Articles with "arginylation" as a keyword



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tRNAArg-Derived Fragments Can Serve as Arginine Donors for Protein Arginylation.

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Published in 2020 at "Cell chemical biology"

DOI: 10.1016/j.chembiol.2020.05.013

Abstract: Arginyltransferase ATE1 mediates posttranslational arginylation and plays key roles in multiple physiological processes. ATE1 utilizes arginyl (Arg)-tRNAArg as the donor of Arg, putting this reaction into a direct competition with the protein synthesis machinery. Here,… read more here.

Keywords: trnaarg derived; trnaarg; arginylation; fragments serve ... See more keywords
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Arginylation Regulates Cytoskeleton Organization and Cell Division and Affects Mitochondria in Fission Yeast

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Published in 2022 at "Molecular and Cellular Biology"

DOI: 10.1128/mcb.00261-22

Abstract: Protein arginylation mediated by arginyltransferase Ate1 is a posttranslational modification of emerging importance implicated in the regulation of mammalian embryogenesis, the cardiovascular system, tissue morphogenesis, cell migration, neurodegeneration, cancer, and aging. Ate1 deletion results in… read more here.

Keywords: cell division; arginylation; yeast; fission yeast ... See more keywords
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α-Synuclein arginylation in the human brain

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Published in 2022 at "Translational Neurodegeneration"

DOI: 10.1186/s40035-022-00295-0

Abstract: Background Alpha-synuclein (α-syn) exhibits pathological misfolding in many human neurodegenerative disorders. We previously showed that α-syn is arginylated in the mouse brain and that lack of arginylation leads to neurodegeneration in mice. Methods Here, we… read more here.

Keywords: synuclein arginylation; pathology; arginylation; human brain ... See more keywords

Functional Interplay between Arginyl-tRNA Synthetases and Arginyltransferase

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Published in 2022 at "International Journal of Molecular Sciences"

DOI: 10.3390/ijms231710160

Abstract: Protein arginylation, mediated by arginyltransferase ATE1, is a posttranslational modification of emerging biological importance that consists of transfer of the amino acid Arg to protein and peptide substrates. ATE1 utilizes charged tRNAArg as the donor… read more here.

Keywords: arginyl trna; trna synthetases; arginylation; functional interplay ... See more keywords