Cell · doi:10.1093/plcell/koae084 · Cited by 18

Etiology of craniofacial and cardiac malformations in a mouse model of SF3B4 -related syndromes

Kumar, S., Bareke, E., Lee, J., Carlson, E., Merkuri, F., Schwager, E. E., Maglio, S., Fish, J. L., Majewski, J., & Jerome‐Majewska, L. A. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2405523121 · Cited by 15

Structural basis of 5′ splice site recognition by the minor spliceosome

Zhao, J., Peter, D., Brandina, I., Liu, X., & Galej, W. P. (2025) · Molecular Cell · doi:10.1016/j.molcel.2024.12.017 · Cited by 15

Structural insights into spliceosome fidelity: DHX35–GPATCH1- mediated rejection of aberrant splicing substrates

Li, Y., Fischer, P. L., Wang, M., Zhou, Q., Song, A., Yuan, R., Meng, W., Chen, F., Lührmann, R., Lau, B., et al. (2025) · Cell Research · doi:10.1038/s41422-025-01084-w · Cited by 15

Cwc24p Is a General Saccharomyces cerevisiae Splicing Factor Required for the Stable U2 snRNP Binding to Primary Transcripts

Coltri, P. P., & Oliveira, C. C. (2012) · PLoS ONE · doi:10.1371/journal.pone.0045678 · Cited by 15

Linkage and Allostery in snRNP Protein/RNA Complexes

Williams, S. G., & Hall, K. B. (2014) · Biochemistry · doi:10.1021/bi500192a · Cited by 15

Brr2p carboxy-terminal Sec63 domain modulates Prp16 splicing RNA helicase

Cordin, O., Hahn, D., Alexander, R. D., Gautam, A., Saveanu, C., Barrass, J. D., & Beggs, J. D. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku1238 · Cited by 15

Binding Affinity and Cooperativity Control U2B″/snRNA/U2A′ RNP Formation

Williams, S. G., & Hall, K. B. (2014) · Biochemistry · doi:10.1021/bi500438e · Cited by 15

Workflow for Genome-Wide Determination of Pre-mRNA Splicing Efficiency from Yeast RNA-seq Data

Převorovský, M., Hálová, M., Abrhámová, K., Libus, J., & Folk, P. (2016) · BioMed Research International · doi:10.1155/2016/4783841 · Cited by 15

Splicing activator RNPS1 suppresses errors in pre-mRNA splicing: A key factor for mRNA quality control

Fukumura, K., Inoue, K., & Mayeda, A. (2018) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2018.01.120 · Cited by 15

Networks of mRNA Processing and Alternative Splicing Regulation in Health and Disease

Jordan, P., Gonçalves, V., Fernandes, S., Marques, T. M., Pereira, M. H. N., & Gama‐Carvalho, M. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-19966-1_1 · Cited by 16

Nuclear proteome analysis of Chlamydomonas with response to CO2 limitation

Arias, C., Obudulu, O., Zhao, X., Ansolia, P., Zhang, X., Paul, S., Bygdell, J., Pirmoradian, M., Zubarev, R. A., Samuelsson, G. S., et al. (2020) · Algal Research · doi:10.1016/j.algal.2019.101765 · Cited by 14

Noncoding Y RNAs regulate the levels, subcellular distribution and protein interactions of their Ro60 autoantigen partner

Leng, Y., Sim, S., Magidson, V., & Wolin, S. L. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa414 · Cited by 15

SRSF9 Regulates Cassette Exon Splicing of Caspase-2 by Interacting with Its Downstream Exon

Ha, J., Jang, H.-N., Choi, N., Oh, J., Min, C., Pradella, D., Jung, D., Williams, D. R., Park, D., Ghigna, C., et al. (2021) · Cells · doi:10.3390/cells10030679 · Cited by 15

