Literature DB >> 12033399

Multienzyme complexes of eukaryotic aminoacyl-tRNA synthetases.

C V Dang1, C V Dang1.   

Abstract

Eukaryotic aminoacyl-tRNA synthetases, unlike their prokaryotic counterparts, may occur as high-Mr multienzyme complexes. Recently, successful purification of synthetase complexes makes possible the elucidation of the structural organization of these high-Mr complexes. Although their physiological significance remains unknown, recent studies suggest some possible functional roles for these complexes.

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Year:  1983        PMID: 12033399     DOI: 10.1007/bf01120696

Source DB:  PubMed          Journal:  Biosci Rep        ISSN: 0144-8463            Impact factor:   3.840


  6 in total

1.  Comparison of the thermolability and hydrophobic properties of high- and low-molecular-weight forms of rabbit liver arginyl-tRNA synthetase.

Authors:  H Berbeć; A Paszkowska
Journal:  Mol Cell Biochem       Date:  1989-04-11       Impact factor: 3.396

Review 2.  Higher eukaryotic aminoacyl-tRNA synthetases in physiologic and pathologic states.

Authors:  C V Dang; C V Dang
Journal:  Mol Cell Biochem       Date:  1986-08       Impact factor: 3.396

Review 3.  Multienzyme complex of aminoacyl-tRNA synthetases: an essence of being eukaryotic.

Authors:  C V Dang; C V Dang
Journal:  Biochem J       Date:  1986-10-15       Impact factor: 3.857

4.  Structural organization of high-Mr mammalian aminoacyl-tRNA synthetases. Comparison of multi-enzyme complexes from different sources.

Authors:  C V Dang; C V Dang
Journal:  Mol Cell Biochem       Date:  1984-09       Impact factor: 3.396

5.  Demonstration of an altered phenylalanyl-tRNA synthetase in an analogue-resistant mutant of Aspergillus nidulans.

Authors:  B N Tiwary; P S Bisen; U Sinha
Journal:  Mol Gen Genet       Date:  1987-08

6.  The eucaryotic aminoacyl-tRNA synthetase complex: suggestions for its structure and function.

Authors:  M P Deutscher
Journal:  J Cell Biol       Date:  1984-08       Impact factor: 10.539

  6 in total

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