about
A genomic survey of the fish parasite Spironucleus salmonicida indicates genomic plasticity among diplomonads and significant lateral gene transfer in eukaryote genome evolutionRole of human mitochondrial Nfs1 in cytosolic iron-sulfur protein biogenesis and iron regulationGlutaredoxin 5 deficiency causes sideroblastic anemia by specifically impairing heme biosynthesis and depleting cytosolic iron in human erythroblastsA role for IOP1 in mammalian cytosolic iron-sulfur protein biogenesisThe essential WD40 protein Cia1 is involved in a late step of cytosolic and nuclear iron-sulfur protein assembly.The eukaryotic P loop NTPase Nbp35: an essential component of the cytosolic and nuclear iron-sulfur protein assembly machineryPhytochemical modulators of mitochondria: the search for chemopreventive agents and supportive therapeuticsHuman iron-sulfur cluster assembly, cellular iron homeostasis, and diseaseWhy chloroplasts and mitochondria retain their own genomes and genetic systems: Colocation for redox regulation of gene expressionThe role of mitochondria in cellular iron-sulfur protein biogenesis: mechanisms, connected processes, and diseasesBattles with iron: manganese in oxidative stress protectionFunctional, structural, and spectroscopic characterization of a glutathione-ligated [2Fe-2S] cluster in poplar glutaredoxin C1Structure of Human J-type Co-chaperone HscB Reveals a Tetracysteine Metal-binding DomainStructural Changes during Cysteine Desulfurase CsdA and Sulfur Acceptor CsdE Interactions Provide Insight into the trans -PersulfurationRole of essential genes in mitochondrial morphogenesis in Saccharomyces cerevisiae.Essential role of Isd11 in mitochondrial iron-sulfur cluster synthesis on Isu scaffold proteins.Thio modification of yeast cytosolic tRNA is an iron-sulfur protein-dependent pathway.A genomewide screen reveals a role of mitochondria in anaerobic uptake of sterols in yeast.Nonredundant roles of mitochondria-associated F-box proteins Mfb1 and Mdm30 in maintenance of mitochondrial morphology in yeast.Assessing systems properties of yeast mitochondria through an interaction map of the organelleProteomic analysis of the yeast mitochondrial outer membrane reveals accumulation of a subclass of preproteinsMitochondrial Iba57p is required for Fe/S cluster formation on aconitase and activation of radical SAM enzymes.The ISC [corrected] proteins Isa1 and Isa2 are required for the function but not for the de novo synthesis of the Fe/S clusters of biotin synthase in Saccharomyces cerevisiae.The Nfs1 interacting protein Isd11 has an essential role in Fe/S cluster biogenesis in mitochondria.Stimulation of the ATPase activity of the yeast mitochondrial ABC transporter Atm1p by thiol compounds.Biogenesis of cytosolic ribosomes requires the essential iron-sulphur protein Rli1p and mitochondria.Oxidative stress and the homeodynamics of iron metabolismInduction of oxidative metabolism by mitochondrial frataxin inhibits cancer growth: Otto Warburg revisitedDual localized AtHscB involved in iron sulfur protein biogenesis in ArabidopsisReconstruction and evaluation of the synthetic bacterial MEP pathway in Saccharomyces cerevisiaeReduced expression of mitochondrial frataxin in mice exacerbates diet-induced obesityRNA silencing of mitochondrial m-Nfs1 reduces Fe-S enzyme activity both in mitochondria and cytosol of mammalian cellsMitoferrin