Research Progress of Totipotent Stem Cells

Cai, J., Chen, H., Xie, S., Hu, Z., & Bai, Y. (2022) · Stem Cells and Development · doi:10.1089/scd.2022.0061 · Cited by 15

Aberrant splicing events caused by insertion of genes of interest into expression vectors

Cheng, Y., Kang, X.-Z., Chan, P., Ye, Z., Chan, C., & Jin, D. (2022) · International Journal of Biological Sciences · doi:10.7150/ijbs.72408 · Cited by 15

Dysregulation of the chromatin environment leads to differential alternative splicing as a mechanism of disease in a human model of autism spectrum disorder

Leung, C. S., Rosenzweig, S. J., Yoon, B., Marinelli, N. A., Hollingsworth, E. W., Maguire, A. M., Cowen, M. H., Schmidt, M., Imitola, J., Uzun, E. D. G., et al. (2023) · Human Molecular Genetics · doi:10.1093/hmg/ddad002 · Cited by 16

Regulation of RNA metabolism is important for in vitro dedifferentiation of plant cells

Ohtani, M. (2015) · Journal of Plant Research · doi:10.1007/s10265-015-0700-4 · Cited by 15

Genetics and biochemistry remain essential in the structural era of the spliceosome

Mayerle, M., & Guthrie, C. (2017) · Methods · doi:10.1016/j.ymeth.2017.01.006 · Cited by 15

Human ribosomal protein eS1 is engaged in cellular events related to processing and functioning of U11 snRNA

Gopanenko, A. V., Malygin, A. A., Tupikin, A. E., Laktionov, P. P., Kabilov, M. R., & Karpova, G. G. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx559 · Cited by 15

Human Cancer-Associated Mutations of SF3B1 Lead to a Splicing Modification of Its Own RNA

Bergot, T., Lippert, É., Douet‐Guilbert, N., Commet, S., Corcos, L., & Bernard, D. G. (2020) · Cancers · doi:10.3390/cancers12030652 · Cited by 15

Structure of a transcribing RNA polymerase II–U1 snRNP complexPreprint

Zhang, S., Aibara, S., Vos, S. M., Agafonov, D. E., Lührmann, R., & Cramer, P. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.10.19.344200 · Cited by 15

Imaging Organization of RNA Processing within the NucleusPreprint

Biswas, J., Li, W., Singer, R. H., & Coleman, R. A. (2021) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a039453 · Cited by 15

Regulation of transcriptome plasticity by mTOR signaling pathway

Yong, J., Kim, H., Lee, E., & Jung, Y. (2025) · Experimental & Molecular Medicine · doi:10.1038/s12276-025-01508-y · Cited by 17

The spliceosomal proteins PPIH and PRPF4 exhibit bi-partite binding

Rajiv, C., Jackson, S. R., Cocklin, S., Eisenmesser, E. Z., & Davis, T. L. (2017) · Biochemical Journal · doi:10.1042/bcj20170366 · Cited by 14

Interaction Network of Porcine Circovirus Type 3 and 4 Capsids with Host Proteins

Zhou, J., Wang, Y., Zhou, L., Qiu, Y., Zhao, J., Dai, B., Feng, X., Hou, L., & Liu, J. (2022) · Viruses · doi:10.3390/v14050939 · Cited by 14

Cooperative engagement and subsequent selective displacement of SR proteins define the pre-mRNA 3D structural scaffold for early spliceosome assembly

Saha, K., & Ghosh, G. (2022) · Nucleic Acids Research · doi:10.1093/nar/gkac636 · Cited by 14

Roles of minor spliceosome in intron recognition and the convergence with the better understood major spliceosome

Ding, Z., Meng, Y., Fan, Y., & Xu, Y. (2022) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1761 · Cited by 14

Prime editing strategies to mediate exon skipping in DMD gene

Mbakam, C. H., Roustant, J., Rousseau, J., Yaméogo, P., Lu, Y., Bigot, A., Mamchaoui, K., Mouly, V., Lamothe, G., & Tremblay, J. P. (2023) · Frontiers in Medicine · doi:10.3389/fmed.2023.1128557 · Cited by 16

