The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.
CLIP Identifies Nova-Regulated RNA Networks in the Brain
Abstract
Nova proteins are neuron-specific antigens targeted in paraneoplastic opsoclonus myoclonus ataxia (POMA), an autoimmune neurologic disease characterized by abnormal motor inhibition.Nova proteins regulate neuronal pre-messenger RNA splicing by directly binding to RNA.To identify Nova RNA targets, we developed a method to purify protein-RNA complexes from mouse brain with the use of ultraviolet cross-linking and immunoprecipitation (CLIP).Thirty-four transcripts were identified multiple times by Nova CLIP.Three-quarters of these encode proteins that function at the neuronal synapse, and one-third are involved in neuronal inhibition.Splicing targets confirmed in Nova –/– mice include c-Jun N-terminal kinase 2, neogenin, and gephyrin; the latter encodes a protein that clusters inhibitory γ-aminobutyric acid and glycine receptors, two previously identified Nova splicing targets.Thus, CLIP reveals that Nova coordinately regulates a biologically coherent set of RNAs encoding multiple components of the inhibitory synapse, an observation that may relate to the cause of abnormal motor inhibition in POMA.
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Many NOVA2 target genes, including the GABAB receptor 2 (Gabbr2), glycine receptor α2 (Glra2), gephyrin (Gphn) and the inward rectifier potassium channel Kir3.2 (Girk2), are involved in inhibitory synapse function99”
From The neurogenetics of alternative splicing (2016) · cites this paper as [99]
Citations
Cites
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
Selective interaction of JNK protein kinase isoforms with transcription factors.
Gupta, S., Barrett, T., Whitmarsh, A. J., Cavanagh, J., Sluss, H. K., Dérijard, B., & Davis, R. J. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00636.x · Cited by 1,341
Lerner, M. R., & STEITZ, J. A. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.11.5495 · Cited by 1,157
Brown, V., Jin, P., Ceman, S., Darnell, J. C., O'Donnell, W. T., Tenenbaum, S. A., Jin, X., Feng, Y., Wilkinson, K. D., Keene, J. D., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00568-2 · Cited by 1,109
Self-citationDeleted in Colorectal Cancer (DCC) encodes a netrin receptor.
Keino-Masu, K., Masu, M., Hinck, L., Leonardo, E., Chan, S., Culotti, J., & Tessier-Lavigne, M. (1996) · Cell · doi:10.1016/s0092-8674(00)81336-7 · Cited by 1,048
Fragile X mental retardation protein targets G quartet mRNAs important for neuronal function
Darnell, J. C., Jensen, K. B., Jin, P., Brown, V., Warren, S. T., & Darnell, R. B. (2001) · Cell · doi:10.1016/s0092-8674(01)00566-9 · Cited by 952
Self-citationLüscher, C., Jan, L. Y., Stoffel, M., Malenka, R. C., & Nicoll, R. A. (1997) · Neuron · doi:10.1016/s0896-6273(00)80381-5 · Cited by 762
Autoantibodies in the diagnosis of systemicrheumatic diseases
von Mühlen, C. A., & Tan, E. M. (1995) · Seminars in Arthritis and Rheumatism · doi:10.1016/s0049-0172(95)80004-2 · Cited by 546
RNA cargoes associating with FMRP reveal deficits in cellular functioning in Fmr1 null mice
Miyashiro, K. Y., Beckel-Mitchener, A., Purk, T. P., Becker, K. G., Barret, T., Liu, L., Carbonetto, S., Weiler, I. J., Greenough, W. T., & Eberwine, J. (2003) · Neuron · doi:10.1016/s0896-6273(03)00034-5 · Cited by 495
Loss of Postsynaptic GABAAReceptor Clustering in Gephyrin-Deficient Mice
Kneussel, M., Brandstätter, J. H., Laube, B., Stahl, S., Müller, U., & Betz, H. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-21-09289.1999 · Cited by 446
Flagged first, then by citations
Research works printed but not linked: 1
- D. Billups, J. G. Hanley, M. Orme, D. Attwell, S. J. Moss, J. Neurosci.20, 8643 (2000).
