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ProteomicsHigh resolution mass spectrometry analysis of P-fructose-labeled Tom22 peptides
After identifying Tom22 as a direct target of fructose, we sought to map the potential sites that fructose binds to Tom22. We analyzed trypsin-digested peptides of P-fructose-labeled recombinant Tom22 by high-resolution mass spectrometry.
ORGANISM(S): Homo sapiens (Human) 
2026-06-05 | PXD047275 | Pride
Small molecule-protein interaction Tom22 Fructose 
ProteomicsReceptor-mediated recruitment of cytosolic J-proteins to the mitochondrial outer membrane promotes assembly of preprotein translocases
Mitochondria possess elaborate machineries for the import of preproteins from the cytosol. Cytosolic factors like Hsp70 chaperones and their co-chaperones, the J-proteins, guide preproteins to the mitochondrial surface. The translocase of the mitochondrial outer membrane (TOM) forms the entry gate f...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2018-11-26 | PXD008203 | Pride
Proteomics Cytosolic j-proteins Yeast Mitochondria Silac 
UnknownIdentification and functional analysis of human Tom22 for protein import into mitochondria.
Not available
S-EPMC86274 | biostudies-literature
UnknownMitochondrial protein import - Functional analysis of the highly diverged Tom22 orthologue of Trypanosoma brucei.
Not available
S-EPMC5240110 | biostudies-literature
UnknownStructural basis of Tom20 and Tom22 cytosolic domains as the human TOM complex receptors.
Not available
S-EPMC9245660 | biostudies-literature
UnknownIn vivo protein-interaction mapping of a mitochondrial translocator protein Tom22 at work.
Not available
S-EPMC3174609 | biostudies-literature
UnknownAnalysis of individual mitochondria via fluorescent immunolabeling with Anti-TOM22 antibodies.
Not available
S-EPMC4332841 | biostudies-literature
UnknownImpaired Mitochondrial Fusion and Oxidative Phosphorylation Triggered by High Glucose Is Mediated by Tom22 in Endothelial Cells.
Not available
S-EPMC6545771 | biostudies-literature
UnknownThe membrane insertion of the pro-apoptotic protein Bax is a Tom22-dependent multi-step process: a study in nanodiscs.
Not available
S-EPMC11266675 | biostudies-literature
UnknownDynamic Coupling between Tom22 Motions and Tom40 Pore Dynamics Modulates Ion Transport in the Mitochondrial TOM Complex.
Not available
S-EPMC12648644 | biostudies-literature
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