Gene Ontology annotation through association of InterPro records with GO terms.
Manual transfer of experimentally-verified manual GO annotation data to orthologs by curator judgment of sequence similarity.
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt.
Gene Ontology annotation based on curation of intracellular localizations of expressed fusion proteins in living cells.
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods.
A proteome-scale map of the human interactome network.
Widespread macromolecular interaction perturbations in human genetic disorders.
Assembly of human mitochondrial ATP synthase through two separate intermediates, F1-c-ring and b-e-g complex.
Extensive disruption of protein interactions by genetic variants across the allele frequency spectrum in human populations.
TMEM70 facilitates biogenesis of mammalian ATP synthase by promoting subunit c incorporation into the rotor structure of the enzyme.
A reference map of the human binary protein interactome.
TMEM70 forms oligomeric scaffolds within mitochondrial cristae promoting in situ assembly of mammalian ATP synthase proton channel.
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
Structure of the human ATP synthase.
Enzyme-bound ATP is released
ADP and Pi bind to ATPase
F1Fo ATP synthase dimerizes
Deep research on ATP5MC1 function
Cyberian deep research on ATP5MC1 function
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The c-subunit ring forms the mitochondrial permeability transition pore (mPTP) under calcium stress, with the central pore occluded by F1 and lipid plug under normal conditions
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The c-ring stoichiometry of 8 subunits in mammals yields an H+/ATP ratio of 2.67, among the most efficient ratios observed in nature
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Trimethylation of Lys-43 by ATPSCKMT/FAM173B is required for proper c-subunit incorporation and optimal mitochondrial respiration
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ATP synthase c-subunit accumulates in lysosomes in neuronal ceroid lipofuscinoses (Batten disease)
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ATP synthase dimers self-assemble into rows at cristae ridges and are required for cristae formation
The ATP synthase--a splendid molecular machine
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Boyer's binding change mechanism explains how c-ring rotation drives ATP synthesis
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The three beta-subunits exist in open, loose, and tight conformational states
Structure and conformational states of the bovine mitochondrial ATP synthase by cryo-EM
Cryo-EM structure of the entire mammalian F-type ATP synthase
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Subunit e anchors a lipid plug that caps the central pore of the c-ring
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Upon calcium treatment, subunit e retracts potentially pulling the lipid plug out
ATP synthase c-subunit ring as the channel of mitochondrial permeability transition: Regulator of metabolism in development and degeneration.
An uncoupling channel within the c-subunit ring of the F1FO ATP synthase is the mitochondrial permeability transition pore
Lysine methylation by the mitochondrial methyltransferase FAM173B optimizes the function of mitochondrial ATP synthase
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ATPSCKMT/FAM173B trimethylates Lys-43 of c-subunit
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Loss of methylation results in aberrant assembly, decreased ATP-generating capacity
Specific storage of subunit c of mitochondrial ATP synthase in lysosomes of neuronal ceroid lipofuscinosis (Batten's disease).
Specific delay of degradation of mitochondrial ATP synthase subunit c in late infantile neuronal ceroid lipofuscinosis (Batten disease).
Oligomycin frames a common drug-binding site in the ATP synthase
Assembly of the membrane domain of ATP synthase in human mitochondria
ATP synthase Evolution, energetics, and membrane interactions
Dimers of mitochondrial ATP synthase induce membrane curvature and self-assemble into rows