RNA targets of wild-type and mutant FET family proteins

The Human Genome Browser at UCSC

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Regulation of Translation Initiation in Eukaryotes: Mechanisms and Biological Targets

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Transcriptome-wide Identification of RNA-Binding Protein and MicroRNA Target Sites by PAR-CLIP

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Mutations in FUS, an RNA Processing Protein, Cause Familial Amyotrophic Lateral Sclerosis Type 6

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Mutations in the FUS/TLS Gene on Chromosome 16 Cause Familial Amyotrophic Lateral Sclerosis

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BioGPS: an extensible and customizable portal for querying and organizing gene annotation resources

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RNA regulons: coordination of post-transcriptional events

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RNA and Disease

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mRNA localization: Gene expression in the spatial dimension

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Pre-mRNA Processing Reaches Back toTranscription and Ahead to Translation

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RNA dysfunction and aggrephagy at the centre of an amyotrophic lateral sclerosis/frontotemporal dementia disease continuum

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Altered mRNP granule dynamics in FTLD pathogenesis

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FET family fusion oncoproteins target the SWI/SNF chromatin remodeling complex

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Synaptic FUS accumulation triggers early misregulation of synaptic RNAs in a mouse model of ALS

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Therapy development for spinal muscular atrophy: perspectives for muscular dystrophies and neurodegenerative disorders

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ALS-associated mutant FUS inhibits macroautophagy which is restored by overexpression of Rab1

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Aberrant Phase Transitions: Side Effects and Novel Therapeutic Strategies in Human Disease

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The RRM domain of human fused in sarcoma protein reveals a non-canonical nucleic acid binding site

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Mutant FUS and ELAVL4 (HuD) Aberrant Crosstalk in Amyotrophic Lateral Sclerosis

De Santis, R., Alfano, V., de Turris, V., Colantoni, A., Santini, L., Garone, M. G., Antonacci, G., Peruzzi, G., Sudria-Lopez, E., Wyler, E., et al. (2019) · Cell Reports · doi:10.1016/j.celrep.2019.05.085 · Cited by 70

FUS-NLS/Transportin 1 Complex Structure Provides Insights into the Nuclear Targeting Mechanism of FUS and the Implications in ALS

Niu, C., Zhang, J. Y., Gao, F., Yang, L., Jia, M., Zhu, H., & Gong, W. (2012) · PLoS ONE · doi:10.1371/journal.pone.0047056 · Cited by 66

FUS Recognizes G Quadruplex Structures Within Neuronal mRNAs

Imperatore, J. A., McAninch, D. S., Valdez‐Sinon, A. N., Bassell, G. J., & Mihailescu, M. (2020) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2020.00006 · Cited by 66

Amyotrophic Lateral Sclerosis: New Insights into Underlying Molecular Mechanisms and Opportunities for Therapeutic Intervention

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RNA-binding protein hnRNPLL regulates mRNA splicing and stability during B-cell to plasma-cell differentiation

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TDP43 and RNA instability in amyotrophic lateral sclerosis

Weskamp, K., & Barmada, S. J. (2018) · Brain Research · doi:10.1016/j.brainres.2018.01.015 · Cited by 68

FUS-related proteinopathies: Lessons from animal models

Lanson, N. A., & Pandey, U. B. (2012) · Brain Research · doi:10.1016/j.brainres.2012.01.039 · Cited by 66

Cytoplasmic sequestration of FUS/TLS associated with ALS alters histone marks through loss of nuclear protein arginine methyltransferase 1

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Entorhinal cortical neurons are the primary targets of FUS mislocalization and ubiquitin aggregation in FUS transgenic rats

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Dual film-like organelles enable spatial separation of orthogonal eukaryotic translation

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Toward a Genome-Wide Landscape of Translational ControlPreprint

Larsson, O. S., Tian, B., & Sonenberg, N. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a012302 · Cited by 67

