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

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

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

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Iron and sulfur in proteins. How does the cell build Fe-S clusters, cofactors essential for life?Iron-sulfur cluster biogenesis in mammalian cells: New insights into the molecular mechanisms of cluster delivery Biosynthesis and functions of sulfur modifications in tRNA Modification of the wobble uridine in bacterial and mitochondrial tRNAs reading NNA/NNG triplets of 2-codon boxes Structure–Function Analysis of Friedreich’s Ataxia Mutants Reveals Determinants of Frataxin Binding and Activation of the Fe–S Assembly Complex Biochemical Discrimination between Selenium and Sulfur 1: A Single Residue Provides Selenium Specificity to Human Selenocysteine Lyase Interaction of J-Protein Co-Chaperone Jac1 with Fe–S Scaffold Isu Is Indispensable In Vivo and Conserved in Evolution Structural Changes during Cysteine Desulfurase CsdA and Sulfur Acceptor CsdE Interactions Provide Insight into the trans -Persulfuration Three-Dimensional Structure and Determinants of Stability of the Iron–Sulfur Cluster Scaffold Protein IscU from Escherichia coli The cysteine desulfurase IscS of Mycobacterium tuberculosis is involved in iron-sulfur cluster biogenesis and oxidative stress defence Functional reconstitution of mitochondrial Fe/S cluster synthesis on Isu1 reveals the involvement of ferredoxin A novel target of IscS in Escherichia coli: participating in DNA phosphorothioation Pseudomonas aeruginosa PA1006 is a persulfide-modified protein that is critical for molybdenum homeostasis Turning Escherichia coli into a Frataxin-Dependent Organism A New Tessera into the Interactome of the isc Operon: A Novel Interaction between HscB and IscS Ferredoxin competes with bacterial frataxin in binding to the desulfurase IscS.Structural, Mechanistic and Coordination Chemistry of Relevance to the Biosynthesis of Iron-Sulfur and Related Iron Cofactors Mitochondrial Cysteine Desulfurase and ISD11 Coexpressed in Escherichia coli Yield Complex Containing Acyl Carrier Protein Mutation in the Fe-S scaffold protein Isu bypasses frataxin deletion.Catalytic Intermediate Crystal Structures of Cysteine Desulfurase from the Archaeon Thermococcus onnurineus NA1.Role of IscX in iron-sulfur cluster biogenesis in Escherichia coli New Techniques for Ancient Proteins: Direct Coupling Analysis Applied on Proteins Involved in Iron Sulfur Cluster Biogenesis Mammalian frataxin: an essential function for cellular viability through an interaction with a preformed ISCU/NFS1/ISD11 iron-sulfur assembly complex.A highly conserved family of domains related to the DNA-glycosylase fold helps predict multiple novel pathways for RNA modifications pH-induced conformational change of IscU at low pH correlates with protonation/deprotonation of two conserved histidine residues.Cytosolic iron-sulfur cluster assembly (CIA) system: factors, mechanism, and relevance to cellular iron regulation The identification of a novel protein involved in molybdenum cofactor biosynthesis in Escherichia coli.Molecular details of the yeast frataxin-Isu1 interaction during mitochondrial Fe-S cluster assembly 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 Human frataxin activates Fe-S cluster biosynthesis by facilitating sulfur transfer chemistry.The sulfur carrier protein TusA has a pleiotropic role in Escherichia coli that also affects molybdenum cofactor biosynthesis The role of zinc in the stability of the marginally stable IscU scaffold protein.Tangled web of interactions among proteins involved in iron-sulfur cluster assembly as unraveled by NMR, SAXS, chemical crosslinking, and functional studies.Abbreviated Pathway for Biosynthesis of 2-Thiouridine in Bacillus subtilis Turning Saccharomyces cerevisiae into a Frataxin-Independent Organism.Deletion of the Proposed Iron Chaperones IscA/SufA Results in Accumulation of a Red Intermediate Cysteine Desulfurase IscS in Escherichia coli.Disordered form of the scaffold protein IscU is the substrate for iron-sulfur cluster assembly on cysteine desulfurase Iron loading site on the Fe-S cluster assembly scaffold protein is distinct from the active site.Biogenesis of iron-sulfur clusters in mammalian cells: new insights and relevance to human disease.Molecular modeling of the binding modes of the iron-sulfur protein to the Jac1 co-chaperone from Saccharomyces cerevisiae by all-atom and coarse-grained approaches

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

http://www.wikidata.org/entity/Q27660665

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2010 nî lūn-bûn

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2010 թուականի Ապրիլին հրատարակուած գիտական յօդուած

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2010 թվականի ապրիլին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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Structural Basis for Fe–S Clus ...... S Protein–Protein Interactions

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JOURNAL.PBIO.1000354

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Structural Basis for Fe–S Clus ...... S Protein–Protein Interactions

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Ariane Proteau

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Ismaïl Moukadiri

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Jean-François Trempe

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Linhua Zhang

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M Eugenia Armengod

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Magda Villarroya

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Rong Shi

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P2860

Genome sequence of enterohaemorrhagic Escherichia coli O157:H7

Cysteine desulfurase activity indicates a role for NIFS in metallocluster biosynthesis

PHENIX: a comprehensive Python-based system for macromolecular structure solution

ConSurf 2005: the projection of evolutionary conservation scores of residues on protein structures

PROCHECK: a program to check the stereochemical quality of protein structures

Processing of X-ray diffraction data collected in oscillation mode

Structure of a NifS homologue: X-ray structure analysis of CsdB, an Escherichia coli counterpart of mammalian selenocysteine lyase

The crystal structure of a sulfurtransferase from Azotobacter vinelandii highlights the evolutionary relationship between the rhodanese and phosphatase enzyme families

Crystal structure of human frataxin

Towards a structural understanding of Friedreich's ataxia: the solution structure of frataxin

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e1000354

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240527

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10.1371/JOURNAL.PBIO.1000354

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4

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Miroslaw Cygler

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2010-04-13T00:00:00Z

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43202286

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20404999

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IscS-IscU complex

IscS-TusA complex

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2854127

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