Abstract: Disclosed herein are methods and compositions for inhibiting neddylation using Glycyl-tRNA synthase (GlyRS) inhibitors. Also disclosed are related compositions and methods for treating diseases such as cancer.

Abstract: Disclosed herein are methods and compositions for modulating angiogenesis, and reducing tumor progression by regulating phoosprylation, of seryl-tRNA synthase (SerRS). Also disclosed are related compositions and methods for treating diseases such as cancer.

Abstract: Methods, compositions and kits for detecting mutated aminoacyl tRNA synthetase (aaRS) in biological samples from a subject suspect of having or suffering from a Charcot-Marie-Tooth (CMT) disease or a CMT-related disease are disclosed herein. In some embodiments, the methods include determining the amount of mutated aaRS bound to Neuropilin 1 (Nrp1). In some embodiments, methods include detection of endogenous vascular endothelial growth factor (VEGF) bound to Nrp1. Also disclosed are methods, compositions and kits for the diagnosis of a CMT or a CMT-related disease through the detection of VEGF and/or mutated aaRS in a subject.

Abstract: Provided are compositions and methods for the treatment of mutant glycyl-tRNA synthetase (GlyRS)-associated diseases, such as Charcot-Marie-Tooth (CMT) diseases, and related compositions and methods for diagnostic, drug discovery, and research applications. Also provided are mutant glycyl-tRNA synthetases and uses thereof.

Abstract: Isolated monomeric aminoacyl-tRNA synthetase polypeptides and polynucleotides having non-canonical biological activities are provided, as well as compositions and methods related thereto.

Abstract: Isolated monomelic aminoacyl-tRNA synthetase polypeptides and polynucleotides having non-canonical biological activities are provided, as well as compositions and methods related thereto.

Abstract: Provided are histidyl-tRNA synthetase variant polypeptides, X-ray crystallographic and NMR spectroscopy structures of HRS polypeptides, and related compositions and methods for therapy and drug discovery.

Abstract: The present invention provides an isolated tyrosyl tRNA synthetase (TyrRS) polypeptide variant which comprises (a) a Rossmann fold region or a portion thereof, preferably including an ?5 coil; and (b) an anticodon recognition domain or portion thereof, preferably including an ?14 coil. Preferably, the ?5 coil and the ?14 coil have a greater spatial separation in the tertiary structure of the variant compared to the corresponding spatial separation in native human TyrRS. The variant preferably comprises an amino acid residue sequence identity of at least about 50% compared to the amino acid residue sequence of human TyrRS (SEQ ID NO: 3), includes at least one non-conservative amino acid residue substitution relative to the amino acid residue sequence of human TyrRS, and preferably presents an exposed ELR motif in the ?5 coil on an external portion of the tertiary structure of the polypeptide. A preferred TyrRS protein variant comprises the amino acid residue sequence of SEQ ID NO: 4 or a portion thereof.

Abstract: Isolated monomelic aminoacyl-tRNA synthetase polypeptides and polynucleotides having non-canonical biological activities are provided, as well as compositions and methods related thereto.

Abstract: The present invention provides an isolated tyrosyl tRNA synthetase (TyrRS) polypeptide variant which comprises (a) a Rossmann fold region or a portion thereof, preferably including an ?5 coil; and (b) an anticodon recognition domain or portion thereof, preferably including an ?14 coil. Preferably, the ?5 coil and the ?14 coil have a greater spatial separation in the tertiary structure of the variant compared to the corresponding spatial separation in native human TyrRS. The variant preferably comprises an amino acid residue sequence identity of at least about 50% compared to the amino acid residue sequence of human TyrRS (SEQ ID NO: 3), includes at least one non-conservative amino acid residue substitution relative to the amino acid residue sequence of human TyrRS, and preferably presents an exposed ELR motif in the ?5 coil on an external portion of the tertiary structure of the polypeptide. A preferred TyrRS protein variant comprises the amino acid residue sequence of SEQ ID NO: 4 or a portion thereof.

Abstract: The present invention provides an isolated tyrosyl tRNA synthetase (TyrRS) polypeptide variant which comprises (a) a Rossmann fold region or a portion thereof, preferably including an 5 coil; and (b) an anticodon recognition domain or portion thereof, preferably including an 14 coil. Preferably, the 5 coil and the 14 coil have a greater spatial separation in the tertiary structure of the variant compared to the corresponding spatial separation in native human TyrRS. The variant preferably comprises an amino acid residue sequence identity of at least about 50% compared to the amino acid residue sequence of human TyrRS (SEQ ID NO: 3), includes at least one non-conservative amino acid residue sequence of human TyrRS, and preferably presents an exposed ELR motif in the 5 coil on an external portion of the tertiary structure of the polypeptide. A preferred TyrRS protein variant comprises the amino acid residue sequence of SEQ ID NO: 4 or a portion thereof.

Abstract: The present invention provides an isolated tyrosyl tRNA synthetase (TyrRS) polypeptide variant which comprises (a) a Rossmann fold region or a portion thereof, preferably including an 5 coil; and (b) an anticodon recognition domain or portion thereof, preferably including an 14 coil. Preferably, the 5 coil and the 14 coil have a greater spatial separation in the tertiary structure of the variant compared to the corresponding spatial separation in native human TyrRS. The variant preferably comprises an amino acid residue sequence identity of at least about 50% compared to the amino acid residue sequence of human TyrRS (SEQ ID NO: 3), includes at least one non-conservative amino acid residue sequence of human TyrRS, and preferably presents an exposed ELR motif in the 5 coil on an external portion of the tertiary structure of the polypeptide. A preferred TyrRS protein variant comprises the amino acid residue sequence of SEQ ID NO: 4 or a portion thereof.