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IMP dehydrogenase : Mechanism of action and inhibition

Author
HEDSTROM, L1
[1] MS 009, Department of Biochemistry, Brandeis University, Waltham, MA 02454, United States
Issue title
Inhibition of inosine monophosphate dehydrogenase (IMPDH)
Author (monograph)
PANKIEWICZ, Krzysztof W (Editor)
Source

Current medicinal chemistry. 1999, Vol 6, Num 7, pp 545-560 ; ref : 89 ref

ISSN
0929-8673
Scientific domain
Biochemistry, molecular biology, biophysics; Pharmacology drugs
Publisher
Bentham Science, Schiphol
Publication country
Netherlands
Document type
Article
Language
English
Keyword (fr)
Acide mycophénolique Article synthèse Cinétique Etat transition IMP dehydrogenase Inhibiteur enzyme Liaison covalente Mécanisme réaction Spécificité substrat Tritrichomonas foetus Isobenzofurane dérivé Enzyme Oxidoreductases Protozoa Trichomonadida
Keyword (en)
Mycophenolic acid Review Kinetics Transition state IMP dehydrogenase Enzyme inhibitor Covalent bond Reaction mechanism Substrate specificity Tritrichomonas foetus Enzyme Oxidoreductases Protozoa Trichomonadida
Keyword (es)
Acido micofenólico Artículo síntesis Cinética Estado transitorio IMP dehydrogenase Inhibidor enzima Enlace covalente Mecanismo reacción Especificidad sustrato Tritrichomonas foetus Enzima Oxidoreductases Protozoa Trichomonadida
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
1898305

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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