Cited by
Sorted by citations
Items 701–800 of 1,001
Maatz, H., Koliński, M., Hübner, N., & Landthaler, M. (2017) · Current Protocols in Molecular Biology · doi:10.1002/cpmb.35 · Cited by 13
Mapping transcriptome‐wide protein‐RNA interactions to elucidate RNA regulatory programs
Hannigan, M. M., Zagore, L. L., & Licatalosi, D. D. (2018) · Quantitative Biology · doi:10.1007/s40484-018-0145-6 · Cited by 13
CLIPick: a sensitive peak caller for expression-based deconvolution of HITS-CLIP signals
Park, S., Ahn, S. H., Cho, E. S., Cho, Y. K., Jang, E.-S., & Chi, S. W. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky917 · Cited by 13
Identifying and validating small molecules interacting with RNA (SMIRNAs)
Disney, M. D., Velagapudi, S. P., Li, Y., Costales, M. G., & Childs‐Disney, J. L. (2019) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2019.04.027 · Cited by 13
Peroxiredoxin 1 post-transcriptionally regulates snoRNA expression
Kim, E.-K., Lee, S. Y., Kim, Y., Ahn, S., & Jang, H. H. (2019) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2019.05.030 · Cited by 13
Методы исследования взаимодействия белков с РНК
Попова, В. В., Куршакова, М. М., & Kopytova, D. V. (2015) · Molecular Biology · doi:10.7868/s0026898415020111 · Cited by 13
Stem Cell Ribonomics: RNA-Binding Proteins and Gene Networks in Stem Cell Differentiation
Shigunov, P., & Dallagiovanna, B. (2015) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2015.00074 · Cited by 14
Memory, Synaptic Translation, and…Prions?
Darnell, R. B. (2003) · Cell · doi:10.1016/s0092-8674(03)01022-5 · Cited by 13
Self-citationCo-profiling of in situ RNA-protein interactions and transcriptome in single cells and tissues
Cheng, Q., Xie, G., Zhang, X., Wang, J., Ding, S., Wu, Y., Shi, M., Duan, F., Wan, Z.-L., Wei, J.-J., et al. (2025) · Nature Methods · doi:10.1038/s41592-025-02774-4 · Cited by 12
Delre, P., Cerchia, C., & Lavecchia, A. (2025) · Drug Discovery Today · doi:10.1016/j.drudis.2025.104488 · Cited by 13
Technological advancements in deciphering RNA-RNA interactions
Ye, R., Zhao, H., Wang, X., & Xue, Y. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.06.036 · Cited by 12
Decoding RNA–Protein Interactions: Methodological Advances and Emerging Challenges
Yi, W., & Yan, J. (2025) · Advanced Genetics · doi:10.1002/ggn2.202500011 · Cited by 12
Assessing Computational Steps for CLIP-Seq Data Analysis
Liu, Q., Zhong, X. Y., Madison, B., Rustgi, A. K., & Shyr, Y. (2015) · BioMed Research International · doi:10.1155/2015/196082 · Cited by 13
The Genetic Control of Stoichiometry Underlying Autism
Darnell, R. B. (2020) · Annual Review of Neuroscience · doi:10.1146/annurev-neuro-100119-024851 · Cited by 12
Self-citationHan, Y. Y., Guo, X., Zhang, T., Wang, J., & Ye, K. (2021) · RNA · doi:10.1261/rna.078896.121 · Cited by 12
RNA-Binding Protein Immunopurification-Microarray (RIP-Chip) Analysis to Profile Localized RNAs
Galgano, A., & Gerber, A. P. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-005-8_23 · Cited by 12
Blencowe, B. J., Brenner, S. E., Hughes, T., & Morris, Q. (2008) · Pacific Symposium on Biocomputing (PSB) · doi:10.1142/9789812836939_0052 · Cited by 12
Silverman, I. M., & Gregory, B. D. (2014) · Methods · doi:10.1016/j.ymeth.2014.10.021 · Cited by 13
Spicuglia, S., Maqbool, M. A., Puthier, D., & Andrau, J. (2013) · Methods · doi:10.1016/j.ymeth.2013.04.003 · Cited by 17
Grozdanov, P. N., & MacDonald, C. C. (2014) · Methods in molecular biology · doi:10.1007/978-1-62703-971-0_17 · Cited by 12
Alternative Splicing in Stem Cell Self-Renewal and Diferentiation
