COX2/Q0250 Literature Guide Help

Other names published for COX2: OXI1, OXII, cytochrome c oxidase subunit 2, Q0250

COX2 - Techniques and Reagents (22)

ReferenceOther Genes Addressed
Hori A, et al.  (2011) Mitochondrial fusion increases the mitochondrial DNA copy number in budding yeast. Genes Cells 16(5):527-44
Braun HP, et al.  (2009) Chapter 10 Purification of the cytochrome C reductase/cytochrome C oxidase super complex of yeast mitochondria. Methods Enzymol 456:183-90
Ding MG, et al.  (2009) Chapter 27 An improved method for introducing point mutations into the mitochondrial cytochrome B gene to facilitate studying the role of cytochrome B in the formation of reactive oxygen species. Methods Enzymol 456:491-506
Gubbens J, et al.  (2009) Photocrosslinking and click chemistry enable the specific detection of proteins interacting with phospholipids at the membrane interface. Chem Biol 16(1):3-14
Stuart RA  (2009) Chapter 11 Supercomplex organization of the yeast respiratory chain complexes and the ADP/ATP carrier proteins. Methods Enzymol 456:191-208
Lemaire C and Dujardin G  (2008) Preparation of Respiratory Chain Complexes from Saccharomyces cerevisiae Wild-Type and Mutant Mitochondria: Activity Measurement and Subunit Composition Analysis. Methods Mol Biol 432:65-81
Brandina I, et al.  (2006) Enolase takes part in a macromolecular complex associated to mitochondria in yeast. Biochim Biophys Acta 1757(9-10):1217-1228
Gonzalez SS, et al.  (2006) Natural hybrids from Saccharomyces cerevisiae, Saccharomyces bayanus and Saccharomyces kudriavzevii in wine fermentations. FEMS Yeast Res 6(8):1221-34
Vogel F, et al.  (2006) Dynamic subcompartmentalization of the mitochondrial inner membrane. J Cell Biol 175(2):237-47
Glover RL, et al.  (2005) Biodiversity of Saccharomyces cerevisiae isolated from a survey of pito production sites in various parts of Ghana. Syst Appl Microbiol 28(8):755-61
He S and Fox TD  (1997) Membrane translocation of mitochondrially coded Cox2p: distinct requirements for export of N and C termini and dependence on the conserved protein Oxa1p. Mol Biol Cell 8(8):1449-60
Geier BM, et al.  (1995) Kinetic properties and ligand binding of the eleven-subunit cytochrome-c oxidase from Saccharomyces cerevisiae isolated with a novel large-scale purification method. Eur J Biochem 227(1-2):296-302
Speno H, et al.  (1995) Identification of essential amino acids within the proposed CuA binding site in subunit II of Cytochrome c oxidase. J Biol Chem 270(43):25363-9
Mulero JJ and Fox TD  (1993) Alteration of the Saccharomyces cerevisiae COX2 mRNA 5'-untranslated leader by mitochondrial gene replacement and functional interaction with the translational activator protein PET111. Mol Biol Cell 4(12):1327-35
Taanman JW and Capaldi RA  (1992) Purification of yeast cytochrome c oxidase with a subunit composition resembling the mammalian enzyme. J Biol Chem 267(31):22481-5
Thorsness PE and Fox TD  (1990) Escape of DNA from mitochondria to the nucleus in Saccharomyces cerevisiae. Nature 346(6282):376-9
Fox TD, et al.  (1988) Plasmids can stably transform yeast mitochondria lacking endogenous mtDNA. Proc Natl Acad Sci U S A 85(19):7288-92
George-Nascimento C and Poyton RO  (1981) Further analysis of the polypeptide subunits of yeast cytochrome c oxidase. Isolation and characterization of subunits III, V, and VII. J Biol Chem 256(17):9363-70
Poyton RO, et al.  (1978) The use of orthacryl two-dimensional polyacrylamide gel electrophoresis to identify and compare the subunit polypeptides of bovine heart and yeast cytochrome c oxidases. J Biol Chem 253(18):6303-6
Phan SH and Mahler HR  (1976) Studies on cytochrome oxidase. Preliminary characterization of an enzyme containing only four subunits. J Biol Chem 251(2):270-6
Poyton RO and Schatz G  (1975) Cytochrome c oxidase from bakers' yeast. III. Physical characterization of isolated subunits and chemical evidence for two different classes of polypeptides. J Biol Chem 250(2):752-61
Poyton RO and Schatz G  (1975) Cytochrome c oxidase from bakers' yeast. IV. Immunological evidence for the participation of a mitochondrially synthesized subunit in enzymatic activity. J Biol Chem 250(2):762-6