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Mammalian AMP-activated protein kinase shares structural and functional homology with the catalytic domain of yeast Snf1 protein kinase

Author
MITCHELHILL, K. I1 ; STAPLETON, D1 ; GUANG GAO; HOUSE, C1 ; MICHELL, B1 ; KATSIS, F1 ; WITTERS, L. A; KEMP, B. E1
[1] St. Vincent's inst. medical res., Fitzroy Victoria 3065, Australia
Source

The Journal of biological chemistry (Print). 1994, Vol 269, Num 4, pp 2361-2364 ; ref : 27 ref

CODEN
JBCHA3
ISSN
0021-9258
Scientific domain
Biochemistry, molecular biology, biophysics; Biotechnology
Publisher
American Society for Biochemistry and Molecular Biology, Bethesda, MD
Publication country
United States
Document type
Article
Language
English
Keyword (fr)
AMP Etude comparative Lipide Métabolisme Porc Protein kinase Sousunité catalytique Protein kinase SnF1 Artiodactyla Enzyme Mammalia Transferases Ungulata Vertebrata
Keyword (en)
AMP Comparative study Lipids Metabolism Pig Protein kinase Catalytic subunit Artiodactyla Enzyme Mammalia Transferases Ungulata Vertebrata
Keyword (es)
AMP Estudio comparativo Lípido Metabolismo Cerdo Protein kinase Subunitad catalítica Artiodactyla Enzima Mammalia Transferases Ungulata Vertebrata
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 / 002A02E03 Transferases

Discipline
Analytical, structural and metabolic biochemistry
Origin
Inist-CNRS
Database
PASCAL
INIST identifier
4008053

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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