Nelles, D. A., & Yeo, G. W.-M. (2010) · Advances in experimental medicine and biology · doi:10.1007/978-1-4419-7037-4_7 · Cited by 12
Baines, R., Giachello, C. N., & Lin, W. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-804066-9.00024-9 · Cited by 13
Kück, U., & Schmitt, O. (2021) · Cells · doi:10.3390/cells10020290 · Cited by 12
Laurent, G. S., Shtokalo, D. N., Heydarian, M., Palyanov, A. Y., Babiy, D., Zhou, J., Kumar, A., & Inchima, S. U. (2012) · Molecular Genetics and Genomics · doi:10.1007/s00438-012-0722-8 · Cited by 13
Dassi, E., & Quattrone, A. (2012) · RNA Biology · doi:10.4161/rna.22035 · Cited by 13
Decoding Abnormal Splicing Code in Human Diseases
Ohno, K. (2015) · Journal of Investigative Genomics · doi:10.15406/jig.2015.02.00016 · Cited by 12
Hernández-Imaz, E., Martín, Y., Conti, L. D., Melean, G., Valero, A., Baralle, M., & Hernández-Chico, C. (2015) · PLoS ONE · doi:10.1371/journal.pone.0141735 · Cited by 12
miCLIP-MaPseq, a Substrate Identification Approach for Radical SAM RNA Methylating Enzymes
Stojković, V., Chu, T., Thérizols, G., Weinberg, D. E., & Fujimori, D. G. (2018) · Journal of the American Chemical Society · doi:10.1021/jacs.8b02618 · Cited by 12
Mapping of In Vivo RNA-Binding Sites by Ultraviolet (UV)-Cross-Linking Immunoprecipitation (CLIP)Preprint
Darnell, J. C., Mele, A., Hung, K. Y. S., & Darnell, R. B. (2018) · Cold Spring Harbor Protocols · doi:10.1101/pdb.top097931 · Cited by 12
Self-citationMaurel, C., Scherer, N. M., Luu, L., Radford, R. A. W., Hogan, A. L., Merjane, J., Vidal-Itriago, A., Don, E. K., Chapman, T. R., Cull, S., et al. (2025) · iScience · doi:10.1016/j.isci.2025.112761 · Cited by 11
CLIP-Seq in Bacteria: Global Recognition Patterns of Bacterial RNA-Binding Proteins
Andresen, L., & Holmqvist, E. (2018) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2018.08.008 · Cited by 11
The role of altered translation in intellectual disability and epilepsy
Malone, T. J., & Kaczmarek, L. K. (2022) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2022.102267 · Cited by 12
Sarnowski, C. P., Knörlein, A., de Vries, T., Götze, M., Beusch, I., Aebersold, R. H., Allain, F. H. ‐., Hall, J., & Leitner, A. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf523 · Cited by 11
Chen, L. (2012) · Statistics in Biosciences · doi:10.1007/s12561-012-9064-7 · Cited by 14
Integrating post‐transcriptional regulation into the embryonic stem cell gene regulatory network
Cassar, P. A., & Stanford, W. L. (2011) · Journal of Cellular Physiology · doi:10.1002/jcp.22787 · Cited by 11
Detection and Analysis of Long Noncoding RNAs
Lai, F., Blumenthal, E., & Shiekhattar, R. (2016) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2016.03.010 · Cited by 11
Evaluation of the iron regulatory protein-1 interactome
Connell, G. J., Danial, J. S., & Haastruthers, C. X. (2018) · BioMetals · doi:10.1007/s10534-018-0076-8 · Cited by 11
Identification of RNA–RBP Interactions in Subcellular Compartments by CLIP-Seq
Sahadevan, S., Pérez‐Berlanga, M., & Polymenidou, M. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-1975-9_19 · Cited by 12
Katsantoni, M., van Nimwegen, E., & Zavolan, M. (2023) · Genome biology · doi:10.1186/s13059-023-02913-0 · Cited by 11
Cross-Linking and Immunoprecipitation of Nuclear RNA-Binding Proteins
Li, Q., Uemura, Y., & Kawahara, Y. (2014) · Methods in molecular biology · doi:10.1007/978-1-4939-2253-6_15 · Cited by 11
Unravelling the RNA-Binding Properties of SAFB Proteins in Breast Cancer Cells
Hong, E., Best, A. J., Gautrey, H., Chin, J. M., Razdan, A., Curk, T., Elliott, D. J., & Tyson-Capper, A. J. (2015) · BioMed Research International · doi:10.1155/2015/395816 · Cited by 11
