The DOI matches its Crossref record; 38 of the 38 references it cites were found in a registry or an index.
RNA sequence‐ and shape‐dependent recognition by proteins in the ribonucleoprotein particle
Open accessAbstract
At all stages of its life (from transcription to translation), an RNA transcript interacts with many different RNA-binding proteins. The composition of this supramolecular assembly, known as a ribonucleoprotein particle, is diverse and highly dynamic. RNA-binding proteins control the generation, maturation and lifespan of the RNA transcript and thus regulate and influence the cellular function of the encoded gene. Here, we review our current understanding of protein-RNA recognition mediated by the two most abundant RNA-binding domains (the RNA-recognition motif and the double-stranded RNA-binding motif) plus the zinc-finger motif, the most abundant nucleic-acid-binding domain. In addition, we discuss how not only the sequence but also the shape of the RNA are recognized by these three classes of RNA-binding protein.
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“family members from fungi, protists and algae have all maintained the presumed ancestral CAC core-recognition specificity17, but differ in their preference for flanking nucleotides”
From A compendium of RNA-binding motifs for decoding gene regulation (2013) · cites this paper as [17]
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Zinc Finger-DNA Recognition: Crystal Structure of a Zif268-DNA Complex at 2.1 Å
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Recognition of Polyadenylate RNA by the Poly(A)-Binding Protein
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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
From Birth to Death: The Complex Lives of Eukaryotic mRNAs
Moore, M. J. (2005) · Science · doi:10.1126/science.1111443 · Cited by 1,035
Structure and function of KH domains
Valverde, R., Edwards, L., & Regan, L. (2008) · FEBS Journal · doi:10.1111/j.1742-4658.2008.06411.x · Cited by 508
Lambert, N. J., Robertson, A. D., Jangi, M., McGeary, S. E., Sharp, P. A., & Burge, C. B. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.04.016 · Cited by 407
Prp8 protein: At the heart of the spliceosome
Grainger, R. J. R., & Beggs, J. D. (2005) · RNA · doi:10.1261/rna.2220705 · Cited by 374
Metadata
- Authors
- Stefl, R., Skrisovska, L., & Allain, F. H. ‐.
- Affiliations
- ETH Zurich (CH)
- Venue
- The EMBO Reports
- Published
- 2005-01-01
- Volume
- 6
- Issue
- 1
- Pages
- 33-38
- ISSN
- 1469-221X (ISSN-L)
- 1469-3178
- PMC
- PMC1299235
- OpenAlex
- W2115539119
- Cited by
- 175
- References
- 38
- Citations by year
- 2026: 4 · 2025: 4 · 2024: 9 · 2023: 7 · 2022: 17 · 2021: 5 · 2020: 12 · 2019: 9 · 2018: 5 · 2017: 9 · 2016: 8 · 2015: 13 · 2014: 10 · 2013: 5 · 2012: 7
- FWCI
- 0.94
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- EMBO Reports (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA regulation and disease
- Keywords
- ribonucleoprotein particles, RNA-binding proteins, protein-RNA recognition, RNA recognition motif, zinc finger, RNA processing, RNA turnover
- MeSH terms
- Animals, Base Sequence, Humans, Nucleic Acid Conformation, Ribonucleoproteins, RNA, Substrate Specificity, Zinc Fingers
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