Human frataxin activates Fe-S cluster biosynthesis by facilitating sulfur transfer chemistry. - Test2 - elhamkhani - TriplyDB

Human frataxin activates Fe-S cluster biosynthesis by facilitating sulfur transfer chemistry.

Human frataxin activates Fe-S cluster biosynthesis by facilitating sulfur transfer chemistry.

http://www.wikidata.org/entity/Q34434217

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PMPCA mutations cause abnormal mitochondrial protein processing in patients with non-progressive cerebellar ataxia.Emerging critical roles of Fe-S clusters in DNA replication and repair.Functional reconstitution of mitochondrial Fe/S cluster synthesis on Isu1 reveals the involvement of ferredoxin Role of Nfu1 and Bol3 in iron-sulfur cluster transfer to mitochondrial clients.Oxidative folding in the mitochondrial intermembrane space: A regulated process important for cell physiology and disease Lymphoblast Oxidative Stress Genes as Potential Biomarkers of Disease Severity and Drug Effect in Friedreich's Ataxia Mitochondrial Cysteine Desulfurase and ISD11 Coexpressed in Escherichia coli Yield Complex Containing Acyl Carrier Protein ISCA1 is essential for mitochondrial Fe4S4 biogenesis in vivo.Overlapping binding sites of the frataxin homologue assembly factor and the heat shock protein 70 transfer factor on the Isu iron-sulfur cluster scaffold protein Tangled web of interactions among proteins involved in iron-sulfur cluster assembly as unraveled by NMR, SAXS, chemical crosslinking, and functional studies.Trading Places-Switching Frataxin Function by a Single Amino Acid Substitution within the [Fe-S] Cluster Assembly Scaffold.Iron loading site on the Fe-S cluster assembly scaffold protein is distinct from the active site.FXN Promoter Silencing in the Humanized Mouse Model of Friedreich Ataxia.A Yeast/Drosophila Screen to Identify New Compounds Overcoming Frataxin Deficiency The Human Iron-Sulfur Assembly Complex Catalyzes the Synthesis of [2Fe-2S] Clusters on ISCU2 That Can Be Transferred to Acceptor Molecules Frataxin Accelerates [2Fe-2S] Cluster Formation on the Human Fe-S Assembly Complex Intrathecal delivery of frataxin mRNA encapsulated in lipid nanoparticles to dorsal root ganglia as a potential therapeutic for Friedreich's ataxia.Architecture of the Yeast Mitochondrial Iron-Sulfur Cluster Assembly Machinery: THE SUB-COMPLEX FORMED BY THE IRON DONOR, Yfh1 PROTEIN, AND THE SCAFFOLD, Isu1 PROTEIN.Mammalian Fe-S proteins: definition of a consensus motif recognized by the co-chaperone HSC20 Oxidative stress in inherited mitochondrial diseases.Frataxin inactivation leads to steroid deficiency in flies and human ovarian cells.Iron-sulfur cluster biogenesis and trafficking in mitochondria.Drosophila melanogaster Models of Metal-Related Human Diseases and Metal Toxicity.Architecture of the Human Mitochondrial Iron-Sulfur Cluster Assembly Machinery Peptide SS-31 upregulates frataxin expression and improves the quality of mitochondria: implications in the treatment of Friedreich ataxia.Friedreich ataxia-induced pluripotent stem cell-derived neurons show a cellular phenotype that is corrected by a benzamide HDAC inhibitor.In vitro characterization of a novel Isu homologue from Drosophila melanogaster for de novo FeS-cluster formation.Zinc and the iron donor frataxin regulate oligomerization of the scaffold protein to form new Fe-S cluster assembly centers.Structure of human Fe-S assembly subcomplex reveals unexpected cysteine desulfurase architecture and acyl-ACP-ISD11 interactions.Protein networks in the maturation of human iron-sulfur proteins.Friedreich's ataxia: clinical features, pathogenesis and management.Overexpression of Drosophila frataxin triggers cell death in an iron-dependent manner.Biogenesis and functions of mammalian iron-sulfur proteins in the regulation of iron homeostasis and pivotal metabolic pathways.Iron-Sulfur Protein Assembly in Human Cells.ISCU(M108I) and ISCU(D39V) Differ from Wild-Type ISCU in Their Failure To Form Cysteine Desulfurase Complexes Containing Both Frataxin and Ferredoxin.Iron Sulfur and Molybdenum Cofactor Enzymes Regulate the Drosophila Life Cycle by Controlling Cell Metabolism.Interactions of iron-bound frataxin with ISCU and ferredoxin on the cysteine desulfurase complex leading to Fe-S cluster assembly.Drosophila melanogaster Models of Friedreich's Ataxia.Fe-S cluster assembly in the supergroup Excavata.Robust Production, Crystallization, Structure Determination, and Analysis of [Fe-S] Proteins: Uncovering Control of Electron Shuttling and Gating in the Respiratory Metabolism of Molybdopterin Guanine Dinucleotide Enzymes.

P2860

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P2860

Human frataxin activates Fe-S cluster biosynthesis by facilitating sulfur transfer chemistry.

http://www.wikidata.org/entity/Q34434217

description

2014 nî lūn-bûn

@nan

2014 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

2014年の論文

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2014年論文

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2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

name

Human frataxin activates Fe-S ...... ing sulfur transfer chemistry.

@ast

Human frataxin activates Fe-S ...... ing sulfur transfer chemistry.

@en

Human frataxin activates Fe-S ...... ing sulfur transfer chemistry.

@nl

type

label

Human frataxin activates Fe-S ...... ing sulfur transfer chemistry.

@ast

Human frataxin activates Fe-S ...... ing sulfur transfer chemistry.

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Human frataxin activates Fe-S ...... ing sulfur transfer chemistry.

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prefLabel

Human frataxin activates Fe-S ...... ing sulfur transfer chemistry.

@ast

Human frataxin activates Fe-S ...... ing sulfur transfer chemistry.

@en

Human frataxin activates Fe-S ...... ing sulfur transfer chemistry.

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Human frataxin activates Fe-S ...... ing sulfur transfer chemistry.

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P2093

Andrew M Winn

http://www.w3.org/2001/XMLSchema#string

Nicholas G Fox

http://www.w3.org/2001/XMLSchema#string

P2860

A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis

Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis

Crystal structure of IscS, a cysteine desulfurase from Escherichia coli

The asymmetric trimeric architecture of [2Fe-2S] IscU: implications for its scaffolding during iron-sulfur cluster biosynthesis

Structural Basis for Fe–S Cluster Assembly and tRNA Thiolation Mediated by IscS Protein–Protein Interactions

Friedreich’s Ataxia Variants I154F and W155R Diminish Frataxin-Based Activation of the Iron–Sulfur Cluster Assembly Complex

Structure–Function Analysis of Friedreich’s Ataxia Mutants Reveals Determinants of Frataxin Binding and Activation of the Fe–S Assembly Complex

(IscS-IscU)2 complex structures provide insights into Fe2S2 biogenesis and transfer

Essential role of Isd11 in mitochondrial iron-sulfur cluster synthesis on Isu scaffold proteins.

The Nfs1 interacting protein Isd11 has an essential role in Fe/S cluster biogenesis in mitochondria.

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4904-4913

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10.1021/BI500532E

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30

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53

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David P Barondeau

Jennifer Bridwell-Rabb

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2014-07-18T00:00:00Z

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24971490

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4215901

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