Synaptic dysfunction in ALS and FTD: anatomical and molecular changes provide insights into mechanisms of disease

Gelon, P. A., Dutchak, P. A., & Sephton, C. F. (2022) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2022.1000183 · Cited by 64

Optimization of PAR-CLIP for transcriptome-wide identification of binding sites of RNA-binding proteins

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Protein Quality Control and the Amyotrophic Lateral Sclerosis/Frontotemporal Dementia Continuum

Shahheydari, H., Ragagnin, A., Walker, A. K., Toth, R. P., Vidal, M., Jagaraj, C. J., Perri, E. R., Konopka, A., Sultana, J. M., & Atkin, J. D. (2017) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2017.00119 · Cited by 61

AnnoLnc: a web server for systematically annotating novel human lncRNAs

Hou, M. L., Tang, X., Tian, F., Shi, F., Liu, F., & Gao, G. (2016) · BMC Genomics · doi:10.1186/s12864-016-3287-9 · Cited by 58

TAF15 is important for cellular proliferation and regulates the expression of a subset of cell cycle genes through miRNAs

Ballarino, M., Jobert, L., Dembélé, D., de la Grange, P., Auboeuf, D., & Tora, L. (2012) · Oncogene · doi:10.1038/onc.2012.490 · Cited by 58

RNA‐binding proteins implicated in neurodegenerative diseases

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Topography of FUS pathology distinguishes late-onset BIBD from aFTLD-U

Lee, E. B., Russ, J., Jung, H., Elman, L. B., Chahine, L. M., Kremens, D. E., Miller, B. L., Coslett, H. B., Trojanowski, J. Q., Deerlin, V. M. V., et al. (2013) · Acta Neuropathologica Communications · doi:10.1186/2051-5960-1-9 · Cited by 58

RNA-Binding Proteins in Acute Leukemias

Schuschel, K., Helwig, M., Hüttelmaier, S., Heckl, D., Klusmann, J., & Hoell, J. I. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21103409 · Cited by 57

Disorder-mediated interactions target proteins to specific condensates

Cruz, N. D. L., Pradhan, P., Veettil, R. T., Conti, B. A., Oppikofer, M., & Sabari, B. R. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.08.017 · Cited by 58

Identification of the RNA recognition element of the RBPMS family of RNA-binding proteins and their transcriptome-wide mRNA targets

Farazi, T. A., Leonhardt, C.-S., Mukherjee, N., Mihailovic, A., Li, S., Max, K. E. A., Meyer, C., Yamaji, M., Čekan, P., Jacobs, N. C., et al. (2014) · RNA · doi:10.1261/rna.045005.114 · Cited by 54

Regulation of FAS Exon Definition and Apoptosis by the Ewing Sarcoma Protein

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Role of RNA Binding Proteins with prion-like domains in muscle and neuromuscular diseases

Picchiarelli, G., & Dupuis, L. (2020) · Cell Stress · doi:10.15698/cst2020.04.217 · Cited by 57

FUS is sequestered in nuclear aggregates in ALS patient fibroblasts

Schwartz, J. C., Podell, E. R., Han, S. S. W., Berry, J. D., Eggan, K. C., & Cech, T. R. (2014) · Molecular Biology of the Cell · doi:10.1091/mbc.e14-05-1007 · Cited by 54

Interaction of amyotrophic lateral sclerosis/frontotemporal lobar degeneration–associated fused-in-sarcoma with proteins involved in metabolic and protein degradation pathways

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Network Analyses Reveal Novel Aspects of ALS Pathogenesis

Sanhueza, M., Chai, A., Smith, C., McCray, B. A., Simpson, T. I., Taylor, J. P., & Pennetta, G. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1005107 · Cited by 53

A loss of FUS/TLS function leads to impaired cellular proliferation

Ward, C. L., Boggio, K. J., Johnson, B. N., Boyd, J. D., Douthwright, S., Shaffer, S. A., Landers, J. E., Glicksman, M. A., & Bosco, D. A. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.508 · Cited by 52

