Functional reconstitution of mitochondrial Fe/S cluster synthesis on Isu1 reveals the involvement of ferredoxin
about
Mitochondrial Bol1 and Bol3 function as assembly factors for specific iron-sulfur proteins.Role of Nfu1 and Bol3 in iron-sulfur cluster transfer to mitochondrial clients.Mitochondrial Cysteine Desulfurase and ISD11 Coexpressed in Escherichia coli Yield Complex Containing Acyl Carrier ProteinThe Eukaryotic-Specific ISD11 Is a Complex-Orphan Protein with Ability to Bind the Prokaryotic IscSThe Human Iron-Sulfur Assembly Complex Catalyzes the Synthesis of [2Fe-2S] Clusters on ISCU2 That Can Be Transferred to Acceptor MoleculesFrataxin Accelerates [2Fe-2S] Cluster Formation on the Human Fe-S Assembly ComplexSynthesis, delivery and regulation of eukaryotic heme and Fe-S cluster cofactors.Protection of scaffold protein Isu from degradation by the Lon protease Pim1 as a component of Fe-S cluster biogenesis regulationArchitecture of the Yeast Mitochondrial Iron-Sulfur Cluster Assembly Machinery: THE SUB-COMPLEX FORMED BY THE IRON DONOR, Yfh1 PROTEIN, AND THE SCAFFOLD, Isu1 PROTEIN.Human Mitochondrial Ferredoxin 1 (FDX1) and Ferredoxin 2 (FDX2) Both Bind Cysteine Desulfurase and Donate Electrons for Iron-Sulfur Cluster Biosynthesis.NqrM (DUF539) Protein Is Required for Maturation of Bacterial Na+-Translocating NADH:Quinone OxidoreductaseInvestigating the role(s) of SufT and the domain of unknown function 59 (DUF59) in the maturation of iron-sulfur proteins.Posttranslational control of the scaffold for Fe-S cluster biogenesis as a compensatory regulatory mechanism.Frataxin inactivation leads to steroid deficiency in flies and human ovarian cells.Mitochondria and Iron: current questions.Iron-sulfur cluster biogenesis and trafficking in mitochondria.Architecture of the Human Mitochondrial Iron-Sulfur Cluster Assembly MachineryEvolutionary conservation and in vitro reconstitution of microsporidian iron-sulfur cluster biosynthesis.Iron-sulfur cluster exchange reactions mediated by the human Nfu protein.Mitochondrial Ferredoxin Determines Vulnerability of Cells to Copper Excess.Structure and functional dynamics of the mitochondrial Fe/S cluster synthesis complex.The Oxidation State of [4Fe4S] Clusters Modulates the DNA-Binding Affinity of DNA Repair Proteins.Biallelic mutations in the ferredoxin reductase gene cause novel mitochondriopathy with optic atrophy.In vitro characterization of a novel Isu homologue from Drosophila melanogaster for de novo FeS-cluster formation.A novel de novo dominant mutation in ISCU associated with mitochondrial myopathy.Structure of human Fe-S assembly subcomplex reveals unexpected cysteine desulfurase architecture and acyl-ACP-ISD11 interactions.Iron-sulfur cluster biosynthesis and trafficking - impact on human disease conditions.Protein networks in the maturation of human iron-sulfur proteins.Molecular chaperones involved in mitochondrial iron-sulfur protein biogenesis.Respiratory Chain Supercomplexes associate with the Cysteine Desulfurase Complex of the Iron-Sulfur Cluster Assembly Machinery.FDXR Mutations Cause Sensorial Neuropathies and Expand the Spectrum of Mitochondrial Fe-S-Synthesis Diseases.Cysteine desulfurase is regulated by phosphorylation of Nfs1 in yeast mitochondria.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.Interactions of iron-bound frataxin with ISCU and ferredoxin on the cysteine desulfurase complex leading to Fe-S cluster assembly.The NMR contribution to protein-protein networking in Fe-S protein maturation.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.NMR as a Tool to Investigate the Processes of Mitochondrial and Cytosolic Iron-Sulfur Cluster Biosynthesis
