ArticleActa crystallographica. Section F, Structural biology and crystallization communications2012
Purification, crystallization and preliminary X-ray crystallographic analysis of mammalian translation elongation factor eEF1A2.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Dynamics and structural features of the eEF1A1 and eEF1A2 paralogs.Nucleic acids research · 2025Article
- Assay for ribosome stimulation of angiogenin nuclease activity.Methods in enzymology · 2025Article
- The eEF1 family of mammalian translation elongation factors.BBA advances · 2023Article
- Oxazole-Benzenesulfonamide Derivatives Inhibit HIV-1 Reverse Transcriptase Interaction with Cellular eEF1A and Reduce Viral Replication.Journal of virology · 2019Article
- Translation Elongation Factor eEF1A2 is a Novel Anticancer Target for the Marine Natural Product Plitidepsin.Scientific reports · 2016Article
- The eEF1A Proteins: At the Crossroads of Oncogenesis, Apoptosis, and Viral Infections.Frontiers in oncology · 2015Review
- Mammalian translation elongation factor eEF1A2: X-ray structure and new features of GDP/GTP exchange mechanism in higher eukaryotes.Nucleic acids research · 2014Article
Corrections and comments
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Authors and funding
7 authors.
Funding
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Abstract
Translation elongation factor eEF1A2 was purified to homogeneity from rabbit muscle by two consecutive ion-exchange column-chromatography steps and this mammalian eEF1A2 was successfully crystallized for the first time. Protein crystals obtained using ammonium sulfate as precipitant diffracted to 2.5 Å resolution and belonged to space group P6(1)22 or P6(3)22 (unit-cell parameters a = b = 135.4, c = 304.6 Å). A complete native data set was collected to 2.7 Å resolution.
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