The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
Functional diversity of the hnRNPs: past, present and perspectives
Abstract
The hnRNPs (heterogeneous nuclear ribonucleoproteins) are RNA-binding proteins with important roles in multiple aspects of nucleic acid metabolism, including the packaging of nascent transcripts, alternative splicing and translational regulation. Although they share some general characteristics, they vary greatly in terms of their domain composition and functional properties. Although the traditional grouping of the hnRNPs as a collection of proteins provided a practical framework, which has guided much of the research on them, this approach is becoming increasingly incompatible with current knowledge about their structural and functional divergence. Hence, we review the current literature to examine hnRNP diversity, and discuss how this impacts upon approaches to the classification of RNA-binding proteins in general.
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Cites
The multifunctional RNA-binding protein hnRNP A1 is required for processing of miR-18a
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Auto- and Cross-Regulation of the hnRNP L Proteins by Alternative Splicing
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Cited by
Splicing mutations in human genetic disorders: Examples, detection, and confirmation
Anna, A., & Monika, G. (2018) · Journal of Applied Genetics · doi:10.1007/s13353-018-0444-7 · Cited by 657
Huelga, S. C., Vu, A. Q., Arnold, J. D., Liang, T. Y., Liu, P. P., Yan, B. Y., Donohue, J. P., Shiue, L., Hoon, S., Brenner, S., et al. (2012) · Cell Reports · doi:10.1016/j.celrep.2012.02.001 · Cited by 470
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Zhang, W., Zeng, F., Liu, Y., Zhao, Y., Lv, H., Niu, L., Teng, M., & Li, X. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.463901 · Cited by 40
Metadata
- Authors
- Han, S. P., Tang, Y. H., & Smith, R.
- Venue
- Biochemical Journal
- Publisher
- Portland Press Ltd.
- Published
- 2010-08-27
- Volume
- 430
- Issue
- 3
- Pages
- 379-392
- ISSN
- 0264-6021 (ISSN-L)
- 1470-8728
- OpenAlex
- W1992274603
- Cited by
- 527
- References
- 6
- FWCI
- 12.88
- Type
- journal article
- Language
- en
- Open access
- closed
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