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CYCS  -  cytochrome c, somatic

Homo sapiens

Synonyms: CYC, Cytochrome c, HCS, THC4
 
 
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Disease relevance of CYCS

 

Psychiatry related information on CYCS

  • The cortical and intracellular localisation of cytochrome c immunoreactivity was examined in Alzheimer's disease and control cases [6].
  • In contrast, there was no relationship between either beta-myosin heavy chain or cytochrome C oxidase expression and locomotor activity [7].
  • Preemptive antiviral therapy was initiated after the second positive PCR result in all patients, as previously reported, and HCS was not considered for clinical decision making [8].
  • To reveal brain regions most significantly related to individual differences in exploratory behaviour, oxidative metabolism was measured by cytochrome c oxidase histochemistry in 2 months old Wistar rats with persistently high (HE) or low (LE) exploratory activity in a novel environment [9].
  • Since no structural modification occurs in the spermatozoon of Acrosternum aseadum after copulation, we used cytochemical studies to show the enzymatic activities variations of acid phosphatase, thiamine pyrophosphatase, glucose-6-phosphatase and cytochrome C oxidase, when the spermatozoon passes through the spermatheca [10].
 

High impact information on CYCS

 

Chemical compound and disease context of CYCS

 

Biological context of CYCS

 

Anatomical context of CYCS

 

Associations of CYCS with chemical compounds

 

Physical interactions of CYCS

  • Our data suggest that Ca(2+) inhibits caspase activation during Ca(2+)-mediated neuron death by triggering the degradation of the cytochrome c-binding protein APAF-1 [29].
  • Mutant and wild-type alpha-synuclein interact with mitochondrial cytochrome C oxidase [30].
  • Contrary to predictions of recent theoretical analysis, 1H NMR spectroscopy indicates that there is no major movement of cytochrome c residue Phe82 on binding to cytochrome b5 [31].
  • Furthermore, the time course of cytochrome c peptide and clathrin binding to hsc70 suggested that rather than binding to polymerized hsc70, they monomerized it by reducing free monomer, thereby shifting the monomer-polymer equilibrium toward monomer [32].
  • No ternary complexes with Anabaena flavodoxin or horse heart cytochrome c were formed, suggesting that the binding site on the enzyme is the same for ferredoxin and flavodoxin and that ferredoxin-NADP+ reductase and cytochrome c bind at a common site on ferredoxin [33].
 

Enzymatic interactions of CYCS

 

Regulatory relationships of CYCS

 

Other interactions of CYCS

 

Analytical, diagnostic and therapeutic context of CYCS

References

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  15. A fused mitochondrial gene associated with cytoplasmic male sterility is developmentally regulated. Young, E.G., Hanson, M.R. Cell (1987) [Pubmed]
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  17. A pharmacologic target of G3139 in melanoma cells may be the mitochondrial VDAC. Lai, J.C., Tan, W., Benimetskaya, L., Miller, P., Colombini, M., Stein, C.A. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  18. Caspase-3 is essential for procaspase-9 processing and cisplatin-induced apoptosis of MCF-7 breast cancer cells. Blanc, C., Deveraux, Q.L., Krajewski, S., Jänicke, R.U., Porter, A.G., Reed, J.C., Jaggi, R., Marti, A. Cancer Res. (2000) [Pubmed]
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  26. Cloning and characterization of a novel human dual flavin reductase. Paine, M.J., Garner, A.P., Powell, D., Sibbald, J., Sales, M., Pratt, N., Smith, T., Tew, D.G., Wolf, C.R. J. Biol. Chem. (2000) [Pubmed]
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  28. Cupric nitrilotriacetate-induced apoptosis in HL-60 cells association with lipid peroxidation, release of cytochrome C from mitochondria, and activation of caspase-3. Ma, Y., Ogino, T., Kawabata, T., Li, J., Eguchi, K., Okada, S. Free Radic. Biol. Med. (1999) [Pubmed]
  29. Ca(2+)-induced inhibition of apoptosis in human SH-SY5Y neuroblastoma cells: degradation of apoptotic protease activating factor-1 (APAF-1). Reimertz, C., Kögel, D., Lankiewicz, S., Poppe, M., Prehn, J.H. J. Neurochem. (2001) [Pubmed]
  30. Mutant and wild-type alpha-synuclein interact with mitochondrial cytochrome C oxidase. Elkon, H., Don, J., Melamed, E., Ziv, I., Shirvan, A., Offen, D. J. Mol. Neurosci. (2002) [Pubmed]
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