Crystal structure of protein farnesyltransferase at 2.25 Angstrom resolution
- Author
- PARK, H.-W1 ; BODULURI, S. R1 ; MOOMAW, J. F2 ; CASEY, P. J1 ; BEESE, L. S1
[1] Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, United States
[2] Department of Molecular Cancer Biology, Duke University Medical Center, Durham, NC 27710, United States - Source
Science (Washington, D.C.). 1997, Vol 275, Num 5307, pp 1800-1804
- CODEN
- SCIEAS
- ISSN
- 0036-8075
- Scientific domain
- Multidisciplinary
- Publisher
- American Association for the Advancement of Science, Washington, DC
- Publication country
- United States
- Document type
- Article
- Language
- English
- Keyword (fr)
- Activité enzymatique Farnesyl-diphosphate farnesyltransferase Modification posttraductionnelle Rat Site actif Structure cristalline Structure moléculaire Prénylation Enzyme Mammalia Rodentia Transferases Vertebrata
- Keyword (en)
- Enzymatic activity Farnesyl-diphosphate farnesyltransferase Posttranslational modification Rat Active site Crystalline structure Molecular structure Enzyme Mammalia Rodentia Transferases Vertebrata
- Keyword (es)
- Actividad enzimática Farnesyl-diphosphate farnesyltransferase Modificación postraduccional Rata Lugar activo Estructura cristalina Estructura molecular Enzima Mammalia Rodentia Transferases 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 / 002A02E03 Transferases
- Discipline
- Analytical, structural and metabolic biochemistry
- Origin
- Inist-CNRS
- Database
- PASCAL
- INIST identifier
- 2618456
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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