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Glutamate-tRNA Ligase
Known as:
Glu tRNA Ligase
, Ligase, Glu-tRNA
, Glutamyl T RNA Synthetase
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An enzyme that activates glutamic acid with its specific transfer RNA. EC 6.1.1.17.
National Institutes of Health
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Related topics
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9 relations
Narrower (1)
AT5G26710 protein, Arabidopsis
EPRS gene
In Blood
Process of secretion
antagonists & inhibitors
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Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2013
Highly Cited
2013
Molecular mechanism of bacterial persistence by HipA.
Elsa Germain
,
Daniel Castro-Roa
,
N. Zenkin
,
K. Gerdes
Molecular cell
2013
Corpus ID: 206988107
Highly Cited
2009
Highly Cited
2009
Dynamical networks in tRNA:protein complexes
A. Sethi
,
J. Eargle
,
Alexis A Black
,
Z. Luthey-Schulten
Proceedings of the National Academy of Sciences
2009
Corpus ID: 13542355
Community network analysis derived from molecular dynamics simulations is used to identify and compare the signaling pathways in…
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Highly Cited
2007
Highly Cited
2007
Identification and fine mapping of a thermo-sensitive chlorophyll deficient mutant in rice (Oryza sativa L.)
Wenzhen Liu
,
Ya-ping Fu
,
+4 authors
Zong-xiu Sun
Planta
2007
Corpus ID: 23362588
A thermo-sensitive chlorophyll deficient mutant was isolated from more than 15,000 transgenic rice lines. The mutant displayed…
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Highly Cited
2003
Highly Cited
2003
ATP binding by glutamyl‐tRNA synthetase is switched to the productive mode by tRNA binding
S. Sekine
,
O. Nureki
,
+5 authors
S. Yokoyama
The EMBO journal
2003
Corpus ID: 26105058
Aminoacyl‐tRNA synthetases catalyze the formation of an aminoacyl‐AMP from an amino acid and ATP, prior to the aminoacyl transfer…
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Highly Cited
1998
Highly Cited
1998
Modular evolution of the Glx-tRNA synthetase family--rooting of the evolutionary tree between the bacteria and archaea/eukarya branches.
M. Siatecka
,
M. Rożek
,
J. Barciszewski
,
M. Mirande
European journal of biochemistry
1998
Corpus ID: 24722318
The accuracy of protein biosynthesis generally rests on a family of 20 aminoacyl-tRNA synthetases, one for each amino acid. In…
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Highly Cited
1998
Highly Cited
1998
Glutamyl-tRNA(Gln) amidotransferase in Deinococcus radiodurans may be confined to asparagine biosynthesis.
A. Curnow
,
D. Tumbula
,
J. Pelaschier
,
B. Min
,
D. Söll
Proceedings of the National Academy of Sciences…
1998
Corpus ID: 19579918
Asparaginyl-tRNA (Asn-tRNA) and glutaminyl-tRNA (Gln-tRNA) are essential components of protein synthesis. They can be formed by…
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Highly Cited
1996
Highly Cited
1996
The yeast protein Arc1p binds to tRNA and functions as a cofactor for the methionyl‐ and glutamyl‐tRNA synthetases.
G. Simos
,
A. Segref
,
+4 authors
E. Hurt
The EMBO journal
1996
Corpus ID: 37852796
Arc1p was found in a screen for components that interact genetically with Los1p, a nuclear pore‐associated yeast protein involved…
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Highly Cited
1995
Highly Cited
1995
Architectures of class-defining and specific domains of glutamyl-tRNA synthetase.
O. Nureki
,
D. Vassylyev
,
+6 authors
K. Morikawa
Science
1995
Corpus ID: 45584811
The crystal structure of a class I aminoacyl-transfer RNA synthetase, glutamyl-tRNA synthetase (GluRS) from Thermus thermophilus…
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Highly Cited
1993
Highly Cited
1993
A 2-thiouridine derivative in tRNAGlu is a positive determinant for aminoacylation by Escherichia coli glutamyl-tRNA synthetase.
L. A. Sylvers
,
K. Rogers
,
M. Shimizu
,
E. Ohtsuka
,
D. Söll
Biochemistry
1993
Corpus ID: 41713893
Early investigations into the interaction between Escherichia coli glutamyl-tRNA synthetase (GluRS) and tRNAGlu have implicated…
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Highly Cited
1986
Highly Cited
1986
A single glutamyl-tRNA synthetase aminoacylates tRNAGlu and tRNAGln in Bacillus subtilis and efficiently misacylates Escherichia coli tRNAGln1 in vitro
J. Lapointe
,
L. Duplain
,
M. Proulx
Journal of bacteriology
1986
Corpus ID: 12653606
In the presence or absence of its regulatory factor, the monomeric glutamyl-tRNA synthetase from Bacillus subtilis can…
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