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Structural basis for the binding of proline-rich peptides to SH3 domains

Author
HONGTAO YU1 ; CHEN, J. K1 ; SIBO FENG1 ; DALGARNO, D. C; BRAUER, A. W; SCHREIBER, S. L1
[1] Harvard univ., dep. chemistry, Cambridge MA 02138, United States
Source

Cell (Cambridge). 1994, Vol 76, Num 5, pp 933-945 ; ref : 1 p. 1/2

CODEN
CELLB5
ISSN
0092-8674
Scientific domain
Biochemistry, molecular biology, biophysics; Cell biology, histology
Publisher
Cell Press, Cambridge, MA
Publication country
United States
Document type
Article
Language
English
Keyword (fr)
1-Phosphatidylinositol 3-kinase Analyse structurale Capacité fixation Motif structural Peptide Relation structure propriété Structure 3 dimensions Structure domaine Séquence consensus Domaine SH3 Enzyme Interaction moléculaire Transferases
Keyword (en)
1-Phosphatidylinositol 3-kinase Structural analysis Binding capacity Structural unit Peptides Property structure relationship Spatial structure Domain structure Consensus sequence SH3 Domain Enzyme Molecular interaction Transferases
Keyword (es)
1-Phosphatidylinositol 3-kinase Análisis estructural Capacidad de fijación Motivo estructural Péptido Relación estructura propiedad Estructura 3 dimensiones Estructura dominio Sequencia consensus Enzima Interacción molecular Transferases
Classification
Pascal
002 Biological and medical sciences / 002A Fundamental and applied biological sciences. Psychology / 002A03 Molecular biophysics / 002A03H Intermolecular phenomena / 002A03H01 Interactions. Associations

Discipline
Molecular biophysics
Origin
Inist-CNRS
Database
PASCAL
INIST identifier
3979678

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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