Old versus New Mechanisms in the Pathogenesis of ALS

Rossi, S., Cozzolino, M., & Carrı̀, M. T. (2016) · Brain Pathology · doi:10.1111/bpa.12355 · Cited by 55

RNA-binding proteins in ALS and FTD: from pathogenic mechanisms to therapeutic insights

Rummens, J., & Cruz, S. D. (2025) · Molecular Neurodegeneration · doi:10.1186/s13024-025-00851-y · Cited by 62

Highly accessible AU-rich regions in 3’ untranslated regions are hotspots for binding of regulatory factors

Plass, M., Rasmussen, S. H., & Krogh, A. (2017) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1005460 · Cited by 55

FUS-mediated alternative splicing in the nervous system: consequences for ALS and FTLD

Orozco, D., & Edbauer, D. (2013) · Journal of Molecular Medicine · doi:10.1007/s00109-013-1077-2 · Cited by 52

Multidimensional Super-Resolution Microscopy Unveils Nanoscale Surface Aggregates in the Aging of FUS Condensates

He, C., Wu, C. Y., Li, W., & Xu, K. (2023) · Journal of the American Chemical Society · doi:10.1021/jacs.3c08674 · Cited by 45

RNA‐binding proteins involved in RNA localization and their implications in neuronal diseases

Tolino, M., Köhrmann, M., & Kiebler, M. A. (2012) · European Journal of Neuroscience · doi:10.1111/j.1460-9568.2012.08160.x · Cited by 51

The prionlike domain of FUS is multiphosphorylated following DNA damage without altering nuclear localization

Rhoads, S. N., Monahan, Z. T., Yee, D. S., Leung, A. Y., Newcombe, C. G., O’Meally, R. N., Cole, R. N., & Shewmaker, F. P. (2018) · Molecular Biology of the Cell · doi:10.1091/mbc.e17-12-0735 · Cited by 51

Domains involved in TAF15 subcellular localisation: Dependence on cell type and ongoing transcription

Marko, M., Vlassis, A., Guialis, A., & Leichter, M. (2012) · Gene · doi:10.1016/j.gene.2012.06.088 · Cited by 48

Gene Expression Responses to FUS, EWS, and TAF15 Reduction and Stress Granule Sequestration Analyses Identifies FET-Protein Non-Redundant Functions

Blechingberg, J., Luo, Y., Bolund, L., Damgaard, C. K., & Nielsen, A. L. (2012) · PLoS ONE · doi:10.1371/journal.pone.0046251 · Cited by 48

FUS/TLS contributes to replication-dependent histone gene expression by interaction with U7 snRNPs and histone-specific transcription factors

Raczyńska, K. D., Ruepp, M., Brzęk, A., Reber, S., Romeo, V., Rindlisbacher, B., Heller, M., Szweykowska-Kulińska, Z., Jarmołowski, A., & Schümperli, D. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv794 · Cited by 47

RNA-Protein Binding Sites Prediction via Multi Scale Convolutional Gated Recurrent Unit Networks

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FUS contributes to mTOR-dependent inhibition of translation

Sévigny, M., Bourdeau‐Julien, I., Venkatasubramani, J. P., Hui, J. B., Dutchak, P. A., & Sephton, C. F. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.013801 · Cited by 49

Translation dysregulation in neurodegenerative diseases: a focus on ALS

Wang, S., & Sun, S. (2023) · Molecular Neurodegeneration · doi:10.1186/s13024-023-00642-3 · Cited by 47

Identification of In Vivo, Conserved, TAF15 RNA Binding Sites Reveals the Impact of TAF15 on the Neuronal Transcriptome

Ibrahim, F., Maragkakis, M., Alexiou, P., Maronski, M., Dichter, M. A., & Mourelatos, Z. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.01.021 · Cited by 47

