Mutation in the Fe-S scaffold protein Isu bypasses frataxin deletion. - Wikidata - awgldk - TriplyDB

Mutation in the Fe-S scaffold protein Isu bypasses frataxin deletion.

Mutation in the Fe-S scaffold protein Isu bypasses frataxin deletion.

http://www.wikidata.org/entity/Q33601694

about

Iron and sulfur in proteins. How does the cell build Fe-S clusters, cofactors essential for life?Understanding the genetic and molecular pathogenesis of Friedreich's ataxia through animal and cellular models Protein stability and dynamics modulation: the case of human frataxin Turning Escherichia coli into a Frataxin-Dependent Organism Frataxin-bypassing Isu1: characterization of the bypass activity in cells and mitochondria Fe-S cluster biogenesis in isolated mammalian mitochondria: coordinated use of persulfide sulfur and iron and requirements for GTP, NADH, and ATP.Turning Saccharomyces cerevisiae into a Frataxin-Independent Organism.A Yeast/Drosophila Screen to Identify New Compounds Overcoming Frataxin Deficiency Coming into view: eukaryotic iron chaperones and intracellular iron delivery.Biogenesis of the cytochrome bc(1) complex and role of assembly factors.Crystal Structure of Bacillus subtilis Cysteine Desulfurase SufS and Its Dynamic Interaction with Frataxin and Scaffold Protein SufU.Iron-sulfur cluster synthesis, iron homeostasis and oxidative stress in Friedreich ataxia.The iron-sulfur cluster assembly machineries in plants: current knowledge and open questions.Frataxin directly stimulates mitochondrial cysteine desulfurase by exposing substrate-binding sites, and a mutant Fe-S cluster scaffold protein with frataxin-bypassing ability acts similarly Apn1 AP-endonuclease is essential for the repair of oxidatively damaged DNA bases in yeast frataxin-deficient cells.Human mitochondrial ferritin improves respiratory function in yeast mutants deficient in iron-sulfur cluster biogenesis, but is not a functional homologue of yeast frataxin.Structure and functional dynamics of the mitochondrial Fe/S cluster synthesis complex.A dynamic model of the proteins that form the initial iron-sulfur cluster biogenesis machinery in yeast mitochondria.ISCU(M108I) and ISCU(D39V) Differ from Wild-Type ISCU in Their Failure To Form Cysteine Desulfurase Complexes Containing Both Frataxin and Ferredoxin.Mechanisms of iron and copper-frataxin interactions.Life without Fe-S clusters.Interactions of iron-bound frataxin with ISCU and ferredoxin on the cysteine desulfurase complex leading to Fe-S cluster assembly.Identification of p38 MAPK as a novel therapeutic target for Friedreich's ataxia.Zinc(II) binding on human wild-type ISCU and Met140 variants modulates NFS1 desulfurase activity NMR as a Tool to Investigate the Processes of Mitochondrial and Cytosolic Iron-Sulfur Cluster Biosynthesis

P2860

Q26829187-E6F8EE12-BB19-450E-8328-1357B9E3D6AA Q26860523-B7602A3D-E723-4E93-9326-141F7F2FBD9B Q28484035-7E836C66-E923-4A96-8B4C-57F0F5319C44 Q28547414-18605E4E-4C06-44FA-AA98-FC25AF03DEB3 Q33613466-BB8D168E-473E-4FD0-92DC-6F4284508403 Q34801755-504172AD-D3DD-48D8-9CA5-221F276960AB Q35634573-71142205-4FE6-4A07-BAB3-8C226C833CE1 Q35828968-3FC751DD-EAF5-45AA-8F1F-A0D9D18CFA28 Q35922222-29284DDF-B4BC-455D-A676-95B47F777589 Q36005582-EB6AD750-02CA-4A4E-80A1-7F806AA8D159 Q36068749-4871A3F1-94DD-4AD4-AF03-BC54C8A0EE63 Q36488119-DD691446-0F1D-45B7-ACDE-1BE6A7060094 Q37040353-637C796A-7848-4BFD-88CD-25AE0E34F04A Q37415565-B96ADBF3-620F-4342-A543-AE1C39F54F48 Q41974951-ED82F4E7-4E09-41A7-AA8D-2A33B0506E76 Q42321003-D264F13A-033A-4866-9E20-5397AB1D614B Q45809936-0D230822-29EC-4D16-BB06-90275D082A56 Q46481763-E961EC13-2C23-4EE3-90F8-17343A9BD3D1 Q50181987-139F4584-20F0-4426-A693-0EFF9EAF6487 Q50606747-DD887DC6-A388-4CA8-A854-B1F500BFCE6F Q51574838-9382E491-C840-4941-9E78-FB532F42F8BB Q52342683-CC603AF2-3BD5-48DC-83C9-1BEC9A4630AB Q52641744-6CF3881B-0B43-487E-B0F7-611F821EFD15 Q58777980-27A0AA25-CFEE-400C-94F1-58D3B80A9F54 Q58778523-EC7A10E3-7737-411F-9CC9-41E446D90909

P2860

Mutation in the Fe-S scaffold protein Isu bypasses frataxin deletion.

http://www.wikidata.org/entity/Q33601694

description

2012 nî lūn-bûn

@nan

2012 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

name

Mutation in the Fe-S scaffold protein Isu bypasses frataxin deletion.

