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ProteomicsCharacterizing the role of OCIAD1 in the proteolytic processing of holocytochrome c1 and CIII2 assembly
To characterize the nature of the cytochrome c1 (CYC1) processivity defect in native CIII2 assemblies we identified CYC1 peptides using mass spectrometry analysis of blue native (BN)-PAGE. Gel slices ranging from ~600-900kDa and containing CIII2 assemblies were excised from U2OS control cells, U2OS ...
ORGANISM(S): Homo sapiens (Human) 
2021-05-18 | PXD025576 | Pride
Cleavage Cytochrome c1 Ociad1 Mitochondria Complex iii Immp2l Processivity 
ProteomicsMapping the interactome of OCIAD1 in human K562 cells
Immunoprecipitation of OCIAD1 followed by mass spectrometry analysis to identify binding partners in human cells. To determine the functional significance of OCIAD1 interactors, we also looked for interactions that were modulated by a loss-of-function mutant (F102A).
ORGANISM(S): Homo sapiens (Human) 
2021-05-14 | PXD025682 | Pride
Affinity purification Cytochrome c1 Ociad1 Mitochondria Complex iii Prohibitin 
ProteomicsMapping perturbations in the cellular proteome of OCIAD1 and OCIAD2 knockdown U2OS cells.
To gain insight into the function of both OCIAD paralogs, we used untargeted quantitative mass spectrometry to compare the whole-cell proteomes of control U2OS cells, U2OS cells with individual or double OCIAD1/OCIAD2 knockdown, and OCIAD1 knockdown cells in which OCIAD1 expression was reintroduced ...
ORGANISM(S): Homo sapiens (Human) 
2021-05-14 | PXD025573 | Pride
Ociad2 Knockdown Cytochrome c1 Ociad1 Mitochondria Complex iii 
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