A Regulatory Circuitry Between Gria2, miR-409, and miR-495 Is Affected by ALS FUS Mutation in ESC-Derived Motor Neurons

Capauto, D., Colantoni, A., Lü, L., Santini, T., Peruzzi, G., Biscarini, S., Morlando, M., Shneider, N. A., Caffarelli, E., Laneve, P., et al. (2018) · Molecular Neurobiology · doi:10.1007/s12035-018-0884-4 · Cited by 46

microCLIP super learning framework uncovers functional transcriptome-wide miRNA interactions

Paraskevopoulou, M. D., Karagkouni, D., Vlachos, I. S., Tastsoglou, S., & Hatzigeorgiou, A. G. (2018) · Nature Communications · doi:10.1038/s41467-018-06046-y · Cited by 46

Prionoid Proteins in the Pathogenesis of Neurodegenerative Diseases

Wells, C., Brennan, S. E., Keon, M., & Saksena, N. (2019) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2019.00271 · Cited by 46

The Skeletal Muscle Emerges as a New Disease Target in Amyotrophic Lateral Sclerosis

Pikatza‐Menoio, O., Elicegui, A., Bengoetxea, X., Naldaiz‐Gastesi, N., de Munaín, A. L., Gereñu, G., Gil-Bea, F. J., & Alonso‐Martín, S. (2021) · Journal of Personalized Medicine · doi:10.3390/jpm11070671 · Cited by 50

fus/TLS orchestrates splicing of developmental regulators during gastrulationPreprint

Dichmann, D. S., & Harland, R. M. (2012) · Genes & Development · doi:10.1101/gad.187278.112 · Cited by 45

A conserved N‐terminal motif is required for complex formation between FUS, EWSR1, TAF15 and their oncogenic fusion proteins

Thomsen, C., Grundevik, P., Elias, P., Ståhlberg, A., & Åman, P. (2013) · The FASEB Journal · doi:10.1096/fj.13-234435 · Cited by 45

RNA Binding Proteins and the Pathogenesis of Frontotemporal Lobar Degeneration

Hofmann, J. W., Seeley, W. W., & Huang, E. J. (2018) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathmechdis-012418-012955 · Cited by 50

RPI-MDLStack: Predicting RNA–protein interactions through deep learning with stacking strategy and LASSO

Yu, B., Wang, X., Zhang, Y., Gao, H., Wang, Y., Liu, Y., & Gao, X. (2022) · Applied Soft Computing · doi:10.1016/j.asoc.2022.108676 · Cited by 43

Dysregulation of chromatin remodelling complexes in amyotrophic lateral sclerosis

Tibshirani, M., Zhao, B., Gentil, B. J., Minotti, S., Marques, C., Keith, J., Rogaeva, E., Zinman, L., Rouaux, C., Robertson, J., et al. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx301 · Cited by 42

Post-Translational Modifications Modulate Proteinopathies of TDP-43, FUS and hnRNP-A/B in Amyotrophic Lateral Sclerosis

Farina, S., Esposito, F., Battistoni, M., Biamonti, G., & Francia, S. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.693325 · Cited by 46

LncRNA INHEG promotes glioma stem cell maintenance and tumorigenicity through regulating rRNA 2’-O-methylation

Liu, L., Liu, Z., Liu, Q., Wu, W., Lin, P., Liu, X., Zhang, Y., Wang, D., Prager, B. C., Gimple, R. C., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-43113-5 · Cited by 45

Neuro‐Cells therapy improves motor outcomes and suppresses inflammation during experimental syndrome of amyotrophic lateral sclerosis in mice

de Munter, J., Shafarevich, I., Люндуп, А. В., Pavlov, D., Wolters, E. C., Вячеславовна, Г. А., Veniaminova, E. A., Umriukhin, A., Kalueff, A. V., Svistunov, A. A., et al. (2019) · CNS Neuroscience & Therapeutics · doi:10.1111/cns.13280 · Cited by 42