Analysis of p53–RNA interactions in cultured human cells
Riley, K. J.-L., & Maher, L. J. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.08.181 · Cited by 13
Cholinergic regulation of striatal Nova mRNAs
Jelen, N., Ule, J., & Živin, M. (2010) · Neuroscience · doi:10.1016/j.neuroscience.2010.05.013 · Cited by 10
Self-citationRevealing the grammar of small RNA secretion using interpretable machine learning
Zirak, B., Naghipourfar, M., Saberi, A., Pouyabahar, D., Zarezadeh, A., Luo, L., Fish, L., Huh, D., Navickas, A., Sharifi‐Zarchi, A., et al. (2024) · Cell Genomics · doi:10.1016/j.xgen.2024.100522 · Cited by 10
Viral RNA Interactome: The Ultimate Researcher’s Guide to RNA–Protein Interactions
Hanson, W. A., Agosto, G. A. R., & Rouskin, S. (2024) · Viruses · doi:10.3390/v16111702 · Cited by 10
Li, H., Sun, C., Wang, Y., Gao, Y., Liu, Y., Gao, Y., Xu, L., & Zhang, C. (2012) · Journal of Histochemistry & Cytochemistry · doi:10.1369/0022155412461255 · Cited by 10
Strategies and technologies for exploring long noncoding RNAs in heart failure
Zhang, Z., Wan, J., Liu, X., & Zhang, W. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110572 · Cited by 10
Feng, H., Lu, X., Maji, S., Liu, L., Ustianenko, D., Rudnick, N. D., & Zhang, C. (2024) · Nature Communications · doi:10.1038/s41467-024-46429-y · Cited by 10
Liang, Q., Yu, T., Kofman, E. R., Jagannatha, P., Rhine, K., Yee, B. A., Corbett, K. D., & Yeo, G. W.-M. (2024) · Nature Communications · doi:10.1038/s41467-024-50363-4 · Cited by 10
High-resolution profiling of protein occupancy on polyadenylated RNA transcripts
Munschauer, M., Schueler, M., Dieterich, C., & Landthaler, M. (2013) · Methods · doi:10.1016/j.ymeth.2013.09.017 · Cited by 10
Budak, G., Srivastava, R., & Janga, S. C. (2017) · RNA · doi:10.1261/rna.059089.116 · Cited by 10
The Secret Life of RNA: Lessons from Emerging Methodologies
Médioni, C., & Besse, F. (2017) · Methods in molecular biology · doi:10.1007/978-1-4939-7213-5_1 · Cited by 11
TRIBE Uncovers the Role of Dis3 in Shaping the Dynamic Transcriptome in Malaria Parasites
Liu, M., Lu, B., Fan, Y., He, X., Shen, S., Jiang, C., & Zhang, Q. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00264 · Cited by 10
RNA Secondary Structure Representation Network for RNA-proteins Binding Prediction
Liu, Z., Luo, F., & Du, B. (2021) · Proceedings of the AAAI Conference on Artificial Intelligence · doi:10.1609/aaai.v35i1.16112 · Cited by 10
Iwasaki, M., Kawahara, Y., Okubo, C., Yamakawa, T., Nakamura, M., Tabata, T., Nishi, Y., Narita, M., Ohta, A., Saito, H., et al. (2022) · iScience · doi:10.1016/j.isci.2022.104289 · Cited by 11
Investigating RNA editing factors from trypanosome mitochondria
Aphasizheva, I., Zhang, L., & Aphasizhev, R. (2016) · Methods · doi:10.1016/j.ymeth.2016.03.020 · Cited by 10
An in Vitro Technique to Identify the RNA Binding-Site Sequences for RNA-Binding Proteins
Choi, S., Park, C., Kim, K. E., & Kim, K. K. (2017) · BioTechniques · doi:10.2144/000114567 · Cited by 10
Shults, C. L., Dingwall, C. B., Kim, C. K., Pinceti, E., Rao, Y. S., & Pak, T. R. (2017) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2017.09.005 · Cited by 11
Approaches to Identify and Characterise the Post-Transcriptional Roles of lncRNAs in Cancer
Carter, J.-M., Ang, D. A., Sim, N., Budiman, A., & Li, Y. (2021) · Non-Coding RNA · doi:10.3390/ncrna7010019 · Cited by 10
Masuda, A., Kawachi, T., & Ohno, K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22105312 · Cited by 11
Gephyrin: does splicing affect its function?
