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tyrosinyl-5'-AMP
Known as:
(S)-5'-adenylic acid, mono(2-amino-3-(4-hydroxyphenyl)propyl) ester
, adenylyl-tyrosine
, tyrosyl adenylate
National Institutes of Health
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Related topics
Related topics
3 relations
Broader (2)
Adenosine Monophosphate
Tyrosine
analogs & derivatives
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2014
Highly Cited
2014
Human Tyr-tRNA synthetase is a potent PARP-1 activating effector target for resveratrol
M. Sajish
,
P. Schimmel
Nature
2014
Corpus ID: 4449316
Resveratrol is reported to extend lifespan and provide cardio-neuro-protective, anti-diabetic, and anti-cancer effects by…
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Highly Cited
1988
Highly Cited
1988
Reconstruction by site-directed mutagenesis of the transition state for the activation of tyrosine by the tyrosyl-tRNA synthetase: a mobile loop envelopes the transition state in an induced-fit…
A. Fersht
,
J. Knill-Jones
,
H. Bedouelle
,
G. Winter
Biochemistry
1988
Corpus ID: 10973494
Site-directed mutagenesis of the tyrosyl-tRNA synthetase followed by kinetic studies has shown that residues which are distant…
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Highly Cited
1987
Highly Cited
1987
Structure-activity relationships in engineered proteins: analysis of use of binding energy by linear free energy relationships.
A. Fersht
,
R. Leatherbarrow
,
T. Wells
Biochemistry
1987
Corpus ID: 46419383
The activity of mutant enzymes can be analyzed quantitatively by structure-activity relationships in a manner analogous to Br…
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Highly Cited
1986
Highly Cited
1986
A model of synthetase/transfer RNA interaction as deduced by protein engineering
H. Bedouelle
,
G. Winter
Nature
1986
Corpus ID: 4307998
The recognition of transfer-RNA by their cognate aminoacyl-tRNA synthetases is the crucial step in the translation of the genetic…
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1986
1986
Internal thermodynamics of position 51 mutants and natural variants of tyrosyl-tRNA synthetase.
C. Ho
,
A. Fersht
Biochemistry
1986
Corpus ID: 24361944
Natural variation and evolution impose structural changes on an enzyme that can affect the energetics of catalysis. The energy…
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Highly Cited
1985
Highly Cited
1985
Transition-state stabilization in the mechanism of tyrosyl-tRNA synthetase revealed by protein engineering.
R. Leatherbarrow
,
A. Fersht
,
G. Winter
Proceedings of the National Academy of Sciences…
1985
Corpus ID: 57274
The principal catalytic factor in the activation of tyrosine by the tyrosyl-tRNA synthetase is found to be improved binding of…
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Highly Cited
1982
Highly Cited
1982
Tyrosyl-tRNA synthetase forms a mononucleotide-binding fold.
T. Bhat
,
D. Blow
,
P. Brick
,
J. Nyborg
Journal of Molecular Biology
1982
Corpus ID: 28562081
Highly Cited
1975
Highly Cited
1975
Demonstration of two reaction pathways for the aminoacylation of tRNA. Application of the pulsed quenched flow technique.
A. Fersht
,
R. Jakes
Biochemistry
1975
Corpus ID: 15199983
A rapid mixing and quenching device is described which operates efficiently in the range of 150 msec to several minutes as well…
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Highly Cited
1975
Highly Cited
1975
Tyrosyl-tRNA synthetase from Escherichia coli. Stoichiometry of ligand binding and half-of-the-sites reactivity in aminoacylation.
R. Jakes
,
A. Fersht
Biochemistry
1975
Corpus ID: 8891614
The tyrosyl-tRNA synthetase from Escherichia coli binds only 1 mol of tRNA, tyrosine, and tyrosyl adenylate per mol of enzyme…
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Highly Cited
1975
Highly Cited
1975
Ligand binding and enzymic catalysis coupled through subunits in tyrosyl-tRNA synthetase.
A. Fersht
,
R. S. Mulvey
,
G. Koch
Biochemistry
1975
Corpus ID: 19268533
The interaction of the tyrosyl-tRNA synthetase from Bacillus stearothermophilus with its substrates in the aminoacyl adenylation…
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