P2860
Q27937154-904704FC-A1FB-4096-9AA4-6EF43BB7634AQ27939764-0CC4487C-3E2F-4B99-9C15-87DD07191A67Q33600999-C2B5D23A-4DB7-421A-93D7-32AB11702E95Q36079884-69287A9A-707A-474B-82AF-58AE08CA3300Q36362583-BB1CC438-EA9F-4F09-AB89-35E4ED1C049EQ36362588-CB93BAD1-7536-49F5-A30F-DC6AAA4678BFQ36667724-D6A39657-65B4-4EF6-85EF-A670FB869582Q36746171-F73C3801-39A1-4430-AAEB-6DF85336F7C5Q36876269-5B018910-D27E-4E9F-8F76-1C96676F6A6DQ37607678-2FE17AE0-F732-4D6E-94B9-8A4AB7FB3461Q38386495-FE128B06-5DA2-4A59-A70E-0ECE48D5E168Q38673933-6626F8AC-8540-4F25-8B5B-71943C217DA3Q38849570-1A7C54BD-6C0B-4BB7-9AEE-5F0BA0A13D4BQ38915798-32CF8FF7-CE85-407A-848D-3AC8FB4F693FQ39027015-7902D56D-5AF0-4A94-94B0-6DF3A6DA00A5Q39374100-6E85FA82-BC44-42FD-BD67-9AC609417EB5Q39756930-B74758E2-BBD5-44AE-BDC9-1D5EB04DAC50Q40832998-7729AD84-1C8D-4269-8D20-A613A7DD1AFAQ41646103-905C9746-93AD-4219-8714-52914DADD58DQ42640010-0797ECBF-6BBA-42F1-A0DA-C0246CBDC35BQ45809936-CE351D21-1811-49D9-B650-F370A8B582F4Q46145452-F92D2702-8309-483D-BAAB-FA3CBCB87148Q46282814-0E8E3849-849E-4056-AB28-4DBEE5836208Q47071253-DD9A3728-24B0-4C18-BDB1-537627C31FD7Q47146900-2E2FB394-1C5F-4E32-9300-DD716DB7F1FBQ47159422-D692E79A-44A2-4B73-9C8E-8CEE990699BAQ47189249-10510779-A4C3-4AE9-8272-157D29B77AE3Q47316088-56D62732-5A8A-49D1-9356-B269C9CD8725Q47417903-FC6FB7F5-C4C5-44D9-A789-8D310B443B4CQ47642148-E443350B-1D72-4FA0-B5F8-D1BC184C6363Q47719193-04146B22-33D0-43E0-BF9F-5DF71F97E4A9Q47755054-B639ED57-E2AF-4562-8987-54FE9D7266CEQ47923323-E4BAE506-094A-4542-94FF-BBC35982AE9BQ50181987-F94771B2-F664-48A1-BCC8-BDCA224D7026Q52342683-996F81FE-9C1E-46BC-A0C4-E58C0E492130Q52641197-0ACAEB3C-9C06-4738-9568-AAC967F7C520Q55689317-F479AD32-F5F2-4DED-B115-0E0E8CBC5365Q58778523-F1B3A579-4D2B-4284-BB3A-44AB218F7283
P2860
Functional reconstitution of mitochondrial Fe/S cluster synthesis on Isu1 reveals the involvement of ferredoxin
description
2014 nî lūn-bûn
@nan
2014 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2014 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2014年の論文
@ja
2014年論文
@yue
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
Functional reconstitution of m ...... the involvement of ferredoxin
@ast
Functional reconstitution of m ...... the involvement of ferredoxin
@en
Functional reconstitution of m ...... the involvement of ferredoxin
@nl
type
label
Functional reconstitution of m ...... the involvement of ferredoxin
@ast
Functional reconstitution of m ...... the involvement of ferredoxin
@en
Functional reconstitution of m ...... the involvement of ferredoxin
@nl
prefLabel
Functional reconstitution of m ...... the involvement of ferredoxin
@ast
Functional reconstitution of m ...... the involvement of ferredoxin
@en
Functional reconstitution of m ...... the involvement of ferredoxin
@nl
P2093
P2860
P50
P3181
P356
P1476
Functional reconstitution of m ...... the involvement of ferredoxin
@en
P2093
Holger Webert
Sven-Andreas Freibert
Torsten Heidenreich
P2860
P2888
P3181
P356
10.1038/NCOMMS6013
P407
P577
2014-10-31T00:00:00Z
P6179
1002625481