An Archaeal Protein with Homology to the Eukaryotic Translation Initiation Factor 5A Shows Ribonucleolytic Activity
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference58 articles.
1. Eukaryotic Ribonuclease P: A Plurality of Ribonucleoprotein Enzymes
2. Assigning a function to a conserved group of proteins: the tRNA 3'-processing enzymes
3. RNomics in Archaea reveals a further link between splicing of archaeal introns and rRNA processing
4. The Exosome: A Conserved Eukaryotic RNA Processing Complex Containing Multiple 3′→5′ Exoribonucleases
5. Protein Complexes in the Archaeon Methanothermobacter thermautotrophicus Analyzed by Blue Native/SDS-PAGE and Mass Spectrometry
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1. Crystal structure of archaeal IF5A-DHS complex reveals insights into the hypusination mechanism;Structure;2024-07
2. Structural–Functional Relationship of the Ribonucleolytic Activity of aIF5A from Sulfolobus solfataricus;Biomolecules;2022-10-06
3. Ribosome profiling in archaea reveals leaderless translation, novel translational initiation sites, and ribosome pausing at single codon resolution;Nucleic Acids Research;2020-05-08
4. Ribosome Profiling in Archaea Reveals Leaderless Translation, Novel Translational Initiation Sites, and Ribosome Pausing at Single Codon Resolution;2020-02-04
5. Indications for a moonlighting function of translation factor aIF5A in the crenarchaeum Sulfolobus solfataricus;RNA Biology;2019-03-05
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