Paarmann, I., Saiyed, T., Schmitt, B., & Betz, H. (2006) · Biochemical Society Transactions · doi:10.1042/bst0340045 · Cited by 10
Kilchert, C., Kecman, T., Priest, E. L., Hester, S., Aydin, E., Kuś, K., Roßbach, O., Castelló, A., Mohammed, S., & Vasiljeva, L. (2020) · Genome Research · doi:10.1101/gr.257006.119 · Cited by 10
Peyda, P., Lin, C.-H., Onwuzurike, K., & Black, D. L. (2025) · Genes & Development · doi:10.1101/gad.352105.124 · Cited by 10
Alternative splicing in addiction
Bhatnagar, A., & Heller, E. A. (2025) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2025.102340 · Cited by 11
Non-Coding RNAs and Immune Evasion in Human Gamma-Herpesviruses
Media, T. S., Cano-Aroca, L., & Tagawa, T. (2025) · Viruses · doi:10.3390/v17071006 · Cited by 11
The splice of life: how alternative splicing shapes regulatory and phenotypic evolution
Hunter, C. E., & Xing, Y. (2026) · The EMBO Journal · doi:10.1038/s44318-025-00666-z · Cited by 9
RASA: Robust Alternative Splicing Analysis for Human Transcriptome Arrays
Seok, J., Xu, W., Davis, R. W., & Xiao, W. (2015) · Scientific Reports · doi:10.1038/srep11917 · Cited by 9
Core spliceosomal Sm proteins as constituents of cytoplasmic mRNPs in plants
Hyjek‐Składanowska, M., Bajczyk, M., Gołębiewski, M., Nuc, P., Kołowerzo‐Lubnau, A., Jarmołowski, A., & Smoliński, D. J. (2020) · The Plant Journal · doi:10.1111/tpj.14792 · Cited by 9
Compendium of Methods to Uncover RNA-Protein Interactions In Vivo
Majumder, M., & Palanisamy, V. (2021) · Methods and Protocols · doi:10.3390/mps4010022 · Cited by 9
Li, Z., Chen, Q., Wang, J., Pan, X., & Lu, W. Z. (2021) · Topics in Current Chemistry · doi:10.1007/s41061-021-00352-8 · Cited by 9
Uncovering Novel Viral Innate Immune Evasion Strategies: What Has SARS-CoV-2 Taught Us?
