Facile transfer of [2Fe-2S] clusters from the diabetes drug target mitoNEET to an apo-acceptor protein
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Chloroplast Iron Transport Proteins - Function and Impact on Plant PhysiologyAllosteric control in a metalloprotein dramatically alters function.A point mutation in the [2Fe–2S] cluster binding region of the NAF-1 protein (H114C) dramatically hinders the cluster donor propertiesNutrient-deprivation autophagy factor-1 (NAF-1): biochemical properties of a novel cellular target for anti-diabetic drugsBinding of Nitric Oxide in CDGSH-type [2Fe-2S] Clusters of the Human Mitochondrial Protein Miner2.Conserved hydrogen bonding networks of MitoNEET tune Fe-S cluster binding and structural stability.Mitoneet mediates TNFα-induced necroptosis promoted by exposure to fructose and ethanol.Minireview: Challenges and opportunities in development of PPAR agonistsThe diabetes drug target MitoNEET governs a novel trafficking pathway to rebuild an Fe-S cluster into cytosolic aconitase/iron regulatory protein 1The mitochondrial complex I activity is reduced in cells with impaired cystic fibrosis transmembrane conductance regulator (CFTR) function.The Fe-S cluster-containing NEET proteins mitoNEET and NAF-1 as chemotherapeutic targets in breast cancer.Accessory NUMM (NDUFS6) subunit harbors a Zn-binding site and is essential for biogenesis of mitochondrial complex I.Strand swapping regulates the iron-sulfur cluster in the diabetes drug target mitoNEETNADPH inhibits [2Fe-2S] cluster protein transfer from diabetes drug target MitoNEET to an apo-acceptor protein.Coming into view: eukaryotic iron chaperones and intracellular iron delivery.Interactions between mitoNEET and NAF-1 in cells.Iron and diabetes riskThe iron-sulfur cluster assembly machineries in plants: current knowledge and open questions.MitoNEET-driven alterations in adipocyte mitochondrial activity reveal a crucial adaptive process that preserves insulin sensitivity in obesity.CFTR activity and mitochondrial function.NAF-1 and mitoNEET are central to human breast cancer proliferation by maintaining mitochondrial homeostasis and promoting tumor growth.Competition of zinc ion for the [2Fe-2S] cluster binding site in the diabetes drug target protein mitoNEET.Redox control of human mitochondrial outer membrane protein MitoNEET [2Fe-2S] clusters by biological thiols and hydrogen peroxide.Phylogenetic analysis of eukaryotic NEET proteins uncovers a link between a key gene duplication event and the evolution of vertebrates.Electron transfer and proton-coupled electron transfer reactivity and self-exchange of synthetic [2Fe-2S] complexes: models for Rieske and mitoNEET clustersMetal ion oxidation state assignment based on coordinating ligand hyperfine interaction.Model of the MitoNEET [2Fe-2S] Cluster Shows Proton Coupled Electron Transfer.Redox Control of the Human Iron-Sulfur Repair Protein MitoNEET Activity via Its Iron-Sulfur Cluster.Novel thiazolidinedione mitoNEET ligand-1 acutely improves cardiac stem cell survival under oxidative stress.CISD1 in association with obesity-associated dysfunctional adipogenesis in human visceral adipose tissue.Cancer-Related NEET Proteins Transfer 2Fe-2S Clusters to Anamorsin, a Protein Required for Cytosolic Iron-Sulfur Cluster Biogenesis.MitoNEET-dependent formation of intermitochondrial junctions.Reduction of mitochondrial protein mitoNEET [2Fe-2S] clusters by human glutathione reductase.Molecular Dynamics Simulations of the [2Fe-2S] Cluster-Binding Domain of NEET Proteins Reveal Key Molecular Determinants That Induce Their Cluster Transfer/Release.Flavin nucleotides act as electron shuttles mediating reduction of the [2Fe-2S] clusters in mitochondrial outer membrane protein mitoNEET.Characterization of Arabidopsis NEET reveals an ancient role for NEET proteins in iron metabolism.Structure of the human monomeric NEET protein MiNT and its role in regulating iron and reactive oxygen species in cancer cells.The mitochondrial outer membrane protein mitoNEET is a redox enzyme catalyzing electron transfer from FMNH2 to oxygen or ubiquinone.Distinguishing the Protonation State of the Histidine Ligand to the Oxidized Iron-Sulfur Cluster from the MitoNEET Family of Proteins.Contribution of Mössbauer spectroscopy to the investigation of Fe/S biogenesis.
P2860
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P2860
Facile transfer of [2Fe-2S] clusters from the diabetes drug target mitoNEET to an apo-acceptor protein
description
2011 nî lūn-bûn
@nan
2011 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Facile transfer of [2Fe-2S] cl ...... EET to an apo-acceptor protein
@ast
Facile transfer of [2Fe-2S] cl ...... EET to an apo-acceptor protein
@en
type
label
Facile transfer of [2Fe-2S] cl ...... EET to an apo-acceptor protein
@ast
Facile transfer of [2Fe-2S] cl ...... EET to an apo-acceptor protein
@en
prefLabel
Facile transfer of [2Fe-2S] cl ...... EET to an apo-acceptor protein
@ast
Facile transfer of [2Fe-2S] cl ...... EET to an apo-acceptor protein
@en
P2093
P2860
P50
P356
P1476
Facile transfer of [2Fe-2S] cl ...... EET to an apo-acceptor protein
@en
P2093
Andrea R Conlan
Dorit Michaeli
John A Zuris
Mark L Paddock
Maya Shvartsman
Patricia A Jennings
Ron Mittler
Sagi Tamir
Yael Harir
Zvi Ioav Cabantchik
P2860
P304
13047-13052
P356
10.1073/PNAS.1109986108
P407
P577
2011-07-25T00:00:00Z