Glutaminyl-tRNA synthetase as a component of the high-molecular weight complex of human aminoacyl-tRNA synthetases. An immunological study
Author:
Publisher
Elsevier BV
Subject
Genetics,Biochemistry,Biophysics,Structural Biology
Reference21 articles.
1. AMINOACYL tRNA SYNTHETASES: GENERAL SCHEME OF STRUCTURE-FUNCTION RELATIONSHIPS IN THE POLYPEPTIDES AND RECOGNITION OF TRANSFER RNAS
2. A model for the structural organization of aminoacyl-tRNA synthetases in mammalian cells
3. Multienzyme complex of aminoacyl-tRNA synthetases: an essence of being eukaryotic
4. Macromolecular complexes from sheep and rabbit containing seven aminoacyl-tRNA synthetases. III. Assignment of aminoacyl-tRNA synthetase activities to the polypeptide components of the complexes.
5. Valyl-tRNA synthetase from rabbit liver
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1. Glutaminyl-tRNA and Asparaginyl-tRNA Biosynthetic Pathways;Comprehensive Natural Products II;2010
2. Review;Biological Chemistry;1997
3. The Human EPRS Locus (Formerly the QARS Locus): A Gene Encoding a Class I and a Class II Aminoacyl-tRNA Synthetase;Genomics;1994-01
4. Reaction of anti-OJ autoantibodies with components of the multi-enzyme complex of aminoacyl-tRNA synthetases in addition to isoleucyl-tRNA synthetase.;Journal of Clinical Investigation;1993-06-01
5. Mammalian prolyl-tRNA synthetase corresponds to the ≈ 150 kDa subunit of the high-Mr aminoacyl-tRNA synthetase complex;Biochimie;1992-02
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