Publications by authors named "Shadi Abou-Eid"

Article Synopsis
  • Disulfide formation in the mitochondrial intermembrane space is crucial for protein functionality and is facilitated by CHCHD4-Mia40, a key oxidoreductase and chaperone.
  • Unfolded reduced proteins form a temporary complex with CHCHD4 during import; if oxidation doesn’t occur, these proteins are sent back to the cytosol for destruction.
  • The study highlights a quality control mechanism for protein import that could explain issues linked to certain human disease mutants related to CHCHD4 substrates.
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Chemotherapeutic treatment regimens often take advantage of synergistic effects of drug combinations. Anticipating that synergistic effects on the cell biological level likely manifest on the proteome level, the analysis of proteome modulations represents an appropriate strategy to study drug combinations on a molecular level. More specifically, the detection of single proteins exhibiting synergistic abundance changes could be helpful to shed light on key molecules, which contribute in mechanisms facilitating the synergistic interaction and therefore represent potential targets for specific therapeutic approaches.

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Seasonal epidemics of influenza A virus are a major cause of severe illness and are of high socio-economic relevance. For the design of effective antiviral therapies, a detailed knowledge of pathways perturbed by virus infection is critical. We performed comprehensive expression and organellar proteomics experiments to study the cellular consequences of influenza A virus infection using three human epithelial cell lines derived from human lung carcinomas: A549, Calu-1 and NCI-H1299.

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