Gene Ontology annotation through association of InterPro records with GO terms
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 immunofluorescence data
Gene Ontology annotation based on curation of intracellular localizations of expressed fusion proteins in living cells
Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c.
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Landmark paper identifying cytochrome c as a required factor for the apoptotic program. Cell-free system showed that cytochrome c is released from mitochondria during apoptosis and its addition to cytosol activates the apoptotic cascade.
"A cell-free system based on cytosols of normally growing cells is established that reproduces aspects of the apoptotic program in vitro"
Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3.
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Identification and cloning of Apaf-1 as the cytochrome c-binding protein that mediates caspase activation. Cytochrome c binds to Apaf-1 to trigger caspase-3 activation.
"Cytochrome c binds to Apaf-1, an event that may trigger the activation of caspase-3, leading to apoptosis"
Cytochrome c in the apoptotic and antioxidant cascades.
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Review describing the dual role of cytochrome c as a pro-apoptotic factor (released from mitochondria to activate caspases via Apaf-1) and as an antioxidant (oxidizing superoxide back to O2 in the IMS).
"cytochrome c is a pro-apoptotic factor. It is released from its places on the outer surface of the inner mitochondrial membrane at early steps of apoptosis and, combining with some cytosolic proteins, activates conversion of the latent apoptosis-promoting protease pro-caspase-9 to its active form"
An APAF-1.cytochrome c multimeric complex is a functional apoptosome that activates procaspase-9.
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Reconstitution of the apoptosome using purified cytochrome c, recombinant APAF-1, and recombinant procaspase-9. Cytochrome c and ATP/dATP hydrolysis promote APAF-1 oligomerization to form the apoptosome, which recruits and activates procaspase-9.
"the binding of cytochrome c promote APAF-1 oligomerization, forming a large multimeric APAF-1.cytochrome c complex. Such a complex can be isolated using gel filtration chromatography and is by itself sufficient to recruit and activate procaspase-9"
A soluble version of the receptor-like protein tyrosine phosphatase kappa stimulates neurite outgrowth via a Grb2/MEK1-dependent signaling cascade.
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This publication is about RPTPkappa stimulating neurite outgrowth and has no apparent connection to cytochrome c or cellular respiration. The reference appears to be incorrectly linked to the CYCS cellular respiration annotation.
"Receptor-like protein tyrosine phosphatase kappa (RPTPkappa) is expressed in the nervous system in a manner consistent with a role in axonal growth and guidance"
Microinjection of cathepsin d induces caspase-dependent apoptosis in fibroblasts.
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Cathepsin D microinjection into cytosol induces apoptosis with cytochrome c redistribution and caspase activation. Cytochrome c release from mitochondria was observed as part of the apoptotic cascade. Used as ISS reference for mouse-to-human apoptotic signaling transfer.
"microinjection of cathepsin D into the cytosol of human fibroblasts caused apoptosis, which was detected as changes in distribution of cytochrome c, cell shrinkage, activation of caspases"
Knockdown of human COX17 affects assembly and supramolecular organization of cytochrome c oxidase.
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COX17 knockdown affects cytochrome c oxidase assembly and supercomplex organization. Study involved cytochrome c in the context of respiratory chain supercomplex function in the mitochondrial IMS.
"Assembly of cytochrome c oxidase, the terminal enzyme of the mitochondrial respiratory chain, requires a concerted activity of a number of chaperones and factors for the insertion of subunits, accessory proteins, cofactors and prosthetic groups"
Bcl-2 family interaction with the mitochondrial morphogenesis machinery.
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Study on Bax/Bak-dependent mitochondrial dynamics and Bcl-2 family regulation of mitochondrial morphology. Cytochrome c release is context for apoptosis studies.
"The regulation of both mitochondrial dynamics and apoptosis is key for maintaining the health of a cell"
Phosphoproteome analysis of functional mitochondria isolated from resting human muscle reveals extensive phosphorylation of inner membrane protein complexes and enzymes.
Proteomic characterization of the human sperm nucleus.
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Mass spectrometry identification of 403 proteins in isolated sperm nuclei. Cytochrome c detection likely represents contamination from the adjacent mitochondrial midpiece sheath.
"sperm nuclei were obtained through CTAB treatment and isolated to over 99.9% purity without any tail fragments, acrosome or mitochondria as assessed by optical microscopy and transmission electron microscopy"
A proteome-scale map of the human interactome network.
Respiratory complexes III and IV can each bind two molecules of cytochrome c at low ionic strength.
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Human cytochrome c interacts with respiratory complexes III and IV with 2:1 stoichiometry at low ionic strength. Extra binding sites facilitate turnover and sliding of cytochrome c within respiratory supercomplexes.
"two cytochrome c molecules per adduct - at low ionic strength. We conclude that such extra binding sites at the surfaces of complexes III and IV can facilitate the turnover and sliding of cytochrome c molecules"
Widespread macromolecular interaction perturbations in human genetic disorders.
Architecture of the human interactome defines protein communities and disease networks.
A reference map of the human binary protein interactome.
Interactome Mapping Provides a Network of Neurodegenerative Disease Proteins and Uncovers Widespread Protein Aggregation in Affected Brains.
Dual proteome-scale networks reveal cell-specific remodeling of the human interactome.
Quantitative high-confidence human mitochondrial proteome and its dynamics in cellular context.
Cleavage of Procaspase-3 by the apoptosome
CYCS:APAF1 binds procaspase-9
Cleavage of Procaspase-9 to caspase-9
Cleavage of Procaspase-7 by the apoptosome
Release of Cytochrome c from mitochondria
Electron transfer from reduced cytochrome c to molecular oxygen
Electron transfer from ubiquinol to cytochrome c of complex III
Superoxide reduces cytochrome c
SIRT5 deacetylates Cytochrome C
CASP9 is phosphorylated at T412
HCCS inserts heme into cytochrome c
Deep research review of CYCS gene function (Falcon provider)
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CYCS encodes human cytochrome c, a dual-role protein essential for mitochondrial respiration (electron carrier from Complex III to Complex IV) and intrinsic apoptosis (released from mitochondria, binds Apaf-1 to form the apoptosome, activates caspase-9). The heme c group is covalently attached. Cytochrome c-cardiolipin interactions modulate both electron transfer and apoptotic release.