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Crystal structure of Miner1: The redox-active 2Fe-2S protein causative in Wolfram Syndrome 2The novel 2Fe–2S outer mitochondrial protein mitoNEET displays conformational flexibility in its N-terminal cytoplasmic tethering domainComplexes of the outer mitochondrial membrane protein mitoNEET with resveratrol-3-sulfateMutation of the His ligand in mitoNEET stabilizes the 2Fe–2S cluster despite conformational heterogeneity in the ligand environmentStructure and Molecular Evolution of CDGSH Iron-Sulfur DomainsAllosteric 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 propertiesA family of metal-dependent phosphatases implicated in metabolite damage-controlNutrient-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.Binding of histidine in the (Cys)3(His)1-coordinated [2Fe-2S] cluster of human mitoNEET.Resonance Raman studies of the (His)(Cys)3 2Fe-2S cluster of MitoNEET: comparison to the (Cys)4 mutant and implications of the effects of pH on the labile metal centerThe diabetes drug target MitoNEET governs a novel trafficking pathway to rebuild an Fe-S cluster into cytosolic aconitase/iron regulatory protein 1Interdomain communication revealed in the diabetes drug target mitoNEETThe yeast iron regulatory proteins Grx3/4 and Fra2 form heterodimeric complexes containing a [2Fe-2S] cluster with cysteinyl and histidyl ligation.Facile transfer of [2Fe-2S] clusters from the diabetes drug target mitoNEET to an apo-acceptor proteinStrand 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.CFTR activity and mitochondrial function.Enzymatically inactive adenylate kinase 4 interacts with mitochondrial ADP/ATP translocaseCompetition 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.Metal ion oxidation state assignment based on coordinating ligand hyperfine interaction.Redox Control of the Human Iron-Sulfur Repair Protein MitoNEET Activity via Its Iron-Sulfur Cluster.Continuous-wave and pulsed EPR characterization of the [2Fe-2S](Cys)3(His)1 cluster in rat MitoNEET.Protective properties afforded by pioglitazone against intrastriatal LPS in Sprague-Dawley rats.Crystallization and preliminary X-ray diffraction studies of the prototypal homologue of mitoNEET (Tth-NEET0026) from the extreme thermophile Thermus thermophilus HB8.Reduction of mitochondrial protein mitoNEET [2Fe-2S] clusters by human glutathione reductase.Engineering the redox potential over a wide range within a new class of FeS proteins.Redox characterization of the FeS protein MitoNEET and impact of thiazolidinedione drug binding.Pioglitazone treatment following spinal cord injury maintains acute mitochondrial integrity and increases chronic tissue sparing and functional recovery.Flavin nucleotides act as electron shuttles mediating reduction of the [2Fe-2S] clusters in mitochondrial outer membrane protein mitoNEET.Characterization of auxiliary iron-sulfur clusters in a radical S-adenosylmethionine enzyme PqqE from Methylobacterium extorquens AM1.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.The unique fold and lability of the [2Fe-2S] clusters of NEET proteins mediate their key functions in health and disease.
P2860
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P2860
description
2007 nî lūn-bûn
@nan
2007 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Crystallographic studies of human MitoNEET
@ast
Crystallographic studies of human MitoNEET
@en
Crystallographic studies of human MitoNEET
@nl
type
label
Crystallographic studies of human MitoNEET
@ast
Crystallographic studies of human MitoNEET
@en
Crystallographic studies of human MitoNEET
@nl
prefLabel
Crystallographic studies of human MitoNEET
@ast
Crystallographic studies of human MitoNEET
@en
Crystallographic studies of human MitoNEET
@nl
P2093
P2860
P356
P1476
Crystallographic studies of human MitoNEET
@en
P2093
Eric J Smart
Haining Zhu
Rujuan Liu
Stuart Ross
Weimin Gong
Xiaowei Hou
P2860
P304
P356
10.1074/JBC.C700172200
P407
P577
2007-11-16T00:00:00Z