A human tRNA synthetase is a potent PARP1-activating effector target for resveratrol

Mathew Sajish; Paul Schimmel

doi:10.1038/nature14028

A human tRNA synthetase is a potent PARP1-activating effector target for resveratrol

Nature ◽

10.1038/nature14028 ◽

2014 ◽

Vol 519 (7543) ◽

pp. 370-373 ◽

Cited By ~ 78

Author(s):

Mathew Sajish ◽

Paul Schimmel

Keyword(s):

Trna Synthetase ◽

Effector Target

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Faculty Opinions recommendation of A human tRNA synthetase is a potent PARP1-activating effector target for resveratrol.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.725287901.793504146 ◽

2015 ◽

Author(s):

Richard J Maraia

Keyword(s):

Trna Synthetase ◽

Effector Target

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Orphan designation: 505 amino acid protein, corresponding to amino acids 2-506 of the wild-type human histidyl-tRNA synthetase, Treatment of limb-girdle muscular dystrophy

Case Medical Research ◽

10.31525/cmr-2935ce2 ◽

2020 ◽

Author(s):

Keyword(s):

Amino Acids ◽

Amino Acid ◽

Muscular Dystrophy ◽

Trna Synthetase ◽

Limb Girdle Muscular Dystrophy ◽

Wild Type ◽

Orphan Designation ◽

Acid Protein ◽

Amino Acid Protein

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Faculty Opinions recommendation of An aminoacyl tRNA synthetase whose sequence fits into neither of the two known classes.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1000088.1101 ◽

2001 ◽

Author(s):

Anne-Catherine Dock-Bregeon

Keyword(s):

Trna Synthetase ◽

Aminoacyl Trna Synthetase

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Faculty Opinions recommendation of A conserved threonine within Escherichia coli leucyl-tRNA synthetase prevents hydrolytic editing of leucyl-tRNALeu.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1000366.1351 ◽

2001 ◽

Author(s):

Anne-Catherine Dock-Bregeon

Keyword(s):

Escherichia Coli ◽

Trna Synthetase

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Faculty Opinions recommendation of Discrimination of tRNA(Leu) isoacceptors by the mutants of Escherichia coli leucyl-tRNA synthetase in editing.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1009103.118807 ◽

2002 ◽

Author(s):

Anne-Catherine Dock-Bregeon

Keyword(s):

Escherichia Coli ◽

Trna Synthetase

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Faculty Opinions recommendation of Crystal structure of a human aminoacyl-tRNA synthetase cytokine.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1010763.176313 ◽

2002 ◽

Author(s):

John Perona

Keyword(s):

Crystal Structure ◽

Trna Synthetase ◽

Aminoacyl Trna Synthetase

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Faculty Opinions recommendation of An active dominant mutation of glycyl-tRNA synthetase causes neuropathy in a Charcot-Marie-Tooth 2D mouse model.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1047563.497530 ◽

2006 ◽

Cited By ~ 1

Author(s):

Brian Popko

Keyword(s):

Mouse Model ◽

Trna Synthetase ◽

Dominant Mutation ◽

Charcot Marie Tooth

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Faculty Opinions recommendation of Pyrrolysyl-tRNA synthetase-tRNA(Pyl) structure reveals the molecular basis of orthogonality.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1159143.619443 ◽

2009 ◽

Author(s):

Pascale Legault

Keyword(s):

Molecular Basis ◽

Trna Synthetase

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Faculty Opinions recommendation of Exome sequencing identifies mitochondrial alanyl-tRNA synthetase mutations in infantile mitochondrial cardiomyopathy.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.12193961.13360056 ◽

2011 ◽

Author(s):

Nereo Bresolin ◽

Dario Ronchi

Keyword(s):

Exome Sequencing ◽

Trna Synthetase ◽

Mitochondrial Cardiomyopathy

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Faculty Opinions recommendation of A major determinant for binding and aminoacylation of tRNA(Ala) in cytoplasmic Alanyl-tRNA synthetase is mutated in dominant axonal Charcot-Marie-Tooth disease.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.3016965.2696063 ◽

2010 ◽

Author(s):

Robert Burgess

Keyword(s):

Trna Synthetase ◽

Major Determinant ◽

Charcot Marie Tooth ◽

Charcot Marie Tooth Disease ◽

Tooth Disease

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