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Formylation of Eukaryotic Cytoplasmic Proteins: Linking Stress to Degradation.
Eldeeb, Mohamed A; Fahlman, Richard P; Esmaili, Mansoore; Fon, Edward A.
Affiliation
  • Eldeeb MA; McGill Parkinson Program, Neurodegenerative Diseases Group, Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, Quebec, Canada. Electronic address: eldeeb@ualberta.ca.
  • Fahlman RP; Department of Biochemistry, University of Alberta, Edmonton, Alberta, Canada. Electronic address: rfahlman@ualberta.ca.
  • Esmaili M; Department of Biochemistry, University of Alberta, Edmonton, Alberta, Canada.
  • Fon EA; McGill Parkinson Program, Neurodegenerative Diseases Group, Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, Montreal, Quebec, Canada. Electronic address: ted.fon@mcgill.ca.
Trends Biochem Sci ; 44(3): 181-183, 2019 03.
Article in En | MEDLINE | ID: mdl-30661830
ABSTRACT
Unlike prokaryotes, N-terminal formylation has been confined to a handful of mitochondrial proteins in eukaryotes. A recent study unveils a new role for eukaryotic cytoplasmic N-terminal formylation linking diverse cellular stresses to N-terminal-dependent protein degradation. These findings suggest broad cellular implications in higher eukaryotes for N-terminal methionine formylation.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Eukaryota Language: En Journal: Trends Biochem Sci Year: 2019 Document type: Article

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Eukaryota Language: En Journal: Trends Biochem Sci Year: 2019 Document type: Article