# |
PMID |
Sentence |
1 |
17766440
|
We report a 1.5 A x-ray crystal structure of the first identified outer mitochondrial membrane Fe-S protein, mitoNEET.
|
2 |
17766440
|
The biophysical properties of mitoNEET suggest that it may participate in a redox-sensitive signaling and/or in Fe-S cluster transfer.
|
3 |
17766440
|
We report a 1.5 A x-ray crystal structure of the first identified outer mitochondrial membrane Fe-S protein, mitoNEET.
|
4 |
17766440
|
The biophysical properties of mitoNEET suggest that it may participate in a redox-sensitive signaling and/or in Fe-S cluster transfer.
|
5 |
19580816
|
Crystal structure of Miner1: The redox-active 2Fe-2S protein causative in Wolfram Syndrome 2.
|
6 |
19580816
|
Mis-splicing of CISD2, which codes for Miner1, is causative in Wolfram Syndrome 2 (WFS2) resulting in early onset optic atrophy, diabetes mellitus, deafness and decreased lifespan.
|
7 |
19580816
|
Although originally annotated as a zinc finger, we show that Miner1 is a homodimer harboring two redox-active 2Fe-2S clusters, indicating for the first time an association of a redox-active FeS protein with WFS2.
|
8 |
19580816
|
Miner1 is the first functionally different protein that shares the NEET fold with its recently identified paralog mitoNEET, an outer mitochondrial membrane protein.
|
9 |
19580816
|
We report the first measurement of the redox potentials (E(m)) of Miner1 and mitoNEET, showing that they are proton-coupled with E(m) approximately 0 mV at pH 7.5.
|
10 |
19791753
|
Here we use protein film voltammetry (PFV) as a means to probe the redox properties of mitoNEET and demonstrate the direct impact of TZD drug binding upon the redox chemistry of the FeS cluster.
|
11 |
19791753
|
In contrast, a His87Cys mutant negates the ability of TZDs to affect the midpoint potential, suggesting a model of drug binding in which His87 is critical to communication with the FeS center of mitoNEET.
|
12 |
19791753
|
Here we use protein film voltammetry (PFV) as a means to probe the redox properties of mitoNEET and demonstrate the direct impact of TZD drug binding upon the redox chemistry of the FeS cluster.
|
13 |
19791753
|
In contrast, a His87Cys mutant negates the ability of TZDs to affect the midpoint potential, suggesting a model of drug binding in which His87 is critical to communication with the FeS center of mitoNEET.
|
14 |
22903132
|
Q-RT-PCR verified that Atp5b (F1-ATPase beta subunit), Col1a1 (collagen type 1 alpha 1), Cox6c (cytochrome c oxidase subunit VIc), Ndufs3 (NADH dehydrogenase [ubiquinone] Fe-S protein 3) and Tgfb1 (transforming growth factor β1) were significantly up-regulated in the DN group.
|