Human frataxin is an allosteric switch that activates the Fe-S cluster biosynthetic complex
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Cardiomyopathy in Friedreich ataxia: clinical findings and researchIron and sulfur in proteins. How does the cell build Fe-S clusters, cofactors essential for life?Chronochemistry in neurodegenerationIron-sulfur cluster biogenesis in mammalian cells: New insights into the molecular mechanisms of cluster deliveryUnderstanding the genetic and molecular pathogenesis of Friedreich's ataxia through animal and cellular modelsThe role of mitochondria in cellular iron-sulfur protein biogenesis: mechanisms, connected processes, and diseasesTransition metals and mitochondrial metabolism in the heartEmerging critical roles of Fe-S clusters in DNA replication and repair.Friedreich’s Ataxia Variants I154F and W155R Diminish Frataxin-Based Activation of the Iron–Sulfur Cluster Assembly ComplexStructure–Function Analysis of Friedreich’s Ataxia Mutants Reveals Determinants of Frataxin Binding and Activation of the Fe–S Assembly ComplexInteraction of J-Protein Co-Chaperone Jac1 with Fe–S Scaffold Isu Is Indispensable In Vivo and Conserved in EvolutionFunctional reconstitution of mitochondrial Fe/S cluster synthesis on Isu1 reveals the involvement of ferredoxinSpecialized function of yeast Isa1 and Isa2 proteins in the maturation of mitochondrial [4Fe-4S] proteins.Role of Nfu1 and Bol3 in iron-sulfur cluster transfer to mitochondrial clients.Oxidative stress and the homeodynamics of iron metabolismProtein stability and dynamics modulation: the case of human frataxinTurning Escherichia coli into a Frataxin-Dependent OrganismLymphoblast Oxidative Stress Genes as Potential Biomarkers of Disease Severity and Drug Effect in Friedreich's AtaxiaFerredoxin competes with bacterial frataxin in binding to the desulfurase IscS.Neurons and cardiomyocytes derived from induced pluripotent stem cells as a model for mitochondrial defects in Friedreich's ataxia.The role of CyaY in iron sulfur cluster assembly on the E. coli IscU scaffold protein.Mitochondrial Cysteine Desulfurase and ISD11 Coexpressed in Escherichia coli Yield Complex Containing Acyl Carrier ProteinMutation in the Fe-S scaffold protein Isu bypasses frataxin deletion.Frataxin-bypassing Isu1: characterization of the bypass activity in cells and mitochondriaISCA1 is essential for mitochondrial Fe4S4 biogenesis in vivo.New Techniques for Ancient Proteins: Direct Coupling Analysis Applied on Proteins Involved in Iron Sulfur Cluster BiogenesisMammalian frataxin: an essential function for cellular viability through an interaction with a preformed ISCU/NFS1/ISD11 iron-sulfur assembly complex.Molecular strategies of microbial iron assimilation: from high-affinity complexes to cofactor assembly systems.Clinical data and characterization of the liver conditional mouse model exclude neoplasia as a non-neurological manifestation associated with Friedreich's ataxia.Overlapping binding sites of the frataxin homologue assembly factor and the heat shock protein 70 transfer factor on the Isu iron-sulfur cluster scaffold proteinHuman frataxin activates Fe-S cluster biosynthesis by facilitating sulfur transfer chemistry.Novel frataxin isoforms may contribute to the pathological mechanism of Friedreich ataxiaThe L-cysteine desulfurase NFS1 is localized in the cytosol where it provides the sulfur for molybdenum cofactor biosynthesis in humansBiophysical investigation of the iron in Aft1-1(up) and Gal-YAH1 Saccharomyces cerevisiae.Biophysical probes of iron metabolism in cells and organellesFe-S cluster biogenesis in isolated mammalian mitochondria: coordinated use of persulfide sulfur and iron and requirements for GTP, NADH, and ATP.Cluster and fold stability of E. coli ISC-type ferredoxin.The fasted/fed mouse metabolic acetylome: N6-acetylation differences suggest acetylation coordinates organ-specific fuel switchingIsd11p protein activates the mitochondrial cysteine desulfurase Nfs1p protein.Turning Saccharomyces cerevisiae into a Frataxin-Independent Organism.
P2860
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P2860
Human frataxin is an allosteric switch that activates the Fe-S cluster biosynthetic complex
description
2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 2010
@ast
im November 2010 veröffentlicher wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2010/11/02)
@sk
vědecký článek publikovaný v roce 2010
@cs
wetenschappelijk artikel (gepubliceerd op 2010/11/02)
@nl
наукова стаття, опублікована в листопаді 2010
@uk
مقالة علمية (نشرت في 2-11-2010)
@ar
name
Human frataxin is an allosteri ...... S cluster biosynthetic complex
@ast
Human frataxin is an allosteri ...... S cluster biosynthetic complex
@en
Human frataxin is an allosteri ...... S cluster biosynthetic complex
@nl
type
label
Human frataxin is an allosteri ...... S cluster biosynthetic complex
@ast
Human frataxin is an allosteri ...... S cluster biosynthetic complex
@en
Human frataxin is an allosteri ...... S cluster biosynthetic complex
@nl
prefLabel
Human frataxin is an allosteri ...... S cluster biosynthetic complex
@ast
Human frataxin is an allosteri ...... S cluster biosynthetic complex
@en
Human frataxin is an allosteri ...... S cluster biosynthetic complex
@nl
P3181
P356
P1433
P1476
Human frataxin is an allosteri ...... S cluster biosynthetic complex
@en
P2093
Chi-Lin Tsai
David P. Barondeau
P304
P3181
P356
10.1021/BI1013062
P407
P577
2010-11-01T00:00:00Z