The DOI matches its Crossref record; 15 of the 15 references it cites were found in a registry or an index.
RNA targets of wild-type and mutant FET family proteins
Open accessAbstract
FUS, EWSR1 and TAF15, constituting the FET protein family, are abundant, highly conserved RNA-binding proteins with important roles in oncogenesis and neuronal disease, yet their RNA targets and recognition elements are unknown. Using PAR-CLIP, we defined global RNA targets for all human FET proteins and two ALS-causing human FUS mutants. FET members showed similar binding profiles, whereas FUS mutants showed a drastically altered binding pattern, consistent with changes in subcellular localization.
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“We found only one instance in which the RNAcompete motif did not have a significant and positive AUROC to at least one corresponding in vivo data set: the RNAcompete motif for FUS produced an AUROC <0.5 when compared to in vivo crosslinking-based data for both FUS and its paralogue TAF15”
From A compendium of RNA-binding motifs for decoding gene regulation (2013) · cites this paper as [14]
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The Human Genome Browser at UCSC
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Self-citationMutations 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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A Liquid-to-Solid Phase Transition of the ALS Protein FUS Accelerated by Disease Mutation
Patel, A., Lee, H. O., Jawerth, L. M., Maharana, S., Jahnel, M., Hein, M. Y., Stoynov, S., Mahamid, J., Saha, S., Franzmann, T. M., et al. (2015) · Cell · doi:10.1016/j.cell.2015.07.047 · Cited by 2,927
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A compendium of RNA-binding motifs for decoding gene regulation
Ray, D., Kazan, H., Cook, K. B., Weirauch, M. T., Najafabadi, H. S., Li, X., Gueroussov, S., Albu, M., Zheng, H., Yang, A., et al. (2013) · Nature · doi:10.1038/nature12311 · Cited by 1,480
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Metadata
- Authors
- Hoell, J. I., Larsson, E., Runge, S., Nusbaum, J. D., Duggimpudi, S., Farazi, T. A., Hafner, M., Borkhardt, A., Sander, C., & Tuschl, T.
- Affiliations
- Howard Hughes Medical Institute (US)
- Memorial Sloan Kettering Cancer Center (US)
- Heinrich Heine University Düsseldorf (DE)
- Corresponding author
- Sander, Chris
- Tuschl, Thomas
- ORCID
- Venue
- Nature Structural & Molecular Biology
- Published
- 2011-11-13
- Volume
- 18
- Issue
- 12
- Pages
- 1428-1431
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- PMC
- PMC3230689
- OpenAlex
- W2038438413
- Cited by
- 350
- References
- 15
- Citations by year
- 2026: 9 · 2025: 10 · 2024: 17 · 2023: 18 · 2022: 21 · 2021: 29 · 2020: 26 · 2019: 16 · 2018: 22 · 2017: 22 · 2016: 32 · 2015: 29 · 2014: 29 · 2013: 30 · 2012: 39
- FWCI
- 12.84
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Structural & Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Howard Hughes Medical Institute
- National Institute of Mental Health (MH08442, R01MH080442)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Health Sciences › Medicine › Clinical Neurology › Amyotrophic Lateral Sclerosis Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Keywords
- FUS, EWSR1, TAF15, RNA-binding proteins, RNA targets, amyotrophic lateral sclerosis, FUS mutations, subcellular localization, PAR-CLIP, RNA-protein interactions
- MeSH terms
- Amyotrophic Lateral Sclerosis, Base Sequence, Binding Sites, Calmodulin-Binding Proteins, Humans, Mutation, RNA, Messenger, Sequence Alignment, RNA-Binding Proteins, Sequence Analysis, DNA, RNA-Binding Protein FUS, RNA-Binding Protein EWS, TATA-Binding Protein Associated Factors, HEK293 Cells
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