CYC1 Antibody

1. Data indicate the equirements for the 7th or 8th position of the TATA element in the cytochrome c isoform 1 (CYC1) promoter. PMID: 26046838
2. Thermodynamic and dynamic properties of iso-1-cytochrome c covalently bound to a bare gold surface are here investigated by large scale atomistic simulations. PMID: 25184441
3. The three-dimensional NMR solution structure of yeast cyt c Y67H variant with high peroxidase activity. PMID: 25210769
4. The current study is consistent with a model for yCc binding to CcP in which yCc binds predominantly near the region defined by crystallographic structure of the 1:1 yCc-CcP complex PMID: 26212209
5. Thermodynamic measurements show that the native conformer is more stable than the His81-heme alkaline conformer for A81H iso-1-cytochrome c. DeltaGu degrees (H2O) is approximately 1.9 kcal/mol for formation of the His81-heme alkaline conformer. PMID: 25671560
6. 1.45-A resolution structure with the Met80 heme ligand swung out of the heme crevice. This conformational change requires adjustments to the main chain of the heme crevice loop and is facilitated by a trimethyllysine 72-to-alanine mutation. PMID: 24760830
7. Data indicate that Y48H missense mutation of cytochrome c (CYCS) gene is associated with growth and respiratory defects. PMID: 24326104
8. pH-jump kinetic studies of the His79-heme alkaline transition show that both the forward and backward rates of conformational change are increased by the Trimethyllysine 72 to Ala substitution. PMID: 23311346
9. yeast CYC1 displays lower stability and, contrary to the equine protein, it does not bind ATP and lacks pro-apoptotic activity PMID: 21946436
10. His26 is not the source of pK(H1). The data also show that the H26N mutation enhances the dynamics of this conformational transition from pH 5 to 10, likely as a result of destabilization of the protein. PMID: 22026475
11. Kinetic studies show that change in His-heme loop stability for aromatic amino acids is caused by a slowdown in the rate of loop breakage, indicating that residual structure is preferentially stabilized in the closed-loop form of the denatured state. PMID: 20850458
12. Site directed mutagenesis reveals stability of variants. PMID: 15723532
13. analysis of electron transfer between monomers when the cytochrome bc1 complex dimer is reduced through center N PMID: 15833742
14. Lys72 most readily deprotonates and replaces M80 as the axial heme iron ligand, whereas Lys73 and Lys79 show comparably higher pKa values and larger transition free energies. PMID: 17243773
15. conformational stability of wild type proteins and muants were compared PMID: 17504090
16. A technique was developed for the detection of fluorescence signals from free single molecules for extended time periods and was applied to the characterization of the unfolded state of CYC1. PMID: 17563378
17. The conformational factor in the denatured state of iso-1-cytchrome c using a five alanine insert in front of a unique histidine in the N-terminal region of the protein, was investigated. PMID: 17583729
18. assessed the importance of Pro-76 and Gly-77 by mutating 1 or both of these residues to alanine such that the range of allowable dihedral angles was altered, and this resulted in significant changes in physicochemical properties and biological activities PMID: 17612631
19. These data indicate that acid unfolding is multi-state for both K79H and wild type proteins and that the His 79-heme alkaline conformer is more stable than a previously reported His 73-heme alkaline conformer. PMID: 17713929
20. simulate the denatured ensemble of cytochrome c using a series of models. Six variants of S cerevisae iso-1-cytochrome c under GuHCl- and acid-denaturing conditions PMID: 19181849

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KEGG: sce:YJR048W

STRING: 4932.YJR048W