Bromodomain-containing Protein 4 regulates innate inflammation via modulation of alternative splicing

Mann, M. W., Fu, Y., Gearhart, R. L., Xu, X., Roberts, D. S., Li, Y., Zhou, J., Ge, Y., & Brasier, A. R. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1212770 · Cited by 18

Evaluation of Chemically Modified Nucleic Acid Analogues for Splice Switching Application

Le, B. T., Chen, S., & Veedu, R. N. (2023) · ACS Omega · doi:10.1021/acsomega.3c07618 · Cited by 14

Productive mRNA chromatin escape is promoted by PRMT5 activity

DeAngelo, J. D., Maron, M. I., Roth, J. S., Hegde, S. S., Silverstein, A. M., Gupta, V., Stransky, S., Basken, J., Azofeifa, J., Query, C. C., et al. (2025) · Molecular Cell · doi:10.1016/j.molcel.2025.09.021 · Cited by 14

Relationship between changes in the exon-recognition machinery and SLC22A1 alternative splicing in hepatocellular carcinoma

Soto, M., Reviejo, M., Al‐Abdulla, R., Romero, M. R., Macı́as, R. I. R., Boix, L., Bruix, J., Serrano, M. A., & Marı́n, J. J. G. (2020) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2020.165687 · Cited by 14

VfoldMCPX: predicting multistrand RNA complexes

Zhang, S., Cheng, Y., Guo, P., & Chen, S.-J. (2022) · RNA · doi:10.1261/rna.079020.121 · Cited by 14

Cancer-associated mutations in SF3B1 disrupt the interaction between SF3B1 and DDX42

Zhao, B., Li, Z., Qian, R., Liu, G., Fan, M., Liang, Z., Hu, X., & Wan, Y. (2022) · The Journal of Biochemistry · doi:10.1093/jb/mvac049 · Cited by 17

Molecular Pathogenesis and New Therapeutic Dimensions for Spinal Muscular Atrophy

López‐Cortés, A., Echeverría‐Garcés, G., & Ramos-Medina, M. J. (2022) · Biology · doi:10.3390/biology11060894 · Cited by 16

RNA splicing: a dual-edged sword for hepatocellular carcinoma

Kashyap, A., Tripathi, G., Tripathi, A., Rao, R., Kashyap, M., Bhat, A., Kumar, D., Rajhans, A., Kumar, P., Chandrashekar, D. S., et al. (2022) · Medical Oncology · doi:10.1007/s12032-022-01726-8 · Cited by 14

Abnormalities in intron retention characterize patients with systemic lupus erythematosus

Sun, X., Liu, Z., Li, Z., Zeng, Z., Peng, W., Zhu, J., Zhao, J., Zhu, C., Zeng, C., Stearrett, N., et al. (2023) · Scientific Reports · doi:10.1038/s41598-023-31890-4 · Cited by 14

SNRPD1 inhibition suppresses the proliferation of hepatocellular carcinoma and promotes autophagy through the PI3K/AKT/mTOR/4EBP1 pathway

Wang, H., Chen, M., Yang, C., Hu, H., Jiang, Y., Yang, F., & Lv, L. (2023) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2023.109661 · Cited by 14

Retention and splicing complex (RES) – the importance of cooperativity

Wysoczański, P., & Zweckstetter, M. (2015) · RNA Biology · doi:10.1080/15476286.2015.1096484 · Cited by 14

Probing Nucleic Acid Interactions and Pre-mRNA Splicing by Förster Resonance Energy Transfer (FRET) Microscopy

Šimková, E., & Staněk, D. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms131114929 · Cited by 13

Nuclear cyclophilins affect spliceosome assembly and function in vitro

Adams, B. M., Coates, M. N., Jackson, S. R., Jurica, M. S., & Davis, T. L. (2015) · Biochemical Journal · doi:10.1042/bj20150396 · Cited by 14

