Synthesis of myristoyl CoA analogues and myristoyl peptides as inhibitors of myristoyl CoA:protein N-myristoyltransferase
- Author
- GUO-QIANG ZHENG1 ; XIUFENG HU1 ; PAIGE, L. A1 ; GEAHLEN, R. L; CASSADY, J. M
[1] Ohio State univ., coll. pharmacy, div. medicinal chemistry pharmacognosy, Columbus OH 43210, United States - Source
Journal of pharmaceutical sciences. 1994, Vol 83, Num 2, pp 233-238
- CODEN
- JPMSAE
- ISSN
- 0022-3549
- Scientific domain
- Pharmacology drugs
- Publisher
- American Pharmaceutical Association, Washington, DC
/
Wiley, Hoboken, NJ
- Publication country
- United States
- Document type
- Article
- Language
- English
- Keyword (fr)
- Activité enzymatique Analogue Antiviral Histidine N-acetyltransferase In vitro Inhibiteur enzyme Peptide Relation structure activité Structure moléculaire Synthèse Myristoyl CoA Acyltransferases Enzyme Transferases
- Keyword (en)
- Enzymatic activity Analog Antiviral Histidine N-acetyltransferase In vitro Enzyme inhibitor Peptides Structure activity relation Molecular structure Synthesis Acyltransferases Enzyme Transferases
- Keyword (es)
- Actividad enzimática Análogo Antiviral Histidine N-acetyltransferase In vitro Inhibidor enzima Péptido Relación estructura actividad Estructura molecular Síntesis Acyltransferases Enzima Transferases
- Classification
- Pascal
- 002 Biological and medical sciences / 002B Medical sciences / 002B02 Pharmacology. Drug treatments / 002B02S Antibiotics. Antiinfectious agents. Antiparasitic agents / 002B02S05 Antiviral agents
- Discipline
- Pharmacological treatments
- Origin
- Inist-CNRS
- Database
- PASCAL
- INIST identifier
- 3927721
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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DOI
10.1002/jps.2600830224 
https://dx.doi.org/10.1002/jps.2600830224
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