Tay, D. J. W., Lew, Z. Z. R., Chu, J. J. H., & Tan, K. S. (2022) · Frontiers in Microbiology · doi:10.3389/fmicb.2022.844447 · Cited by 9
Wu, X., Tan, D., Qiao, Q., Yin, W., Xu, Z., & Liu, X. (2022) · Physical Chemistry Chemical Physics · doi:10.1039/d2cp00759b · Cited by 9
Studying miRNA–mRNA Interactions: An Optimized CLIP-Protocol for Endogenous Ago2-Protein
Stebel, S. E., Breuer, J., & Roßbach, O. (2022) · Methods and Protocols · doi:10.3390/mps5060096 · Cited by 9
Sun, H., Fu, B., Qian, X., Xu, P., & Qin, W. (2024) · Nature Communications · doi:10.1038/s41467-024-44987-9 · Cited by 9
Photoactivatable mRNA 5′ Cap Analogs for RNA‐Protein Crosslinking
Warmiński, M., Grab, K., Szczepanski, K., Śpiewla, T., Zuberek, J., Kowalska, J., & Jemielity, J. (2024) · Advanced Science · doi:10.1002/advs.202400994 · Cited by 9
Emerman, A. B., & Blower, M. D. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.003718 · Cited by 9
Clip for studying protein-RNA interactions that regulate virus replication
Mugisha, C. S., Tenneti, K., & Kutluay, S. B. (2019) · Methods · doi:10.1016/j.ymeth.2019.11.011 · Cited by 9
Desideri, F., D’Ambra, E., Laneve, P., & Ballarino, M. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.1004746 · Cited by 9
The RNA interactome in the Hallmarks of Cancer
Gabryelska, M., & Conn, S. J. (2023) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1786 · Cited by 9
Isolation and analyses of axonal ribonucleoprotein complexes
Doron‐Mandel, E., Alber, S., Osés-Prieto, J. A., Medzihradszky, K. F., Burlingame, A. L., Fainzilber, M., Twiss, J. L., & Lee, S. J. (2015) · Methods in cell biology · doi:10.1016/bs.mcb.2015.06.010 · Cited by 9
Studying RNA–Protein Interactions of Pre-mRNA Complexes by Mass Spectrometry
Qamar, S., Kramer, K., & Urlaub, H. (2015) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2015.02.010 · Cited by 9
Analysis of Alternative SplicingIn Vivousing Minigenes
Tang, Y., Novoyatleva, T., Benderska, N., Kishore, S., Thanaraj, A. T., & Stamm, S. (2005) · Wiley eBooks · doi:10.1002/9783527619504.ch46 · Cited by 9
A disproportionate impact of G9a methyltransferase deficiency on the X chromosomePreprint
Szántó, A., Aguilar, R., Kesner, B., Blum, R., Wang, D., Cifuentes‐Rojas, C., Rosario, B. C. D., Kis‐Tóth, K., & Lee, J. T. (2021) · Genes & Development · doi:10.1101/gad.337592.120 · Cited by 10
RNA binding proteins in cardiovascular development and disease
Verma, S. K., & Kuyumcu‐Martinez, M. N. (2024) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2024.01.007 · Cited by 8
Global Protein–RNA Interaction Mapping at Single Nucleotide Resolution by iCLIP-Seq
Yao, C., Weng, L., & Shi, Y. (2014) · Methods in molecular biology · doi:10.1007/978-1-62703-980-2_27 · Cited by 8
Physical and Functional Interaction between 5-HT6 Receptor and Nova-1
Kim, S.-H., Seo, M., Hwang, H., Moon, D.-M., Son, G. H., Kim, K., & Rhim, H. (2019) · Experimental Neurobiology · doi:10.5607/en.2019.28.1.17 · Cited by 8
Alvarado-Hernandez, B., Ma, Y., Sharma, N. R., Majerciak, V., Lobanov, A., Cam, M., Zhu, J., & Zheng, Z.-M. (2021) · Journal of Virology · doi:10.1128/jvi.01782-21 · Cited by 8
Emerging Roles of Long Noncoding RNAs in Breast Cancer Epigenetics and Epitranscriptomics
Wanowska, E., Samorowska, K., & Szcześniak, M. W. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.922351 · Cited by 8
PIE-seq: identifying RNA-binding protein targets by dual RNA-deaminase editing and sequencing
Ruan, X., Hu, K., & Zhang, X. (2023) · Nature Communications · doi:10.1038/s41467-023-39054-8 · Cited by 8
A Method for Finding Sites of Selective Adenosine Deamination
Ohlson, J., & Öhman, M. (2007) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(07)24013-3 · Cited by 8
High-throughput sequencing methods to study neuronal RNA–protein interactions
