About: Caryn E. Outten

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Biochemistry and Molecular Biology researcher

Attributes	Values
rdf:type	Item
description	forskare (sv) 연구원 (ko) গবেষক (bn) 研究者 (ja) araştırmacı (tr) wetenschapper (nl) дослідниця (uk) изилдөөчү (ky) 研究者 (zh) հետազոտող (hy) hulumtuese (sq) Biochemistry and Molecular Biology researcher (en)
rdfs:label	Caryn E. Outten (en) Caryn E. Outten (es) Caryn E. Outten (nl) Caryn E. Outten (sl) Caryn E. Outten (ast)
skos:prefLabel	Caryn E. Outten (en) Caryn E. Outten (es) Caryn E. Outten (nl) Caryn E. Outten (sl) Caryn E. Outten (ast)
name	Caryn E. Outten (en) Caryn E. Outten (es) Caryn E. Outten (nl) Caryn E. Outten (sl) Caryn E. Outten (ast)
Scopus author ID	wds:Q41908969-8FCBD907-06F5-4930-8017-790ED5E4E1C0
Scopus author ID	6602780095
given name	wds:Q41908969-163BB3F8-0DA9-4F5E-96C5-32E10530884B
given name	Caryn
instance of	wds:Q41908969-5EE95247-425A-40F1-961C-0F425D28C1C6
instance of	Homo sapiens
award received	wds:Q41908969-5234cbb3-4060-bbcf-0696-e6e297fd159a
award received	Fellow of the American Association for the Advancement of Science
skos:altLabel	Caryn Elizabeth Outten (en) Caryn Outten (en)
occupation	wds:Q41908969-D8065B67-C206-4F83-BD85-7204A4CCBEF1
employer	wds:Q41908969-7C72D9DE-788F-46DB-85D6-55F127A40614 wds:Q41908969-8C384008-0130-464C-B0B4-8F4DC3FF2820 wds:Q41908969-C9D0DD02-5DC2-463B-BA73-0045ECB823C1
X username	wds:Q41908969-A86A65EF-D333-4B93-85D1-9E6888A2C8D0
sex or gender	wds:Q41908969-F6B9C18E-03B9-47B0-8970-3DA7DE03D6E4
educated at	wds:Q41908969-9E2874B7-997F-4F34-BB40-630697729300 wds:Q41908969-E2C0E781-A030-4A14-ADDC-3E8360EC3A80 wds:Q41908969-E8F05369-7DDB-4F18-98DF-1BD12BC94BE0
family name	wds:Q41908969-FEA08C6E-8A61-4697-A6A9-0AB884852DA8
occupation	researcher
employer	University of South Carolina
X username	CarynOutten
sex or gender	female organism
educated at	Northwestern University College of William & Mary Johns Hopkins University
family name	Outten
ORCID iD	wds:Q41908969-436CF135-A2FB-48E0-90D8-B3C7A90BC332
ORCID iD	https://orcid.org/0000-0003-0335-6531
ORCID iD	0000-0003-0335-6531
ResearcherID	wds:Q41908969-892A56AC-37F1-40F4-A191-2B368069911F
ResearcherID	I-9433-2019
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q41908969
is author of	Identification of FRA1 and FRA2 as genes involved in regulating the yeast iron regulon in response to decreased mitochondrial iron-sulfur cluster synthesis A novel NADH kinase is the mitochondrial source of NADPH in Saccharomyces cerevisiae Characterization of the metal receptor sites in Escherichia coli Zur, an ultrasensitive zinc(II) metalloregulatory protein. Molecular basis of metal-ion selectivity and zeptomolar sensitivity by CueR Femtomolar sensitivity of metalloregulatory proteins controlling zinc homeostasis The iron metallome in eukaryotic organisms Histidine 103 in Fra2 is an iron-sulfur cluster ligand in the [2Fe-2S] Fra2-Grx3 complex and is required for in vivo iron signaling in yeast The yeast iron regulatory proteins Grx3/4 and Fra2 form heterodimeric complexes containing a [2Fe-2S] cluster with cysteinyl and histidyl ligation. The redox environment in the mitochondrial intermembrane space is maintained separately from the cytosol and matrix A new zinc-protein coordination site in intracellular metal trafficking: solution structure of the Apo and Zn(II) forms of ZntA(46-118) Functions and cellular compartmentation of the thioredoxin and glutathione pathways in yeast. Monothiol CGFS glutaredoxins and BolA-like proteins: [2Fe-2S] binding partners in iron homeostasis The Ferric Uptake Regulation (Fur) Repressor Is a Zinc Metalloprotein† Monothiol glutaredoxins and A-type proteins: partners in Fe-S cluster trafficking Human glutaredoxin 3 forms [2Fe-2S]-bridged complexes with human BolA2. Molecular mechanism and structure of the Saccharomyces cerevisiae iron regulator Aft2 Activation 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 Extreme zinc-binding thermodynamics of the metal sensor/regulator protein, ZntR. Iron sensing and regulation in Saccharomyces cerevisiae: Ironing out the mechanistic details Redox properties of the disulfide bond of human Cu,Zn superoxide dismutase and the effects of human glutaredoxin 1 Forging ahead: new mechanistic insights into iron biochemistry. Cellular factors required for protection from hyperoxia toxicity in Saccharomyces cerevisiae Endoplasmic Reticulum Transport of Glutathione by Sec61 Is Regulated by Ero1 and Bip. Structure of the thioredoxin-like domain of yeast glutaredoxin 3 The Escherichia coli BolA Protein IbaG Forms a Histidine-Ligated [2Fe-2S]-Bridged Complex with Grx4. Schizosaccharomyces pombe Grx4 regulates the transcriptional repressor Php4 via [2Fe-2S] cluster binding. Checks and balances for the iron bank. Cytosolic Fe-S Cluster Protein Maturation and Iron Regulation Are Independent of the Mitochondrial Erv1/Mia40 Import System. Characterization of Glutaredoxin Fe–S Cluster-Binding Interactions Using Circular Dichroism Spectroscopy Iron-sulfur cluster signaling: The common thread in fungal iron regulation The Myeloablative Drug Busulfan Converts Cysteine to Dehydroalanine and Lanthionine in Redoxins The conserved CDC motif in the yeast iron regulator Aft2 mediates iron-sulfur cluster exchange and protein-protein interactions with Grx3 and Bol2
is author of	wds:Q27935816-14E9F2AE-70E5-43DD-A58A-99E0B76E29DC wds:Q54053056-B9CCB45F-9FA7-4A40-B6DD-540E4ED487EE wds:Q27641964-DE63F6EE-D6C7-4798-BDA4-DA8A4E8B6400 wds:Q27651590-B9C0AA0A-69C2-460C-AD04-806DE329D787 wds:Q29615199-117EDBD6-6336-40F6-B0C7-2BF81E9B4BC0

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