Selective Inhibition of a Regulatory Subunit of Protein Phosphatase 1 Restores Proteostasis
- Author
- TSAYTLER, Pavel1 ; HARDING, Heather P2 ; RON, David2 ; BERTOLOTTI, Anne1
[1] MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, United Kingdom
[2] Institute of Metabolic Sciences, University of Cambridge, Cambridge CB2 0QQ, United Kingdom - Source
Science (Washington, D.C.). 2011, Vol 332, Num 6025, pp 91-94, 4 p ; ref : 16 ref
- 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)
- Homme Homéostasie Inhibition Phosphoprotein phosphatase Protéine Sousunité régulation Stress Composé biochimique Enzyme Esterases Hydrolases Phosphoric monoester hydrolases
- Keyword (en)
- Human Homeostasis Inhibition Phosphoprotein phosphatase Protein Regulatory subunit Stress Biochemical compound Enzyme Esterases Hydrolases Phosphoric monoester hydrolases
- Keyword (es)
- Hombre Homeostasis Inhibición Phosphoprotein phosphatase Proteína Subunitad regulación Estrés Compuesto bioquímico Enzima Esterases Hydrolases Phosphoric monoester hydrolases
- Classification
- Pascal
- 002 Biological and medical sciences / 002A Fundamental and applied biological sciences. Psychology / 002A04 Molecular and cellular biology / 002A04H Cell physiology / 002A04H18 Miscellaneous
- Discipline
- Molecular and cell biology
- Origin
- Inist-CNRS
- Database
- PASCAL
- INIST identifier
- 24041415
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
10.1126/science.1201396 
https://dx.doi.org/10.1126/science.1201396
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