Ontology highlight
ABSTRACT:
INSTRUMENT(S): LTQ
ORGANISM(S): Escherichia Coli
SUBMITTER: Didier Vertommen
LAB HEAD: Jean-François Collet
PROVIDER: PXD002804 | Pride | 2015-09-16
REPOSITORIES: Pride
Action | DRS | |||
---|---|---|---|---|
BCHM220_Ctrl_Metonly_MultiConsensus.pep.xml | Pepxml | |||
BCHM220_Ctrl_frac1.RAW | Raw | |||
BCHM220_Ctrl_frac1.msf | Msf | |||
BCHM220_Ctrl_frac10.RAW | Raw | |||
BCHM220_Ctrl_frac10.msf | Msf |
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Gennaris Alexandra A Ezraty Benjamin B Henry Camille C Agrebi Rym R Vergnes Alexandra A Oheix Emmanuel E Bos Julia J Leverrier Pauline P Espinosa Leon L Szewczyk Joanna J Vertommen Didier D Iranzo Olga O Collet Jean-François JF Barras Frédéric F
Nature 20151207 7582
The reactive species of oxygen and chlorine damage cellular components, potentially leading to cell death. In proteins, the sulfur-containing amino acid methionine is converted to methionine sulfoxide, which can cause a loss of biological activity. To rescue proteins with methionine sulfoxide residues, living cells express methionine sulfoxide reductases (Msrs) in most subcellular compartments, including the cytosol, mitochondria and chloroplasts. Here we report the identification of an enzymati ...[more]