The DOI matches its Crossref record; 160 of the 163 references it cites were found in a registry or an index.
Spliceosome Structure and Function
Open accessAbstract
Pre-mRNA splicing is catalyzed by the spliceosome, a multimegadalton ribonucleoprotein (RNP) complex comprised of five snRNPs and numerous proteins. Intricate RNA-RNA and RNP networks, which serve to align the reactive groups of the pre-mRNA for catalysis, are formed and repeatedly rearranged during spliceosome assembly and catalysis. Both the conformation and composition of the spliceosome are highly dynamic, affording the splicing machinery its accuracy and flexibility, and these remarkable dynamics are largely conserved between yeast and metazoans. Because of its dynamic and complex nature, obtaining structural information about the spliceosome represents a major challenge. Electron microscopy has revealed the general morphology of several spliceosomal complexes and their snRNP subunits, and also the spatial arrangement of some of their components. X-ray and NMR studies have provided high resolution structure information about spliceosomal proteins alone or complexed with one or more binding partners. The extensive interplay of RNA and proteins in aligning the pre-mRNA's reactive groups, and the presence of both RNA and protein at the core of the splicing machinery, suggest that the spliceosome is an RNP enzyme. However, elucidation of the precise nature of the spliceosome's active site, awaits the generation of a high-resolution structure of its RNP core.
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“Alternative splicing patterns (BOX 1) are regulated by specialized pre-mRNA binding proteins that alter spliceosome assembly at specific splice sites5–8”
From The neurogenetics of alternative splicing (2016) · cites this paper as [5]
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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
Self-citationExpansion 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
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Splicing regulation: From a parts list of regulatory elements to an integrated splicing code
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Exon Recognition in Vertebrate Splicing
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3 of the 163 references couldn’t be matched to a known paper.
Research works printed but not linked: 1
- Stark H, Lührmann R 2006. Electron cryomicroscopy of spliceosomal components. Ann Rev Biophy Biomol Struct 35: 435–457 [DOI] [PubMed] [Google Scholar]
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TET dioxygenases localize at splicing speckles and promote RNA splicing
Hastert, F. D., Weber, J., Bauer, C., Zhadan, A., Singh, D. N. D., Dix, T. C., Arnold, R., Bessonov, S., Soller, M., Leonhardt, H., et al. (2025) · Nucleus · doi:10.1080/19491034.2025.2536902 · Cited by 5
“Splicing enhancer sequences within the exon (ESEs) recruit proteins of the SR protein family (among them SC35), which establish a network of protein–protein interactions between the different components of the spliceosome (Figure 2A) [77].”
Metadata
- Authors
- Will, C. L., & Luhrmann, R.
- Affiliations
- Max Planck Institute for Biophysical Chemistry (DE)
- Venue
- Cold Spring Harbor Perspectives in Biology
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2010-12-30
- Volume
- 3
- Issue
- 7
- Pages
- a003707-a003707
- ISSN
- 1943-0264 (ISSN-L)
- PMC
- PMC3119917
- OpenAlex
- W2148393113
- Cited by
- 1,829
- References
- 163
- Citations by year
- 2026: 89 · 2025: 130 · 2024: 141 · 2023: 135 · 2022: 127 · 2021: 170 · 2020: 142 · 2019: 141 · 2018: 122 · 2017: 111 · 2016: 123 · 2015: 100 · 2014: 91 · 2013: 77 · 2012: 63
- Type
- posted content
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Cold Spring Harbor Perspectives in Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Deutsche Forschungsgemeinschaft
- 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
- spliceosome, pre-mRNA splicing, small nuclear ribonucleoproteins, ribonucleoprotein complexes, spliceosome assembly, RNA-RNA interactions, spliceosome structure, active site, RNA-protein interactions
- MeSH terms
- Humans, Models, Genetic, Models, Molecular, Nucleic Acid Conformation, Protein Processing, Post-Translational, Ribonucleoproteins, RNA Precursors, RNA Splicing, Spliceosomes, Ribonucleoproteins, Small Nuclear, Protein Structure, Tertiary, Crystallography, X-Ray, Nuclear Magnetic Resonance, Biomolecular, Catalytic Domain
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