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Histidine-tRNA Ligase
Known as:
Jo 1 Antigen
, Histidyl tRNA Synthetase
, Ligase, His-tRNA
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An enzyme that activates histidine with its specific transfer RNA. EC 6.1.1.21.
National Institutes of Health
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Related topics
Related topics
8 relations
HARS 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
2010
Highly Cited
2010
Interference with histidyl-tRNA synthetase by a CRISPR spacer sequence as a factor in the evolution of Pelobacter carbinolicus
Muktak Aklujkar
,
D. Lovley
BMC Evolutionary Biology
2010
Corpus ID: 1210139
BackgroundPelobacter carbinolicus, a bacterium of the family Geobacteraceae, cannot reduce Fe(III) directly or produce…
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Highly Cited
2000
Highly Cited
2000
A mammalian homologue of GCN2 protein kinase important for translational control by phosphorylation of eukaryotic initiation factor-2alpha.
R. Sood
,
A. Porter
,
D. Olsen
,
D. Cavener
,
R. Wek
Genetics
2000
Corpus ID: 31524438
A family of protein kinases regulates translation in response to different cellular stresses by phosphorylation of the alpha…
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Highly Cited
1997
Highly Cited
1997
Crystal structure analysis of the activation of histidine by Thermus thermophilus histidyl-tRNA synthetase.
A. Åberg
,
A. Yaremchuk
,
M. Tukalo
,
B. Rasmussen
,
S. Cusack
Biochemistry
1997
Corpus ID: 21990513
The crystal structure at 2.7 A resolution of histidyl-tRNA synthetase (HisRS) from Thermus thermophilus in complex with its amino…
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Highly Cited
1997
Highly Cited
1997
The first step of aminoacylation at the atomic level in histidyl-tRNA synthetase.
J. Arnez
,
J. Augustine
,
D. Moras
,
C. Francklyn
Proceedings of the National Academy of Sciences…
1997
Corpus ID: 42666731
The crystal structure of an enzyme-substrate complex with histidyl-tRNA synthetase from Escherichia coli, ATP, and the amino acid…
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Highly Cited
1994
Highly Cited
1994
A motif in human histidyl-tRNA synthetase which is shared among several aminoacyl-tRNA synthetases is a coiled-coil that is essential for enzymatic activity and contains the major autoantigenic…
N. Raben
,
R. Nichols
,
+5 authors
P. Plotz
Journal of Biological Chemistry
1994
Corpus ID: 31431133
Highly Cited
1994
Highly Cited
1994
A broadened spectrum of juvenile myositis. Myositis-specific autoantibodies in children.
L. Rider
,
F. Miller
,
+6 authors
P. Plotz
Arthritis & Rheumatism
1994
Corpus ID: 35153695
OBJECTIVE Myositis-specific autoantibodies (MSA) define relatively homogeneous clinical and immunogenetic patient groups in…
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Highly Cited
1992
Highly Cited
1992
Mutations activating the yeast eIF-2 alpha kinase GCN2: isolation of alleles altering the domain related to histidyl-tRNA synthetases
M. Ramírez
,
R. Wek
,
C R Vazquez de Aldana
,
B. M. Jackson
,
B. Freeman
,
A. Hinnebusch
Molecular and Cellular Biology
1992
Corpus ID: 25839350
The protein kinase GCN2 stimulates expression of the yeast transcriptional activator GCN4 at the translational level by…
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Highly Cited
1972
Highly Cited
1972
[Mutant tRNA His ineffective in repression and lacking two pseudouridine modifications].
C. Singer
,
C. Singer
,
C. Singer
,
Gerald R. Smith
,
R. Cortese
,
B. Ames
Nature: New biology
1972
Corpus ID: 28246669
TRANSFER RNA has been implicated in the regulation of a number of amino-acid biosynthetic operons1–4. Histidyl-tRNAHis has been…
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Highly Cited
1966
Highly Cited
1966
Histidine regulatory mutants in Salmonella typhimurium. I. Isolation and general properties.
J. Roth
,
D. N. Antón
,
P. Hartman
Journal of Molecular Biology
1966
Corpus ID: 27835024
Highly Cited
1966
Highly Cited
1966
Histidine regulatory mutants in Salmonella typhimurium II. Histidine regulatory mutants having altered histidyl-tRNA synthetase.
J. Roth
,
B. Ames
Journal of Molecular Biology
1966
Corpus ID: 25157428
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