The DOI matches its Crossref record; 42 of the 42 references it cites were found in a registry or an index.
eEF1A: Thinking Outside the Ribosome
Open accessAbstract
Eukaryotic translation elongation factor 1A (eEF1A) is one of the most abundant protein synthesis factors. eEF1A is responsible for the delivery of all aminoacyl-tRNAs to the ribosome, aside from initiator and selenocysteine tRNAs. In addition to its roles in polypeptide chain elongation, unique cellular and viral activities have been attributed to eEF1A in eukaryotes from yeast to plants and mammals. From preliminary, speculative associations to well characterized biochemical and biological interactions, it is clear that eEF1A, of all the translation factors, has been ascribed the most functions outside of protein synthesis. A mechanistic understanding of these non-canonical functions of eEF1A will shed light on many important biological questions, including viral-host interaction, subcellular organization, and the integration of key cellular pathways.
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Cites
Global landscape of protein complexes in the yeast Saccharomyces cerevisiae
Krogan, N. J., Cagney, G., Yu, H., Zhong, G., Guo, X., Ignatchenko, A., Li, J., Pu, S., Datta, N., Tikuisis, A. P., et al. (2006) · Nature · doi:10.1038/nature04670 · Cited by 2,952
Translational control of gene expression
Sonenberg, N., Hershey, J. W. B., & Mathews, M. B. (2000) · Cold Spring Harbor Laboratory eBooks · Cited by 1,379
mRNA localization: Gene expression in the spatial dimension
Martin, K. C., & Ephrussi, A. (2009) · Cell · doi:10.1016/j.cell.2009.01.044 · Cited by 1,048
The Crystal Structure of the Ribosome Bound to EF-Tu and Aminoacyl-tRNA
Schmeing, T. M., Voorhees, R. M., Kelley, A. C., Gao, Y.-G., Murphy, F. V., Weir, J. R., & Ramakrishnan, V. (2009) · Science · doi:10.1126/science.1179700 · Cited by 546
Identification of an actin-binding protein from Dictyostelium as elongation factor 1a
Yang, F., Demma, M., Warren, V., Dharmawardhane, S., & Condeelis, J. (1990) · Nature · doi:10.1038/347494a0 · Cited by 345
Gross, S. R., & Kinzy, T. G. (2005) · Nature Structural & Molecular Biology · doi:10.1038/nsmb979 · Cited by 269
Self-citationMicrotubule Severing by Elongation Factor 1α
Shiina, N., Gotoh, Y., Kubomura, N., Iwamatsu, A., & Nishida, E. (1994) · Science · doi:10.1126/science.7939665 · Cited by 251
Bohnsack, M. T., Regener, K., Schwappach, B., Saffrich, R., Paraskeva, E., Hartmann, E., & Görlich, D. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf613 · Cited by 243
Exportin-5-mediated nuclear export of eukaryotic elongation factor 1A and tRNA
Calado, A., Treichel, N., Müller, E.-C., Otto, A., & Kutay, U. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf620 · Cited by 205
Emerging role for the cytoskeleton as an organizer and regulator of translation
Kim, S., & Coulombe, P. A. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2818 · Cited by 198
Cited by
Plant Translation Factors and Virus Resistance
Sanfaçon, H. (2015) · Viruses · doi:10.3390/v7072778 · Cited by 272
Elongation factor Tu is a multifunctional and processed moonlighting protein
Widjaja, M., Harvey, K. L., Hagemann, L., Berry, I. J., Jarocki, V. M., Raymond, B. B. A., Tacchi, J. L., Gründel, A., Steele, J. R., Padula, M. P., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-10644-z · Cited by 131
Metadata
- Authors
- Mateyak, M. K., & Kinzy, T. G.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2010-07
- Volume
- 285
- Issue
- 28
- Pages
- 21209-21213
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2039869230
- Cited by
- 273
- References
- 42
- FWCI
- 7.68
- Type
- journal article
- Language
- en
- Open access
- hybrid
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
