Author: Munday, Diane C.; Emmott, Edward; Surtees, Rebecca; Lardeau, Charles-Hugues; Wu, Weining; Duprex, W. Paul; Dove, Brian K.; Barr, John N.; Hiscox, Julian A.
Title: Quantitative Proteomic Analysis of A549 Cells Infected with Human Respiratory Syncytial Virus Document date: 2010_7_20
ID: 2zhaknbi_45
Snippet: A diagrammatic representation shows the inner and outer mitochondrial membranes with representative proteins identified in the quantitative proteomic analysis shown in their appropriate mitochondrial localizations. In the outer mitochondrial membrane, Tom20 and Tom22 interact with other Toms (some of which were identified in this analysis) to form a pore through which premitochondrial proteins are transported. Transmembrane pores such as VDACs ma.....
Document: A diagrammatic representation shows the inner and outer mitochondrial membranes with representative proteins identified in the quantitative proteomic analysis shown in their appropriate mitochondrial localizations. In the outer mitochondrial membrane, Tom20 and Tom22 interact with other Toms (some of which were identified in this analysis) to form a pore through which premitochondrial proteins are transported. Transmembrane pores such as VDACs may participate in the formation of the permeability transition pore complex, which is responsible for the release of mitochondrial products such as cytochrome c that trigger apoptosis. The inner membrane contains the protein complexes involved in the electron transport chain. Respiratory Complexes 1, 3, and 4 are proton pumps. Those proteins involved in cell proliferation and integrity such as PHB subunits PHB1 and PHB2 are also found in mitochondria.
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