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  • Title: Highlight Commentary on "Redox proteomics analysis of oxidatively modified proteins in G93A-SOD1 transgenic mice--a model of familial amyotrophic lateral sclerosis".
    Author: Calabrese V.
    Journal: Free Radic Biol Med; 2007 Jul 15; 43(2):160-2. PubMed ID: 17603925.
    Abstract:
    Amyotrophic lateral sclerosis (ALS) is a fatal motor neuron disease characterized by rapid degeneration of and loss of function in the motor cortex, brain stem, and spinal cord, particularly the anterior horn cells. Since the pioneering work of Brown and colleagues, more than 100 mutations in Cu,Zn superoxide dismutase (SOD1) have been described (P. Pasinelli, R. H. Brown, Nat. Rev. Neurosci.7, 710-723, 2006). There are toxic gain-of-function alterations in SOD1, because the enzymatic activity of this protein is not different in ALS from that of controls. The paper by Butterfield and colleagues reporting the use of redox proteomics to identify oxidatively modified proteins in the spinal cord in the G93A-SOD1 mouse model of familial amyotrophic lateral sclerosis was identified by the SCOPUS science literature information system to be one of the top 20 downloaded papers for 2005-2006 in Free Radical Biology and Medicine. Here my thoughts on the importance and impact of this paper are reported.
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