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Probing the role of two hydrophobic active site residues in the human dihydrofolate reductase by site-directed mutagenesis

Author
SCHWEITZER, B. I1 ; SRINIVASAN SRIMATKANDADA; GRITSMAN, H; SHERIDAN, R; RENGACHARI VENKATARAGHAVAN; BERTINO, J. R
[1] Memorial Sloan-Kettering cancer cent., New York NY 10021, United States
Source

The Journal of biological chemistry (Print). 1989, Vol 264, Num 34, pp 20786-20795 ; ref : 48 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)
Activité enzymatique Cinétique Constante dissociation Fixation ligand Homme Interaction moléculaire Mutagenèse dirigée Recombinaison Structure 3 dimensions Tetrahydrofolate dehydrogenase Vecteur
Keyword (en)
Enzymatic activity Kinetics Dissociation constant Ligand binding Human Molecular interaction Site directed mutagenesis Recombination Spatial structure Tetrahydrofolate dehydrogenase Vector
Keyword (es)
Actividad enzimática Cinética Constante disociación Fijación ligando Hombre Interacción molecular Mutagénesis dirigida Recombinación Estructura 3 dimensiones Tetrahydrofolate dehydrogenase Vector
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 / 002A02E02 Oxidoreductases

Discipline
Analytical, structural and metabolic biochemistry
Origin
Inist-CNRS
Database
PASCAL
INIST identifier
6929264

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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