CISD1 Antibody

1. The [2Fe-2S] clusters of mitoNEET are reduced via the formation of a transient complex that brings the [2Fe-2S] clusters of mitoNEET close to the redox-active [2Fe-2S] cluster of anamorsin. PMID: 28648056
2. The results suggest that flavin nucleotides may act as electron shuttles to reduce the mitoNEET [2Fe-2S] clusters and regulate mitochondrial functions in human cells. PMID: 27923678
3. Data suggest that, compared with oxygen, ubiquinone-2 is more efficient in oxidizing mitoNEET [2Fe-2S] clusters, suggesting that ubiquinone could be an intrinsic electron acceptor of reduced mitoNEET [2Fe-2S] clusters in mitochondrial outer membrane. PMID: 28461337
4. CISD1 inhibits ferroptosis by protecting the cells against mitochondrial lipid peroxidation. PMID: 27510639
5. the redox-sensing function of mNT is a key component of the cellular adaptive response to help stress-sensitive Fe-S proteins recover from oxidative injury. PMID: 26887944
6. A possible role of CISD1 in obesity-associated dysfunctional adipogenesis in human visceral adipose tissue. PMID: 26692580
7. Our results confirm the observation that mitoNEET is important in transferring the iron sulfur clusters to the cytosolic aconitase in living cells and the His-87 ligand in mitoNEET plays important role in this process. PMID: 26778000
8. Glutathione reductase reduces mitochondrial protein mitoNEET [2Fe-2S] clusters. PMID: 25645953
9. Studies indicate that NEET proteins are associated with diseases including cancer and diabetes. PMID: 25448035
10. SNPs in three genes CYP26B1 rs2241057, CISD1 rs2251039, rs2590370, and TBX1 rs4819522 were involved in six potential pathways to influence serum prostate-specific antigen levels. PMID: 25168891
11. In this review, we evaluate the current understanding regarding how mitoNEET regulates cellular bioenergetics as well as the structural requirements for drug compound association with mitoNEET PMID: 24814435
12. MitoNEET governs a novel trafficking pathway to rebuild an Fe-S cluster into cytosolic aconitase/IRP1. PMID: 25012650
13. pioglitazone may modulate the function of mitoNEET by blocking the thiol-mediated reduction of [2Fe-2S] clusters in the protein. PMID: 24403080
14. The MitoNEET forms a covalent complex with GDH1 through disulfide bond formation and acts as an activator. PMID: 24295216
15. Data show that the protein levels of NAF-1 (CISD2) and mNT (CISD1) are elevated in human epithelial breast cancer cells. PMID: 23959881
16. a loop (L2) 20 A away from the metal center exerts allosteric control over the cluster binding domain and regulates multiple properties of the metal center. Mutagenesis of L2 results in significant shifts in the redox potential of the [2Fe-2S] cluster. PMID: 23271805
17. NADPH can regulate both mitoNEET [2Fe-2S] cluster levels in the cell as well as the ability of the protein to transfer [2Fe-2S] clusters to cytosolic or mitochondrial acceptors. PMID: 22351774
18. These findings suggest a likely role for mNT in [2Fe-2S] and/or iron transfer to acceptor proteins. PMID: 21788481
19. crystal structure of H87C mitoNEET was determined to 1.7 A resolution (R factor = 18%) to investigate the structural basis of the changes in the properties of the 2Fe-2S cluster PMID: 21636891
20. The iron-sulfur cluster-containing protein mitoNEET interacts with two potentially redox active substances at the surface of mitochondria; mitoNEET forms complexes with resveratrol-3-sulfate, a primary metabolite of the natural product resveratrol. PMID: 21591687
21. Results describe the discovery of potential mitoNEET ligand binding sites and novel ligands, and suggests the possibility for detailed structural studies of mitoNEET-ligand complexes. PMID: 21531159
22. Results describe the folding landscape of mitoNEET, and uncover communication between distal regions of the protein. PMID: 21402934
23. Reduced nicotinamide adenine dinucleotide phosphate (NADPH) can bind to homodimeric mitoNEET, influencing the stability of the [2Fe-2S] cluster that is bound within a loop region (Y71-H87) in each subunit. PMID: 20932062
24. We use electron paramagnetic resonance spectroscopy to investigate the [2Fe-2S]cluster in mitoNEET. PMID: 20099820
25. mito- NEET is an important iron-containing protein involved in the control of maximal mitochondrial respiratory rates PMID: 17376863
26. Spectroscopic studies show that the 2Fe-2S cluster is coordinated by Cys-3 and His-1. The His ligand is shown to be involved in the observed pH lability of the cluster, indicating that loss of this ligand via protonation triggered release of the cluster. PMID: 17584744
27. Crystal structure of mitoNEET reveals distinct groups of iron sulfur proteins. PMID: 17766439
28. biophysical properties of mitoNEET suggest that it may participate in a redox-sensitive signaling and/or in Fe-S cluster transfer PMID: 17766440
29. X-ray crystallographic studies show that mitoNEET dimer may interact with other proteins via the surface residues in close proximity to the [2Fe-2S] cluster PMID: 17905743
30. A CISD1-GFP chimera was found to be located into mitochondria. PMID: 18047834
31. The physiologically relevant acid ionization constant (pKa) of histidine residues makes histidine87 a likely candidate for modulating the lability of the metal cluster in mitoNEET. PMID: 19388667
32. There is considerable flexibility in the position of the cytoplasmic tethering arms, resulting in two different conformations in the crystal structure of mitoNEET. PMID: 19574633

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HGNC: 30880

OMIM: 611932

KEGG: hsa:55847

STRING: 9606.ENSP00000363041

UniGene: Hs.370102