Therapeutic Potential of Polyphenols in Amyotrophic Lateral Sclerosis and Frontotemporal Dementia

Novak, V., Rogelj, B., & Župunski, V. (2021) · Antioxidants · doi:10.3390/antiox10081328 · Cited by 42

Ewing sarcoma from molecular biology to the clinic

Dupuy, M., Lamoureux, F., Mullard, M., Postec, A., Regnier, L., Baud’huin, M., Georges, S., Royer, B. B.-L., Ory, B., Rédiní, F., et al. (2023) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2023.1248753 · Cited by 44

Single-cell RNA-sequencing reveals early mitochondrial dysfunction unique to motor neurons shared across FUS- and TARDBP-ALS

Schweingruber, C., Nijssen, J., Mechtersheimer, J., Reber, S., Lebœuf, M., O’Brien, N. L., Mei, I., Hedges, E. C., Keuper, M., Benitez, J. A., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-59679-1 · Cited by 43

FUS ‐mediated regulation of alternative RNA processing in neurons: insights from global transcriptome analysis

Masuda, A., Takeda, J., & Ohno, K. (2016) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1338 · Cited by 42

FUS-regulated RNA metabolism and DNA damage repair

Zhou, Y., Liu, S., Öztürk, A., & Hicks, G. G. (2014) · Rare Diseases · doi:10.4161/rdis.29515 · Cited by 50

ALS mutations in TLS/FUS disrupt target gene expressionPreprint

Coady, T. H., & Manley, J. L. (2015) · Genes & Development · doi:10.1101/gad.267286.115 · Cited by 41

Neuronal RNA ‐binding proteins in health and disease

Lenzken, S. C., Achsel, T., Carrì, M. T., & Barabino, S. M. L. (2014) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1231 · Cited by 40

Long noncoding RNAs in TDP-43 and FUS/TLS-related frontotemporal lobar degeneration (FTLD)

Lourenco, G. F., Janitz, M., Huang, Y. M., & Halliday, G. M. (2015) · Neurobiology of Disease · doi:10.1016/j.nbd.2015.07.011 · Cited by 42

Crowd Control: Effects of Physical Crowding on Cargo Movement in Healthy and Diseased Neurons

Sabharwal, V., & Koushika, S. P. (2019) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2019.00470 · Cited by 35

Transcriptome-wide identification of RNA binding sites by CLIP-seq

Murigneux, V., Saulière, J., Crollius, H. R., & Hir, H. L. (2013) · Methods · doi:10.1016/j.ymeth.2013.03.022 · Cited by 39

Muscleblind acts as a modifier of FUS toxicity by modulating stress granule dynamics and SMN localization

Casci, I., Krishnamurthy, K., Kour, S., Tripathy, V., Ramesh, N., Anderson, E. N., Marrone, L., Grant, R. A., Oliver, S. L., Gochenaur, L., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-13383-z · Cited by 34

The intriguing case of motor neuron disease: ALS and SMA come closer

Achsel, T., Barabino, S. M. L., Cozzolino, M., & Carrì, M. T. (2013) · Biochemical Society Transactions · doi:10.1042/bst20130142 · Cited by 33

TDP-43 high throughput screening analyses in neurodegeneration: Advantages and pitfalls

Buratti, E., Romano, M., & Baralle, F. E. (2013) · Molecular and Cellular Neuroscience · doi:10.1016/j.mcn.2013.03.001 · Cited by 32

How do the RNA-binding proteins TDP-43 and FUS relate to amyotrophic lateral sclerosis and frontotemporal degeneration, and to each other?

