Cargando…
The zinc-binding domain of mammalian prolyl-tRNA synthetase is indispensable for catalytic activity and organism viability
Aminoacyl-tRNA synthetases (AARS) participate in decoding the genome by catalyzing conjugation of amino acids to their cognate tRNAs. During evolution, biochemical and environmental conditions markedly influenced the sequence and structure of the 20 AARSs, revealing adaptations dictating canonical a...
Autores principales: | Vasu, Kommireddy, Ramachandiran, Iyappan, Terenzi, Fulvia, Khan, Debjit, China, Arnab, Khan, Krishnendu, Chechi, Aayushi, Baleanu-Gogonea, Camelia, Gogonea, Valentin, Fox, Paul L. |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Elsevier
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7960942/ https://www.ncbi.nlm.nih.gov/pubmed/33748704 http://dx.doi.org/10.1016/j.isci.2021.102215 |
Ejemplares similares
-
3-Dimensional architecture of the human multi-tRNA synthetase complex
por: Khan, Krishnendu, et al.
Publicado: (2020) -
Translational control of murine adiponectin expression by an upstream open reading frame element
por: Vasu, Kommireddy, et al.
Publicado: (2023) -
An optimized protocol for in vitro and in cellulo structural determination of the multi-tRNA synthetase complex by cross-linking mass spectrometry
por: Khan, Krishnendu, et al.
Publicado: (2022) -
Multimodal cotranslational interactions direct assembly of the human multi-tRNA synthetase complex
por: Khan, Krishnendu, et al.
Publicado: (2022) -
Aminoacyl-tRNA synthetases of the multi-tRNA synthetase complex and their role in tumorigenesis
por: Khan, Krishnendu, et al.
Publicado: (2022)