about
Iron sensing and regulation in Saccharomyces cerevisiae: Ironing out the mechanistic detailsA novel NADH kinase is the mitochondrial source of NADPH in Saccharomyces cerevisiaeThe iron metallome in eukaryotic organismsCellular factors required for protection from hyperoxia toxicity in Saccharomyces cerevisiae.The yeast iron regulatory proteins Grx3/4 and Fra2 form heterodimeric complexes containing a [2Fe-2S] cluster with cysteinyl and histidyl ligation.Monothiol CGFS glutaredoxins and BolA-like proteins: [2Fe-2S] binding partners in iron homeostasisCytosolic Fe-S Cluster Protein Maturation and Iron Regulation Are Independent of the Mitochondrial Erv1/Mia40 Import System.Redox properties of the disulfide bond of human Cu,Zn superoxide dismutase and the effects of human glutaredoxin 1Monothiol glutaredoxins and A-type proteins: partners in Fe-S cluster trafficking.The redox environment in the mitochondrial intermembrane space is maintained separately from the cytosol and matrixActivation of Cu,Zn-superoxide dismutase in the absence of oxygen and the copper chaperone CCS.The effects of glutaredoxin and copper activation pathways on the disulfide and stability of Cu,Zn superoxide dismutase.Functions and cellular compartmentation of the thioredoxin and glutathione pathways in yeast.Checks and balances for the iron bank.Human glutaredoxin 3 forms [2Fe-2S]-bridged complexes with human BolA2.The Myeloablative Drug Busulfan Converts Cysteine to Dehydroalanine and Lanthionine in Redoxins.Characterization of the metal receptor sites in Escherichia coli Zur, an ultrasensitive zinc(II) metalloregulatory protein.Extreme zinc-binding thermodynamics of the metal sensor/regulator protein, ZntR.The Escherichia coli BolA Protein IbaG Forms a Histidine-Ligated [2Fe-2S]-Bridged Complex with Grx4.Endoplasmic Reticulum Transport of Glutathione by Sec61 Is Regulated by Ero1 and Bip.Schizosaccharomyces pombe Grx4 regulates the transcriptional repressor Php4 via [2Fe-2S] cluster binding.Forging ahead: new mechanistic insights into iron biochemistry.Characterization of Glutaredoxin Fe–S Cluster-Binding Interactions Using Circular Dichroism SpectroscopyThe Ferric Uptake Regulation (Fur) Repressor Is a Zinc Metalloprotein†Iron-sulfur cluster signaling: The common thread in fungal iron regulationThe conserved CDC motif in the yeast iron regulator Aft2 mediates iron-sulfur cluster exchange and protein-protein interactions with Grx3 and Bol2
P50
Q26864824-E74BB00B-7627-4CD6-8C14-897BB404D653Q27937404-01002C00-5DEB-499D-BF77-592F03F45807Q28109405-D0761189-82F9-4783-84B0-452D1B8F521CQ31140322-D71AC4A3-3A83-4E01-B0D1-BC24A517ADF0Q35000114-40057E09-1BF7-4F06-B75E-4B21A8E4BF25Q36250073-E242ED04-78E0-40D0-8EC1-417A2B63981EQ36282929-BE4DCDFD-4FE2-4535-B96B-6BCBF4842391Q36497696-70F5E3A9-D349-4A63-A31E-783D0D0CFBD6Q36627228-0E781469-2753-4E02-8DFA-9FF34283900DQ36944848-36EFE6D7-BD20-45F3-AC85-164F82A123A4Q37372995-3F71C866-CD03-4DD5-9C61-EE9145484EACQ37375579-1D3C859A-3065-4F68-9B4C-348571FEEA9DQ38063935-6CB6152D-ED25-4FAB-9E85-A95FE213D109Q41685377-2F91E5DD-5AB0-46FB-8365-69BF8C779022Q41908918-144F4CFE-4FDD-4794-B880-BAC970773050Q42086998-6E8A216B-E013-4FB5-90A7-D733308265CAQ43720801-6C295372-8E91-4B1A-817D-0254FAA4B2E5Q43721952-437C3CF7-B176-4894-BF14-820C74E5F62FQ45841258-90B83726-3BFD-4ACF-8299-7F91F9F599E1Q47790181-65446903-84F2-4D9D-8C9F-759097374159Q50880981-791E7D8C-3B07-42E3-B7F0-001563D24128Q54053056-B9CCB45F-9FA7-4A40-B6DD-540E4ED487EEQ61758570-3D4705EC-5C0E-4662-AAE3-D1F5095F5512Q61758576-7D619900-4AAD-4F8E-9C65-9157616BF505Q90800993-9E443E86-1E6D-4BBB-85FB-2F31138F67A5Q93164052-B5E0B306-337F-484E-8917-6C29D964EF33
P50
description
hulumtuese
@sq
researcher
@en
wetenschapper
@nl
հետազոտող
@hy
name
Caryn E. Outten
@ast
Caryn E. Outten
@en
Caryn E. Outten
@es
Caryn E. Outten
@nl
Caryn E. Outten
@sl
type
label
Caryn E. Outten
@ast
Caryn E. Outten
@en
Caryn E. Outten
@es
Caryn E. Outten
@nl
Caryn E. Outten
@sl
prefLabel
Caryn E. Outten
@ast
Caryn E. Outten
@en
Caryn E. Outten
@es
Caryn E. Outten
@nl
Caryn E. Outten
@sl
P106
P1153
6602780095
P21
P31
P496
0000-0003-0335-6531