MitoFluor™ Red 589 -"DISCONTINUED" - Citations

MitoFluor™ Red 589 -"DISCONTINUED" - Citations

View additional product information for MitoFluor™ Red 589 -"DISCONTINUED" - Citations (M22424)

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Citations & References
Abstract
Mitochondrial nitric oxide synthase is not eNOS, nNOS or iNOS.
AuthorsLacza Z, Snipes JA, Zhang J, Horváth EM, Figueroa JP, Szabó C, Busija DW
JournalFree Radic Biol Med
PubMed ID14607521
'Recent studies indicated that there is a distinct mitochondrial nitric oxide synthase (mtNOS) enzyme, which may be identical to the other known NOS isoforms. We investigated the possible involvement of the endothelial, the neuronal, and the inducible NOS isoforms (eNOS, nNOS, iNOS, respectively) in mitochondrial NO production. Mouse liver mitochondria ... More
The antioxidant function of the p53 tumor suppressor.
AuthorsSablina AA, Budanov AV, Ilyinskaya GV, Agapova LS, Kravchenko JE, Chumakov PM
JournalNat Med
PubMed ID16286925
It is widely accepted that the p53 tumor suppressor restricts abnormal cells by induction of growth arrest or by triggering apoptosis. Here we show that, in addition, p53 protects the genome from oxidation by reactive oxygen species (ROS), a major cause of DNA damage and genetic instability. In the absence ... More
The WD-repeats of Net2p interact with Dnm1p and Fis1p to regulate division of mitochondria.
AuthorsCerveny KL, Jensen RE
JournalMol Biol Cell
PubMed ID14517324
The Net2, Fis1, and Dnm1 proteins are required for the division of mitochondria in the yeast Saccharomyces cerevisiae. Net2p has an amino-terminal region that contains predicted coiled-coil motifs and a carboxyl-terminal domain composed of WD-40 repeats. We found that the amino-terminal part of Net2p interacts with Fis1p, whereas the carboxyl-terminal ... More
Mmm1p spans both the outer and inner mitochondrial membranes and contains distinct domains for targeting and foci formation.
AuthorsKondo-Okamoto N, Shaw JM, Okamoto K
JournalJ Biol Chem
PubMed ID12972421
In the yeast Saccharomyces cerevisiae, the integral membrane protein Mmm1p is required for maintenance of mitochondrial morphology and retention of mitochondrial DNA (mtDNA). Mmm1p localizes to discrete foci on mitochondria that are adjacent to mtDNA nucleoids in the matrix, raising the possibility that this protein plays a direct role in ... More