RNPS 1 is modulated by ubiquitin‐specific protease 4

Kwon, S., Kim, E., & Baek, K. (2016) · FEBS Letters · doi:10.1002/1873-3468.12531 · Cited by 14

A central role of Cwc25 in spliceosome dynamics during the catalytic phase of pre-mRNA splicing

Tseng, C. K., Chung, C.-S., Chen, H.-C., & Cheng, S.-C. (2017) · RNA · doi:10.1261/rna.059204.116 · Cited by 14

Nineteen complex–related factor Prp45 is required for the early stages of cotranscriptional spliceosome assembly

Hálová, M., Gahura, O., Převorovský, M., Cit, Z., Novotný, M., Valentová, A., Abrhámová, K., Půta, F., & Folk, P. (2017) · RNA · doi:10.1261/rna.061986.117 · Cited by 13

Functional and Biochemical Characterization of Dib1's Role in Pre-Messenger RNA Splicing

Schreib, C. C., Bowman, E. K., Hernandez, C., Wilson, A. L., Potts, C., & Maeder, C. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2018.04.027 · Cited by 14

RNA-seq Analysis of the SCN1A-KO Model based on CRISPR/Cas9 Genome Editing Technology

Shi, X., He, W., Guo, S., Zhang, B., Ren, S., Liu, K., Sun, T., & Cui, J. (2018) · Neuroscience · doi:10.1016/j.neuroscience.2018.11.052 · Cited by 14

Effect of RNA splicing machinery gene mutations on prognosis of patients with MDS

Wang, X., Song, X., & Yan, X. (2019) · Medicine · doi:10.1097/md.0000000000015743 · Cited by 14

Activation of Prp28 ATPase by phosphorylated Npl3 at a critical step of spliceosome remodeling

Yeh, F.-L., Chang, S., Ahmed, G. R., Liu, H.-I., Tung, L., Yeh, C.-S., Lanier, L. S., Maeder, C., Lin, C.-M., Tsai, S., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-23459-4 · Cited by 14

Multiomics analysis of the NAD+–PARP1 axis reveals a role for site-specific ADP-ribosylation in splicing in embryonic stem cellsPreprint

Jones, A., & Kraus, W. L. (2022) · Genes & Development · doi:10.1101/gad.349335.121 · Cited by 15

Integrating metagenomics, lipidomics and proteomics to explore the effect and mechanism of ginsenoside Rb1 on atherosclerosis co-depression disease

Zhao, Y., Song, T., Ren, P., Wu, X., Luo, Q., Xie, J., Lai, H., Li, X., Wen, Y., Liao, X.-X., et al. (2025) · Phytomedicine · doi:10.1016/j.phymed.2025.157301 · Cited by 13

Splicing of an intervening sequence by protein-free human snRNAs

Jaladat, Y., Zhang, B., Mohammadi, A., & Valadkhan, S. (2011) · RNA Biology · doi:10.4161/rna.8.3.15386 · Cited by 13

Alterations in the expression and activity of pre-mRNA splicing factors in hepatocarcinogenesis

Berasain, C., Elizalde, M., Urtasun, R., Castillo, J., García‐Irigoyen, O., Uriarte, I., Latasa, M. U., Prìeto, J., & Avila, M. A. (2014) · Hepatic Oncology · doi:10.2217/hep.13.17 · Cited by 13

Expanding the genotypic spectrum of TXNL4A variants in Burn‐McKeown syndrome

Wood, K., Ellingford, J. M., Thomas, H. B., Douzgou, S., Beaman, G. M., Hobson, E., Prescott, K., O’Keefe, R. T., & Newman, W. G. (2021) · Clinical Genetics · doi:10.1111/cge.14082 · Cited by 13

Major and minor U small nuclear RNAs genes characterization in a neotropical fish genome: Chromosomal remodeling and repeat units dispersion in Parodontidae