@ast

Mutation in the Fe-S scaffold protein Isu bypasses frataxin deletion.

@en

type

label

Mutation in the Fe-S scaffold protein Isu bypasses frataxin deletion.

@ast

Mutation in the Fe-S scaffold protein Isu bypasses frataxin deletion.

@en

prefLabel

Mutation in the Fe-S scaffold protein Isu bypasses frataxin deletion.

@ast

Mutation in the Fe-S scaffold protein Isu bypasses frataxin deletion.

@en

P1433

Q33601694-E91B2A81-3A9B-4A92-B737-C3323361E299

P1476

Q33601694-BC6A21B8-4414-4C1E-9CCA-65EA58B2D408

P2093

Q33601694-127BCE66-EC74-4709-88BB-CC61824C15F9

Q33601694-1B2719BD-81F8-4FEF-88B8-1825BD637263

Q33601694-52BD44E3-4B46-464A-B48E-D91A82F8C9AF

Q33601694-845CD5DE-F6C8-4362-87D8-C337F0BA6137

Q33601694-896B8A39-6489-40F4-8BC5-4F6A6715005A

Q33601694-9B627AF8-A8E8-4A2B-8C6B-364F886E709C

Q33601694-CC5CF4EE-A1B8-4262-8261-806C683F5DC1

Q33601694-FDC19528-48A0-4E01-A933-8CC83F70B2F3

P2860

Q33601694-041DF2EE-77E2-476E-8C83-B18B1790C9A4

Q33601694-0C4CFCB1-DAA7-45BE-BD1F-7EABA1807D37

Q33601694-1CEEE75C-7B5C-4E80-A919-179124EB03CB

Q33601694-1E71599A-5DDE-4DA8-881A-1AA12E19AE6E

Q33601694-287CFC3A-82E1-489F-B528-747E0E0D6DAC

Q33601694-29F2A7BF-C125-4D6C-8A66-E809002BD8B1

Q33601694-2F2123A7-B886-4ED0-9BBB-D85EC8FEDD07

Q33601694-2F5250FA-9E09-495D-A661-1305DFCDF0BA

Q33601694-32F55493-5F81-4490-A407-8B34BEC04A8D

Q33601694-5352E67E-13E3-4692-9A88-964BC2899712

P304

Q33601694-9702946B-B08D-42EA-9624-6D04FB8E9A35

P31

Q33601694-F7C4759A-7875-454A-B3B8-28ABE4A4187E

P356

Q33601694-BC48A056-B998-4DAF-837F-69C82660F436

P407

Q33601694-35820BA9-8BDC-4E93-BA70-1293D7A045E7

P433

Q33601694-6F56B224-22B1-43F4-A010-391950AB55DD

P478

Q33601694-9B00968D-4430-4154-AD26-8076C0353021

P577

Q33601694-EE4463C2-F7DC-48E3-8E7F-51503257739D

P698

Q33601694-A8318D18-511F-42F6-97EA-744CA0BC5CCB

P932

Q33601694-127C706C-2C74-4DEA-99DD-DEC993756BD4

P356

P1433

Biochemical Journal

P1476

Mutation in the Fe-S scaffold protein Isu bypasses frataxin deletion.

@en

P2093

Andrew Dancis

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

Debkumar Pain

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

Elise R Lyver

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

Emmanuel Lesuisse

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

Heeyong Yoon

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

Jason E Donald

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

Jayashree Pain

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

Ramesh Golla

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

P2860

Human iron-sulfur cluster assembly, cellular iron homeostasis, and disease

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

Additional modules for versatile and economical PCR-based gene deletion and modification in Saccharomyces cerevisiae

Regulation of mitochondrial iron accumulation by Yfh1p, a putative homolog of frataxin

Respiratory deficiency due to loss of mitochondrial DNA in yeast lacking the frataxin homologue

Purification and properties of coproporphyrinogen oxidase from the yeast Saccharomyces cerevisiae

An interaction between frataxin and Isu1/Nfs1 that is crucial for Fe/S cluster synthesis on Isu1.

Human frataxin is an allosteric switch that activates the Fe-S cluster biosynthetic complex

Bacterial frataxin CyaY is the gatekeeper of iron-sulfur cluster formation catalyzed by IscS

Localization and functionality of microsporidian iron-sulphur cluster assembly proteins

P304

473-480

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

P31

scholarly article

P356

10.1042/BJ20111637

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

P407

P433

1

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

P478

441

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

P577

2012-01-01T00:00:00Z

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

P698

21936771

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

P932

4018837

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