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Protein palmitoylation regulates diverse aspects of cellular function and organization and plays a key role in host immune responses to infection. Palmitoylation also modulates the function and localization of virus-encoded proteins. In Serwa et al. (doi:10.1016/j.chembiol.2015.06.024), we employed ...
ORGANISM(S): Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) Human herpesvirus 2 (strain 186) (HHV-2) (Human herpes simplex virus 2) Human herpesvirus 1 (strain KOS) (HHV-1) (Human herpes simplex virus 1) 
2022-03-02 | PXD002708 | Pride
Protein N-myristoylation is a ubiquitous co- and post-translational modification that has been implicated in the development and progression of a range of human diseases. In E. Thinon, R. A. Serwa, et al., Nature Communications 2014, doi:10.1038/ncomms5919, we report the global N-myristoylated prote...
ORGANISM(S): Homo sapiens (Human) 
2018-07-31 | PXD002687 | Pride
We report a novel application for Sortase A (SrtA), labeling N-terminal Gly proteins across the proteome at endogenous levels. We combined SrtA labeling of whole-cell lysates with a potent and selective NMT inhibitor, delivering a method capable of quantifying changes in cellular NMT activity in mul...
ORGANISM(S): Homo sapiens (Human) 
2018-10-25 | PXD010634 | Pride
We describe here the first example of global chemoproteomic screening and substrate validation for HYPE mediated AMPylation in mammalian cell lysate. Through quantitative mass spectrometry-based proteomics coupled with novel chemoproteomic tools providing MS/MS evidence of AMP modification we identi...
ORGANISM(S): Homo sapiens (Human) 
2015-12-02 | PXD002601 | Pride
We describe here the first example of global chemoproteomic screening for HYPE mediated AMPylation sites of human proteins. Catalytically active mutant HYPE E234G was applied in combination with an alkynylated ATP and an alkynyl-biotinylated side ID reagent for capture of chemoenzymatically tagged ...
ORGANISM(S): Homo sapiens (Human) 
2015-12-02 | PXD003053 | Pride
Dysfunction of the motor subunit of the TIM23 translocase, the PAM complex located on the matrix side of the mitochondrial inner membrane in Saccharomyces cerevisiae, was shown to cause a decrease in mitochondrial protein import and precursor accumulation in the cytosol. We used an analogous model t...
ORGANISM(S): Homo sapiens (Human) Caenorhabditis elegans 
2021-05-19 | PXD023830 | Pride
To investigate the interactome of the human translocase of the outer mitochondrial membrane (TOM) complex, we performed immunoaffinity purification of TOMM22-FLAG from HEK293T cells followed by LC-MS/MS analysis. This approach allowed us to identify proteins that co-purify with the TOM complex under...
ORGANISM(S): Homo sapiens (Human) 
2026-03-17 | PXD064520 | Pride
To investigate the effects of FKBP8 depletion in HEK293T cells, cells were transfected with siRNA targeting FKBP8 or with a non-targeting control siRNA for 48 hours. After transfection, cells were collected; 10% of the material was used for whole-cell proteome analysis, and the remaining 90% was use...
ORGANISM(S): Homo sapiens (Human) 
2026-03-17 | PXD070730 | Pride
Interactome of OCIAD1-FLAG was studied. TMT-based relative quantification of protein levels was performed in eluates from mitochondria of HEK293 cells that expressed OCIAD1-FLAG vs empty vector and from mitochondria of OCIAD1-KO cells that expressed OCIAD1-FLAG vs empty vector.
ORGANISM(S): Homo sapiens (Human) 
2024-11-08 | PXD043863 | Pride
Assembly of the oxidative phoshorylation dimeric complex III (CIII2) in the mitochondrial inner membrane is an intricate process in which many factors are involved. Despite many studies this process is yet to be completely understood. Here we report the identification of human OCIAD2 (Ovarian Carcin...
ORGANISM(S): Homo sapiens (Human) 
2022-08-12 | PXD023025 | Pride
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