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Cytochrome c was upregulated in the primary Sjogren's syndrome patients, indicating the potential role of cytochrome c in the pathogenesis and development of primary Sjogren's syndrome.
The caspase-8/Bid/cytochrome c axis links signals from death receptors to mitochondrial reactive oxygen species production.
This work reveals a direct conformational link between the 40-57 Omega-loop of cytochrome c in which residue 41 resides and the dynamical properties of the axial ligand to the heme iron.
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 at Ser71 and increased reactive oxygen species (ROS) levels by facilitating the interaction between Rac1b and cytochrome c. Conversely, ROCK inactivation abolished their interaction, concomitant with ROS reduction.
Data suggest that although HCCS 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 = holocytochrome c synthase]
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 causes rapid and dramatic translocation of both Bak and Bax, which subsequently triggers mitochondrial cytochrome c release and consequent caspase activation.
The mitochondrial metalloprotease OMA1 was activated in a Bax- and Bak-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
proposed that mutation of residue 41, and interaction with cardiolipin, increase peroxidase activity by altering the 40-57 Omega loop and its hydrogen bond network with the propionate of haem ring A; these changes enhance access of hydrogen peroxide and substrate to the haem
Data indicate a novel missense mutation (Y48H) of the cytochrome c (CYCS) gene responsible for thrombocytopenia.
results suggest the impact of residue 41 on the conformation of cytochrome c influences its ability to act in both of its physiological roles, electron transport and caspase activation
structural characterization of cytochrome c in micelle
Data indicate that the formation of cytochrome c-Apaf-1 apoptosome and the presence of Smac are absolutely required for PSAP-induced apoptosis.
Spectroscopic analyses of HCCS alone and complexes of HCCS with site-directed variants of cytochrome c revealed the fundamental steps of heme attachment and maturation.
The levels of cellular apoptosis-associated proteins such as Smac/DIABLO, Cyto C, and the activated fragment of caspase-3 increased in pancreatic cancer cells, but the expression of XIAP was significantly decreased after 24 h treatment with the combination of TRAIL and gemcitabine.
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.
horse cyt c interaction with cardiolipin is strongly influenced by the ionic strength of the solution and ATP
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 but forms a much more dynamic complex. A single conservative mutation of Lys-13 to ARG reduces the dynamics and enhances the specificity. The K13A mutation of Cc increases the dynamic nature of the complex with CcP.
X-ray crystallographic evidence for functional models of horse cytochrome c.
The fluorescence Stokes shift response in Zn-cytochrome c includes a significant contribution from the surrounding hydration shell, which assumes a perturbed hydrogen-bonding network owing to the binding of guanidinium(+) ions to the protein surface.
Cytochrome C may form amorphous aggregates and fibrils in the presence of phenolic acids used in the food and cosmetic industries.
These observations indicate that the Lys72, Lys73, and Lys79 residues stabilize the native axial Met80-Fe(III) coordination as well as the tertiary structure of cytochrome c.
The results reveal the existence of two native-like conformations of cytochrome c that present significantly different electron-transfer reorganization free energy values.
Aminoacetone, putatively accumulated in diabetes, may directly reduce ferricytochrome c yielding methylglyoxal and free radicals, thereby triggering redox imbalance and adverse mitochondrial responses.
Although the secondary structure of dimeric cytochrome c did not change on addition of cyanide ion, the dimer dissociation rate at 45 degrees C increased from (8.9 +/- 0.7) x 10(-6) to (3.8 +/- 0.2) x 10(-5) s(-1).
Horse-heart cytochrome c exhibits significant hydration-state change in the trifluoroacetic-acid-unfolding process.
This paper reports the discovery of a (meta)stable partially unfolded state of horse heart ferricytochrome c that was obtained after exposing the protein to a solution with an alkaline pH of 11.5 for 1 week.
Ferric cytochrome c/cardiolipin complex binds nitric oxide tightly through a multistep process.
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.
It was found from temporal changes of the anti-Stokes Ultraviolet resonance Raman intensities that the energy flow from the heme to Trp59 and the energy release from Trp59 took place with the time constants of 1-3 and ~8 ps, respectively.
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 oligomers bind to BAK on the membrane and induce apoptotic BAK 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 C-terminus mutant from cytosol to mitochondria to mediate cytochrome C release: implications for Bak and Bax 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.
Resveratrol induces p53-independent, X-linked inhibitor of apoptosis protein (XIAP)-mediated Bax protein oligomerization on mitochondria to initiate cytochrome c release and caspase activation.
High concentration glucose administration caused significantly increased expression of NF-kappaB, Bax and cytochrome C.
Membrane-associated XIAP induces mitochondrial outer membrane permeabilization leading to cytochrome c and Smac release, which is dependent on Bax and Bak.
The course of etoposide-induced apoptosis from damage to DNA and p53 activation to mitochondrial release of cytochrome c.
results suggest that activation of mitochondrial ATP-dependent potassium channels protects neurons against apoptosis by preventing cytochrome c release from the mitochondria
Both neurons and cancer cells strictly inhibit cytochrome c-mediated apoptosis by a mechanism dependent on glucose metabolism.
CHCHD2 dynamically regulates the functions of cytochrome c in both oxidative phosphorylation and cell death in response to mitochondrial stress.
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
DARK-mediated DRONC activation occurs independently of Cyt-c-p
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.
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, Cytochrome C, expressed in somatic tissues
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, cytochrome c, somatic pseudogene