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A retroviral-like metal binding motif in an aminoacyl-tRNA synthetase is important for tRNA recognition

Author
MILLER, W. T; SCHIMMEL, P
Massachusetts inst. technology, dep. biology, Cambridge MA 02139, United States
Source

Proceedings of the National Academy of Sciences of the United States of America. 1992, Vol 89, Num 6, pp 2032-2035 ; ref : 40 ref

CODEN
PNASA6
ISSN
0027-8424
Scientific domain
Multidisciplinary
Publisher
National Academy of Sciences of the United States of America, Washington, DC
Publication country
United States
Document type
Article
Language
English
Keyword (fr)
Alanyl-tRNA synthetase Escherichia coli Homologie Nucléocapside RNA transfert Reconnaissance Retroviridae Site fixation Séquence aminoacide Zinc Protéine liaison RNA Bactérie Enterobacteriaceae Enzyme Virus
Keyword (en)
Alanyl-tRNA synthetase Escherichia coli Homology Nucleocapside t-RNA Recognition Retroviridae Binding site Aminoacid sequence Zinc RNA binding protein Bacteria Enterobacteriaceae Enzyme Virus
Keyword (es)
Alanyl-tRNA synthetase Escherichia coli Homología Nucleocápside ARN transferencia Reconocimiento Retroviridae Sitio fijación Secuencia aminoácido Zinc Bacteria Enterobacteriaceae Enzima Virus
Classification
Pascal
002 Biological and medical sciences / 002A Fundamental and applied biological sciences. Psychology / 002A02 Analytical, structural and metabolic biochemistry / 002A02E Enzymes and enzyme inhibitors / 002A02E07 Ligases

Discipline
Analytical, structural and metabolic biochemistry
Origin
Inist-CNRS
Database
PASCAL
INIST identifier
5153427

Sauf mention contraire ci-dessus, le contenu de cette notice bibliographique peut être utilisé dans le cadre d’une licence CC BY 4.0 Inist-CNRS / Unless otherwise stated above, the content of this bibliographic record may be used under a CC BY 4.0 licence by Inist-CNRS / A menos que se haya señalado antes, el contenido de este registro bibliográfico puede ser utilizado al amparo de una licencia CC BY 4.0 Inist-CNRS

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