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Association of PTP-PEST with the SH3 domain of p130cas; a novel mechanism of protein tyrosine phosphatase substrate recognition

Author
GARTON, A. J1 ; BURNHAM, M. R2 ; BOUTON, A. H2 ; TONKS, N. K1
[1] Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724-2208, United States
[2] Department of Microbiology and Cancer Center, University of Virginia, Box 441 Health Sciences Center, Charlottesville, Virginia, United States
Source

Oncogene (Basingstoke). 1997, Vol 15, Num 8, pp 877-885 ; ref : 48 ref

ISSN
0950-9232
Scientific domain
Cell biology, histology; Medical oncology; Genetics
Publisher
Nature Publishing, Basingstoke
Publication country
United Kingdom
Document type
Article
Language
English
Keyword (fr)
Activité enzymatique Interaction moléculaire Mammalia Mutation Protein-tyrosine-phosphatase Relation structure activité Site catalytique Site fixation Spécificité substrat Structure domaine Transduction signal Domaine SH3 Protéine cas Enzyme Esterases Hydrolases Phosphoric monoester hydrolases Vertebrata
Keyword (en)
Enzymatic activity Molecular interaction Mammalia Mutation Protein-tyrosine-phosphatase Structure activity relation Catalytic site Binding site Substrate specificity Domain structure Signal transduction SH3 Domain Enzyme Esterases Hydrolases Phosphoric monoester hydrolases Vertebrata
Keyword (es)
Actividad enzimática Interacción molecular Mammalia Mutación Protein-tyrosine-phosphatase Relación estructura actividad Sitio catalítico Sitio fijación Especificidad sustrato Estructura dominio Transducción señal Enzima Esterases Hydrolases Phosphoric monoester hydrolases 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 / 002A02E04 Hydrolases

Discipline
Analytical, structural and metabolic biochemistry
Origin
Inist-CNRS
Database
PASCAL
INIST identifier
2788888

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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