Highly homologous eEF1A1 and eEF1A2 exhibit differential post-translationalmodification with significant enrichment around localised sites of sequence variation-Reference-Cited by-同舟云学术

Highly homologous eEF1A1 and eEF1A2 exhibit differential post-translationalmodification with significant enrichment around localised sites of sequence variation

Published:2013-11-13 Issue:1 Volume:8 Page:
ISSN:1745-6150
Container-title:Biology Direct
language:en
Short-container-title:Biol Direct

Author:

Soares Dinesh C,Abbott Catherine M

Publisher

Springer Science and Business Media LLC

Subject

Applied Mathematics,General Agricultural and Biological Sciences,General Biochemistry, Genetics and Molecular Biology,Modelling and Simulation,Ecology, Evolution, Behavior and Systematics,Immunology

Link

http://link.springer.com/content/pdf/10.1186/1745-6150-8-29.pdf

Reference33 articles.

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2. Lee S, Francoeur AM, Liu S, Wang E: Tissue-specific expression in mammalian brain, heart, and muscle of S1, a member of the elongation factor-1 alpha gene family. J Biol Chem. 1992, 267: 24064-24068.

3. Chambers DM, Peters J, Abbott CM: The lethal mutation of the mouse wasted (wst) is a deletion that abolishes expression of a tissue-specific isoform of translation elongation factor 1alpha, encoded by the Eef1a2 gene. Proc Natl Acad Sci USA. 1998, 95: 4463-4468. 10.1073/pnas.95.8.4463.

4. Kahns S, Lund A, Kristensen P, Knudsen CR, Clark BF, Cavallius J, Merrick WC: The elongation factor 1 A-2 isoform from rabbit: cloning of the cDNA and characterization of the protein. Nucleic Acids Res. 1998, 26: 1884-1890. 10.1093/nar/26.8.1884.

5. Soares DC, Barlow PN, Newbery HJ, Porteous DJ, Abbott CM: Structural models of human eEF1A1 and eEF1A2 reveal two distinct surface clusters of sequence variation and potential differences in phosphorylation. PLoS One. 2009, 4: e6315-10.1371/journal.pone.0006315.

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