Azambuja, M., Schemberger, M. O., Nogaroto, V., Moreira‐Filho, O., Martins, C., & Vicari, M. R. (2022) · Gene · doi:10.1016/j.gene.2022.146459 · Cited by 13

MDF is a conserved splicing factor and modulates cell division and stress response inArabidopsis

de Luxán‐Hernández, C., Lohmann, J., Tranque, E., Chumová, J., Binarová, P., Salinas, J., & Weingartner, M. (2022) · Life Science Alliance · doi:10.26508/lsa.202201507 · Cited by 13

Identification of transient intermediates during spliceosome activation by single molecule fluorescence microscopy

Fu, X., Kaur, H., Rodgers, M. L., Montemayor, E., Butcher, S. E., & Hoskins, A. A. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2206815119 · Cited by 13

Secondary-Type Mutations in Acute Myeloid Leukemia: Updates from ELN 2022

Bouligny, I. M., Maher, K. R., & Grant, S. (2023) · Cancers · doi:10.3390/cancers15133292 · Cited by 13

Sm complex assembly and 5′ cap trimethylation promote selective processing of snRNAs by the 3′ exonuclease TOE1

Ma, T., Xiong, E., Lardelli, R. M., & Lykke‐Andersen, J. (2024) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2315259121 · Cited by 13

Xrp1 governs the stress response program to spliceosome dysfunction

Stanković, D., Tain, L. S., & Uhlířová, M. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae055 · Cited by 14

FUBP1 in human cancer: Characteristics, functions, and potential applications

Zhang, F., Xiong, Q., Wang, M., Cao, X., & Zhou, C. (2024) · Translational Oncology · doi:10.1016/j.tranon.2024.102066 · Cited by 13

Condensation of ZFP207 and U1 snRNP promotes spliceosome assembly

Zhou, Y., Tong, C., Shi, Z., Zhang, Y., Xiong, X., Shen, X., Li, X., & Yin, Y. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-025-01501-z · Cited by 15

Structural and Functional Characterization of the N Terminus of Schizosaccharomyces pombe Cwf10

Livesay, S. B., Collier, S. E., Bitton, D. A., Bähler, J., & Ohi, M. D. (2013) · Eukaryotic Cell · doi:10.1128/ec.00140-13 · Cited by 13

Structural and mechanistic insights into human splicing factor SF3b complex derived using an integrated approach guided by the cryo-EM density maps

Rakesh, R., Joseph, A. P., Bhaskara, R. M., & Srinivasan, N. (2016) · RNA Biology · doi:10.1080/15476286.2016.1218590 · Cited by 13

Proteomics provides insights into the inhibition of Chinese hamster V79 cell proliferation in the deep underground environment

Liu, J., Ma, T., Gao, M., Liu, Y., Liu, J., Wang, S., Xie, Y., Wang, L., Cheng, J., Liu, S., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-71154-z · Cited by 13

Combining genetic constraint with predictions of alternative splicing to prioritize deleterious splicing in rare disease studies

Cormier, M. J., Pedersen, B. S., Bayrak‐Toydemir, P., & Quinlan, A. R. (2022) · BMC Bioinformatics · doi:10.1186/s12859-022-05041-x · Cited by 11

Stable tri-snRNP integration is accompanied by a major structural rearrangement of the spliceosome that is dependent on Prp8 interaction with the 5′ splice site

Boesler, C., Rigo, N., Agafonov, D. E., Kastner, B., Urlaub, H., Will, C. L., & Lührmann, R. (2015) · RNA · doi:10.1261/rna.053991.115 · Cited by 13

Characterization of SCL33 splicing patterns during diverse virus infections in Brachypodium distachyon

Mandadi, K. K., Pyle, J. D., & Scholthof, K. G. (2015) · Plant Signaling & Behavior · doi:10.1080/15592324.2015.1042641 · Cited by 13