Baloh, R. H. (2012) · Current Opinion in Neurology · doi:10.1097/wco.0b013e32835a269b · Cited by 33

Intrinsic Regulatory Role of RNA Structural Arrangement in Alternative Splicing Control

Taylor, K., & Sobczak, K. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21145161 · Cited by 32

RNA-binding proteins of COSMIC importance in cancer

Choi, P. S., & Thomas‐Tikhonenko, A. (2021) · Journal of Clinical Investigation · doi:10.1172/jci151627 · Cited by 32

RNA Deregulation in Amyotrophic Lateral Sclerosis: The Noncoding Perspective

Laneve, P., Tollis, P., & Caffarelli, E. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221910285 · Cited by 32

RNA-Binding Proteins in Amyotrophic Lateral Sclerosis and Neurodegeneration

Ugras, S. E., & Shorter, J. (2012) · Neurology Research International · doi:10.1155/2012/432780 · Cited by 32

A working model for condensate RNA-binding proteins as matchmakers for protein complex assembly

Chen, X., & Mayr, C. (2021) · RNA · doi:10.1261/rna.078995.121 · Cited by 29

A Model-Based Approach to Identify Binding Sites in CLIP-Seq Data

Wang, T., Chen, B., Kim, M., Xie, Y., & Xiao, G. (2014) · PLoS ONE · doi:10.1371/journal.pone.0093248 · Cited by 27

The potential of engineered eukaryotic RNA‐binding proteins as molecular tools and therapeutics

Shotwell, C. R., Cleary, J. D., & Berglund, J. A. (2019) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1573 · Cited by 25

EWS and FUS bind a subset of transcribed genes encoding proteins enriched in RNA regulatory functions

Luo, Y., Blechingberg, J., Fernandes, A. M., Li, S., Fryland, T., Børglum, A. D., Bolund, L., & Nielsen, A. L. (2015) · BMC Genomics · doi:10.1186/s12864-015-2125-9 · Cited by 31

RNA regulons and the RNA-protein interaction network

Imig, J., Kanitz, A., & Gerber, A. P. (2012) · BioMolecular Concepts · doi:10.1515/bmc-2012-0016 · Cited by 28

RNA quality control and protein aggregates in amyotrophic lateral sclerosis: A review

Verma, A. K., & Tandan, R. (2012) · Muscle & Nerve · doi:10.1002/mus.23673 · Cited by 27

NEAT1 lncRNA and amyotrophic lateral sclerosis

Nishimoto, Y., Nakagawa, S., & Okano, H. (2021) · Neurochemistry International · doi:10.1016/j.neuint.2021.105175 · Cited by 28

The RNA binding protein EWS is broadly involved in the regulation of pri-miRNA processing in mammalian cells

Ouyang, H., Zhang, K., Fox-Walsh, K. L., Yang, Y., Zhang, C., Huang, J. S., Li, H., Zhou, Y., & Fu, X. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx912 · Cited by 27

A deep boosting based approach for capturing the sequence binding preferences of RNA-binding proteins from high-throughput CLIP-seq data

Li, S., Dong, F., Wu, Y., Zhang, S., Zhang, C., Liu, X., Jiang, T., & Zeng, J. (2017) · Nucleic Acids Research · doi:10.1093/nar/gkx492 · Cited by 25

A network of RNA and protein interactions in Fronto Temporal Dementia

Fontana, F., Siva, K., & Denti, M. A. (2015) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2015.00009 · Cited by 30

SeAMotE: a method for high-throughput motif discovery in nucleic acid sequences

Agostini, F., Cirillo, D., Ponti, R. D., & Tartaglia, G. G. (2014) · BMC Genomics · doi:10.1186/1471-2164-15-925 · Cited by 25

Characterization of FUS Mutations in Amyotrophic Lateral Sclerosis Using RNA-Seq

van Blitterswijk, M., Wang, E. T., Friedman, B. A., Keagle, P. J., Lowe, P., LeClerc, A. L., van den Berg, L. H., Housman, D. E., Veldink, J. H., & Landers, J. E. (2013) · PLoS ONE · doi:10.1371/journal.pone.0060788 · Cited by 26

FUS (fused in sarcoma) is a component of the cellular response to topoisomerase I–induced DNA breakage and transcriptional stress

