CYC7/YEL039C Literature Guide Help

Other names published for CYC7: iso-2-cytochrome c, YEL039C

CYC7 - Protein/Nucleic Acid Structure (19)

ReferenceOther Genes Addressed
Nyola A and Hunte C  (2008) A structural analysis of the transient interaction between the cytochrome bc(1) complex and its substrate cytochrome c. Biochem Soc Trans 36(Pt 5):981-5
Fisher A, et al.  (2000) Functional correlation in amino acid residue mutations of yeast iso-2-cytochrome c that is consistent with the prediction of the concomitantly variable codon theory in cytochrome c evolution. Biochem Genet 38(5-6):181-200
Lukens AK, et al.  (2000) Structure of HAP1-PC7 bound to DNA: implications for DNA recognition and allosteric effects of DNA-binding on transcriptional activation. Nucleic Acids Res 28(20):3853-63
Panda M, et al.  (2000) Cytochrome c folds through a smooth funnel. Protein Sci 9(3):536-43
Raman CS, et al.  (2000) Antibody-detected folding: kinetics of surface epitope formation are distinct from other folding phases. Protein Sci 9(1):129-37
Pierce MM and Nall BT  (1997) Fast folding of cytochrome c. Protein Sci 6(3):618-27
Liggins JR, et al.  (1994) Differential scanning calorimetric study of the thermal unfolding transitions of yeast iso-1 and iso-2 cytochromes c and three composite isozymes. Biochemistry 33(31):9209-19
Sokolik CW and Cohen RE  (1991) The structures of ubiquitin conjugates of yeast Iso-2-cytochrome c. J Biol Chem 266(14):9100-7
Leung CJ, et al.  (1989) Crystallization of yeast iso-2-cytochrome c using a novel hair seeding technique. J Mol Biol 206(4):783-5
Nall BT, et al.  (1989) Replacement of a conserved proline and the alkaline conformational change in iso-2-cytochrome c. Biochemistry 28(25):9834-9
Wood LC, et al.  (1988) Replacement of a conserved proline eliminates the absorbance-detected slow folding phase of iso-2-cytochrome c. Biochemistry 27(23):8562-8
Nall BT  (1986) Native or nativelike species are transient intermediates in folding of alkaline iso-2 cytochrome c. Biochemistry 25(10):2974-8
Osterhout JJ Jr and Nall BT  (1985) Slow refolding kinetics in yeast iso-2 cytochrome c. Biochemistry 24(27):7999-8005
Osterhout JJ Jr, et al.  (1985) pH-induced conformation changes and equilibrium unfolding in yeast iso-2 cytochrome c. Biochemistry 24(23):6680-4
Nall BT  (1983) Structural intermediates in folding of yeast iso-2 cytochrome c. Biochemistry 22(6):1423-9
Senn H, et al.  (1983) Determination of the coordination geometry at the heme iron in three cytochromes c from Saccharomyces cerevisiae and from Candida krusei based on individual 1H-NMR assignments for heme c and the axially coordinated amino acids. Biochim Biophys Acta 743(1):58-68
Zuniga EH and Nall BT  (1983) Folding of yeast iso-1-AM cytochrome c. Biochemistry 22(6):1430-7
Nall BT and Landers TA  (1981) Guanidine hydrochloride induced unfolding of yeast iso-2 cytochrome c. Biochemistry 20(19):5403-11
Looze Y, et al.  (1976) Iso-cytochrome c species from baker's yeast. Analysis of their circular-dichroism spectra. Biochem J 157(3):773-5