Caryn E. Outten

发表

Femtomolar Sensitivity of Metalloregulatory Proteins Controlling Zinc Homeostasis

C. Outten, and Thomas V. O'Halloran, Caryn E. Outten, 2001, Science.

Molecular Basis of Metal-Ion Selectivity and Zeptomolar Sensitivity by CueR

A. Mondragón, T. O’Halloran, C. Outten, 2003, Science.

Transcriptional Activation of an Escherichia coliCopper Efflux Regulon by the Chromosomal MerR Homologue, CueR*

T. O’Halloran, F. W. Outten, C. Outten, 2000, The Journal of Biological Chemistry.

The iron metallome in eukaryotic organisms.

C. Outten, Caryn E. Outten, Adrienne C. Dlouhy, 2013, Metal ions in life sciences.

The Redox Environment in the Mitochondrial Intermembrane Space Is Maintained Separately from the Cytosol and Matrix*

Lixue Dong, C. Outten, Caryn E. Outten, 2008, Journal of Biological Chemistry.

Functions and cellular compartmentation of the thioredoxin and glutathione pathways in yeast.

A. Delaunay-Moisan, Caryn E. Outten, Aeid Igbaria, 2013, Antioxidants & redox signaling.

Activation of Cu,Zn-Superoxide Dismutase in the Absence of Oxygen and the Copper Chaperone CCS*

P. Hart, L. T. Jensen, V. Culotta, 2009, The Journal of Biological Chemistry.

A novel NADH kinase is the mitochondrial source of NADPH in Saccharomyces cerevisiae

V. Culotta, C. Outten, Valeria C Culotta, 2003, The EMBO journal.

Redox properties of the disulfide bond of human Cu,Zn superoxide dismutase and the effects of human glutaredoxin 1.

P. Hart, C. Outten, Caryn E. Outten, 2012, The Biochemical journal.

Extreme zinc-binding thermodynamics of the metal sensor/regulator protein, ZntR.

T. O’Halloran, Y. Hitomi, C. Outten, 2001, Journal of the American Chemical Society.

Monothiol CGFS glutaredoxins and BolA-like proteins: [2Fe-2S] binding partners in iron homeostasis.

C. Outten, Caryn E. Outten, Haoran Li, 2012, Biochemistry.

DNA Distortion Mechanism for Transcriptional Activation by ZntR, a Zn(II)-responsive MerR Homologue in Escherichia coli *

T. O’Halloran, F. W. Outten, C. Outten, 1999, The Journal of Biological Chemistry.

The Effects of Glutaredoxin and Copper Activation Pathways on the Disulfide and Stability of Cu,Zn Superoxide Dismutase*

W. Watson, P. Hart, L. T. Jensen, 2006, Journal of Biological Chemistry.

Alternative Start Sites in the Saccharomyces cerevisiae GLR1 Gene Are Responsible for Mitochondrial and Cytosolic Isoforms of Glutathione Reductase*

V. Culotta, C. Outten, Valeria C Culotta, 2004, Journal of Biological Chemistry.

Identification of FRA1 and FRA2 as Genes Involved in Regulating the Yeast Iron Regulon in Response to Decreased Mitochondrial Iron-Sulfur Cluster Synthesis*

D. Winge, E. M. Adkins, A. Kumánovics, 2008, Journal of Biological Chemistry.

The conserved CDC motif in the yeast iron regulator Aft2 mediates iron–sulfur cluster exchange and protein–protein interactions with Grx3 and Bol2

C. Outten, Caryn E. Outten, Haoran Li, 2019, JBIC Journal of Biological Inorganic Chemistry.

Iron sensing and regulation in Saccharomyces cerevisiae: Ironing out the mechanistic details.

C. Outten, Caryn E. Outten, Angela-Nadia Albetel, 2013, Current opinion in microbiology.

Cytosolic Fe-S Cluster Protein Maturation and Iron Regulation Are Independent of the Mitochondrial Erv1/Mia40 Import System*

J. Balk, J. Barycki, Caryn E. Outten, 2015, The Journal of Biological Chemistry.

Cytosolic FeS Cluster Protein Maturation and Iron Regulation Are Independent of the Mitochondrial Erv 1 / Mia 40 Import System *

J. Balk, J. Barycki, C. Outten, 2017 .

The yeast iron regulatory proteins Grx3/4 and Fra2 form heterodimeric complexes containing a [2Fe-2S] cluster with cysteinyl and histidyl ligation.

B. Hoffman, S. Naik, B. Huynh, 2009, Biochemistry.

Monothiol glutaredoxins and A-type proteins: partners in Fe-S cluster trafficking.

N. Rouhier, Bo Zhang, Michael K. Johnson, 2013, Dalton transactions.

Endoplasmic Reticulum Transport of Glutathione by Sec61 Is Regulated by Ero1 and Bip.

J. Winther, B. D'Autréaux, Samia Miled, 2017, Molecular cell.

A new zinc-protein coordination site in intracellular metal trafficking: solution structure of the Apo and Zn(II) forms of ZntA(46-118).

I. Bertini, T. O’Halloran, L. Banci, 2002, Journal of molecular biology.

Schizosaccharomyces pombe Grx4 regulates the transcriptional repressor Php4 via [2Fe-2S] cluster binding.

J. Beaudoin, S. Labbé, C. Outten, 2017, Metallomics.

Iron homeostasis proteins Grx4 and Fra2 control activity of the Schizosaccharomyces pombe iron repressor Fep1 by facilitating [2Fe-2S] cluster removal

S. Labbé, Ariane Brault, Caryn E. Outten, 2023, The Journal of biological chemistry.

Iron-Sulfur Cluster Biogenesis, Trafficking, and Signaling: Roles for CGFS Glutaredoxins and BolA Proteins.

C. Outten, Caryn E. Outten, Evan Talib, 2020, Biochimica et biophysica acta. Molecular cell research.

Iron-sulfur cluster signaling: The common thread in fungal iron regulation.

C. Outten, Caryn E. Outten, Malini Gupta, 2020, Current opinion in chemical biology.

The Escherichia coli BolA Protein IbaG Forms a Histidine-Ligated [2Fe-2S]-Bridged Complex with Grx4.

Bo Zhang, Michael K. Johnson, Sajini Randeniya, 2016, Biochemistry.

Molecular mechanism and structure of the Saccharomyces cerevisiae iron regulator Aft2

Chuan He, James R. Hinshaw, R. Sanishvili, 2014, Proceedings of the National Academy of Sciences.

Human glutaredoxin 3 forms [2Fe-2S]-bridged complexes with human BolA2.

Michael K. Johnson, Sajini Randeniya, Daphne T. Mapolelo, 2012, Biochemistry.

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*

D. Winge, Michael K. Johnson, Daphne T. Mapolelo, 2010, The Journal of Biological Chemistry.

The E. coli BolA protein IbaG forms a histidine-ligated [2Fe-2S] bridged complex with Grx4

Bo Zhang, Michael K. Johnson, Sajini Randeniya, 2017 .