Martínez-Macías, M. I., Moore, D. A. Q., Green, R. L., Gómez-Herreros, F., Naumann, M., Hermann, A., Damme, P. V., Hafezparast, M., & Caldecott, K. W. (2019) · Life Science Alliance · doi:10.26508/lsa.201800222 · Cited by 28

Dysregulated axonal RNA translation in amyotrophic lateral sclerosis

Yasuda, K., & Mili, S. (2016) · Wiley Interdisciplinary Reviews - RNA · doi:10.1002/wrna.1352 · Cited by 27

High-affinity RNA targets of the Survival Motor Neuron protein reveal diverse preferences for sequence and structural motifs

Ottesen, E. W., Singh, N. N., Luo, D., & Singh, R. N. (2018) · Nucleic Acids Research · doi:10.1093/nar/gky770 · Cited by 26

ZNF384-Related Fusion Genes in Acute Lymphoblastic Leukemia

Zhu, L., Bai, W., Cheng, Q., & Fang, J. (2023) · Cancer Control · doi:10.1177/10732748231182787 · Cited by 24

Conditional depletion of Fus in oligodendrocytes leads to motor hyperactivity and increased myelin deposition associated with Akt and cholesterol activation

Guzman, K., Brink, L. E., Bey, G. R., Bodnar, R. J., Kuang, L., Xing, B., Sullivan, M. L. G., Park, H. J., Koppes, E., Zhu, H., et al. (2020) · Glia · doi:10.1002/glia.23825 · Cited by 23

Characterization of genetic loss-of-function of Fus in zebrafish

Lebedeva, S., Domingues, A. M. D. J., Butter, F., & Ketting, R. F. (2016) · RNA Biology · doi:10.1080/15476286.2016.1256532 · Cited by 24

SWI/SNF-type complexes–transcription factor interplay: a key regulatory interaction

Maassen, A., Steciuk, J., Wilga, M., Szurmak, J., Garbicz, D., Sarnowska, E. A., & Sarnowski, T. J. (2025) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-025-00704-y · Cited by 23

The binding specificity of Translocated in LipoSarcoma/FUsed in Sarcoma with lncRNA transcribed from the promoter region of cyclin D1

Yoneda, R., Suzuki, S., Mashima, T., Kondo, K., Nagata, T., Katahira, M., & Kurokawa, R. (2016) · Cell & Bioscience · doi:10.1186/s13578-016-0068-8 · Cited by 23

Quantitative proteomics identifies proteins that resist translational repression and become dysregulated in ALS-FUS

Baron, D. M., Matheny, T., Lin, Y., Leszyk, J., Kenna, K. P., Gall, K. V., Santos, D. P., Tischbein, M., Funes, S., Hayward, L. J., et al. (2019) · Human Molecular Genetics · doi:10.1093/hmg/ddz048 · Cited by 22

Functional characterization of the FET family of RNA-binding proteins

Baethge, K. (2014) · doi:10.18452/16996

FET proteins in frontotemporal dementia and amyotrophic lateral sclerosis

Mackenzie, I. R., & Neumann, M. (2011) · Brain Research · doi:10.1016/j.brainres.2011.12.010 · Cited by 96

Biochemical Properties and Biological Functions of FET Proteins

Schwartz, J. C., Cech, T. R., & Parker, R. (2014) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060614-034325 · Cited by 236

FUS and TAF15 safeguard the critical functions of the ribonucleoprotein network formed by EWSR1 and newly synthesized RNAPreprint

Rajan, S. S., Khan, I., Jones, T., Brownmiller, T., Ebegboni, V. J., Lim, L., Tran, A. D., Kruhlak, M. J., & Caplen, N. J. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.03.24.713985

RNA metabolism in neurological disease

Gao, F., & Taylor, J. P. (2014) · Brain Research · doi:10.1016/j.brainres.2014.09.011 · Cited by 7