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The naturally occurring Y48H variant of cytochrome c in its oxidized heme state is more peroxidatic than either the Wild Type protein or the G41S variant that is also implicated in thrombocytopenia.
ROCK activation phosphorylated Rac1b (show RAC3 Proteins) at Ser71 and increased reactive oxygen species (ROS (show ROS1 Proteins)) levels by facilitating the interaction between Rac1b (show RAC3 Proteins) and cytochrome c. Conversely, ROCK inactivation abolished their interaction, concomitant with ROS (show ROS1 Proteins) reduction.
Data suggest that although HCCS (show HCCS Proteins) mediates heme attachment to N-terminal cysteine in heme-attachment site (CXXXH) of cytochrome C variants, up to 50% of cytochrome C produced is modified in an oxygen-dependent manner, resulting in a mixed population of cytochrome c. [HCCS (show HCCS Proteins) = holocytochrome c synthase (show HCCS Proteins)]
Data suggest that the stronger effect of K72A mutation on the peroxidase activity of human versus yeast cytochrome c results from relief of steric interactions between side chains at positions 72 and 81 (Ile in human vs Ala in yeast), which suppresses the dynamics of omega-loop D necessary for the intrinsic peroxidase activity of cytochrome c.
These findings establish a framework for understanding the molecular basis of cytochrome c-mediated blocking of SET/TAF-Ibeta.
Monitoring of serum cytochrome c might also serve as a sensitive apoptotic marker in vivo reflecting chemotherapy-induced cell death burden in patients with non-small cell lung cancer.
G-Rh2 (show RHAG Proteins) causes rapid and dramatic translocation of both Bak (show BAK1 Proteins) and Bax (show BAX Proteins), which subsequently triggers mitochondrial cytochrome c release and consequent caspase (show CASP3 Proteins) activation.
The mitochondrial metalloprotease OMA1 (show OMA1 Proteins) was activated in a Bax (show BAX Proteins)- and Bak (show BAK1 Proteins)-dependent fashion.
In vitro ultrastructural changes of MCF-7 for metastasise bone cancer and induction of apoptosis via mitochondrial cytochrome C released by CaCO3/Dox nanocrystals
a mechanism of multiple radical formations in the cytochrome c-phospholipid complexes under H2O2 treatment, consistent with the stabilization of the radical in the G41S mutant, which elicits a greater peroxidase activity from cytochrome c
Results suggest that excess or restricted protein supply during pregnancy alters expression of CYCS and leads to hypomethylation of CpG sites in promoter in liver of offspring. (5' flanking region: amino acid sequence; nucleic acid sequence homology)
Tissue expression profile analysis revealed that swine CYCS gene was highly expressed in muscle, fat and lung, moderately expressed in ovary, kidney, and liver, and weekly expressed in heart, spleen and small intestine.
Using mass spectrometry, this study demonstrates the occurrence of cytochrome c self-oxidation in the presence of H2O2. The newly generated oxidized proteoforms are shown to possess significantly enhanced peroxidase activity.
Cytochrome c undergoes large structural fluctuations, using the interacting regions with cytochrome c oxidase as a fulcrum.
Data suggest that ferric forms of variants of cytochrome c (wild type, T49V mutation, and Y67R/M80A mutations) are Lysine-ligated at neutral pH; hydrogen-bonding network appears to be important in controlling ligation of the native Met80 to the heme iron.
analysis of CO photo-dissociation from chloramine-T modified horse heart cytochrome-c
The effect of pH on thermodynamic stability and folding kinetics of horse cytochrome c has been described.
The cardiolipin binding and the peroxidase activity of cytochrome c depend on conformational heterogeneity and oligomerization.
The data suggest a two-step process of thermal unfolding of cytochrome c for all protonation states.
The study shows that cardiolipin modulates allosterically the nitrite reductase activity of horse heart cytochrome c.