Ule, J. (2009) · Biochemical Society Transactions · doi:10.1042/bst0371278 · Cited by 8
Self-citationMonitoring Protein-RNA Interaction Dynamics in vivo at High Temporal Resolution using χCRAC
McKellar, S. W., Ivanova, I., van Nues, R. W., Cordiner, R. A., Chauhan, M., Christopoulou, N., Worboys, W., Langford, A., Jensen, T. H., & Granneman, S. (2020) · Journal of Visualized Experiments · doi:10.3791/61027 · Cited by 8
Genome-Wide Analysis of RNA–Protein Interactions in Plasmodium falciparum Using eCLIP-Seq
Hollin, T., Abel, S., & Roch, K. G. L. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1681-9_9 · Cited by 8
Identifying Protein Interactomes of Target RNAs Using HyPR-MS
Henke, K. B., Miller, R., Knoener, R. A., Scalf, M., Spiniello, M., & Smith, L. M. (2021) · Methods in molecular biology · doi:10.1007/978-1-0716-1851-6_12 · Cited by 8
Haroon, M., Tariq, H., Afzal, R., Anas, M., Nasar, S., Kainat, N., Fiaz, S., Irfan, U., Idrees, F., & Zafar, M. M. (2023) · South African Journal of Botany · doi:10.1016/j.sajb.2023.07.002 · Cited by 8
Joining the dots – protein‐ RNA interactions mediating local mRNA translation in neurons
Gallagher, C., & Ramos, A. (2018) · FEBS Letters · doi:10.1002/1873-3468.13121 · Cited by 8
Fallon, J. R., & Taylor, A. B. (2013) · Wiley eBooks · doi:10.1002/9780470015902.a0000050.pub2 · Cited by 8
Post-transcriptional control of gene expression by β-catenin: expanding the non-canonical ARMoury
Sevim, O., Park, H., & Morgan, R. G. (2025) · Oncogene · doi:10.1038/s41388-025-03470-5 · Cited by 7
Automated Image Analysis Reveals Different Localization of Synaptic Gephyrin C4 Splice Variants
Liebsch, F., Eggersmann, F. R., Merkler, Y., Kloppenburg, P., & Schwarz, G. (2022) · eNeuro · doi:10.1523/eneuro.0102-22.2022 · Cited by 10
Metadata
- Authors
- Ule, J., Jensen, K. B., Ruggiu, M., Mele, A., Ule, A., & Darnell, R. B.
- Affiliations
- Howard Hughes Medical Institute (US)
- Howard Hughes Medical Institute, Rockefeller University, New York, NY 10021, USA.
- Corresponding author
- Ule, Jernej
- Jensen, Kirk B.
- Darnell, Robert B.
- Venue
- Science
- Published
- 2003-11-14
- Volume
- 302
- Issue
- 5648
- Pages
- 1212-1215
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2053998703
- Cited by
- 1,120
- References
- 32
- Citations by year
- 2026: 36 · 2025: 49 · 2024: 37 · 2023: 32 · 2022: 46 · 2021: 60 · 2020: 49 · 2019: 74 · 2018: 63 · 2017: 68 · 2016: 56 · 2015: 70 · 2014: 72 · 2013: 62 · 2012: 60
- FWCI
- 9.54
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- UvA-DARE (University of Amsterdam) (publishedVersion)
- Adelaide Research & Scholarship (AR&S) (University of Adelaide) (submittedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Data Archiving and Networked Services (DANS) (submittedVersion)
- Funders
- National Institutes of Health (5k01mh064753-02)
- National Institute of Mental Health (K01 MH64753)
- National Institute of Neurological Disorders and Stroke (R01NS040955, R01 NS34389, R01NS034389, NS40955)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA regulation and disease
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
- Keywords
- RNA splicing regulation, CLIP, inhibitory synapses, GABA receptors, glycine receptor, gephyrin, neogenin, motor inhibition
- MeSH terms
- Neuro-Oncological Ventral Antigen, Animals, Antigens, Neoplasm, Brain, Carrier Proteins, Exons, Introns, Membrane Proteins, Nerve Tissue Proteins, Neural Inhibition, Neurons, Precipitin Tests, RNA Precursors, RNA, Messenger, Ultraviolet Rays, RNA-Binding Proteins, Alternative Splicing, Reverse Transcriptase Polymerase Chain Reaction, 3' Untranslated Regions, Mitogen-Activated Protein Kinases, Mitogen-Activated Protein Kinase 9, Mice
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