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ProteomicsRTN4IP1 deficiency causes a severe CI assembly defect
Here we used complexome profiling to characterize the functional consequences of RTN4IP1 mutations in RTN4IP1 cells.
ORGANISM(S): Homo sapiens (Human) 
2025-08-08 | PXD064861 | Pride
Oxidative phosphorylation system Lc-msms Complexome profiling Complex i assembly 
UnknownRTN4IP1 Contributes to ESCC via Regulation of Amino Acid Transporters.
Not available
S-EPMC11848606 | biostudies-literature
ProteomicsRTN4IP1 is essential for the final stages of mitochondrial complex I assembly
A biochemical deficiency of mitochondrial complex I (CI) underlies ~30% of cases of primary mitochondrial disease, yet the inventory of molecular machinery required for CI assembly remains incomplete. We previously characterised patients with isolated CI deficiency caused by segregating variants in ...
ORGANISM(S): Homo sapiens (Human) 
2025-08-08 | PXD055511 | Pride
Oxidative phosphorylation system Lc-msms Complexome profiling Complex i assembly 
UnknownRecessive Mutations in RTN4IP1 Cause Isolated and Syndromic Optic Neuropathies.
Not available
S-EPMC4667133 | biostudies-literature
UnknownMitochondrial matrix RTN4IP1/OPA10 is an oxidoreductase for coenzyme Q synthesis.
Not available
S-EPMC10830421 | biostudies-literature
UnknownRTN4IP1 is required for the final stages of mitochondrial complex I assembly and CoQ biosynthesis.
Not available
S-EPMC12489013 | biostudies-literature
UnknownHigh expression of RTN4IP1 predicts adverse prognosis for patients with breast cancer.
Not available
S-EPMC10174766 | biostudies-literature
UnknownNeurologic Phenotypes Associated With Mutations in RTN4IP1 (OPA10) in Children and Young Adults.
Not available
S-EPMC5833489 | biostudies-literature
UnknownExome sequencing identifies novel missense and deletion variants in RTN4IP1 associated with optic atrophy, global developmental delay, epilepsy, ataxia, and choreoathetosis.
Not available
S-EPMC8388561 | biostudies-literature
ProteomicsTissue-specific in vivo mitochondrial matrix proteome profiling in mouse
Targeting proximity labeling enzymes to specific cellular locations is a viable strategy for profiling subcellular proteomes with minimal perturbance to normal physiology. Here, we generate transgenic mice expressing a mitochondrial matrix-targeted ascorbate peroxidase (MTS-APEX2) to enable analysis...
ORGANISM(S): Mus musculus (Mouse) Homo sapiens (Human) 
2023-08-31 | PXD026793 | Pride
Coenzyme q Proximity labeling Mitochondrial proteome Apex Rtn4ip1 Nadph Muscle Lc-ms/ms 
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