Horse Cc binds CcP (show CRYGD Proteins) but forms a much more dynamic complex. A single conservative mutation of Lys (show LYZ Proteins)-13 to ARG reduces the dynamics and enhances the specificity. The K13A mutation of Cc increases the dynamic nature of the complex with CcP (show CRYGD Proteins).
X-ray crystallographic evidence for functional models of horse cytochrome c.
This study determines the apoptosis process mediated by cytochrome c after its release from mitochondria and the factors that affect the activation processes.
Data using ribose 5-P suggest that glycation of cyt c (at lysines in ATP binding site) results in cyto c being less able to transfer electrons to cytochrome oxidase and in reduced affinity of cyt c for cardiolipin-containing liposomes.
The presence of structural collective motions on a picosecond timescale for the heme protein, cytochrome c, as a function of oxidation and hydration, was investigated.
peroxidase activity shown by cardiolipin-bound cytochrome c is indicative of a less packed protein tertiary conformation in the complex
the amount of cytochrome c in lymphomyeloid cells does not affect their development and normal functioning
Abeta (show APP Proteins) oligomers bind to BAK (show BAK1 Proteins) on the membrane and induce apoptotic BAK (show BAK1 Proteins) pores and cytochrome c release
Data suggest that peroxidase activation of cytochrome c may induce apoptosis and contribute to anti-cancer properties of alpha-tocopherol succinate.
Data indicate that mitochondrial alpha 7 nicotinic acetylcholine receptors (alpha7 nAChRs) regulate cytochrome c (cyt c) release by engaging intramitochondrial protein kinases.
Data indicate that Y48H missense mutation of cytochrome c (CYCS) gene is associated with respiratory reduction and increased apoptosis in fibroblast.
Translocation of a Bak (show BAK1 Proteins) C-terminus mutant from cytosol to mitochondria to mediate cytochrome C release: implications for Bak (show BAK1 Proteins) and Bax (show BAX Proteins) apoptotic function.
mitochondrial import and direct electron transfer from cytochrome c to Rac1 modulates mitochondrial H(2)O(2) production in alveolar macrophages pulmonary fibrosis.
Fluoride exposure significantly elevated the protein expressions of cytochrome c and active caspase-3 (show CASP3 Proteins).
Resveratrol induces p53 (show TP53 Proteins)-independent, X-linked inhibitor of apoptosis protein (XIAP (show XIAP Proteins))-mediated Bax (show BAX Proteins) protein oligomerization on mitochondria to initiate cytochrome c release and caspase (show CASP3 Proteins) activation.
High concentration glucose administration caused significantly increased expression of NF-kappaB (show NFKB1 Proteins), Bax (show BAX Proteins) and cytochrome C.
results reveal Blanks to be a unique component of a nuclear siRNA/dsRNA-binding complex that contributes to essential RNA silencing-related pathways in the male germ line
We further identified loss-of-function mutations in one of the two Drosophila cyt-c genes, cyt-c-d, which block caspase (show CASP3 Proteins) activation and subsequent spermatid terminal differentiation.
DARK-mediated DRONC activation occurs independently of Cyt-c-p
We found that cyt c-d--as with ark (show APAF1 Proteins) and dronc-regulates scutellar bristle number, which is known to depend on caspase (show CASP3 Proteins) activity. Collectively, our results indicate a role of Cyt c in caspase (show CASP3 Proteins) regulation of Drosophila somatic cells.
This gene encodes a small heme protein that functions as a central component of the electron transport chain in mitochondria. The encoded protein associates with the inner membrane of the mitochondrion where it accepts electrons from cytochrome b and transfers them to the cytochrome oxidase complex. This protein is also involved in initiation of apoptosis. Mutations in this gene are associated with autosomal dominant nonsyndromic thrombocytopenia. Numerous processed pseudogenes of this gene are found throughout the human genome.
, cytochrome c, testis-specific
, cytochrome c, testis
, somatic cytochrome c
, cytochrome c, somatic
, Cytochrome C, expressed in somatic tissues
, cytochrome c distal
, cytochrome c DC4
, cytochrome c proximal
, Cytochrome c
, cytochrome c, somatic pseudogene