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UnknownIndependent accretion of TIM22 complex subunits in the animal and fungal lineages.
Not available
S-EPMC7523481 | biostudies-literature
UnknownDefining the Substrate Spectrum of the TIM22 Complex Identifies Pyruvate Carrier Subunits as Unconventional Cargos.
Not available
S-EPMC7090383 | biostudies-literature
UnknownTim29 is a novel subunit of the human TIM22 translocase and is involved in complex assembly and stability.
Not available
S-EPMC5016092 | biostudies-literature
UnknownTim18p, a new subunit of the TIM22 complex that mediates insertion of imported proteins into the yeast mitochondrial inner membrane.
Not available
S-EPMC85242 | biostudies-literature
UnknownThe TIM22 complex mediates the import of sideroflexins and is required for efficient mitochondrial one-carbon metabolism.
Not available
S-EPMC8101445 | biostudies-literature
ProteomicsA hybrid TIM complex mediates protein import into hydrogenosomes of Trichomonas vaginalis
Hydrogenosomes are a specific type of mitochondria that have adapted for life under anaerobiosis. Limited availability of oxygen has resulted in the loss of the membrane- associated respiratory chain, and consequently in the generation of minimal inner membrane potential (), and inefficient ATP synt...
ORGANISM(S): Trichomonas vaginalis 
2024-06-16 | PXD047649 | Pride
Presequence translocase-associated motor Parasite Protein import machinery Tim22 complex Mitochondria Tim23 complex Trichomonas vaginalis Hydrogenosomes 
UnknownStructure of the mitochondrial TIM22 complex from yeast.
Not available
S-EPMC8027178 | biostudies-literature
UnknownCryo-EM structure of the human mitochondrial translocase TIM22 complex.
Not available
S-EPMC8027037 | biostudies-literature
UnknownA hybrid TIM complex mediates protein import into hydrogenosomes of Trichomonas vaginalis.
Not available
S-EPMC11145794 | biostudies-literature
ProteomicsAIM32 is a dual-localized 2Fe-2S mitochondrial protein that functions in redox quality control
Maintaining redox homeostasis under normal and stress conditions in the mitochondrion is complex. We used mass spectrometry analysis to identify key proteins that interacted with the sulfhydryl oxidase Erv1 of the mitochondrial intermembrane space assembly (MIA) pathway. Results: Aim32, a thioredoxi...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2022-02-16 | PXD021662 | Pride
Aim32 Oxa1 Mitochondrion is complex. mass spectrometry Tim23 Tim22 
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