Double-sieving-defective aminoacyl-tRNA synthetase causes protein mistranslation and affects cellular physiology and development
J Lu, M Bergert, A Walther, B Suter - Nature communications, 2014 - nature.com
Aminoacyl-tRNA synthetases (aaRSs) constitute a family of ubiquitously expressed essential
enzymes that ligate amino acids to their cognate tRNAs for protein synthesis. Recently …
enzymes that ligate amino acids to their cognate tRNAs for protein synthesis. Recently …
Eukaryotic cytosolic and mitochondrial phenylalanyl-tRNA synthetases catalyze the charging of tRNA with the meta-tyrosine
L Klipcan, N Moor, N Kessler… - Proceedings of the …, 2009 - National Acad Sciences
The accumulation of proteins damaged by reactive oxygen species (ROS), conventionally
regarded as having pathological potentials, is associated with age-related diseases such as …
regarded as having pathological potentials, is associated with age-related diseases such as …
Structure of human cytosolic phenylalanyl-tRNA synthetase: evidence for kingdom-specific design of the active sites and tRNA binding patterns
I Finarov, N Moor, N Kessler, L Klipcan, MG Safro - Structure, 2010 - cell.com
The existence of three types of phenylalanyl-tRNA synthetase (PheRS), bacterial (αβ) 2,
eukaryotic/archaeal cytosolic (αβ) 2, and mitochondrial α, is a prominent example of …
eukaryotic/archaeal cytosolic (αβ) 2, and mitochondrial α, is a prominent example of …
A translation-independent function of PheRS activates growth and proliferation in Drosophila
MT Ho, J Lu, D Brunßen… - Disease Models & …, 2021 - journals.biologists.com
Aminoacyl transfer RNA (tRNA) synthetases (aaRSs) not only load the appropriate amino
acid onto their cognate tRNAs, but many of them also perform additional functions that are …
acid onto their cognate tRNAs, but many of them also perform additional functions that are …
Bacterial and eukaryotic phenylalanyl-tRNA synthetases catalyze misaminoacylation of tRNAPhe with 3, 4-dihydroxy-L-phenylalanine
N Moor, L Klipcan, MG Safro - Chemistry & Biology, 2011 - cell.com
Aminoacyl-tRNA synthetases exert control over the accuracy of translation by selective
pairing the correct amino acids with their cognate tRNAs, and proofreading the misacylated …
pairing the correct amino acids with their cognate tRNAs, and proofreading the misacylated …
[HTML][HTML] Large-scale movement of functional domains facilitates aminoacylation by human mitochondrial phenylalanyl-tRNA synthetase
SS Yadavalli, L Klipcan, A Zozulya, R Banerjee… - FEBS letters, 2009 - Elsevier
Structural studies suggest rearrangement of the RNA-binding and catalytic domains of
human mitochondrial PheRS (mtPheRS) is required for aminoacylation. Crosslinking the …
human mitochondrial PheRS (mtPheRS) is required for aminoacylation. Crosslinking the …
Recombinant expression and purification of phenylalanyl-tRNA synthetase from wheat: a long-lasting poly (U)-dependent poly (Phe) synthesis system
H Furukawa, Y Nagashio, K Tsutsumi… - Preparative …, 2024 - Taylor & Francis
Synthetic genes for the two subunits of phenylalanyl-tRNA synthetase (PheRS) from wheat
were expressed in Escherichia coli. When each gene was induced individually, the α …
were expressed in Escherichia coli. When each gene was induced individually, the α …
Prokaryotic and Eukaryotic Tetrameric Phenylalanyl-tRNA Synthetases Display Conservation of the Binding Mode of the tRNAPhe CCA End
N Moor, O Lavrik, A Favre, M Safro - Biochemistry, 2003 - ACS Publications
The interaction of human phenylalanyl-tRNA synthetase, a eukaryotic prototype with an
unknown three-dimensional structure, with the tRNAPhe acceptor end was studied by s4U …
unknown three-dimensional structure, with the tRNAPhe acceptor end was studied by s4U …
Structural aspects of phenylalanylation and quality control in three major forms of phenylalanyl‐tRNA synthetase
L Klipcan, I Finarov, N Moor, MG Safro - Journal of amino acids, 2010 - Wiley Online Library
Aminoacyl‐tRNA synthetases (aaRSs) are a canonical set of enzymes that specifically
attach corresponding amino acids to their cognate transfer RNAs in the cytoplasm …
attach corresponding amino acids to their cognate transfer RNAs in the cytoplasm …
Phenylalanine-tRNA aminoacylation is compromised by ALS/FTD-associated C9orf72 C4G2 repeat RNA
M Malnar Črnigoj, U Čerček, X Yin, MT Ho… - Nature …, 2023 - nature.com
The expanded hexanucleotide GGGGCC repeat mutation in the C9orf72 gene is the main
genetic cause of amyotrophic lateral sclerosis and frontotemporal dementia. Under one …
genetic cause of amyotrophic lateral sclerosis and frontotemporal dementia. Under one …