is essential for erythroid iron assimilationIscR acts as an activator in response to oxidative stress for the suf operon encoding Fe-S assembly proteins.In silico pathway reconstruction: Iron-sulfur cluster biogenesis in Saccharomyces cerevisiae.Effects of the deletion of the Escherichia coli frataxin homologue CyaY on the respiratory NADH:ubiquinone oxidoreductaseFrom endosymbiont to host-controlled organelle: the hijacking of mitochondrial protein synthesis and metabolismThe structure and function of frataxin.Nitric oxide and frataxin: two players contributing to maintain cellular iron homeostasis.Increased levels of reduced cytochrome b and mitophagy components are required to trigger nonspecific autophagy following induced mitochondrial dysfunction
P2860
Q21093368-3E7B73CA-DD9A-4439-BC6A-9C4FAB95DDFDQ24297460-7D61F64C-F25F-41EA-9E39-EFF9E79103ADQ24305534-C937AD08-4803-4F11-9E7C-A252A9458B7FQ24313143-7EE45B9D-4BAA-4E33-A60C-4570DE65D6C1Q24535003-D2D21CD1-7146-459B-85CE-1DFBFCB1A18FQ24556514-2663CE53-07DC-4953-AF27-101F408F296FQ24562914-3DD09F81-23D8-4CBF-B28E-64F941F21723Q24634143-F15BF448-26D3-4C50-B02E-6056260B8B75Q26796678-819B5837-6347-4FF9-9C60-1B036747C22FQ26865882-0FF2755F-0B69-4EFF-9285-D0565CB8EE96Q27025367-4DC3EC45-E27B-42D4-9789-0F449C2C508AQ27644610-65877F3B-EECC-45CA-96F4-93E577B55381Q27651682-E0F5A6A7-DD66-4477-8577-55F8707DFECDQ27679365-923EAADA-B09A-4E5B-92E7-2A194EAD35F1Q27933698-BBD34794-187B-4852-B569-2A266A89E086Q27934369-C23597C8-19C5-46A3-B29B-E447B0B880B4Q27934633-F6D1A956-9866-414B-A88B-5BA48A1B35CEQ27936829-E171FB6A-51DD-401C-86F8-37E5454DE12AQ27936897-F1385082-9EAF-4219-A504-C466E86BD9E2Q27937134-56E3A295-6076-4D98-9D6E-66D552678B87Q27937249-93452C34-CE4D-4635-B6B2-56CF5836ADCEQ27937403-CF10C70F-D4E0-4154-8737-FE4DD9240640Q27938255-BD37DF1B-BFC8-440F-9BE2-124CE46663D1Q27938366-FBEB8F14-B4CC-4ED0-B471-B1F2B47515C2Q27938803-D54D0855-A76E-49D7-A2EA-A0AC54C8EB82Q27939225-EAB85E01-D281-4FB2-8DFF-184D270F4371Q28082925-BD2EC5FA-8F59-43F6-A7BB-C319F6D7311CQ28279921-3B2B6DF5-AE5F-493D-A9CD-BE1724C9E2CBQ28471663-DD2E2F47-989F-40C5-9EE1-2A48D094BD33Q28484642-A42C9CAB-1284-4595-AB13-1F3E4C976ED5Q28511723-49415E0E-4B58-4E5F-A6B1-4E34156BDFE8Q28586228-F232ADD9-ED78-495D-AAF4-D4FAD5EAB974Q28587125-769DE94E-2C5E-4F1A-BB25-5FFECB551F1AQ33249072-4F3CFCE4-EBEF-43CC-BB01-5D44B831C7CFQ33281129-3FE19DB2-D0D1-403C-8B8C-1DAEA87E4EA3Q33291592-CEEC2A96-C1AD-4FBA-BFB2-4AA281EBDA89Q33305008-48CB92BF-2187-4D2F-9FF8-6A5D66EDAD99Q33808205-74E1F7D2-3F0D-4523-ACE3-5231078BFA46Q33811450-66658A0B-AF81-471B-9F33-B669549C03D2Q33818093-1AC910FC-DD13-4D8A-AFEA-55618D7AA0B7
P2860
description
2005 nî lūn-bûn
@nan
2005 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի մարտին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Iron-sulfur-protein biogenesis in eukaryotes.
@ast
Iron-sulfur-protein biogenesis in eukaryotes.
@en
Iron-sulfur-protein biogenesis in eukaryotes.
@nl
type
label
Iron-sulfur-protein biogenesis in eukaryotes.
@ast
Iron-sulfur-protein biogenesis in eukaryotes.
@en
Iron-sulfur-protein biogenesis in eukaryotes.
@nl
prefLabel
Iron-sulfur-protein biogenesis in eukaryotes.
@ast
Iron-sulfur-protein biogenesis in eukaryotes.
@en
Iron-sulfur-protein biogenesis in eukaryotes.
@nl
P1476
Iron-sulfur-protein biogenesis in eukaryotes.
@en
P2093
Ulrich Mühlenhoff
P304
P356
10.1016/J.TIBS.2005.01.006
P50
P577
2005-03-01T00:00:00Z