Intronic features that determine the selection of the 3′ splice site

Pérez‐Valle, J., & Vilardell, J. (2012) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1131 · Cited by 13

Interaction between RNA helicase ROOT INITIATION DEFECTIVE 1 and GAMETOPHYTIC FACTOR 1 is involved in female gametophyte development in Arabidopsis

Zhu, D. Z., Zhao, X. F., Liu, C., Fang, F., Wang, F., Gao, X., & Zhang, X. S. (2016) · Journal of Experimental Botany · doi:10.1093/jxb/erw341 · Cited by 13

Fluorescent Branched RNAs for High-Throughput Analysis of Dbr1 Enzyme Kinetics and Inhibition

Katolik, A., Clark, N. E., Tago, N., Montemayor, E., Hart, P. J., & Damha, M. J. (2017) · ACS Chemical Biology · doi:10.1021/acschembio.6b00971 · Cited by 13

Structural studies of the endogenous spliceosome – The supraspliceosome

Sperling, J. M., & Sperling, R. (2017) · Methods · doi:10.1016/j.ymeth.2017.04.005 · Cited by 13

Prp8 impacts cryptic but not alternative splicing frequency

Mayerle, M., Yitiz, S., Soulette, C. M., Rogel-Hernandez, L. E., Ramirez, A., Ragle, J. M., Katzman, S. J., Guthrie, C., & Zahler, A. M. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1819020116 · Cited by 13

RNA-Binding Proteins in Pulmonary Hypertension

Zhang, H., Brown, R. D., Stenmark, K. R., & Hu, C. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21113757 · Cited by 14

The integral spliceosomal component CWC15 is required for development in Arabidopsis

Slane, D., Lee, C. H., Kolb, M., Dent, C., Miao, Y., Franz‐Wachtel, M., Lau, S., Maček, B., Balasubramanian, S., Bayer, M. J., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-70324-3 · Cited by 11

Splicing Enhancers at Intron–Exon Borders Participate in Acceptor Splice Sites Recognition

Kováčová, T., Souček, P., Hujová, P., Freiberger, T., & Grodecká, L. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21186553 · Cited by 12

Analysis of Synthetic Lethality Reveals Genetic Interactions Between the GTPase Snu114p and snRNAs in the Catalytic Core of the Saccharomyces cerevisiae Spliceosome

Frazer, L. N., Lovell, S. C., & O’Keefe, R. T. (2009) · Genetics · doi:10.1534/genetics.109.107243 · Cited by 13

Molecular recognition of the environment and mechanisms of the origin of species in quantum-like modeling of evolution

Melkikh, A. V., & Khrennikov, A. Y. (2017) · Progress in Biophysics and Molecular Biology · doi:10.1016/j.pbiomolbio.2017.04.008 · Cited by 13

Exercise does not induce browning of WAT at thermoneutrality and induces an oxidative, myogenic signature in BATPreprint

Aldiss, P., Lewis, J. E., Lupini, I., Boocock, D. J., Miles, A. K., Ebling, F. J. P., Budge, H., & Symonds, M. E. (2019) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/649061 · Cited by 13

SHIFTR enables the unbiased identification of proteins bound to specific RNA regions in live cells

Aydin, J., Gabel, A., Zielinski, S., Ganskih, S., Schmidt, N., Hartigan, C. R., Schenone, M., Carr, S. A., & Munschauer, M. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae038 · Cited by 12

Structures of aberrant spliceosome intermediates on their way to disassembly

Soni, K., Horvath, A., Dybkov, O., Schwan, M., Trakansuebkul, S., Flemming, D., Wild, K., Urlaub, H., Fischer, T., & Sinning, I. (2025) · Nature Structural & Molecular Biology · doi:10.1038/s41594-024-01480-7 · Cited by 14

Modulation of HIV-1 gene expression by binding of a ULM motif in the Rev protein to UHM-containing splicing factors

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