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ProteomicsProteomic analysis of highly purified bovine F0F1 ATP Synthase
We performed a proteomic analysis of highly purified bovine F0F1 ATP synthase to assess the quality of the purification procedure adopted to isolate the protein complex and identify possible contaminant proteins.
ORGANISM(S): Bos taurus (Bovine) 
2019-09-25 | PXD015108 | Pride
Bovine atp synthase Lc-ms/ms 
UnknownSuperresolution microscopy reveals spatial separation of UCP4 and F0F1-ATP synthase in neuronal mitochondria.
Not available
S-EPMC4291679 | biostudies-literature
UnknownSingle-molecule analysis of F0F1-ATP synthase inhibited by N,N-dicyclohexylcarbodiimide.
Not available
S-EPMC3764779 | biostudies-literature
UnknownEvolution of the F0F1 ATP synthase complex in light of the patchy distribution of different bioenergetic pathways across prokaryotes.
Not available
S-EPMC4154653 | biostudies-literature
UnknownTorque generation and utilization in motor enzyme F0F1-ATP synthase: half-torque F1 with short-sized pushrod helix and reduced ATP Synthesis by half-torque F0F1.
Not available
S-EPMC3265869 | biostudies-literature
UnknownEpigallocatechin-3-Gallate Plus Omega-3 Restores the Mitochondrial Complex I and F0F1-ATP Synthase Activities in PBMCs of Young Children with Down Syndrome: A Pilot Study of Safety and Efficacy.
Not available
S-EPMC8002266 | biostudies-literature
UnknownF0F1 ATP synthase regulates extracellular calcium influx in human neutrophils by interacting with Cav2.3 and modulates neutrophil accumulation in the lipopolysaccharide-challenged lung.
Not available
S-EPMC7001235 | biostudies-literature
UnknownMovements of the epsilon-subunit during catalysis and activation in single membrane-bound H(+)-ATP synthase.
Not available
S-EPMC1150879 | biostudies-literature
UnknownATP Synthase Subunit Epsilon Overexpression Promotes Metastasis by Modulating AMPK Signaling to Induce Epithelial-to-Mesenchymal Transition and Is a Poor Prognostic Marker in Colorectal Cancer Patients.
Not available
S-EPMC6678251 | biostudies-literature
ProteomicsMitochondria inside acute myeloid leukemia cells hydrolyze ATP to resist chemotherapy
Despite early optimism, therapeutics targeting oxidative phosphorylation (OxPhos) have faced clinical setbacks, primarily stemming from their inability to distinguish healthy from cancerous mitochondria. Herein, we describe an actionable bioenergetic mechanism unique to cancerous mitochondria inside...
ORGANISM(S): Homo Sapiens (human) 
2025-04-02 | PXD051129 | JPOST Repository
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